data_27434 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H chemical shift assignment of the Interfacial contact of phycocyanobilin chromophore in the plant phytochrome A in its Pfr state. ; _BMRB_accession_number 27434 _BMRB_flat_file_name bmr27434.str _Entry_type original _Submission_date 2018-03-26 _Accession_date 2018-03-26 _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 Song Chen . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 86 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2018-05-22 original BMRB . stop_ _Original_release_date 2018-03-26 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; 3D Structures of Plant Phytochrome A as Pr and Pfr From Solid-State NMR: Implications for Molecular Function ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 29740459 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Song Chen . . 2 Mroginski 'Maria Andrea' A. . 3 Lang Christina . . 4 Kopycki Jakub . . 5 Gartner Wolfgang . . 6 Matysik Jorg . . 7 Hughes Jon . . stop_ _Journal_abbreviation 'Front. Plant Sci.' _Journal_name_full 'Frontiers in plant science' _Journal_volume 9 _Journal_issue . _Journal_ISSN 1664-462X _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 498 _Page_last 498 _Year 2018 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'oat phyA3' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'oat phyA3' $oat_phyA3 PCB $entity_PCB 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_oat_phyA3 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common oat_phyA3 _Molecular_mass . _Mol_thiol_state unknown _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 527 _Mol_residue_sequence ; SEKVIAYLQXIQKGKLIQTF GCLLALDEKSFNVIAFSENA PEMLTTVSXAVPSVDDPPRL GIGTNVRSLFSDQGATALXK ALGFADVSLLNPILVQCKTS GKPFYAIVXRATGCLVVDFE PVKPTEFPATAAGALQSYKL AAKAISKIQSLPGGSMEVLC NTVVKEVFDLTGYDRVMAYK FXEDDXGEVFSEITKPGLEP YLGLXYPATDIPQAARLLFM KNKVRMICDCRARSIKVIEA EALPFDISLCGSALRAPXSC XLQYMENMNSIASLVMAVVV NENEEDDEAESEQPAQQQKK KKLWGLLVCXXESPRYVPFP LRYACEFLAQVFAVXVNREF ELEKQLREKNILKMQTMLSD MLFREASPLTIVSGTPNIMD LVKCDGAALLYGGKVWRLRN APTESQIXDIAFWLSDVXRD STGLSTDSLXDAGYPGAAAL GDMICGMAVAKINSKDILFW FRSXTAAEIRWGGAKNDPSD MDDSRRMXPRLSFKAFLEVV KMKSLPWSDYEMDAIXSLQL ILRGTLN ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 63 SER 2 64 GLU 3 65 LYS 4 66 VAL 5 67 ILE 6 68 ALA 7 69 TYR 8 70 LEU 9 71 GLN 10 72 HSE 11 73 ILE 12 74 GLN 13 75 LYS 14 76 GLY 15 77 LYS 16 78 LEU 17 79 ILE 18 80 GLN 19 81 THR 20 82 PHE 21 83 GLY 22 84 CYS 23 85 LEU 24 86 LEU 25 87 ALA 26 88 LEU 27 89 ASP 28 90 GLU 29 91 LYS 30 92 SER 31 93 PHE 32 94 ASN 33 95 VAL 34 96 ILE 35 97 