data_50474 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Methyl assignments of Hsp90 FL AIM LV pro-R labeled bound to AMP-PNP ; _BMRB_accession_number 50474 _BMRB_flat_file_name bmr50474.str _Entry_type original _Submission_date 2020-09-21 _Accession_date 2020-09-21 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Assignments of methyl groups of yeast Hsp90 in complex with the ATP analog AMP-PNP, using AIM LV pro-R labeling' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lopez Abraham . . 2 Sattler Michael . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 179 "13C chemical shifts" 179 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-12-16 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 50472 'Methyl assignments of Hsp90 FL AIM LV pro-R labeled' stop_ _Original_release_date 2020-09-21 save_ ############################# # Citation for this entry # ############################# save_citations_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; The co-chaperone p23 coordinates client binding and progression of the Hsp90 chaperone cycle via flexible regions ; _Citation_status 'in preparation' _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 Lopez Abraham . . 2 Sattler Michael . . stop_ _Journal_abbreviation 'Nature Communications' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . loop_ _Keyword 'Chaperone, heat shock protein 90 (Hsp90), intrinsically disordered regions, chaperone mechanism' stop_ save_ ################################## # Molecular system description # ################################## save_assembly_1 _Saveframe_category molecular_system _Mol_system_name 'Hsp90-AMPPNP complex' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Hsp90 $entity_1 AMP-PNP $entity_ANP stop_ _System_molecular_weight 162000 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 Hsp90 stop_ loop_ _Biological_function 'Molecular chaperoning' stop_ _Database_query_date . _Details ; Complex of yeast Hsp90 bound to the non-hydrolyzable ATP analog AMP-PNP: Formula: C10H17N6O12P3; Formula weight: 506.20; Formal charge: 4-. ; save_ ######################## # Monomeric polymers # ######################## save_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass . _Mol_thiol_state 'not present' loop_ _Biological_function 'Molecular chaperone' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 709 _Mol_residue_sequence ; MASETFEFQAEITQLMSLII NTVYSNKEIFLRELISNASD ALDKIRYKSLSDPKQLETEP DLFIRITPKPEQKVLEIRDS GIGMTKAELINNLGTIAKSG TKAFMEALSAGADVSMIGQF GVGFYSLFLVADRVQVISKS NDDEQYIWESNAGGSFTVTL DEVNERIGRGTILRLFLKDD QLEYLEEKRIKEVIKRHSEF VAYPIQLVVTKEVEKEVPIP EEEKKDEEKKDEEKKDEDDK KPKLEEVDEEEEKKPKTKKV KEEVQEIEELNKTKPLWTRN PSDITQEEYNAFYKSISNDW EDPLYVKHFSVEGQLEFRAI LFIPKRAPFDLFESKKKKNN IKLYVRRVFITDEAEDLIPE WLSFVKGVVDSEDLPLNLSR EMLQQNKIMKVIRKNIVKKL IEAFNEIAEDSEQFEKFYSA FSKNIKLGVHEDTQNRAALA KLLRYNSTKSVDELTSLTDY VTRMPEHQKNIYYITGESLK AVEKSPFLDALKAKNFEVLF LTDPIDEYAFTQLKEFEGKT LVDITKDFELEETDEEKAER EKEIKEYEPLTKALKEILGD QVEKVVVSYKLLDAPAAIRT GQFGWSANMERIMKAQALRD SSMSSYMSSKKTFEISPKSP