data_2651 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Site-Directed Mutagenesis and 1H NMR Spectroscopy of an Interdomain Segment in the Pyruvate Dehydrogenase Multienzyme Complex of Escherichia coli ; _BMRB_accession_number 2651 _BMRB_flat_file_name bmr2651.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-03-25 _Entry_origination BMRB _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 Texter Frieda L. . 2 Radford Sheena E. . 3 Laue Ernest D. . 4 Perham Richard N. . 5 Miles John S. . 6 Guest John R. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 2 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-17 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Texter, Frieda L., Radford, Sheena E., Laue, Ernest D., Perham, Richard N., Miles, John S., Guest, John R., "Site-Directed Mutagenesis and 1H NMR Spectroscopy of an Interdomain Segment in the Pyruvate Dehydrogenase Multienzyme Complex of Escherichia coli," Biochemistry 27 (1), 289-296 (1988). ; _Citation_title ; Site-Directed Mutagenesis and 1H NMR Spectroscopy of an Interdomain Segment in the Pyruvate Dehydrogenase Multienzyme Complex of Escherichia coli ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Texter Frieda L. . 2 Radford Sheena E. . 3 Laue Ernest D. . 4 Perham Richard N. . 5 Miles John S. . 6 Guest John R. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 27 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 289 _Page_last 296 _Year 1988 _Details . save_ ################################## # Molecular system description # ################################## save_system_lipoate_acetyltransferase _Saveframe_category molecular_system _Mol_system_name 'lipoate acetyltransferase' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'lipoate acetyltransferase' $lipoate_acetyltransferase stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_lipoate_acetyltransferase _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'lipoate acetyltransferase' _Name_variant 'interdomain segment' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 424 _Mol_residue_sequence ; AIEIKVPDIGADEVEITEIL VKVGDKVEAEQSLITVEGDK ASMEVPAPFAGVVKELKVNV GDKVKTGSLIMIFEVEGAAP AAAPAKHEAAAPAPAAKAEA PAAAPAAKAEGKSEFAENDA YVHATPLIRRLAREFGVNLA KVKGTGRKGRILREDVQAYV KEAIKRAEAAPAATGGGIPG MLPWPKVDFSKFGEIEEVEL GRIQKISGANLSRNWVMIPH VTHFDKTDITELEAFRKQQN EEAAKRKLDVKITPVVFIMK AVAAALEQMPRFNSSLSEDG QRLTLKKYINIGVAVDTPNG LVVPVFKDVNKKGIIELSRE LMTISKKARDGKLTAGEMQG GCFTISSGGLGTTHFAPIVN APEVAILGVSKSAMEPVWNG KEFVPRLMLPISLSFDHRVI DGADGARFITIINNTLSDIR RLVM ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 ILE 3 GLU 4 ILE 5 LYS 6 VAL 7 PRO 8 ASP 9 ILE 10 GLY 11 ALA 12 ASP 13 GLU 14 VAL 15 GLU 16 ILE 17 THR 18 GLU 19 ILE 20 LEU 21 VAL 22 LYS 23 VAL 24 GLY 25 ASP 26 LYS 27 VAL 28 GLU 29 ALA 30 GLU 31 GLN 32 SER 33 LEU 34 ILE 35 THR 36 VAL 37 GLU 38 GLY 39 ASP 40 LYS 41 ALA 42 SER 43 MET 44 GLU 45 VAL 46 PRO 47 ALA 48 