data_50472 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Methyl assignments of Hsp90 FL AIM LV pro-R labeled ; _BMRB_accession_number 50472 _BMRB_flat_file_name bmr50472.str _Entry_type original _Submission_date 2020-09-20 _Accession_date 2020-09-20 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Assignments of methyl groups of yeast Hsp90 full length, 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" 183 "13C chemical shifts" 183 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-12-16 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 50474 'Methyl assignments of Hsp90 FL AIM LV pro-R labeled bound to AMP-PNP' stop_ _Original_release_date 2020-09-20 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 Hsp90 stop_ save_ ################################## # Molecular system description # ################################## save_assembly_1 _Saveframe_category molecular_system _Mol_system_name Homodimer _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label protomer1 $entity_1 protomer2 $entity_1 stop_ _System_molecular_weight 165000 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'Molecular chaperoning' stop_ _Database_query_date . _Details . 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 . 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 _Vector_type _Vector_name $entity_1 'recombinant technology' . Escherichia coli BL21 plasmid pETM11 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '100 uM in deuterated Tris buffer pH 7.5' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 100 uM '[U-2H; 99% 1HD-13CD-Ile,Leu; 99% 1HG-13CG-Val, 99%; 1HE-13CE-Met, 99%; 1HB-13CB-Ala, 99%]' 'Tris buffer deuterated' 0.1 M 'natural abundance' 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 CcpNMR _Version 2.4.2 loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_software_3 _Saveframe_category software _Name NMRPipe _Version . loop_ _Task processing 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_3D_1H-13C_NOESY_aliphatic_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY aliphatic' _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 protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 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' '3D 1H-13C NOESY aliphatic' 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 protomer1 _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 2.107 . 1 2 1 1 MET CE C 16.980 . 1 3 2 2 ALA HB H 1.455 . 1 4 2 2 ALA CB C 19.110 . 1 5 10 10 ALA HB H 1.464 . 1 6 10 10 ALA CB C 18.532 . 1 7 12 12 ILE HD1 H 0.852 . 1 8 12 12 ILE CD1 C 12.332 . 1 9 15 15 LEU HD1 H 0.990 . 1 10 15 15 LEU CD1 C 24.028 . 1 11 16 16 MET HE H 1.149 . 1 12 16 16 MET CE C 15.580 . 1 13 18 18 LEU HD1 H 0.779 . 1 14 18 18 LEU CD1 C 25.092 . 1 15 19 19 ILE HD1 H 0.668 . 