IIKELKKRVDEGGAQDKTVK DLTKLLYETALLTSGFSLDE PTSFASRINRLISLGLNIDE DEETETAPEASTAAPVEEVP ADTEMEEVD ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 SER 4 GLU 5 THR 6 PHE 7 GLU 8 PHE 9 GLN 10 ALA 11 GLU 12 ILE 13 THR 14 GLN 15 LEU 16 MET 17 SER 18 LEU 19 ILE 20 ILE 21 ASN 22 THR 23 VAL 24 TYR 25 SER 26 ASN 27 LYS 28 GLU 29 ILE 30 PHE 31 LEU 32 ARG 33 GLU 34 LEU 35 ILE 36 SER 37 ASN 38 ALA 39 SER 40 ASP 41 ALA 42 LEU 43 ASP 44 LYS 45 ILE 46 ARG 47 TYR 48 LYS 49 SER 50 LEU 51 SER 52 ASP 53 PRO 54 LYS 55 GLN 56 LEU 57 GLU 58 THR 59 GLU 60 PRO 61 ASP 62 LEU 63 PHE 64 ILE 65 ARG 66 ILE 67 THR 68 PRO 69 LYS 70 PRO 71 GLU 72 GLN 73 LYS 74 VAL 75 LEU 76 GLU 77 ILE 78 ARG 79 ASP 80 SER 81 GLY 82 ILE 83 GLY 84 MET 85 THR 86 LYS 87 ALA 88 GLU 89 LEU 90 ILE 91 ASN 92 ASN 93 LEU 94 GLY 95 THR 96 ILE 97 ALA 98 LYS 99 SER 100 GLY 101 THR 102 LYS 103 ALA 104 PHE 105 MET 106 GLU 107 ALA 108 LEU 109 SER 110 ALA 111 GLY 112 ALA 113 ASP 114 VAL 115 SER 116 MET 117 ILE 118 GLY 119 GLN 120 PHE 121 GLY 122 VAL 123 GLY 124 PHE 125 TYR 126 SER 127 LEU 128 PHE 129 LEU 130 VAL 131 ALA 132 ASP 133 ARG 134 VAL 135 GLN 136 VAL 137 ILE 138 SER 139 LYS 140 SER 141 ASN 142 ASP 143 ASP 144 GLU 145 GLN 146 TYR 147 ILE 148 TRP 149 GLU 150 SER 151 ASN 152 ALA 153 GLY 154 GLY 155 SER 156 PHE 157 THR 158 VAL 159 THR 160 LEU 161 ASP 162 GLU 163 VAL 164 ASN 165 GLU 166 ARG 167 ILE 168 GLY 169 ARG 170 GLY 171 THR 172 ILE 173 LEU 174 ARG 175 LEU 176 PHE 177 LEU 178 LYS 179 ASP 180 ASP 181 GLN 182 LEU 183 GLU 184 TYR 185 LEU 186 GLU 187 GLU 188 LYS 189 ARG 190 ILE 191 LYS 192 GLU 193 VAL 194 ILE 195 LYS 196 ARG 197 HIS 198 SER 199 GLU 200 PHE 201 VAL 202 ALA 203 TYR 204 PRO 205 ILE 206 GLN 207 LEU 208 VAL 209 VAL 210 THR 211 LYS 212 GLU 213 VAL 214 GLU 215 LYS 216 GLU 217 VAL 218 PRO 219 ILE 220 PRO 221 GLU 222 GLU 223 GLU 224 LYS 225 LYS 226 ASP 227 GLU 228 GLU 229 LYS 230 LYS 231 ASP 232 GLU 233 GLU 234 LYS 235 LYS 236 ASP 237 GLU 238 ASP 239 ASP 240 LYS 241 LYS 242 PRO 243 LYS 244 LEU 245 GLU 246 GLU 247 VAL 248 ASP 249 GLU 250 GLU 251 GLU 252 GLU 253 LYS 254 LYS 255 PRO 256 LYS 257 THR 258 LYS 259 LYS 260 VAL 261 LYS 262 GLU 263 GLU 264 VAL 265 GLN 266 GLU 267 ILE 268 GLU 269 GLU 270 LEU 271 ASN 272 LYS 273 THR 274 LYS 275 PRO 276 LEU 277 TRP 278 THR 279 ARG 280 ASN 281 PRO 282 SER 283 ASP 284 ILE 285 THR 286 GLN 287 GLU 288 GLU 289 TYR 290 ASN 291 ALA 292 PHE 293 TYR 294 LYS 295 SER 296 ILE 297 SER 298 ASN 299 ASP 300 TRP 301 GLU 302 ASP 303 PRO 304 LEU 305 TYR 306 VAL 307 LYS 308 HIS 309 PHE 310 SER 311 VAL 312 GLU 313 GLY 314 GLN 315 LEU 316 GLU 317 PHE 318 ARG 319 ALA 320 ILE 321 LEU 322 PHE 323 ILE 324 PRO 325 LYS 326 ARG 327 ALA 328 PRO 329 PHE 330 ASP 331 LEU 332 PHE 333 GLU 334 SER 335 LYS 336 LYS 337 LYS 338 LYS 339 ASN 340 ASN 341 ILE 342 LYS 343 LEU 344 TYR 345 VAL 346 ARG 347 ARG 348 VAL 349 PHE 350 ILE 351 THR 352 ASP 353 GLU 354 ALA 355 GLU 356 ASP 357 LEU 358 ILE 359 PRO 360 GLU 361 TRP 362 LEU 363 SER 364 PHE 365 VAL 366 LYS 367 GLY 368 VAL 369 VAL 370 ASP 371 SER 372 GLU 373 ASP 374 LEU 375 PRO 376 LEU 377 ASN 