data_18381 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The backbone chemical shifts of IscU complexed with HscA ; _BMRB_accession_number 18381 _BMRB_flat_file_name bmr18381.str _Entry_type original _Submission_date 2012-04-08 _Accession_date 2012-04-08 _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 Kim 'Jin Hae' . . 2 Tonelli Marco . . 3 Markley John L. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 71 "13C chemical shifts" 219 "15N chemical shifts" 71 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-10-30 update BMRB 'complete entry, etc.' 2012-09-14 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 17836 'The chemical shifts of apo-IscU in the disordered conformation' 17837 'The chemical shifts of apo-IscU in the structured conformation' 18359 IscU(D39V) 18360 IscU(E111A) 18361 IscU(N90A) 18362 IscU(S107A) stop_ _Original_release_date 2012-04-09 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Specialized Hsp70 Chaperone (HscA) Binds Preferentially to the Disordered Form, whereas J-protein (HscB) Binds Preferentially to the Structured Form of the Iron-Sulfur Cluster Scaffold Protein (IscU). ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22782893 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kim 'Jin Hae' . . 2 Tonelli Marco . . 3 Frederick Ronnie O. . 4 Chow 'Darius C-F' . . 5 Markley John L. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 287 _Journal_issue 37 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 31406 _Page_last 31413 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name IscU-HscA _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label IscU $IscU HscA $HscA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'HscA facilitates the iron-sulfur cluster transfer from IscU.' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_IscU _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common IscU _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 128 _Mol_residue_sequence ; MAYSEKVIDHYENPRNVGSF DNNDENVGSGMVGAPACGDV MKLQIKVNDEGIIEDARFKT YGCGSAIASSSLVTEWVKGK SLDEAQAIKNTDIAEELELP PVKIHCSILAEDAIKAAIAD YKSKREAK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 ALA 3 3 TYR 4 4 SER 5 5 GLU 6 6 LYS 7 7 VAL 8 8 ILE 9 9 ASP 10 10 HIS 11 11 TYR 12 12 GLU 13 13 ASN 14 14 PRO 15 15 ARG 16 16 ASN 17 17 VAL 18 18 GLY 19 19 SER 20 20 PHE 21 21 ASP 22 22 ASN 23 23 ASN 24 24 ASP 25 25 GLU 26 26 ASN 27 27 VAL 28 28 GLY 29 29 SER 30 30 GLY 31 31 MET 32 32 VAL 33 33 GLY 34 34 ALA 35 35 PRO 36 36 ALA 37 37 CYS 38 38 GLY 39 39 ASP 40 40 VAL 41 41 MET 42 42 LYS 43 43 LEU 44 44 GLN 45 45 ILE 46 46 LYS 47 47 VAL 48 48 ASN 49 49 ASP 50 50 GLU 51 51 GLY 52 52 ILE 53 53 ILE 54 54 GLU 55 55 ASP 56 56 ALA 57 57 ARG 58 58 PHE 59 59 LYS 60 60 THR 61 61 TYR 62 62 GLY 63 63 CYS 64 64 GLY 65 65 