1 16 19 19 ILE CD1 C 12.179 . 1 17 20 20 ILE HD1 H 0.820 . 1 18 20 20 ILE CD1 C 13.865 . 1 19 29 29 ILE HD1 H 0.710 . 1 20 29 29 ILE CD1 C 14.686 . 1 21 31 31 LEU HD1 H 0.649 . 1 22 31 31 LEU CD1 C 23.459 . 1 23 34 34 LEU HD1 H 0.869 . 1 24 34 34 LEU CD1 C 26.573 . 1 25 35 35 ILE HD1 H 0.637 . 1 26 35 35 ILE CD1 C 11.708 . 1 27 38 38 ALA HB H 1.461 . 1 28 38 38 ALA CB C 18.396 . 1 29 41 41 ALA HB H 1.596 . 1 30 41 41 ALA CB C 18.531 . 1 31 42 42 LEU HD1 H 0.082 . 1 32 42 42 LEU CD1 C 25.518 . 1 33 45 45 ILE HD1 H 0.944 . 1 34 45 45 ILE CD1 C 14.263 . 1 35 50 50 LEU HD1 H 0.898 . 1 36 50 50 LEU CD1 C 25.316 . 1 37 56 56 LEU HD1 H 0.987 . 1 38 56 56 LEU CD1 C 24.612 . 1 39 62 62 LEU HD1 H 0.983 . 1 40 62 62 LEU CD1 C 25.854 . 1 41 64 64 ILE HD1 H 0.756 . 1 42 64 64 ILE CD1 C 14.582 . 1 43 74 74 VAL HG1 H 0.467 . 1 44 74 74 VAL CG1 C 22.755 . 1 45 75 75 LEU HD1 H 0.910 . 1 46 75 75 LEU CD1 C 22.728 . 1 47 77 77 ILE HD1 H 0.785 . 1 48 77 77 ILE CD1 C 15.403 . 1 49 82 82 ILE HD1 H 0.845 . 1 50 82 82 ILE CD1 C 15.450 . 1 51 84 84 MET HE H 1.693 . 1 52 84 84 MET CE C 17.812 . 1 53 87 87 ALA HB H 1.257 . 1 54 87 87 ALA CB C 17.983 . 1 55 89 89 LEU HD1 H 0.796 . 1 56 89 89 LEU CD1 C 26.876 . 1 57 90 90 ILE HD1 H 0.543 . 1 58 90 90 ILE CD1 C 15.479 . 1 59 93 93 LEU HD1 H -0.840 . 1 60 93 93 LEU CD1 C 23.277 . 1 61 96 96 ILE HD1 H 0.800 . 1 62 96 96 ILE CD1 C 12.634 . 1 63 97 97 ALA HB H 1.454 . 1 64 97 97 ALA CB C 18.726 . 1 65 103 103 ALA HB H 1.632 . 1 66 103 103 ALA CB C 18.181 . 1 67 105 105 MET HE H 1.991 . 1 68 105 105 MET CE C 16.566 . 1 69 107 107 ALA HB H 1.264 . 1 70 107 107 ALA CB C 17.025 . 1 71 108 108 LEU HD1 H 0.298 . 1 72 108 108 LEU CD1 C 24.999 . 1 73 110 110 ALA HB H 1.475 . 1 74 110 110 ALA CB C 18.895 . 1 75 112 112 ALA HB H 1.161 . 1 76 112 112 ALA CB C 19.179 . 1 77 114 114 VAL HG1 H 0.607 . 1 78 114 114 VAL CG1 C 20.504 . 1 79 116 116 MET HE H 2.088 . 1 80 116 116 MET CE C 17.131 . 1 81 117 117 ILE HD1 H 0.588 . 1 82 117 117 ILE CD1 C 14.361 . 1 83 122 122 VAL HG1 H 0.945 . 1 84 122 122 VAL CG1 C 22.457 . 1 85 127 127 LEU HD1 H -0.588 . 1 86 127 127 LEU CD1 C 23.364 . 1 87 129 129 LEU HD1 H 1.003 . 1 88 129 129 LEU CD1 C 26.198 . 1 89 130 130 VAL HG1 H 0.408 . 1 90 130 130 VAL CG1 C 21.756 . 1 91 131 131 ALA HB H 1.021 . 1 92 131 131 ALA CB C 21.991 . 1 93 134 134 VAL HG1 H 1.265 . 1 94 134 134 VAL CG1 C 20.351 . 1 95 136 136 VAL HG1 H 0.645 . 1 96 136 136 VAL CG1 C 21.198 . 1 97 137 137 ILE HD1 H 0.793 . 1 98 137 137 ILE CD1 C 14.698 . 1 99 147 147 ILE HD1 H 0.830 . 1 100 147 147 ILE CD1 C 15.291 . 1 101 152 152 ALA HB H 1.135 . 1 102 152 152 ALA CB C 16.794 . 1 103 158 158 VAL HG1 H 1.058 . 1 104 158 158 VAL CG1 C 22.334 . 1 105 160 160 LEU HD1 H 0.593 . 1 106 160 160 LEU CD1 C 23.227 . 1 107 163 163 VAL HG1 H 0.853 . 