378 LEU 379 SER 380 ARG 381 GLU 382 MET 383 LEU 384 GLN 385 GLN 386 ASN 387 LYS 388 ILE 389 MET 390 LYS 391 VAL 392 ILE 393 ARG 394 LYS 395 ASN 396 ILE 397 VAL 398 LYS 399 LYS 400 LEU 401 ILE 402 GLU 403 ALA 404 PHE 405 ASN 406 GLU 407 ILE 408 ALA 409 GLU 410 ASP 411 SER 412 GLU 413 GLN 414 PHE 415 GLU 416 LYS 417 PHE 418 TYR 419 SER 420 ALA 421 PHE 422 SER 423 LYS 424 ASN 425 ILE 426 LYS 427 LEU 428 GLY 429 VAL 430 HIS 431 GLU 432 ASP 433 THR 434 GLN 435 ASN 436 ARG 437 ALA 438 ALA 439 LEU 440 ALA 441 LYS 442 LEU 443 LEU 444 ARG 445 TYR 446 ASN 447 SER 448 THR 449 LYS 450 SER 451 VAL 452 ASP 453 GLU 454 LEU 455 THR 456 SER 457 LEU 458 THR 459 ASP 460 TYR 461 VAL 462 THR 463 ARG 464 MET 465 PRO 466 GLU 467 HIS 468 GLN 469 LYS 470 ASN 471 ILE 472 TYR 473 TYR 474 ILE 475 THR 476 GLY 477 GLU 478 SER 479 LEU 480 LYS 481 ALA 482 VAL 483 GLU 484 LYS 485 SER 486 PRO 487 PHE 488 LEU 489 ASP 490 ALA 491 LEU 492 LYS 493 ALA 494 LYS 495 ASN 496 PHE 497 GLU 498 VAL 499 LEU 500 PHE 501 LEU 502 THR 503 ASP 504 PRO 505 ILE 506 ASP 507 GLU 508 TYR 509 ALA 510 PHE 511 THR 512 GLN 513 LEU 514 LYS 515 GLU 516 PHE 517 GLU 518 GLY 519 LYS 520 THR 521 LEU 522 VAL 523 ASP 524 ILE 525 THR 526 LYS 527 ASP 528 PHE 529 GLU 530 LEU 531 GLU 532 GLU 533 THR 534 ASP 535 GLU 536 GLU 537 LYS 538 ALA 539 GLU 540 ARG 541 GLU 542 LYS 543 GLU 544 ILE 545 LYS 546 GLU 547 TYR 548 GLU 549 PRO 550 LEU 551 THR 552 LYS 553 ALA 554 LEU 555 LYS 556 GLU 557 ILE 558 LEU 559 GLY 560 ASP 561 GLN 562 VAL 563 GLU 564 LYS 565 VAL 566 VAL 567 VAL 568 SER 569 TYR 570 LYS 571 LEU 572 LEU 573 ASP 574 ALA 575 PRO 576 ALA 577 ALA 578 ILE 579 ARG 580 THR 581 GLY 582 GLN 583 PHE 584 GLY 585 TRP 586 SER 587 ALA 588 ASN 589 MET 590 GLU 591 ARG 592 ILE 593 MET 594 LYS 595 ALA 596 GLN 597 ALA 598 LEU 599 ARG 600 ASP 601 SER 602 SER 603 MET 604 SER 605 SER 606 TYR 607 MET 608 SER 609 SER 610 LYS 611 LYS 612 THR 613 PHE 614 GLU 615 ILE 616 SER 617 PRO 618 LYS 619 SER 620 PRO 621 ILE 622 ILE 623 LYS 624 GLU 625 LEU 626 LYS 627 LYS 628 ARG 629 VAL 630 ASP 631 GLU 632 GLY 633 GLY 634 ALA 635 GLN 636 ASP 637 LYS 638 THR 639 VAL 640 LYS 641 ASP 642 LEU 643 THR 644 LYS 645 LEU 646 LEU 647 TYR 648 GLU 649 THR 650 ALA 651 LEU 652 LEU 653 THR 654 SER 655 GLY 656 PHE 657 SER 658 LEU 659 ASP 660 GLU 661 PRO 662 THR 663 SER 664 PHE 665 ALA 666 SER 667 ARG 668 ILE 669 ASN 670 ARG 671 LEU 672 ILE 673 SER 674 LEU 675 GLY 676 LEU 677 ASN 678 ILE 679 ASP 680 GLU 681 ASP 682 GLU 683 GLU 684 THR 685 GLU 686 THR 687 ALA 688 PRO 689 GLU 690 ALA 691 SER 692 THR 693 ALA 694 ALA 695 PRO 696 VAL 697 GLU 698 GLU 699 VAL 700 PRO 701 ALA 702 ASP 703 THR 704 GLU 705 MET 706 GLU 707 GLU 708 VAL 709 ASP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . 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 2cg9 Hsp90 . . . . . stop_ save_ ############# # Ligands # ############# save_ANP _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' _BMRB_code ANP _PDB_code ANP _Molecular_mass 506.196 _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 PG PG P . 0 . ? O1G O1G O . 