data_26595 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C and 15N chemical shift assignments for hTRF1 bound to ADP-DnaK ; _BMRB_accession_number 26595 _BMRB_flat_file_name bmr26595.str _Entry_type original _Submission_date 2015-06-30 _Accession_date 2015-06-30 _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 Sekhar Ashok . . 2 Rosenzweig Rina . . 3 Bouvignies Guillaume . . 4 Kay Lewis E. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 42 "13C chemical shifts" 120 "15N chemical shifts" 42 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2017-01-13 update BMRB 'update entry citation' 2015-07-29 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 26594 'hTRF1 monomer' stop_ _Original_release_date 2015-07-29 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Mapping the conformation of a client protein through the Hsp70 functional cycle ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 26240333 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sekhar Ashok . . 2 Rosenzweig Rina . . 3 Bouvignies Guillaume . . 4 Kay Lewis E. . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_volume 112 _Journal_issue 33 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 10395 _Page_last 10400 _Year 2015 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'hTRF1-DnaK complex' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label hTRF1 $hTRF1 DnaK $DnaK stop_ _System_molecular_weight 77000 _System_physical_state 'partially disordered' _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details 'Complex of hTRF1 with DnaK in the ADP nucleotide state' save_ ######################## # Monomeric polymers # ######################## save_hTRF1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common hTRF1 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 53 _Mol_residue_sequence ; RKRQAWLWEEDKNLRSGVRK YGEGNWSKILLHYKFNNRTS VMLKDRWRTMKKL ; loop_ _Residue_seq_code _Residue_label 1 ARG 2 LYS 3 ARG 4 GLN 5 ALA 6 TRP 7 LEU 8 TRP 9 GLU 10 GLU 11 ASP 12 LYS 13 ASN 14 LEU 15 ARG 16 SER 17 GLY 18 VAL 19 ARG 20 LYS 21 TYR 22 GLY 23 GLU 24 GLY 25 ASN 26 TRP 27 SER 28 LYS 29 ILE 30 LEU 31 LEU 32 HIS 33 TYR 34 LYS 35 PHE 36 ASN 37 ASN 38 ARG 39 THR 40 SER 41 VAL 42 MET 43 LEU 44 LYS 45 ASP 46 ARG 47 TRP 48 ARG 49 THR 50 MET 51 LYS 52 LYS 53 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ save_DnaK _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common DnaK _Molecular_mass . _Mol_thiol_state 'all free' _Details . _Residue_count 638 _Mol_residue_sequence ; MGKIIGIDLGTTNSCVAIMD GTTPRVLENAEGDRTTPSII AYTQDGETLVGQPAKRQAVT NPQNTLFAIKRLIGRRFQDE