1 108 163 163 VAL CG1 C 20.886 . 1 109 167 167 ILE HD1 H 0.524 . 1 110 167 167 ILE CD1 C 13.694 . 1 111 172 172 ILE HD1 H 0.767 . 1 112 172 172 ILE CD1 C 13.799 . 1 113 173 173 LEU HD1 H 0.968 . 1 114 173 173 LEU CD1 C 26.444 . 1 115 175 175 LEU HD1 H 0.737 . 1 116 175 175 LEU CD1 C 25.483 . 1 117 177 177 LEU HD1 H 0.816 . 1 118 177 177 LEU CD1 C 26.705 . 1 119 182 182 LEU HD1 H 0.997 . 1 120 182 182 LEU CD1 C 25.429 . 1 121 185 185 LEU HD1 H 0.959 . 1 122 185 185 LEU CD1 C 27.479 . 1 123 190 190 ILE HD1 H 0.827 . 1 124 190 190 ILE CD1 C 13.668 . 1 125 193 193 VAL HG1 H 0.983 . 1 126 193 193 VAL CG1 C 23.541 . 1 127 194 194 ILE HD1 H 0.728 . 1 128 194 194 ILE CD1 C 14.168 . 1 129 201 201 VAL HG1 H 1.103 . 1 130 201 201 VAL CG1 C 20.798 . 1 131 202 202 ALA HB H 1.110 . 1 132 202 202 ALA CB C 18.716 . 1 133 205 205 ILE HD1 H 0.793 . 1 134 205 205 ILE CD1 C 14.594 . 1 135 244 244 LEU HD1 H 0.904 . 1 136 244 244 LEU CD1 C 24.624 . 1 137 267 267 ILE HD1 H 0.743 . 1 138 267 267 ILE CD1 C 12.977 . 1 139 276 276 LEU HD1 H 0.579 . 1 140 276 276 LEU CD1 C 24.674 . 1 141 284 284 ILE HD1 H 0.667 . 1 142 284 284 ILE CD1 C 14.224 . 1 143 296 296 ILE HD1 H 0.721 . 1 144 296 296 ILE CD1 C 14.119 . 1 145 304 304 LEU HD1 H 1.129 . 1 146 304 304 LEU CD1 C 24.748 . 1 147 306 306 VAL HG1 H -0.163 . 1 148 306 306 VAL CG1 C 18.498 . 1 149 311 311 VAL HG1 H 0.838 . 1 150 311 311 VAL CG1 C 20.735 . 1 151 315 315 LEU HD1 H 0.960 . 1 152 315 315 LEU CD1 C 25.919 . 1 153 320 320 ILE HD1 H 0.354 . 1 154 320 320 ILE CD1 C 14.356 . 1 155 321 321 LEU HD1 H 0.872 . 1 156 321 321 LEU CD1 C 27.208 . 1 157 323 323 ILE HD1 H 0.952 . 1 158 323 323 ILE CD1 C 13.772 . 1 159 327 327 ALA HB H 1.223 . 1 160 327 327 ALA CB C 17.813 . 1 161 331 331 LEU HD1 H 0.813 . 1 162 331 331 LEU CD1 C 24.343 . 1 163 341 341 ILE HD1 H 0.429 . 1 164 341 341 ILE CD1 C 11.269 . 1 165 343 343 LEU HD1 H 0.693 . 1 166 343 343 LEU CD1 C 22.839 . 1 167 345 345 VAL HG1 H 0.966 . 1 168 345 345 VAL CG1 C 21.053 . 1 169 348 348 VAL HG1 H 0.845 . 1 170 348 348 VAL CG1 C 21.277 . 1 171 350 350 ILE HD1 H 0.619 . 1 172 350 350 ILE CD1 C 9.337 . 1 173 354 354 ALA HB H 1.145 . 1 174 354 354 ALA CB C 17.760 . 1 175 357 357 LEU HD1 H 0.709 . 1 176 357 357 LEU CD1 C 24.815 . 1 177 358 358 ILE HD1 H 0.397 . 1 178 358 358 ILE CD1 C 13.371 . 1 179 362 362 LEU HD1 H 0.281 . 1 180 362 362 LEU CD1 C 25.758 . 1 181 365 365 VAL HG1 H 0.684 . 1 182 365 365 VAL CG1 C 21.993 . 1 183 368 368 VAL HG1 H 0.462 . 1 184 368 368 VAL CG1 C 20.508 . 1 185 369 369 VAL HG1 H 0.633 . 1 186 369 369 VAL CG1 C 20.414 . 1 187 374 374 LEU HD1 H 0.794 . 1 188 374 374 LEU CD1 C 25.447 . 1 189 376 376 LEU HD1 H 0.825 . 1 190 376 376 LEU CD1 C 24.838 . 1 191 378 378 LEU HD1 H 0.871 . 1 192 378 378 LEU CD1 C 25.050 . 1 193 382 382 MET HE H 2.098 . 