SER 66 66 ALA 67 67 ILE 68 68 ALA 69 69 SER 70 70 SER 71 71 SER 72 72 LEU 73 73 VAL 74 74 THR 75 75 GLU 76 76 TRP 77 77 VAL 78 78 LYS 79 79 GLY 80 80 LYS 81 81 SER 82 82 LEU 83 83 ASP 84 84 GLU 85 85 ALA 86 86 GLN 87 87 ALA 88 88 ILE 89 89 LYS 90 90 ASN 91 91 THR 92 92 ASP 93 93 ILE 94 94 ALA 95 95 GLU 96 96 GLU 97 97 LEU 98 98 GLU 99 99 LEU 100 100 PRO 101 101 PRO 102 102 VAL 103 103 LYS 104 104 ILE 105 105 HIS 106 106 CYS 107 107 SER 108 108 ILE 109 109 LEU 110 110 ALA 111 111 GLU 112 112 ASP 113 113 ALA 114 114 ILE 115 115 LYS 116 116 ALA 117 117 ALA 118 118 ILE 119 119 ALA 120 120 ASP 121 121 TYR 122 122 LYS 123 123 SER 124 124 LYS 125 125 ARG 126 126 GLU 127 127 ALA 128 128 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ save_HscA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common HscA _Molecular_mass . _Mol_thiol_state 'all free' _Details . _Residue_count 616 _Mol_residue_sequence ; MALLQISEPGLSAAPHQRRL AAGIDLGTTNSLVATVRSGQ AETLADHEGRHLLPSVVHYQ QQGHSVGYDARTNAALDTAN TISSVKRLMGRSLADIQQRY PHLPYQFQASENGLPMIETA AGLLNPVRVSADILKALAAR ATEALAGELDGVVITVPAYF DDAQRQGTKDAARLAGLHVL RLLNEPTAAAIAYGLDSGQE GVIAVYDLGGGTFDISILRL SRGVFEVLATGGDSALGGDD FDHLLADYIREQAGIPDRSD NRVQRELLDAAIAAKIALSD ADSVTVNVAGWQGEISREQF NELIAPLVKRTLLACRRALK DAGVEADEVLEVVMVGGSTR VPLVRERVGEFFGRPPLTSI DPDKVVAIGAAIQADILVGN KPDSEMLLLDVIPLSLGLET MGGLVEKVIPRNTTIPVARA QDFTTFKDGQTAMSIHVMQG ERELVQDCRSLARFALRGIP ALPAGGAHIRVTFQVDADGL LSVTAMEKSTGVEASIQVKP SYGLTDSEIASMIKDSMSYA EQDVKARMLAEQKVEAARVL ESLHGALAADAALLSAAERQ VIDDAAAHLSEVAQGDDVDA IEKAIKNVDKQTQDFAARRM DQSVRRALKGHSVDEV ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 LEU 4 LEU 5 GLN 6 ILE 7 SER 8 GLU 9 PRO 10 GLY 11 LEU 12 SER 13 ALA 14 ALA 15 PRO 16 HIS 17 GLN 18 ARG 19 ARG 20 LEU 21 ALA 22 ALA 23 GLY 24 ILE 25 ASP 26 LEU 27 GLY 28 THR 29 THR 30 ASN 31 SER 32 LEU 33 VAL 34 ALA 35 THR 36 VAL 37 ARG 38 SER 39 GLY 40 GLN 41 ALA 42 GLU 43 THR 44 LEU 45 ALA 46 ASP 47 HIS 48 GLU 49 GLY 50 ARG 51 HIS 52 LEU 53 LEU 54 PRO 55 SER 56 VAL 57 VAL 58 HIS 59 TYR 60 GLN 61 GLN 62 GLN 63 GLY 64 HIS 65 SER 66 VAL 67 GLY 68 TYR 69 ASP 70 ALA 71 ARG 72 THR 73 ASN 74 ALA 75 ALA 76 LEU 77 ASP 78 THR 79 ALA 80 ASN 81 THR 82 ILE 83 SER 84 SER 85 VAL 86 LYS 87 ARG 88 LEU 89 MET 90 GLY 91 ARG 92 SER 93 LEU 94 ALA 95 ASP 96 ILE 97 GLN 98 GLN 99 ARG 100 TYR 101 PRO 102 HIS 103 LEU 104 PRO 105 TYR 106 GLN 107 PHE 108 GLN 109 ALA 110 SER 111 GLU 112 ASN 113 GLY 114 LEU 115 PRO 116 MET 117 ILE 118 GLU 119 THR 120 ALA 121 ALA 122 GLY 123 LEU 124 LEU 125 ASN 126 PRO 127 VAL 128 ARG 129 VAL 130 SER 131 ALA 132 ASP 133 ILE 134 LEU 135 LYS 136 ALA 137 LEU 138 ALA 139 ALA 140 ARG 141 ALA 142 THR 143 GLU 144 ALA 145 LEU 146 ALA 147 GLY 148 GLU 149 LEU 150 ASP 151 GLY 152 VAL 153 VAL 154 ILE 155 THR 156 VAL 157 PRO 158 ALA 159 TYR 160 PHE 161 ASP 162 ASP 163 