EVQRDVSIMPFKIIAADNGD AWVEVKGQKMAPPQISAEVL KKMKKTAEDYLGEPVTEAVI TVPAYFNDAQRQATKDAGRI AGLEVKRIINEPTAAALAYG LDKGTGNRTIAVYDLGGGTF DISIIEIDEVDGEKTFEVLA TNGDTHLGGEDFDSRLINYL VEEFKKDQGIDLRNDPLAMQ RLKEAAEKAKIELSSAQQTD VNLPYITADATGPKHMNIKV TRAKLESLVEDLVNRSIEPL KVALQDAGLSVSDIDDVILV GGQTRMPMVQKKVAEFFGKE PRKDVNPDEAVAIGAAVQGG VLTGDVKDVLLLDVTPLSLG IETMGGVMTTLIAKNTTIPT KHSQVFSTAEDNQSAVTIHV LQGERKRAADNKSLGQFNLD GINPAPRGMPQIEVTFDIDA DGILHVSAKDKNSGKEQKIT IKASSGLNEDEIQKMVRDAE ANAEADRKFEELVQTRNQGD HLLHSTRKQVEEAGDKLPAD DKTAIESALTALETALKGED KAAIEAKMQELAQVSQKLME IAQQQHAQQQTAGADASANN AKDDDVVDAEFEEVKDKK ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLY 3 LYS 4 ILE 5 ILE 6 GLY 7 ILE 8 ASP 9 LEU 10 GLY 11 THR 12 THR 13 ASN 14 SER 15 CYS 16 VAL 17 ALA 18 ILE 19 MET 20 ASP 21 GLY 22 THR 23 THR 24 PRO 25 ARG 26 VAL 27 LEU 28 GLU 29 ASN 30 ALA 31 GLU 32 GLY 33 ASP 34 ARG 35 THR 36 THR 37 PRO 38 SER 39 ILE 40 ILE 41 ALA 42 TYR 43 THR 44 GLN 45 ASP 46 GLY 47 GLU 48 THR 49 LEU 50 VAL 51 GLY 52 GLN 53 PRO 54 ALA 55 LYS 56 ARG 57 GLN 58 ALA 59 VAL 60 THR 61 ASN 62 PRO 63 GLN 64 ASN 65 THR 66 LEU 67 PHE 68 ALA 69 ILE 70 LYS 71 ARG 72 LEU 73 ILE 74 GLY 75 ARG 76 ARG 77 PHE 78 GLN 79 ASP 80 GLU 81 GLU 82 VAL 83 GLN 84 ARG 85 ASP 86 VAL 87 SER 88 ILE 89 MET 90 PRO 91 PHE 92 LYS 93 ILE 94 ILE 95 ALA 96 ALA 97 ASP 98 ASN 99 GLY 100 ASP 101 ALA 102 TRP 103 VAL 104 GLU 105 VAL 106 LYS 107 GLY 108 GLN 109 LYS 110 MET 111 ALA 112 PRO 113 PRO 114 GLN 115 ILE 116 SER 117 ALA 118 GLU 119 VAL 120 LEU 121 LYS 122 LYS 123 MET 124 LYS 125 LYS 126 THR 127 ALA 128 GLU 129 ASP 130 TYR 131 LEU 132 GLY 133 GLU 134 PRO 135 VAL 136 THR 137 GLU 138 ALA 139 VAL 140 ILE 141 THR 142 VAL 143 PRO 144 ALA 145 TYR 146 PHE 147 ASN 148 ASP 149 ALA 150 GLN 151 ARG 152 GLN 153 ALA 154 THR 155 LYS 156 ASP 157 ALA 158 GLY 159 ARG 160 ILE 161 ALA 162 GLY 163 LEU 164 GLU 165 VAL 166 LYS 167 ARG 168 ILE 169 ILE 170 ASN 171 GLU 172 PRO 173 THR 174 ALA 175 ALA 176 ALA 177 LEU 178 ALA 179 TYR 180 GLY 181 LEU 182 ASP 183 LYS 184 GLY 185 THR 186 GLY 187 ASN 188 ARG 189 THR 190 ILE 191 ALA 192 VAL 193 TYR 194 ASP 195 LEU 196 GLY 197 GLY 198 GLY 199 THR 200 PHE 201 ASP 202 ILE 203 SER 204 ILE 205 ILE 206 GLU 207 ILE 208 ASP 209 GLU 210 VAL 211 ASP 212 GLY 213 GLU 214 LYS 215 THR 216 PHE 217 GLU 218 VAL 219 LEU 220 ALA 221 THR 222 ASN 223 GLY 224 ASP 225 THR 226 HIS 227 LEU 228 GLY 229 GLY 230 GLU 231 ASP 232 PHE 233 ASP 234 SER 235 ARG 236 LEU 237 ILE 238 ASN 239 TYR 240 LEU 241 VAL 242 GLU 243 GLU 244 PHE 245 LYS 246 LYS 247 ASP 248 GLN 249 GLY 250 ILE 251 ASP 252 LEU 253 ARG 254 ASN 255 ASP 256 PRO 257 LEU 258 ALA 259 MET 260 GLN 261 ARG 262 LEU 263 