ALA 36 98 PHE 37 99 SER 38 100 GLU 39 101 ASN 40 102 ALA 41 103 PRO 42 104 GLU 43 105 MET 44 106 LEU 45 107 THR 46 108 THR 47 109 VAL 48 110 SER 49 111 HSD 50 112 ALA 51 113 VAL 52 114 PRO 53 115 SER 54 116 VAL 55 117 ASP 56 118 ASP 57 119 PRO 58 120 PRO 59 121 ARG 60 122 LEU 61 123 GLY 62 124 ILE 63 125 GLY 64 126 THR 65 127 ASN 66 128 VAL 67 129 ARG 68 130 SER 69 131 LEU 70 132 PHE 71 133 SER 72 134 ASP 73 135 GLN 74 136 GLY 75 137 ALA 76 138 THR 77 139 ALA 78 140 LEU 79 141 HSD 80 142 LYS 81 143 ALA 82 144 LEU 83 145 GLY 84 146 PHE 85 147 ALA 86 148 ASP 87 149 VAL 88 150 SER 89 151 LEU 90 152 LEU 91 153 ASN 92 154 PRO 93 155 ILE 94 156 LEU 95 157 VAL 96 158 GLN 97 159 CYS 98 160 LYS 99 161 THR 100 162 SER 101 163 GLY 102 164 LYS 103 165 PRO 104 166 PHE 105 167 TYR 106 168 ALA 107 169 ILE 108 170 VAL 109 171 HSD 110 172 ARG 111 173 ALA 112 174 THR 113 175 GLY 114 176 CYS 115 177 LEU 116 178 VAL 117 179 VAL 118 180 ASP 119 181 PHE 120 182 GLU 121 183 PRO 122 184 VAL 123 185 LYS 124 186 PRO 125 187 THR 126 188 GLU 127 189 PHE 128 190 PRO 129 191 ALA 130 192 THR 131 193 ALA 132 194 ALA 133 195 GLY 134 196 ALA 135 197 LEU 136 198 GLN 137 199 SER 138 200 TYR 139 201 LYS 140 202 LEU 141 203 ALA 142 204 ALA 143 205 LYS 144 206 ALA 145 207 ILE 146 208 SER 147 209 LYS 148 210 ILE 149 211 GLN 150 212 SER 151 213 LEU 152 214 PRO 153 215 GLY 154 216 GLY 155 217 SER 156 218 MET 157 219 GLU 158 220 VAL 159 221 LEU 160 222 CYS 161 223 ASN 162 224 THR 163 225 VAL 164 226 VAL 165 227 LYS 166 228 GLU 167 229 VAL 168 230 PHE 169 231 ASP 170 232 LEU 171 233 THR 172 234 GLY 173 235 TYR 174 236 ASP 175 237 ARG 176 238 VAL 177 239 MET 178 240 ALA 179 241 TYR 180 242 LYS 181 243 PHE 182 244 HSD 183 245 GLU 184 246 ASP 185 247 ASP 186 248 HSD 187 249 GLY 188 250 GLU 189 251 VAL 190 252 PHE 191 253 SER 192 254 GLU 193 255 ILE 194 256 THR 195 257 LYS 196 258 PRO 197 259 GLY 198 260 LEU 199 261 GLU 200 262 PRO 201 263 TYR 202 264 LEU 203 265 GLY 204 266 LEU 205 267 HSD 206 268 TYR 207 269 PRO 208 270 ALA 209 271 THR 210 272 ASP 211 273 ILE 212 274 PRO 213 275 GLN 214 276 ALA 215 277 ALA 216 278 ARG 217 279 LEU 218 280 LEU 219 281 PHE 220 282 MET 221 283 LYS 222 284 ASN 223 285 LYS 224 286 VAL 225 287 ARG 226 288 MET 227 289 ILE 228 290 CYS 229 291 ASP 230 292 CYS 231 293 ARG 232 294 ALA 233 295 ARG 234 296 SER 235 297 ILE 236 298 LYS 237 299 VAL 238 300 ILE 239 301 GLU 240 302 ALA 241 303 GLU 242 304 ALA 243 305 LEU 244 306 PRO 245 307 PHE 246 308 ASP 247 309 ILE 248 310 SER 249 311 LEU 250 312 CYS 251 313 GLY 252 314 SER 253 315 ALA 254 316 LEU 255 317 ARG 256 318 ALA 257 319 PRO 258 