0 . ? O2G O2G O . 0 . ? O3G O3G O . 0 . ? PB PB P . 0 . ? O1B O1B O . 0 . ? O2B O2B O . 0 . ? N3B N3B N . 0 . ? PA PA P . 0 . ? O1A O1A O . 0 . ? O2A O2A O . 0 . ? O3A O3A O . 0 . ? O5' O5' O . 0 . ? C5' C5' C . 0 . ? C4' C4' C . 0 . ? O4' O4' O . 0 . ? C3' C3' C . 0 . ? O3' O3' O . 0 . ? C2' C2' C . 0 . ? O2' O2' O . 0 . ? C1' C1' C . 0 . ? N9 N9 N . 0 . ? C8 C8 C . 0 . ? N7 N7 N . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? N6 N6 N . 0 . ? N1 N1 N . 0 . ? C2 C2 C . 0 . ? N3 N3 N . 0 . ? C4 C4 C . 0 . ? HOG2 HOG2 H . 0 . ? HOG3 HOG3 H . 0 . ? HOB2 HOB2 H . 0 . ? HNB1 HNB1 H . 0 . ? HOA2 HOA2 H . 0 . ? H5'1 H5'1 H . 0 . ? H5'2 H5'2 H . 0 . ? H4' H4' H . 0 . ? H3' H3' H . 0 . ? HO3' HO3' H . 0 . ? H2' H2' H . 0 . ? HO2' HO2' H . 0 . ? H1' H1' H . 0 . ? H8 H8 H . 0 . ? HN61 HN61 H . 0 . ? HN62 HN62 H . 0 . ? H2 H2 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 PG O1G ? ? SING PG O2G ? ? SING PG O3G ? ? SING PG N3B ? ? SING O2G HOG2 ? ? SING O3G HOG3 ? ? DOUB PB O1B ? ? SING PB O2B ? ? SING PB N3B ? ? SING PB O3A ? ? SING O2B HOB2 ? ? SING N3B HNB1 ? ? DOUB PA O1A ? ? SING PA O2A ? ? SING PA O3A ? ? SING PA O5' ? ? SING O2A HOA2 ? ? SING O5' C5' ? ? SING C5' C4' ? ? SING C5' H5'1 ? ? SING C5' H5'2 ? ? SING C4' O4' ? ? SING C4' C3' ? ? SING C4' H4' ? ? SING O4' C1' ? ? SING C3' O3' ? ? SING C3' C2' ? ? SING C3' H3' ? ? SING O3' HO3' ? ? SING C2' O2' ? ? SING C2' C1' ? ? SING C2' H2' ? ? SING O2' HO2' ? ? SING C1' N9 ? ? SING C1' H1' ? ? SING N9 C8 ? ? SING N9 C4 ? ? DOUB C8 N7 ? ? SING C8 H8 ? ? SING N7 C5 ? ? SING C5 C6 ? ? DOUB C5 C4 ? ? SING C6 N6 ? ? DOUB C6 N1 ? ? SING N6 HN61 ? ? SING N6 HN62 ? ? SING N1 C2 ? ? DOUB C2 N3 ? ? SING C2 H2 ? ? SING N3 C4 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source_1 _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity_1 "baker's yeast" 4932 Eukaryota Fungi Saccharomyces cerevisiae stop_ save_ ######################### # Experimental source # ######################### save_experimental_source_1 _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_type _Vector_name $entity_1 'recombinant technology' . Escherichia coli BL21 DE3 plasmid pETM11 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'Sample 100 uM approx, in Tris D11 buffer pH 7, 100 mM NaCl, 5 mM MgCl2' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 100 uM ; [U-2H; 99%, 13CD; 1HD-Ile,Leu; 99%, U-2H; 99%, 13CE; 1HE-Met; 99%, U-2H; 99%, 13CG; 1HDG-Val; 99%, U-2H; 99%, 13CDB; 1HB-Ala; 99%] ; $entity_ANP 5 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' TRIS 25 mM [U-2H] stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name TOPSPIN _Version 3.5 loop_ _Task collection stop_ _Details . save_ save_software_2 _Saveframe_category software _Name NMRPipe _Version . loop_ _Task processing stop_ _Details . save_ save_software_3 _Saveframe_category software _Name CcpNMR _Version 2.4.2 loop_ _Task 'data analysis' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model 'AVANCE III' _Field_strength 950 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-13C_HMQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HMQC' _Sample_label $sample_1 save_ save_4D_CC_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '4D CC NOESY' _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' 0.1 . M pH* 7 . pH pressure 1 . atm temperature 303 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_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 carbons' ppm 0 internal direct . . . 