LYS 264 GLU 265 ALA 266 ALA 267 GLU 268 LYS 269 ALA 270 LYS 271 ILE 272 GLU 273 LEU 274 SER 275 SER 276 ALA 277 GLN 278 GLN 279 THR 280 ASP 281 VAL 282 ASN 283 LEU 284 PRO 285 TYR 286 ILE 287 THR 288 ALA 289 ASP 290 ALA 291 THR 292 GLY 293 PRO 294 LYS 295 HIS 296 MET 297 ASN 298 ILE 299 LYS 300 VAL 301 THR 302 ARG 303 ALA 304 LYS 305 LEU 306 GLU 307 SER 308 LEU 309 VAL 310 GLU 311 ASP 312 LEU 313 VAL 314 ASN 315 ARG 316 SER 317 ILE 318 GLU 319 PRO 320 LEU 321 LYS 322 VAL 323 ALA 324 LEU 325 GLN 326 ASP 327 ALA 328 GLY 329 LEU 330 SER 331 VAL 332 SER 333 ASP 334 ILE 335 ASP 336 ASP 337 VAL 338 ILE 339 LEU 340 VAL 341 GLY 342 GLY 343 GLN 344 THR 345 ARG 346 MET 347 PRO 348 MET 349 VAL 350 GLN 351 LYS 352 LYS 353 VAL 354 ALA 355 GLU 356 PHE 357 PHE 358 GLY 359 LYS 360 GLU 361 PRO 362 ARG 363 LYS 364 ASP 365 VAL 366 ASN 367 PRO 368 ASP 369 GLU 370 ALA 371 VAL 372 ALA 373 ILE 374 GLY 375 ALA 376 ALA 377 VAL 378 GLN 379 GLY 380 GLY 381 VAL 382 LEU 383 THR 384 GLY 385 ASP 386 VAL 387 LYS 388 ASP 389 VAL 390 LEU 391 LEU 392 LEU 393 ASP 394 VAL 395 THR 396 PRO 397 LEU 398 SER 399 LEU 400 GLY 401 ILE 402 GLU 403 THR 404 MET 405 GLY 406 GLY 407 VAL 408 MET 409 THR 410 THR 411 LEU 412 ILE 413 ALA 414 LYS 415 ASN 416 THR 417 THR 418 ILE 419 PRO 420 THR 421 LYS 422 HIS 423 SER 424 GLN 425 VAL 426 PHE 427 SER 428 THR 429 ALA 430 GLU 431 ASP 432 ASN 433 GLN 434 SER 435 ALA 436 VAL 437 THR 438 ILE 439 HIS 440 VAL 441 LEU 442 GLN 443 GLY 444 GLU 445 ARG 446 LYS 447 ARG 448 ALA 449 ALA 450 ASP 451 ASN 452 LYS 453 SER 454 LEU 455 GLY 456 GLN 457 PHE 458 ASN 459 LEU 460 ASP 461 GLY 462 ILE 463 ASN 464 PRO 465 ALA 466 PRO 467 ARG 468 GLY 469 MET 470 PRO 471 GLN 472 ILE 473 GLU 474 VAL 475 THR 476 PHE 477 ASP 478 ILE 479 ASP 480 ALA 481 ASP 482 GLY 483 ILE 484 LEU 485 HIS 486 VAL 487 SER 488 ALA 489 LYS 490 ASP 491 LYS 492 ASN 493 SER 494 GLY 495 LYS 496 GLU 497 GLN 498 LYS 499 ILE 500 THR 501 ILE 502 LYS 503 ALA 504 SER 505 SER 506 GLY 507 LEU 508 ASN 509 GLU 510 ASP 511 GLU 512 ILE 513 GLN 514 LYS 515 MET 516 VAL 517 ARG 518 ASP 519 ALA 520 GLU 521 ALA 522 ASN 523 ALA 524 GLU 525 ALA 526 ASP 527 ARG 528 LYS 529 PHE 530 GLU 531 GLU 532 LEU 533 VAL 534 GLN 535 THR 536 ARG 537 ASN 538 GLN 539 GLY 540 ASP 541 HIS 542 LEU 543 LEU 544 HIS 545 SER 546 THR 547 ARG 548 LYS 549 GLN 550 VAL 551 GLU 552 GLU 553 ALA 554 GLY 555 ASP 556 LYS 557 LEU 558 PRO 559 ALA 560 ASP 561 ASP 562 LYS 563 THR 564 ALA 565 ILE 566 GLU 567 SER 568 ALA 569 LEU 570 THR 571 ALA 572 LEU 573 GLU 574 THR 575 ALA 576 LEU 577 LYS 578 GLY 579 GLU 580 ASP 581 LYS 582 ALA 583 ALA 584 ILE 585 GLU 586 ALA 587 LYS 588 MET 589 GLN 