1 194 382 382 MET CE C 17.168 . 1 195 383 383 LEU HD1 H 0.809 . 1 196 383 383 LEU CD1 C 25.552 . 1 197 388 388 ILE HD1 H 0.820 . 1 198 388 388 ILE CD1 C 12.736 . 1 199 389 389 MET HE H 1.827 . 1 200 389 389 MET CE C 17.344 . 1 201 391 391 VAL HG1 H 1.019 . 1 202 391 391 VAL CG1 C 22.351 . 1 203 392 392 ILE HD1 H 0.458 . 1 204 392 392 ILE CD1 C 12.564 . 1 205 396 396 ILE HD1 H 0.649 . 1 206 396 396 ILE CD1 C 14.221 . 1 207 397 397 VAL HG1 H 1.015 . 1 208 397 397 VAL CG1 C 21.301 . 1 209 400 400 LEU HD1 H 0.648 . 1 210 400 400 LEU CD1 C 27.604 . 1 211 401 401 ILE HD1 H 0.868 . 1 212 401 401 ILE CD1 C 13.545 . 1 213 403 403 ALA HB H 1.352 . 1 214 403 403 ALA CB C 17.301 . 1 215 407 407 ILE HD1 H 0.153 . 1 216 407 407 ILE CD1 C 13.668 . 1 217 408 408 ALA HB H 1.004 . 1 218 408 408 ALA CB C 17.289 . 1 219 420 420 ALA HB H 0.304 . 1 220 420 420 ALA CB C 18.770 . 1 221 425 425 ILE HD1 H 0.726 . 1 222 425 425 ILE CD1 C 11.114 . 1 223 427 427 LEU HD1 H 0.970 . 1 224 427 427 LEU CD1 C 24.912 . 1 225 429 429 VAL HG1 H 0.859 . 1 226 429 429 VAL CG1 C 22.700 . 1 227 437 437 ALA HB H 1.415 . 1 228 437 437 ALA CB C 17.433 . 1 229 438 438 ALA HB H 1.537 . 1 230 438 438 ALA CB C 18.542 . 1 231 439 439 LEU HD1 H 0.387 . 1 232 439 439 LEU CD1 C 25.037 . 1 233 440 440 ALA HB H 1.561 . 1 234 440 440 ALA CB C 18.535 . 1 235 442 442 LEU HD1 H 1.254 . 1 236 442 442 LEU CD1 C 27.653 . 1 237 443 443 LEU HD1 H 1.168 . 1 238 443 443 LEU CD1 C 24.705 . 1 239 451 451 VAL HG1 H 1.042 . 1 240 451 451 VAL CG1 C 21.523 . 1 241 454 454 LEU HD1 H 0.770 . 1 242 454 454 LEU CD1 C 24.928 . 1 243 457 457 LEU HD1 H 0.321 . 1 244 457 457 LEU CD1 C 24.287 . 1 245 461 461 VAL HG1 H 1.063 . 1 246 461 461 VAL CG1 C 21.563 . 1 247 464 464 MET HE H 1.705 . 1 248 464 464 MET CE C 15.876 . 1 249 471 471 ILE HD1 H 0.670 . 1 250 471 471 ILE CD1 C 14.662 . 1 251 474 474 ILE HD1 H 0.918 . 1 252 474 474 ILE CD1 C 14.283 . 1 253 479 479 LEU HD1 H 0.702 . 1 254 479 479 LEU CD1 C 24.279 . 1 255 481 481 ALA HB H 1.444 . 1 256 481 481 ALA CB C 19.084 . 1 257 482 482 VAL HG1 H 0.682 . 1 258 482 482 VAL CG1 C 21.565 . 1 259 488 488 LEU HD1 H 1.135 . 1 260 488 488 LEU CD1 C 25.786 . 1 261 491 491 LEU HD1 H 0.382 . 1 262 491 491 LEU CD1 C 24.929 . 1 263 493 493 ALA HB H 1.430 . 1 264 493 493 ALA CB C 17.882 . 1 265 498 498 VAL HG1 H 0.792 . 1 266 498 498 VAL CG1 C 21.486 . 1 267 499 499 LEU HD1 H 0.226 . 1 268 499 499 LEU CD1 C 26.131 . 1 269 501 501 LEU HD1 H -0.451 . 1 270 501 501 LEU CD1 C 22.908 . 1 271 505 505 ILE HD1 H 0.763 . 1 272 505 505 ILE CD1 C 13.658 . 1 273 509 509 ALA HB H 1.630 . 1 274 509 509 ALA CB C 16.889 . 1 275 513 513 LEU HD1 H 0.705 . 1 276 513 513 LEU CD1 C 23.714 . 1 277 521 521 LEU HD1 H 0.199 . 1 278 521 521 LEU CD1 C 25.188 . 1 279 522 522 VAL HG1 H 0.799 . 1 280 522 522 VAL CG1 C 20.924 . 