1 DSS H 1 'methyl protons' ppm 0 internal direct . . . 1 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_chemical_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $software_1 $software_2 $software_3 stop_ loop_ _Experiment_label '2D 1H-13C HMQC' '4D CC NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chem_shift_reference_1 _Mol_system_component_name Hsp90 _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 1 1 MET HE H 2.105 . 1 2 1 1 MET CE C 16.976 . 1 3 2 2 ALA HB H 1.452 . 1 4 2 2 ALA CB C 19.098 . 1 5 10 10 ALA HB H 1.474 . 1 6 10 10 ALA CB C 18.653 . 1 7 12 12 ILE HD1 H 0.823 . 1 8 12 12 ILE CD1 C 11.251 . 1 9 15 15 LEU HD1 H 0.970 . 1 10 15 15 LEU CD1 C 24.111 . 1 11 16 16 MET HE H 1.096 . 1 12 16 16 MET CE C 15.888 . 1 13 18 18 LEU HD1 H 0.815 . 1 14 18 18 LEU CD1 C 24.833 . 1 15 19 19 ILE HD1 H 0.731 . 1 16 19 19 ILE CD1 C 12.879 . 1 17 20 20 ILE HD1 H 0.833 . 1 18 20 20 ILE CD1 C 13.857 . 1 19 29 29 ILE HD1 H 0.721 . 1 20 29 29 ILE CD1 C 14.757 . 1 21 31 31 LEU HD1 H 0.661 . 1 22 31 31 LEU CD1 C 23.496 . 1 23 34 34 LEU HD1 H 0.898 . 1 24 34 34 LEU CD1 C 26.465 . 1 25 35 35 ILE HD1 H 0.654 . 1 26 35 35 ILE CD1 C 11.734 . 1 27 41 41 ALA HB H 1.447 . 1 28 41 41 ALA CB C 19.156 . 1 29 42 42 LEU HD1 H 0.094 . 1 30 42 42 LEU CD1 C 25.577 . 1 31 45 45 ILE HD1 H 0.979 . 1 32 45 45 ILE CD1 C 14.368 . 1 33 50 50 LEU HD1 H 0.912 . 1 34 50 50 LEU CD1 C 25.374 . 1 35 56 56 LEU HD1 H 1.000 . 1 36 56 56 LEU CD1 C 24.625 . 1 37 62 62 LEU HD1 H 1.005 . 1 38 62 62 LEU CD1 C 25.908 . 1 39 64 64 ILE HD1 H 0.751 . 1 40 64 64 ILE CD1 C 14.363 . 1 41 74 74 VAL HG1 H 0.479 . 1 42 74 74 VAL CG1 C 22.730 . 1 43 75 75 LEU HD1 H 0.912 . 1 44 75 75 LEU CD1 C 22.689 . 1 45 77 77 ILE HD1 H 0.808 . 1 46 77 77 ILE CD1 C 15.572 . 1 47 82 82 ILE HD1 H 0.894 . 1 48 82 82 ILE CD1 C 15.575 . 1 49 84 84 MET HE H 0.480 . 1 50 84 84 MET CE C 16.645 . 1 51 87 87 ALA HB H 1.245 . 1 52 87 87 ALA CB C 17.982 . 1 53 89 89 LEU HD1 H 0.753 . 1 54 89 89 LEU CD1 C 26.994 . 1 55 90 90 ILE HD1 H 0.549 . 1 56 90 90 ILE CD1 C 15.611 . 1 57 93 93 LEU HD1 H -1.004 . 1 58 93 93 LEU CD1 C 23.691 . 1 59 96 96 ILE HD1 H 0.800 . 1 60 96 96 ILE CD1 C 12.509 . 1 61 97 97 ALA HB H 1.414 . 1 62 97 97 ALA CB C 18.966 . 1 63 103 103 ALA HB H 1.573 . 1 64 103 103 ALA CB C 18.055 . 1 65 105 105 MET HE H 2.013 . 1 66 105 105 MET CE C 16.493 . 1 67 107 107 ALA HB H 1.270 . 1 68 107 107 ALA CB C 16.850 . 1 69 108 108 LEU HD1 H 0.366 . 1 70 108 108 LEU CD1 C 24.823 . 1 71 110 110 ALA HB H 1.463 . 1 72 110 110 ALA CB C 18.755 . 1 73 112 112 ALA HB H 1.182 . 1 74 112 112 ALA CB C 19.160 . 1 75 117 117 ILE HD1 H 0.658 . 