590 GLU 591 LEU 592 ALA 593 GLN 594 VAL 595 SER 596 GLN 597 LYS 598 LEU 599 MET 600 GLU 601 ILE 602 ALA 603 GLN 604 GLN 605 GLN 606 HIS 607 ALA 608 GLN 609 GLN 610 GLN 611 THR 612 ALA 613 GLY 614 ALA 615 ASP 616 ALA 617 SER 618 ALA 619 ASN 620 ASN 621 ALA 622 LYS 623 ASP 624 ASP 625 ASP 626 VAL 627 VAL 628 ASP 629 ALA 630 GLU 631 PHE 632 GLU 633 GLU 634 VAL 635 LYS 636 ASP 637 LYS 638 LYS 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 $hTRF1 Human 9606 Eukaryota Metazoa Homo sapiens $DnaK '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 $hTRF1 'recombinant technology' . Escherichia coli . pET29b $DnaK 'recombinant technology' . Escherichia coli . pCA528 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 $hTRF1 0.5 mM '[U-13C; U-15N; U-2H]' $DnaK 1.4 mM [U-2H] MES 25 mM 'natural abundance' KCl 25 mM 'natural abundance' 'magnesium chloride' 5 mM 'natural abundance' 'adenosine diphosphate' 5 mM 'natural abundance' TCEP 1 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . 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 Varian _Model INOVA _Field_strength 600 _Details 'cold probe' 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_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _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' 0.05 . M pH 6.0 . pH pressure 1 . atm temperature 308 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details ; 1H referencing was done using water at the appropriate temperature and 15N and 13C referencing was done indirectly using the appropriate ratios. ; 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 water C 13 protons ppm 4.677 internal indirect . . . 0.2514953 water H 1 protons ppm 4.677 internal direct . . . 1.0 water N 15 protons ppm 4.677 internal 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 HNCA' '3D HNCO' '3D HNCACB' '3D HN(CO)CA' '3D CBCA(CO)NH' '3D HN(CA)CO' 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 hTRF1 _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 ARG H H 8.386 . 1 2 1 1 ARG CA C 56.202 . 1 3 1 1 ARG CB C 30.410 . 1 4 1 1 ARG N N 123.132 . 1 5 2 2 LYS H H 8.430 . 1 6 2 2 LYS CA C 56.269 . 1 7 2 2 LYS CB C 32.504 . 1 8 2 2 LYS N N 123.228 . 1 9 3 3 ARG H H 8.326 . 1 10 3 3 ARG CA C 56.212 . 1 11 3 3 ARG CB C 30.201 . 1 12 3 3 ARG N N 122.802 . 1 13 4 4 GLN H H 8.302 . 1 14 4 4 GLN C C 175.479 . 1 15 4 4 GLN CA C 55.783 . 1 16 4 4 GLN CB C 28.801 . 1 17 4 4 GLN N N 121.727 . 1 18 5 5 ALA H H 8.176 . 1 19 5 5 ALA C C 177.244 . 1 20 5 5 ALA CA C 52.820 . 1 21 5 5 ALA CB C 18.779 . 1 22 5 5 ALA N N 124.525 . 1 23 6 6 TRP H H 7.857 . 1 24 6 6 TRP C C 175.225 . 