1 281 524 524 ILE HD1 H 0.721 . 1 282 524 524 ILE CD1 C 15.384 . 1 283 538 538 ALA HB H 1.474 . 1 284 538 538 ALA CB C 17.908 . 1 285 544 544 ILE HD1 H 0.945 . 1 286 544 544 ILE CD1 C 13.626 . 1 287 553 553 ALA HB H 1.534 . 1 288 553 553 ALA CB C 18.144 . 1 289 554 554 LEU HD1 H 0.802 . 1 290 554 554 LEU CD1 C 25.681 . 1 291 557 557 ILE HD1 H 0.839 . 1 292 557 557 ILE CD1 C 14.022 . 1 293 558 558 LEU HD1 H 0.001 . 1 294 558 558 LEU CD1 C 25.174 . 1 295 562 562 VAL HG1 H 0.595 . 1 296 562 562 VAL CG1 C 22.949 . 1 297 566 566 VAL HG1 H 0.835 . 1 298 566 566 VAL CG1 C 21.236 . 1 299 567 567 VAL HG1 H 0.413 . 1 300 567 567 VAL CG1 C 21.674 . 1 301 571 571 LEU HD1 H 0.474 . 1 302 571 571 LEU CD1 C 24.556 . 1 303 574 574 ALA HB H 1.419 . 1 304 574 574 ALA CB C 19.825 . 1 305 577 577 ALA HB H 1.329 . 1 306 577 577 ALA CB C 23.476 . 1 307 578 578 ILE HD1 H 0.712 . 1 308 578 578 ILE CD1 C 12.008 . 1 309 589 589 MET HE H 1.857 . 1 310 589 589 MET CE C 16.817 . 1 311 592 592 ILE HD1 H 0.717 . 1 312 592 592 ILE CD1 C 12.856 . 1 313 593 593 MET HE H 1.927 . 1 314 593 593 MET CE C 16.860 . 1 315 595 595 ALA HB H 1.421 . 1 316 595 595 ALA CB C 18.527 . 1 317 598 598 LEU HD1 H 0.857 . 1 318 598 598 LEU CD1 C 24.831 . 1 319 603 603 MET HE H 1.991 . 1 320 603 603 MET CE C 16.969 . 1 321 607 607 MET HE H 1.980 . 1 322 607 607 MET CE C 16.896 . 1 323 615 615 ILE HD1 H 0.571 . 1 324 615 615 ILE CD1 C 13.833 . 1 325 621 621 ILE HD1 H 0.856 . 1 326 621 621 ILE CD1 C 13.505 . 1 327 622 622 ILE HD1 H 0.537 . 1 328 622 622 ILE CD1 C 7.368 . 1 329 625 625 LEU HD1 H 0.772 . 1 330 625 625 LEU CD1 C 24.763 . 1 331 639 639 VAL HG1 H 0.671 . 1 332 639 639 VAL CG1 C 20.218 . 1 333 645 645 LEU HD1 H 0.796 . 1 334 645 645 LEU CD1 C 25.155 . 1 335 650 650 ALA HB H 1.552 . 1 336 650 650 ALA CB C 17.306 . 1 337 651 651 LEU HD1 H 0.531 . 1 338 651 651 LEU CD1 C 25.861 . 1 339 652 652 LEU HD1 H 0.685 . 1 340 652 652 LEU CD1 C 26.709 . 1 341 658 658 LEU HD1 H 0.367 . 1 342 658 658 LEU CD1 C 25.745 . 1 343 668 668 ILE HD1 H 0.314 . 1 344 668 668 ILE CD1 C 11.549 . 1 345 671 671 LEU HD1 H 0.776 . 1 346 671 671 LEU CD1 C 24.485 . 1 347 674 674 LEU HD1 H 0.907 . 1 348 674 674 LEU CD1 C 24.156 . 1 349 676 676 LEU HD1 H 0.739 . 1 350 676 676 LEU CD1 C 26.424 . 1 351 678 678 ILE HD1 H 0.711 . 1 352 678 678 ILE CD1 C 13.900 . 1 353 687 687 ALA HB H 1.355 . 1 354 687 687 ALA CB C 18.044 . 1 355 690 690 ALA HB H 1.392 . 1 356 690 690 ALA CB C 19.139 . 1 357 693 693 ALA HB H 1.383 . 1 358 693 693 ALA CB C 19.250 . 1 359 694 694 ALA HB H 1.337 . 1 360 694 694 ALA CB C 17.939 . 1 361 701 701 ALA HB H 1.345 . 1 362 701 701 ALA CB C 19.216 . 1 363 705 705 MET HE H 2.086 . 1 364 705 705 MET CE C 16.867 . 1 365 708 708 VAL HG1 H 0.949 . 1 366 708 708 VAL CG1 C 20.760 . 1 stop_ save_