1 76 117 117 ILE CD1 C 14.286 . 1 77 122 122 VAL HG1 H 0.849 . 1 78 122 122 VAL CG1 C 22.345 . 1 79 127 127 LEU HD1 H -0.546 . 1 80 127 127 LEU CD1 C 23.471 . 1 81 129 129 LEU HD1 H 1.016 . 1 82 129 129 LEU CD1 C 26.189 . 1 83 130 130 VAL HG1 H 0.409 . 1 84 130 130 VAL CG1 C 21.750 . 1 85 131 131 ALA HB H 1.017 . 1 86 131 131 ALA CB C 21.771 . 1 87 134 134 VAL HG1 H 1.236 . 1 88 134 134 VAL CG1 C 20.726 . 1 89 136 136 VAL HG1 H 0.397 . 1 90 136 136 VAL CG1 C 21.222 . 1 91 137 137 ILE HD1 H 0.786 . 1 92 137 137 ILE CD1 C 14.801 . 1 93 147 147 ILE HD1 H 0.817 . 1 94 147 147 ILE CD1 C 15.233 . 1 95 152 152 ALA HB H 1.186 . 1 96 152 152 ALA CB C 16.743 . 1 97 158 158 VAL HG1 H 1.036 . 1 98 158 158 VAL CG1 C 22.354 . 1 99 160 160 LEU HD1 H 0.575 . 1 100 160 160 LEU CD1 C 23.200 . 1 101 163 163 VAL HG1 H 0.849 . 1 102 163 163 VAL CG1 C 20.881 . 1 103 167 167 ILE HD1 H 0.531 . 1 104 167 167 ILE CD1 C 13.743 . 1 105 172 172 ILE HD1 H 0.776 . 1 106 172 172 ILE CD1 C 13.748 . 1 107 173 173 LEU HD1 H 0.963 . 1 108 173 173 LEU CD1 C 25.827 . 1 109 175 175 LEU HD1 H 0.752 . 1 110 175 175 LEU CD1 C 25.651 . 1 111 177 177 LEU HD1 H 0.813 . 1 112 177 177 LEU CD1 C 26.705 . 1 113 182 182 LEU HD1 H 0.999 . 1 114 182 182 LEU CD1 C 25.427 . 1 115 185 185 LEU HD1 H 0.955 . 1 116 185 185 LEU CD1 C 27.476 . 1 117 190 190 ILE HD1 H 0.827 . 1 118 190 190 ILE CD1 C 13.741 . 1 119 193 193 VAL HG1 H 0.983 . 1 120 193 193 VAL CG1 C 23.684 . 1 121 194 194 ILE HD1 H 0.732 . 1 122 194 194 ILE CD1 C 14.196 . 1 123 201 201 VAL HG1 H 1.106 . 1 124 201 201 VAL CG1 C 20.916 . 1 125 202 202 ALA HB H 1.138 . 1 126 202 202 ALA CB C 18.629 . 1 127 205 205 ILE HD1 H 0.796 . 1 128 205 205 ILE CD1 C 14.504 . 1 129 244 244 LEU HD1 H 0.905 . 1 130 244 244 LEU CD1 C 24.625 . 1 131 267 267 ILE HD1 H 0.739 . 1 132 267 267 ILE CD1 C 12.986 . 1 133 276 276 LEU HD1 H 0.558 . 1 134 276 276 LEU CD1 C 24.620 . 1 135 284 284 ILE HD1 H 0.669 . 1 136 284 284 ILE CD1 C 14.218 . 1 137 296 296 ILE HD1 H 0.714 . 1 138 296 296 ILE CD1 C 14.105 . 1 139 304 304 LEU HD1 H 1.129 . 1 140 304 304 LEU CD1 C 24.754 . 1 141 306 306 VAL HG1 H -0.164 . 1 142 306 306 VAL CG1 C 18.499 . 1 143 311 311 VAL HG1 H 0.837 . 1 144 311 311 VAL CG1 C 20.741 . 1 145 315 315 LEU HD1 H 0.959 . 1 146 315 315 LEU CD1 C 25.925 . 1 147 320 320 ILE HD1 H 0.342 . 1 148 320 320 ILE CD1 C 14.317 . 1 149 321 321 LEU HD1 H 0.870 . 1 150 321 321 LEU CD1 C 27.200 . 1 151 323 323 ILE HD1 H 0.952 . 1 152 323 323 ILE CD1 C 13.774 . 1 153 327 327 ALA HB H 1.228 . 1 154 327 327 ALA CB C 17.679 . 1 155 331 331 LEU HD1 H 0.806 . 1 156 331 331 LEU CD1 C 24.371 . 1 157 341 341 ILE HD1 H 0.424 . 1 158 341 341 ILE CD1 C 11.323 . 1 159 343 343 LEU HD1 H 0.688 . 1 160 343 343 LEU CD1 C 22.836 . 1 161 345 345 VAL HG1 H 0.975 . 1 162 345 345 VAL CG1 C 21.069 . 1 163 348 348 VAL HG1 H 0.849 . 1 164 348 348 VAL CG1 C 21.274 . 1 165 350 350 ILE HD1 H 0.624 . 1 166 350 350 ILE CD1 C 9.448 . 1 167 354 354 ALA HB H 1.149 . 1 168 354 354 ALA CB C 17.791 . 1 169 357 357 LEU HD1 H 0.703 . 