320 HSE 259 321 SER 260 322 CYS 261 323 HSE 262 324 LEU 263 325 GLN 264 326 TYR 265 327 MET 266 328 GLU 267 329 ASN 268 330 MET 269 331 ASN 270 332 SER 271 333 ILE 272 334 ALA 273 335 SER 274 336 LEU 275 337 VAL 276 338 MET 277 339 ALA 278 340 VAL 279 341 VAL 280 342 VAL 281 343 ASN 282 344 GLU 283 345 ASN 284 346 GLU 285 347 GLU 286 348 ASP 287 349 ASP 288 350 GLU 289 351 ALA 290 352 GLU 291 353 SER 292 354 GLU 293 355 GLN 294 356 PRO 295 357 ALA 296 358 GLN 297 359 GLN 298 360 GLN 299 361 LYS 300 362 LYS 301 363 LYS 302 364 LYS 303 365 LEU 304 366 TRP 305 367 GLY 306 368 LEU 307 369 LEU 308 370 VAL 309 371 CYS 310 372 HSE 311 373 HSD 312 374 GLU 313 375 SER 314 376 PRO 315 377 ARG 316 378 TYR 317 379 VAL 318 380 PRO 319 381 PHE 320 382 PRO 321 383 LEU 322 384 ARG 323 385 TYR 324 386 ALA 325 387 CYS 326 388 GLU 327 389 PHE 328 390 LEU 329 391 ALA 330 392 GLN 331 393 VAL 332 394 PHE 333 395 ALA 334 396 VAL 335 397 HSD 336 398 VAL 337 399 ASN 338 400 ARG 339 401 GLU 340 402 PHE 341 403 GLU 342 404 LEU 343 405 GLU 344 406 LYS 345 407 GLN 346 408 LEU 347 409 ARG 348 410 GLU 349 411 LYS 350 412 ASN 351 413 ILE 352 414 LEU 353 415 LYS 354 416 MET 355 417 GLN 356 418 THR 357 419 MET 358 420 LEU 359 421 SER 360 422 ASP 361 423 MET 362 424 LEU 363 425 PHE 364 426 ARG 365 427 GLU 366 428 ALA 367 429 SER 368 430 PRO 369 431 LEU 370 432 THR 371 433 ILE 372 434 VAL 373 435 SER 374 436 GLY 375 437 THR 376 438 PRO 377 439 ASN 378 440 ILE 379 441 MET 380 442 ASP 381 443 LEU 382 444 VAL 383 445 LYS 384 446 CYS 385 447 ASP 386 448 GLY 387 449 ALA 388 450 ALA 389 451 LEU 390 452 LEU 391 453 TYR 392 454 GLY 393 455 GLY 394 456 LYS 395 457 VAL 396 458 TRP 397 459 ARG 398 460 LEU 399 461 ARG 400 462 ASN 401 463 ALA 402 464 PRO 403 465 THR 404 466 GLU 405 467 SER 406 468 GLN 407 469 ILE 408 470 HSD 409 471 ASP 410 472 ILE 411 473 ALA 412 474 PHE 413 475 TRP 414 476 LEU 415 477 SER 416 478 ASP 417 479 VAL 418 480 HSD 419 481 ARG 420 482 ASP 421 483 SER 422 484 THR 423 485 GLY 424 486 LEU 425 487 SER 426 488 THR 427 489 ASP 428 490 SER 429 491 LEU 430 492 HSD 431 493 ASP 432 494 ALA 433 495 GLY 434 496 TYR 435 497 PRO 436 498 GLY 437 499 ALA 438 500 ALA 439 501 ALA 440 502 LEU 441 503 GLY 442 504 ASP 443 505 MET 444 506 ILE 445 507 CYS 446 508 GLY 447 509 MET 448 510 ALA 449 511 VAL 450 512 ALA 451 513 LYS 452 514 ILE 453 515 ASN 454 516 SER 455 517 LYS 456 518 ASP 457 519 ILE 458 520 LEU 459 521 PHE 460 522 TRP 461 523 PHE 462 524 ARG 463 525 SER 464 526 HSD 465 527 THR 466 528 ALA 467 529 ALA 468 530 GLU 469 531 ILE 470 532 ARG 471 533 TRP 472 534 GLY 473 535 GLY 474 536 ALA 475 