PRO 49 PHE 50 ALA 51 GLY 52 VAL 53 VAL 54 LYS 55 GLU 56 LEU 57 LYS 58 VAL 59 ASN 60 VAL 61 GLY 62 ASP 63 LYS 64 VAL 65 LYS 66 THR 67 GLY 68 SER 69 LEU 70 ILE 71 MET 72 ILE 73 PHE 74 GLU 75 VAL 76 GLU 77 GLY 78 ALA 79 ALA 80 PRO 81 ALA 82 ALA 83 ALA 84 PRO 85 ALA 86 LYS 87 HIS 88 GLU 89 ALA 90 ALA 91 ALA 92 PRO 93 ALA 94 PRO 95 ALA 96 ALA 97 LYS 98 ALA 99 GLU 100 ALA 101 PRO 102 ALA 103 ALA 104 ALA 105 PRO 106 ALA 107 ALA 108 LYS 109 ALA 110 GLU 111 GLY 112 LYS 113 SER 114 GLU 115 PHE 116 ALA 117 GLU 118 ASN 119 ASP 120 ALA 121 TYR 122 VAL 123 HIS 124 ALA 125 THR 126 PRO 127 LEU 128 ILE 129 ARG 130 ARG 131 LEU 132 ALA 133 ARG 134 GLU 135 PHE 136 GLY 137 VAL 138 ASN 139 LEU 140 ALA 141 LYS 142 VAL 143 LYS 144 GLY 145 THR 146 GLY 147 ARG 148 LYS 149 GLY 150 ARG 151 ILE 152 LEU 153 ARG 154 GLU 155 ASP 156 VAL 157 GLN 158 ALA 159 TYR 160 VAL 161 LYS 162 GLU 163 ALA 164 ILE 165 LYS 166 ARG 167 ALA 168 GLU 169 ALA 170 ALA 171 PRO 172 ALA 173 ALA 174 THR 175 GLY 176 GLY 177 GLY 178 ILE 179 PRO 180 GLY 181 MET 182 LEU 183 PRO 184 TRP 185 PRO 186 LYS 187 VAL 188 ASP 189 PHE 190 SER 191 LYS 192 PHE 193 GLY 194 GLU 195 ILE 196 GLU 197 GLU 198 VAL 199 GLU 200 LEU 201 GLY 202 ARG 203 ILE 204 GLN 205 LYS 206 ILE 207 SER 208 GLY 209 ALA 210 ASN 211 LEU 212 SER 213 ARG 214 ASN 215 TRP 216 VAL 217 MET 218 ILE 219 PRO 220 HIS 221 VAL 222 THR 223 HIS 224 PHE 225 ASP 226 LYS 227 THR 228 ASP 229 ILE 230 THR 231 GLU 232 LEU 233 GLU 234 ALA 235 PHE 236 ARG 237 LYS 238 GLN 239 GLN 240 ASN 241 GLU 242 GLU 243 ALA 244 ALA 245 LYS 246 ARG 247 LYS 248 LEU 249 ASP 250 VAL 251 LYS 252 ILE 253 THR 254 PRO 255 VAL 256 VAL 257 PHE 258 ILE 259 MET 260 LYS 261 ALA 262 VAL 263 ALA 264 ALA 265 ALA 266 LEU 267 GLU 268 GLN 269 MET 270 PRO 271 ARG 272 PHE 273 ASN 274 SER 275 SER 276 LEU 277 SER 278 GLU 279 ASP 280 GLY 281 GLN 282 ARG 283 LEU 284 THR 285 LEU 286 LYS 287 LYS 288 TYR 289 ILE 290 ASN 291 ILE 292 GLY 293 VAL 294 ALA 295 VAL 296 ASP 297 THR 298 PRO 299 ASN 300 GLY 301 LEU 302 VAL 303 VAL 304 PRO 305 VAL 306 PHE 307 LYS 308 ASP 309 VAL 310 ASN 311 LYS 312 LYS 313 GLY 314 ILE 315 ILE 316 GLU 317 LEU 318 SER 319 ARG 320 GLU 321 LEU 322 MET 323 THR 324 ILE 325 SER 326 LYS 327 LYS 328 ALA 329 ARG 330 ASP 331 GLY 332 LYS 333 LEU 334 THR 335 ALA 336 GLY 337 GLU 338 MET 339 GLN 340 GLY 341 GLY 342 CYS 343 PHE 344 THR 345 ILE 346 SER 347 SER 348 GLY 349 GLY 350 LEU 351 GLY 352 THR 353 THR 354 HIS 355 PHE 356 ALA 357 PRO 358 ILE 359 VAL 360 ASN 361 ALA 362 PRO 363 GLU 364 VAL 365 ALA 366 ILE 367 LEU 368 GLY 369 VAL 370 SER 371 LYS 372 SER 373 ALA 374 MET 375 GLU 376 PRO 377 VAL 378 TRP 379 ASN 380 GLY 381 LYS 382 GLU 383 PHE 384 VAL 385 PRO 386 ARG 387 LEU 388 MET 389 LEU 390 PRO 391 ILE 392 SER 393 LEU 394 SER 395 PHE 396 ASP 397 HIS 398 ARG 399 VAL 400 ILE 401 ASP 402 GLY 403 ALA 404 ASP 405 GLY 406 ALA 407 ARG 408 PHE 409 ILE 410 THR 411 ILE 412 ILE 413 ASN 414 ASN 415 THR 416 LEU 417 SER 