1 170 357 357 LEU CD1 C 24.820 . 1 171 358 358 ILE HD1 H 0.393 . 1 172 358 358 ILE CD1 C 13.402 . 1 173 362 362 LEU HD1 H 0.280 . 1 174 362 362 LEU CD1 C 25.764 . 1 175 365 365 VAL HG1 H 0.681 . 1 176 365 365 VAL CG1 C 21.967 . 1 177 368 368 VAL HG1 H 0.487 . 1 178 368 368 VAL CG1 C 20.571 . 1 179 369 369 VAL HG1 H 0.635 . 1 180 369 369 VAL CG1 C 20.421 . 1 181 374 374 LEU HD1 H 0.792 . 1 182 374 374 LEU CD1 C 25.438 . 1 183 376 376 LEU HD1 H 0.821 . 1 184 376 376 LEU CD1 C 24.838 . 1 185 378 378 LEU HD1 H 0.875 . 1 186 378 378 LEU CD1 C 25.048 . 1 187 382 382 MET HE H 2.100 . 1 188 382 382 MET CE C 17.163 . 1 189 383 383 LEU HD1 H 0.816 . 1 190 383 383 LEU CD1 C 25.563 . 1 191 388 388 ILE HD1 H 0.821 . 1 192 388 388 ILE CD1 C 12.741 . 1 193 389 389 MET HE H 1.827 . 1 194 389 389 MET CE C 17.336 . 1 195 391 391 VAL HG1 H 1.018 . 1 196 391 391 VAL CG1 C 22.347 . 1 197 392 392 ILE HD1 H 0.458 . 1 198 392 392 ILE CD1 C 12.567 . 1 199 396 396 ILE HD1 H 0.641 . 1 200 396 396 ILE CD1 C 14.213 . 1 201 397 397 VAL HG1 H 1.017 . 1 202 397 397 VAL CG1 C 21.298 . 1 203 400 400 LEU HD1 H 0.647 . 1 204 400 400 LEU CD1 C 27.615 . 1 205 401 401 ILE HD1 H 0.868 . 1 206 401 401 ILE CD1 C 13.533 . 1 207 403 403 ALA HB H 1.352 . 1 208 403 403 ALA CB C 17.303 . 1 209 407 407 ILE HD1 H 0.159 . 1 210 407 407 ILE CD1 C 13.689 . 1 211 408 408 ALA HB H 1.007 . 1 212 408 408 ALA CB C 17.287 . 1 213 420 420 ALA HB H 0.294 . 1 214 420 420 ALA CB C 18.724 . 1 215 425 425 ILE HD1 H 0.725 . 1 216 425 425 ILE CD1 C 11.099 . 1 217 427 427 LEU HD1 H 0.962 . 1 218 427 427 LEU CD1 C 24.912 . 1 219 429 429 VAL HG1 H 0.877 . 1 220 429 429 VAL CG1 C 22.718 . 1 221 437 437 ALA HB H 1.416 . 1 222 437 437 ALA CB C 17.428 . 1 223 438 438 ALA HB H 1.533 . 1 224 438 438 ALA CB C 18.538 . 1 225 439 439 LEU HD1 H 0.389 . 1 226 439 439 LEU CD1 C 25.042 . 1 227 440 440 ALA HB H 1.565 . 1 228 440 440 ALA CB C 18.543 . 1 229 442 442 LEU HD1 H 1.253 . 1 230 442 442 LEU CD1 C 27.643 . 1 231 443 443 LEU HD1 H 1.162 . 1 232 443 443 LEU CD1 C 24.704 . 1 233 451 451 VAL HG1 H 1.042 . 1 234 451 451 VAL CG1 C 21.522 . 1 235 454 454 LEU HD1 H 0.770 . 1 236 454 454 LEU CD1 C 24.928 . 1 237 457 457 LEU HD1 H 0.320 . 1 238 457 457 LEU CD1 C 24.277 . 1 239 461 461 VAL HG1 H 1.065 . 1 240 461 461 VAL CG1 C 21.568 . 1 241 464 464 MET HE H 1.704 . 1 242 464 464 MET CE C 15.867 . 1 243 471 471 ILE HD1 H 0.666 . 1 244 471 471 ILE CD1 C 14.665 . 1 245 474 474 ILE HD1 H 0.917 . 1 246 474 474 ILE CD1 C 14.327 . 1 247 479 479 LEU HD1 H 0.704 . 1 248 479 479 LEU CD1 C 24.267 . 1 249 481 481 ALA HB H 1.444 . 1 250 481 481 ALA CB C 19.088 . 1 251 482 482 VAL HG1 H 0.683 . 1 252 482 482 VAL CG1 C 21.571 . 1 253 488 488 LEU HD1 H 1.137 . 1 254 488 488 LEU CD1 C 25.782 . 1 255 491 491 LEU HD1 H 0.380 . 1 256 491 491 LEU CD1 C 24.892 . 1 257 493 493 ALA HB H 1.431 . 1 258 493 493 ALA CB C 17.871 . 1 259 498 498 VAL HG1 H 0.795 . 1 260 498 498 VAL CG1 C 21.478 . 1 261 499 499 LEU HD1 H 0.229 . 1 262 499 499 LEU CD1 C 26.140 . 1 263 501 501 LEU HD1 H -0.451 . 1 264 501 501 LEU CD1 C 22.921 . 