537 LYS 476 538 ASN 477 539 ASP 478 540 PRO 479 541 SER 480 542 ASP 481 543 MET 482 544 ASP 483 545 ASP 484 546 SER 485 547 ARG 486 548 ARG 487 549 MET 488 550 HSD 489 551 PRO 490 552 ARG 491 553 LEU 492 554 SER 493 555 PHE 494 556 LYS 495 557 ALA 496 558 PHE 497 559 LEU 498 560 GLU 499 561 VAL 500 562 VAL 501 563 LYS 502 564 MET 503 565 LYS 504 566 SER 505 567 LEU 506 568 PRO 507 569 TRP 508 570 SER 509 571 ASP 510 572 TYR 511 573 GLU 512 574 MET 513 575 ASP 514 576 ALA 515 577 ILE 516 578 HSD 517 579 SER 518 580 LEU 519 581 GLN 520 582 LEU 521 583 ILE 522 584 LEU 523 585 ARG 524 586 GLY 525 587 THR 526 588 LEU 527 589 ASN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ###################### # Polymer residues # ###################### save_chem_comp_HSE _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common L-HOMOSERINE _BMRB_code HSE _PDB_code HSE _Standard_residue_derivative . _Molecular_mass 119.119 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons NA NA N . 0 . ? C1 C1 C . 0 . ? C2 C2 C . 0 . ? C3 C3 C . 0 . ? O1 O1 O . 0 . ? O2 O2 O . 0 . ? C4 C4 C . 0 . ? O3 O3 O . 0 . ? HN1 HN1 H . 0 . ? HN2 HN2 H . 0 . ? H1 H1 H . 0 . ? H31 H31 H . 0 . ? H32 H32 H . 0 . ? HO2 HO2 H . 0 . ? H41 H41 H . 0 . ? H42 H42 H . 0 . ? HO3 HO3 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING NA C1 ? ? SING NA HN1 ? ? SING NA HN2 ? ? SING C1 C2 ? ? SING C1 C3 ? ? SING C1 H1 ? ? DOUB C2 O1 ? ? SING C2 O2 ? ? SING C3 C4 ? ? SING C3 H31 ? ? SING C3 H32 ? ? SING O2 HO2 ? ? SING C4 O3 ? ? SING C4 H41 ? ? SING C4 H42 ? ? SING O3 HO3 ? ? stop_ save_ save_chem_comp_HSD _Saveframe_category polymer_residue _Mol_type NON-POLYMER _Name_common (1S,2S,3R,6R)-6-amino-4-(hydroxymethyl)cyclohex-4-ene-1,2,3-triol _BMRB_code HSD _PDB_code HSD _Standard_residue_derivative . _Molecular_mass 175.182 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N1 N1 N . 0 . ? C1 C1 C . 0 . ? C2 C2 C . 0 . ? C3 C3 C . 0 . ? C4 C4 C . 0 . ? O1 O1 O . 0 . ? C5 C5 C . 0 . ? O2 O2 O . 0 . ? C6 C6 C . 0 . ? O3 O3 O . 0 . ? C7 C7 C . 0 . ? O4 O4 O . 0 . ? H1 H1 H . 0 . ? H2 H2 H . 0 . ? H3 H3 H . 0 . ? H4 H4 H . 0 . ? H5 H5 H . 0 . ? H6 H6 H . 0 . ? H7 H7 H . 0 . ? H8 H8 H . 0 . ? H9 H9 H . 0 . ? H10 H10 H . 0 . ? H11 H11 H . 0 . ? H12 H12 H . 