1 25 6 6 TRP CA C 57.044 . 1 26 6 6 TRP CB C 29.072 . 1 27 6 6 TRP N N 118.843 . 1 28 7 7 LEU H H 7.745 . 1 29 7 7 LEU C C 176.756 . 1 30 7 7 LEU CA C 55.369 . 1 31 7 7 LEU CB C 41.625 . 1 32 7 7 LEU N N 123.032 . 1 33 8 8 TRP H H 7.723 . 1 34 8 8 TRP C C 176.113 . 1 35 8 8 TRP CA C 57.364 . 1 36 8 8 TRP CB C 29.130 . 1 37 8 8 TRP N N 120.307 . 1 38 9 9 GLU H H 7.988 . 1 39 9 9 GLU C C 176.186 . 1 40 9 9 GLU CA C 56.690 . 1 41 9 9 GLU CB C 29.820 . 1 42 9 9 GLU N N 121.515 . 1 43 10 10 GLU H H 8.126 . 1 44 10 10 GLU C C 176.278 . 1 45 10 10 GLU CA C 56.761 . 1 46 10 10 GLU CB C 29.898 . 1 47 10 10 GLU N N 121.070 . 1 48 11 11 ASP H H 8.240 . 1 49 11 11 ASP C C 176.801 . 1 50 11 11 ASP CA C 54.637 . 1 51 11 11 ASP CB C 40.874 . 1 52 11 11 ASP N N 120.968 . 1 53 12 12 LYS H H 8.179 . 1 54 12 12 LYS C C 176.906 . 1 55 12 12 LYS CA C 57.236 . 1 56 12 12 LYS CB C 31.921 . 1 57 12 12 LYS N N 121.799 . 1 58 13 13 ASN H H 8.339 . 1 59 13 13 ASN C C 175.523 . 1 60 13 13 ASN CA C 53.885 . 1 61 13 13 ASN CB C 38.489 . 1 62 13 13 ASN N N 117.878 . 1 63 14 14 LEU H H 7.918 . 1 64 14 14 LEU C C 177.621 . 1 65 14 14 LEU CA C 55.686 . 1 66 14 14 LEU CB C 41.513 . 1 67 14 14 LEU N N 121.381 . 1 68 15 15 ARG H H 8.121 . 1 69 15 15 ARG C C 176.529 . 1 70 15 15 ARG CA C 56.295 . 1 71 15 15 ARG CB C 29.867 . 1 72 15 15 ARG N N 120.204 . 1 73 16 16 SER H H 8.089 . 1 74 16 16 SER C C 175.056 . 1 75 16 16 SER CA C 58.615 . 1 76 16 16 SER CB C 63.548 . 1 77 16 16 SER N N 115.544 . 1 78 17 17 GLY H H 8.287 . 1 79 17 17 GLY C C 174.007 . 1 80 17 17 GLY CA C 45.380 . 1 81 17 17 GLY N N 110.465 . 1 82 18 18 VAL H H 7.836 . 1 83 18 18 VAL C C 176.075 . 1 84 18 18 VAL CA C 62.323 . 1 85 18 18 VAL CB C 32.121 . 1 86 18 18 VAL N N 119.066 . 1 87 19 19 ARG H H 8.225 . 1 88 19 19 ARG C C 175.946 . 1 89 19 19 ARG CA C 55.931 . 1 90 19 19 ARG CB C 30.177 . 1 91 19 19 ARG N N 124.261 . 1 92 20 20 LYS H H 8.176 . 1 93 20 20 LYS C C 176.087 . 1 94 20 20 LYS CA C 55.866 . 1 95 20 20 LYS CB C 32.633 . 1 96 20 20 LYS N N 122.476 . 1 97 21 21 TYR H H 8.162 . 1 98 21 21 TYR C C 176.518 . 1 99 21 21 TYR CA C 58.033 . 1 100 21 21 TYR CB C 38.402 . 1 101 21 21 TYR N N 120.919 . 1 102 22 22 GLY H H 8.154 . 1 103 22 22 GLY C C 173.909 . 1 104 22 22 GLY CA C 45.205 . 1 105 22 22 GLY N N 110.435 . 1 106 23 23 GLU H H 8.136 . 1 107 23 23 GLU C C 176.858 . 1 108 23 23 GLU CA C 56.672 . 1 109 23 23 GLU CB C 29.918 . 1 110 23 23 GLU N N 120.225 . 1 111 24 24 GLY H H 8.233 . 1 112 24 24 GLY C C 173.857 . 1 113 24 24 GLY CA C 45.253 . 1 114 24 24 GLY N N 109.235 . 1 115 25 25 ASN H H 8.112 . 1 116 25 25 ASN C C 174.966 . 