1 265 505 505 ILE HD1 H 0.767 . 1 266 505 505 ILE CD1 C 13.666 . 1 267 509 509 ALA HB H 1.629 . 1 268 509 509 ALA CB C 16.874 . 1 269 513 513 LEU HD1 H 0.706 . 1 270 513 513 LEU CD1 C 23.720 . 1 271 521 521 LEU HD1 H 0.195 . 1 272 521 521 LEU CD1 C 25.216 . 1 273 522 522 VAL HG1 H 0.791 . 1 274 522 522 VAL CG1 C 20.874 . 1 275 524 524 ILE HD1 H 0.720 . 1 276 524 524 ILE CD1 C 15.383 . 1 277 538 538 ALA HB H 1.474 . 1 278 538 538 ALA CB C 17.917 . 1 279 544 544 ILE HD1 H 0.943 . 1 280 544 544 ILE CD1 C 13.618 . 1 281 553 553 ALA HB H 1.535 . 1 282 553 553 ALA CB C 18.128 . 1 283 554 554 LEU HD1 H 0.800 . 1 284 554 554 LEU CD1 C 25.692 . 1 285 557 557 ILE HD1 H 0.835 . 1 286 557 557 ILE CD1 C 13.986 . 1 287 558 558 LEU HD1 H 0.004 . 1 288 558 558 LEU CD1 C 25.164 . 1 289 562 562 VAL HG1 H 0.594 . 1 290 562 562 VAL CG1 C 22.950 . 1 291 566 566 VAL HG1 H 0.837 . 1 292 566 566 VAL CG1 C 21.238 . 1 293 567 567 VAL HG1 H 0.411 . 1 294 567 567 VAL CG1 C 21.668 . 1 295 571 571 LEU HD1 H 0.478 . 1 296 571 571 LEU CD1 C 24.538 . 1 297 572 572 LEU HD1 H 0.856 . 1 298 572 572 LEU CD1 C 24.838 . 1 299 574 574 ALA HB H 1.425 . 1 300 574 574 ALA CB C 19.839 . 1 301 577 577 ALA HB H 1.337 . 1 302 577 577 ALA CB C 23.482 . 1 303 578 578 ILE HD1 H 0.713 . 1 304 578 578 ILE CD1 C 11.991 . 1 305 589 589 MET HE H 1.859 . 1 306 589 589 MET CE C 16.818 . 1 307 592 592 ILE HD1 H 0.720 . 1 308 592 592 ILE CD1 C 12.868 . 1 309 593 593 MET HE H 1.927 . 1 310 593 593 MET CE C 16.862 . 1 311 595 595 ALA HB H 1.420 . 1 312 595 595 ALA CB C 18.529 . 1 313 603 603 MET HE H 1.990 . 1 314 603 603 MET CE C 16.972 . 1 315 607 607 MET HE H 1.984 . 1 316 607 607 MET CE C 16.906 . 1 317 615 615 ILE HD1 H 0.569 . 1 318 615 615 ILE CD1 C 13.825 . 1 319 621 621 ILE HD1 H 0.858 . 1 320 621 621 ILE CD1 C 13.507 . 1 321 622 622 ILE HD1 H 0.542 . 1 322 622 622 ILE CD1 C 7.362 . 1 323 639 639 VAL HG1 H 0.673 . 1 324 639 639 VAL CG1 C 20.191 . 1 325 645 645 LEU HD1 H 0.807 . 1 326 645 645 LEU CD1 C 25.164 . 1 327 650 650 ALA HB H 1.554 . 1 328 650 650 ALA CB C 17.290 . 1 329 651 651 LEU HD1 H 0.530 . 1 330 651 651 LEU CD1 C 25.852 . 1 331 652 652 LEU HD1 H 0.687 . 1 332 652 652 LEU CD1 C 26.718 . 1 333 658 658 LEU HD1 H 0.366 . 1 334 658 658 LEU CD1 C 25.742 . 1 335 668 668 ILE HD1 H 0.317 . 1 336 668 668 ILE CD1 C 11.554 . 1 337 671 671 LEU HD1 H 0.776 . 1 338 671 671 LEU CD1 C 24.479 . 1 339 674 674 LEU HD1 H 0.908 . 1 340 674 674 LEU CD1 C 24.152 . 1 341 676 676 LEU HD1 H 0.741 . 1 342 676 676 LEU CD1 C 26.428 . 1 343 678 678 ILE HD1 H 0.712 . 1 344 678 678 ILE CD1 C 13.900 . 1 345 687 687 ALA HB H 1.355 . 1 346 687 687 ALA CB C 18.040 . 1 347 690 690 ALA HB H 1.392 . 1 348 690 690 ALA CB C 19.135 . 1 349 693 693 ALA HB H 1.383 . 1 350 693 693 ALA CB C 19.254 . 1 351 694 694 ALA HB H 1.338 . 1 352 694 694 ALA CB C 17.936 . 1 353 701 701 ALA HB H 1.346 . 1 354 701 701 ALA CB C 19.216 . 1 355 705 705 MET HE H 2.087 . 1 356 705 705 MET CE C 16.866 . 1 357 708 708 VAL HG1 H 0.949 . 1 358 708 708 VAL CG1 C 20.756 . 1 stop_ save_