0 . ? H13 H13 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N1 C1 ? ? SING C1 C2 ? ? DOUB C2 C3 ? ? SING C3 C4 ? ? SING C4 O1 ? ? SING C3 C5 ? ? SING C5 O2 ? ? SING C5 C6 ? ? SING C6 O3 ? ? SING C6 C7 ? ? SING C1 C7 ? ? SING C7 O4 ? ? SING N1 H1 ? ? SING N1 H2 ? ? SING C1 H3 ? ? SING C2 H4 ? ? SING C4 H5 ? ? SING C4 H6 ? ? SING O1 H7 ? ? SING C5 H8 ? ? SING O2 H9 ? ? SING C6 H10 ? ? SING O3 H11 ? ? SING C7 H12 ? ? SING O4 H13 ? ? stop_ save_ ############# # Ligands # ############# save_PCB _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common "entity_PCB (4,4'-BIS([H]METHYLSULFONYL)-2,2',5,5'-TETRACHLOROBIPHENYL)" _BMRB_code PCB _PDB_code PCB _Molecular_mass 448.169 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C . 0 . ? C2 C2 C . 0 . ? CL2 CL2 CL . 0 . ? C3 C3 C . 0 . ? C4 C4 C . 0 . ? C5 C5 C . 0 . ? CL5 CL5 CL . 0 . ? C6 C6 C . 0 . ? S S S . 0 . ? O1 O1 O . 0 . ? O2 O2 O . 0 . ? CM CM C . 0 . ? C1' C1' C . 0 . ? C2' C2' C . 0 . ? CL2' CL2' CL . 0 . ? C3' C3' C . 0 . ? C4' C4' C . 0 . ? C5' C5' C . 0 . ? CL5' CL5' CL . 0 . ? C6' C6' C . 0 . ? S' S' S . 0 . ? O1' O1' O . 0 . ? O2' O2' O . 0 . ? CM' CM' C . 0 . ? H3 H3 H . 0 . ? H6 H6 H . 0 . ? HM1 HM1 H . 0 . ? HM2 HM2 H . 0 . ? HM3 HM3 H . 0 . ? H3' H3' H . 0 . ? H6' H6' H . 0 . ? HM'1 HM'1 H . 0 . ? HM'2 HM'2 H . 0 . ? HM'3 HM'3 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name DOUB C1 C2 ? ? SING C1 C6 ? ? SING C1 C1' ? ? SING C2 CL2 ? ? SING C2 C3 ? ? DOUB C3 C4 ? ? SING C3 H3 ? ? SING C4 C5 ? ? SING C4 S ? ? SING C5 CL5 ? ? DOUB C5 C6 ? ? SING C6 H6 ? ? DOUB S O1 ? ? DOUB S O2 ? ? SING S CM ? ? SING CM HM1 ? ? SING CM HM2 ? ? SING CM HM3 ? ? DOUB C1' C2' ? ? SING C1' C6' ? ? SING C2' CL2' ? ? SING C2' C3' ? ? DOUB C3' C4' ? ? SING C3' H3' ? ? SING C4' C5' ? ? SING C4' S' ? ? SING C5' CL5' ? ? DOUB C5' C6' ? ? SING C6' H6' ? ? DOUB S' O1' ? ? DOUB S' O2' ? ? SING S' CM' ? ? SING CM' HM'1 ? ? SING CM' HM'2 ? ? SING CM' HM'3 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $oat_phyA3 'Thale cress' 3702 Eukaryota Viridiplantae Arabidopsis thaliana 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 $oat_phyA3 'recombinant technology' . Escherichia coli . n.a. stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solid _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $oat_phyA3 2 mM '[U-100% 13C; U-100% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.115 loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 750 _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_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 233 . 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 TMS H 1 protons ppm 0 external direct . . . 