1 117 25 25 ASN CA C 53.237 . 1 118 25 25 ASN CB C 38.568 . 1 119 25 25 ASN N N 118.533 . 1 120 26 26 TRP H H 7.956 . 1 121 26 26 TRP C C 176.070 . 1 122 26 26 TRP CA C 57.300 . 1 123 26 26 TRP CB C 29.188 . 1 124 26 26 TRP N N 120.948 . 1 125 27 27 SER H H 7.968 . 1 126 27 27 SER CA C 58.210 . 1 127 27 27 SER CB C 63.576 . 1 128 27 27 SER N N 116.661 . 1 129 38 38 ARG C C 176.577 . 1 130 38 38 ARG CB C 29.487 . 1 131 39 39 THR H H 8.030 . 1 132 39 39 THR C C 174.681 . 1 133 39 39 THR CA C 62.194 . 1 134 39 39 THR CB C 69.588 . 1 135 39 39 THR N N 114.393 . 1 136 40 40 SER H H 8.201 . 1 137 40 40 SER C C 174.673 . 1 138 40 40 SER CA C 58.606 . 1 139 40 40 SER CB C 63.480 . 1 140 40 40 SER N N 117.733 . 1 141 41 41 VAL H H 7.988 . 1 142 41 41 VAL C C 176.141 . 1 143 41 41 VAL CA C 62.630 . 1 144 41 41 VAL CB C 32.088 . 1 145 41 41 VAL N N 121.270 . 1 146 42 42 MET H H 8.242 . 1 147 42 42 MET C C 176.240 . 1 148 42 42 MET CA C 55.770 . 1 149 42 42 MET CB C 32.358 . 1 150 42 42 MET N N 122.960 . 1 151 43 43 LEU H H 8.096 . 1 152 43 43 LEU C C 177.502 . 1 153 43 43 LEU CA C 55.641 . 1 154 43 43 LEU CB C 41.493 . 1 155 43 43 LEU N N 123.158 . 1 156 44 44 LYS H H 8.096 . 1 157 44 44 LYS C C 176.477 . 1 158 44 44 LYS CA C 56.891 . 1 159 44 44 LYS CB C 32.177 . 1 160 44 44 LYS N N 120.798 . 1 161 45 45 ASP H H 8.119 . 1 162 45 45 ASP C C 176.761 . 1 163 45 45 ASP CA C 54.633 . 1 164 45 45 ASP CB C 40.838 . 1 165 45 45 ASP N N 119.984 . 1 166 46 46 ARG H H 8.016 . 1 167 46 46 ARG C C 176.555 . 1 168 46 46 ARG CA C 57.120 . 1 169 46 46 ARG CB C 29.666 . 1 170 46 46 ARG N N 120.776 . 1 171 47 47 TRP H H 7.971 . 1 172 47 47 TRP C C 176.532 . 1 173 47 47 TRP CA C 57.388 . 1 174 47 47 TRP CB C 29.021 . 1 175 47 47 TRP N N 119.666 . 1 176 48 48 ARG H H 7.780 . 1 177 48 48 ARG C C 176.528 . 1 178 48 48 ARG CA C 56.863 . 1 179 48 48 ARG CB C 30.036 . 1 180 48 48 ARG N N 120.735 . 1 181 49 49 THR H H 7.938 . 1 182 49 49 THR C C 174.528 . 1 183 49 49 THR CA C 62.088 . 1 184 49 49 THR CB C 69.497 . 1 185 49 49 THR N N 113.507 . 1 186 50 50 MET H H 8.113 . 1 187 50 50 MET C C 175.812 . 1 188 50 50 MET CA C 55.528 . 1 189 50 50 MET CB C 32.569 . 1 190 50 50 MET N N 122.400 . 1 191 51 51 LYS H H 8.136 . 1 192 51 51 LYS C C 175.792 . 1 193 51 51 LYS CA C 56.058 . 1 194 51 51 LYS N N 122.476 . 1 195 52 52 LYS H H 8.216 . 1 196 52 52 LYS C C 175.280 . 1 197 52 52 LYS CA C 56.220 . 1 198 52 52 LYS CB C 32.479 . 1 199 52 52 LYS N N 123.614 . 1 200 53 53 LEU H H 7.833 . 1 201 53 53 LEU C C 175.524 . 1 202 53 53 LEU CA C 56.541 . 1 203 53 53 LEU CB C 42.3 . 1 204 53 53 LEU N N 129.619 . 1 stop_ save_