ALA 164 GLN 165 ARG 166 GLN 167 GLY 168 THR 169 LYS 170 ASP 171 ALA 172 ALA 173 ARG 174 LEU 175 ALA 176 GLY 177 LEU 178 HIS 179 VAL 180 LEU 181 ARG 182 LEU 183 LEU 184 ASN 185 GLU 186 PRO 187 THR 188 ALA 189 ALA 190 ALA 191 ILE 192 ALA 193 TYR 194 GLY 195 LEU 196 ASP 197 SER 198 GLY 199 GLN 200 GLU 201 GLY 202 VAL 203 ILE 204 ALA 205 VAL 206 TYR 207 ASP 208 LEU 209 GLY 210 GLY 211 GLY 212 THR 213 PHE 214 ASP 215 ILE 216 SER 217 ILE 218 LEU 219 ARG 220 LEU 221 SER 222 ARG 223 GLY 224 VAL 225 PHE 226 GLU 227 VAL 228 LEU 229 ALA 230 THR 231 GLY 232 GLY 233 ASP 234 SER 235 ALA 236 LEU 237 GLY 238 GLY 239 ASP 240 ASP 241 PHE 242 ASP 243 HIS 244 LEU 245 LEU 246 ALA 247 ASP 248 TYR 249 ILE 250 ARG 251 GLU 252 GLN 253 ALA 254 GLY 255 ILE 256 PRO 257 ASP 258 ARG 259 SER 260 ASP 261 ASN 262 ARG 263 VAL 264 GLN 265 ARG 266 GLU 267 LEU 268 LEU 269 ASP 270 ALA 271 ALA 272 ILE 273 ALA 274 ALA 275 LYS 276 ILE 277 ALA 278 LEU 279 SER 280 ASP 281 ALA 282 ASP 283 SER 284 VAL 285 THR 286 VAL 287 ASN 288 VAL 289 ALA 290 GLY 291 TRP 292 GLN 293 GLY 294 GLU 295 ILE 296 SER 297 ARG 298 GLU 299 GLN 300 PHE 301 ASN 302 GLU 303 LEU 304 ILE 305 ALA 306 PRO 307 LEU 308 VAL 309 LYS 310 ARG 311 THR 312 LEU 313 LEU 314 ALA 315 CYS 316 ARG 317 ARG 318 ALA 319 LEU 320 LYS 321 ASP 322 ALA 323 GLY 324 VAL 325 GLU 326 ALA 327 ASP 328 GLU 329 VAL 330 LEU 331 GLU 332 VAL 333 VAL 334 MET 335 VAL 336 GLY 337 GLY 338 SER 339 THR 340 ARG 341 VAL 342 PRO 343 LEU 344 VAL 345 ARG 346 GLU 347 ARG 348 VAL 349 GLY 350 GLU 351 PHE 352 PHE 353 GLY 354 ARG 355 PRO 356 PRO 357 LEU 358 THR 359 SER 360 ILE 361 ASP 362 PRO 363 ASP 364 LYS 365 VAL 366 VAL 367 ALA 368 ILE 369 GLY 370 ALA 371 ALA 372 ILE 373 GLN 374 ALA 375 ASP 376 ILE 377 LEU 378 VAL 379 GLY 380 ASN 381 LYS 382 PRO 383 ASP 384 SER 385 GLU 386 MET 387 LEU 388 LEU 389 LEU 390 ASP 391 VAL 392 ILE 393 PRO 394 LEU 395 SER 396 LEU 397 GLY 398 LEU 399 GLU 400 THR 401 MET 402 GLY 403 GLY 404 LEU 405 VAL 406 GLU 407 LYS 408 VAL 409 ILE 410 PRO 411 ARG 412 ASN 413 THR 414 THR 415 ILE 416 PRO 417 VAL 418 ALA 419 ARG 420 ALA 421 GLN 422 ASP 423 PHE 424 THR 425 THR 426 PHE 427 LYS 428 ASP 429 GLY 430 GLN 431 THR 432 ALA 433 MET 434 SER 435 ILE 436 HIS 437 VAL 438 MET 439 GLN 440 GLY 441 GLU 442 ARG 443 GLU 444 LEU 445 VAL 446 GLN 447 ASP 448 CYS 449 ARG 450 SER 451 LEU 452 ALA 453 ARG 454 PHE 455 ALA 456 LEU 457 ARG 458 GLY 459 ILE 460 PRO 461 ALA 462 LEU 463 PRO 464 ALA 465 GLY 466 GLY 467 ALA 468 HIS 469 ILE 470 ARG 471 VAL 472 THR 473 PHE 474 GLN 475 VAL 476 ASP 477 ALA 478 ASP 479 GLY 480 LEU 481 LEU 482 SER 483 VAL 484 THR 485 ALA 486 MET 487 GLU 488 LYS 489 SER 490 THR 491 GLY 492 VAL 493 GLU 494 ALA 495 SER 496 ILE 497 GLN 498 VAL 499 LYS 500 PRO 501 SER 502 TYR 503 GLY 504 LEU 505 THR 506 ASP 507 SER 508 GLU 509 ILE 510 ALA 511 SER 512 MET 