418 ASP 419 ILE 420 ARG 421 ARG 422 LEU 423 VAL 424 MET stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 4N72 "Catalytic Domain From Dihydrolipoamide Acetyltransferase Of Pyruvate Dehydrogenase From Escherichia Coli" 58.73 249 99.60 99.60 1.44e-176 EMBL CEE08973 "dihydrolipoyllysine-residue acetyltransferase E2 component of pyruvate dehydrogenase complex [Escherichia coli]" 87.97 373 99.20 99.46 0.00e+00 EMBL CSE31214 "dihydrolipoamide acetyltransferase [Shigella sonnei]" 66.98 284 98.94 99.65 0.00e+00 EMBL CSE76615 "dihydrolipoamide acetyltransferase [Shigella sonnei]" 90.33 383 99.22 99.48 0.00e+00 EMBL CSE88811 "dihydrolipoamide acetyltransferase [Shigella sonnei]" 90.33 383 99.22 99.48 0.00e+00 EMBL CSE95192 "dihydrolipoamide acetyltransferase [Shigella sonnei]" 87.97 373 98.93 99.46 0.00e+00 GB AIW88354 "dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex [Bacillus weihenstephanensis]" 90.33 383 98.96 99.48 0.00e+00 GB EFI22553 "dihydrolipoamide acetyltransferase [Escherichia coli FVEC1302]" 96.70 410 98.54 99.27 0.00e+00 GB EFW65012 "Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex [Escherichia coli O157:H7 str. EC1212]" 62.74 266 99.25 99.62 0.00e+00 GB EFZ46147 "dihydrolipoyllysine-residue acetyltransferase E2 component of pyruvate dehydrogenase complex [Escherichia coli E128010]" 99.76 440 97.64 98.82 0.00e+00 GB EGB41640 "2-oxoacid dehydrogenase acyltransferase [Escherichia coli H120]" 96.93 411 98.54 99.27 0.00e+00 REF WP_000295776 "dihydrolipoamide acetyltransferase, partial [Escherichia coli]" 99.76 429 97.64 98.82 0.00e+00 REF WP_000374927 "hypothetical protein, partial [Escherichia coli]" 96.93 411 98.54 99.27 0.00e+00 REF WP_032206848 "pyruvate dehydrogenase, partial [Escherichia coli]" 100.24 477 98.12 99.06 0.00e+00 REF WP_032230881 "pyruvate dehydrogenase, partial [Escherichia coli]" 97.17 412 98.54 99.27 0.00e+00 REF WP_050541395 "pyruvate dehydrogenase, partial [Escherichia coli]" 97.41 433 98.06 99.27 0.00e+00 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _ICTVdb_decimal_code _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $lipoate_acetyltransferase . Eubacteria 562 . . Escherichia coli generic 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 $lipoate_acetyltransferase 'not available' . Escherichia coli 'JRG1342(aceEF-lpd del recA)' . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7 . na temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _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_citation_label _Correction_value_citation_label TSP H . . ppm 0 . . . . . $entry_citation $entry_citation 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_chemical_shift_assignment_data_set_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name 'lipoate acetyltransferase' _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 . 87 HIS HD2 H 7.05 . 1 2 . 87 HIS HE1 H 7.94 . 1 stop_ save_