1.0 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_PCB_in_oat_phyA_as_Pfr _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' 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 'oat phyA3' _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 63 1 SER HG H 6.9 0.1 1 2 67 5 ILE HG12 H 2.2 0.1 1 3 67 5 ILE HG13 H 2.2 0.1 1 4 67 5 ILE HG2 H 2.2 0.1 1 5 67 5 ILE HD1 H 1.3 0.1 1 6 69 7 TYR HD2 H 9.4 0.1 1 7 69 7 TYR HE2 H 10.1 0.1 1 8 241 179 TYR HB2 H 3.2 0.1 1 9 241 179 TYR HB3 H 3.2 0.1 1 10 241 179 TYR HD2 H 8.6 0.1 1 11 241 179 TYR HE2 H 8.8 0.1 1 12 242 180 LYS H H 12.3 0.1 1 13 243 181 PHE HD1 H 8.5 0.1 1 14 243 181 PHE HE1 H 7.9 0.1 1 15 243 181 PHE HZ H 7.0 0.1 1 16 248 186 HSD H H 11.7 0.1 1 17 248 186 HSD HA2 H 4.5 0.1 1 18 248 186 HSD HA3 H 4.5 0.1 1 19 250 188 GLU H H 10.8 0.1 1 20 250 188 GLU HA H 5.5 0.1 1 21 268 206 TYR HB2 H 3.7 0.1 1 22 268 206 TYR HB3 H 3.7 0.1 1 23 268 206 TYR HE2 H 10.5 0.1 1 24 271 209 THR HB H 4.7 0.1 1 25 271 209 THR HG1 H 9.7 0.1 1 26 272 210 ASP HA H 5.3 0.1 1 27 272 210 ASP HB2 H 2.9 0.1 1 28 272 210 ASP HB3 H 2.9 0.1 1 29 273 211 ILE HA H 4.8 0.1 1 30 273 211 ILE HG12 H 1.4 0.1 1 31 273 211 ILE HG13 H 1.4 0.1 1 32 273 211 ILE HD1 H 2.0 0.1 1 33 274 212 PRO HB2 H 2.9 0.1 1 34 274 212 PRO HB3 H 2.9 0.1 1 35 274 212 PRO HG2 H 3.7 0.1 1 36 274 212 PRO HG3 H 3.7 0.1 1 37 274 212 PRO HD2 H 6.2 0.1 1 38 274 212 PRO HD3 H 6.2 0.1 1 39 277 215 ALA HB H 2.3 0.1 1 40 281 219 PHE HE1 H 7.7 0.1 1 41 281 219 PHE HZ H 7.1 0.1 1 42 287 225 ARG HD2 H 5.0 0.1 1 43 287 225 ARG HD3 H 5.0 0.1 1 44 287 225 ARG HE H 10.0 0.1 1 45 287 225 ARG HH22 H 9.9 0.1 1 46 289 227 ILE HD1 H 1.9 0.1 1 47 317 255 ARG HH11 H 11.7 0.1 1 48 317 255 ARG HH22 H 8.5 0.1 1 49 319 257 PRO HA H 5.8 0.1 1 50 319 257 PRO HB2 H 2.9 0.1 1 51 319 257 PRO HB3 H 2.9 0.1 1 52 320 258 HSE H H 12.4 0.1 1 53 320 258 HSE HA H 5.0 0.1 1 54 322 260 CYS H H 12.0 0.1 1 55 322 260 CYS HA H 5.8 0.1 1 56 322 260 CYS HB2 H 4.9 0.1 1 57 322 260 CYS HB3 H 4.9 0.1 1 58 323 261 HSE HA H 5.4 0.1 1 59 323 261 HSE HB2 H 4.3 0.1 1 60 323 261 HSE HB3 H 4.3 0.1 1 61 323 261 HSE HE1 H 12.3 0.1 1 62 323 261 HSE HE2 H 13.5 0.1 1 63 326 264 TYR HD1 H 10.5 0.1 1 64 326 264 TYR HE1 H 11.7 0.1 1 65 326 264 TYR HE2 H 10.8 0.1 1 66 326 264 TYR HH H 10.0 0.1 1 67 330 268 MET HE H 3.3 0.1 1 68 335 273 SER HB2 H 4.0 0.1 1 69 335 273 SER HB3 H 4.0 0.1 1 70 337 275 VAL HB H 2.3 0.1 1 71 337 275 VAL HG1 H 1.1 0.1 1 72 368 306 LEU HB2 H 2.9 0.1 1 73 368 306 LEU HB3 H 2.9 0.1 1 74 368 306 LEU HD1 H 1.8 0.1 1 75 370 308 VAL HG1 H 1.1 0.1 1 76 372 310 HSE HD2 H 11.5 0.1 1 77 372 310 HSE HE1 H 9.9 0.1 1 78 372 310 HSE HE2 H 12.8 0.1 1 79 548 486 ARG HB2 H 3.3 0.1 1 80 548 486 ARG HB3 H 3.3 0.1 1 81 549 487 MET HG2 H 4.3 0.1 1 82 549 487 MET HG3 H 4.3 0.1 1 83 549 487 MET HE H 2.9 0.1 1 84 554 492 SER HB2 H 5.2 0.1 1 85 554 492 SER HB3 H 5.2 0.1 1 86 554 492 SER HG H 6.8 0.1 1 stop_ save_