513 ILE 514 LYS 515 ASP 516 SER 517 MET 518 SER 519 TYR 520 ALA 521 GLU 522 GLN 523 ASP 524 VAL 525 LYS 526 ALA 527 ARG 528 MET 529 LEU 530 ALA 531 GLU 532 GLN 533 LYS 534 VAL 535 GLU 536 ALA 537 ALA 538 ARG 539 VAL 540 LEU 541 GLU 542 SER 543 LEU 544 HIS 545 GLY 546 ALA 547 LEU 548 ALA 549 ALA 550 ASP 551 ALA 552 ALA 553 LEU 554 LEU 555 SER 556 ALA 557 ALA 558 GLU 559 ARG 560 GLN 561 VAL 562 ILE 563 ASP 564 ASP 565 ALA 566 ALA 567 ALA 568 HIS 569 LEU 570 SER 571 GLU 572 VAL 573 ALA 574 GLN 575 GLY 576 ASP 577 ASP 578 VAL 579 ASP 580 ALA 581 ILE 582 GLU 583 LYS 584 ALA 585 ILE 586 LYS 587 ASN 588 VAL 589 ASP 590 LYS 591 GLN 592 THR 593 GLN 594 ASP 595 PHE 596 ALA 597 ALA 598 ARG 599 ARG 600 MET 601 ASP 602 GLN 603 SER 604 VAL 605 ARG 606 ARG 607 ALA 608 LEU 609 LYS 610 GLY 611 HIS 612 SER 613 VAL 614 ASP 615 GLU 616 VAL 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 _Strain _Gene_mnemonic $IscU 'E. Coli' 562 Bacteria . Escherichia coli K-12 iscu $HscA 'E. Coli' 562 Bacteria . Escherichia coli K-12 hsca 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 $IscU 'recombinant technology' . Escherichia coli BL21 pTrc99a $HscA 'recombinant technology' . Escherichia coli BL21 pTrc99a 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $IscU . mM 1.0 1.5 '[U-13C; U-15N]' TRIS 50 mM . . 'natural abundance' DTT 5 mM . . 'natural abundance' EDTA 0.5 mM . . 'natural abundance' $HscA . mM 2.0 3.0 'natural abundance' DSS 0.7 mM . . 'natural abundance' D2O 7 % . . '[U-99% 2H]' 'sodium azide' 0.02 % . . 'natural abundance' D2O 7 % . . '[U-99% 2H]' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_VNMRJ _Saveframe_category software _Name VNMRJ _Version . loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task collection stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model VNMRS _Field_strength 600 _Details 'Equipped with a cryoprobe' save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model VNMRS _Field_strength 900 _Details 'Equipped with a cryoprobe' 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_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _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_ ####################### # 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 . M pH 7.5 . pH pressure 1 . atm temperature 298 . 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 DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na 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 CBCA(CO)NH' '3D HNCO' '3D HNCACB' '3D HN(CO)CA' 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 IscU _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 4 4 SER C C 173.771 0.2 1 2 4 4 SER CA C 57.851 0.2 1 3 4 4 SER CB C 64.174 0.2 1 4 5 5 GLU H H 8.357 0.02 1 5 5 5 GLU C C 176.109 0.2 1 6 5 5 GLU CA C 56.512 0.2 1 7 5 5 GLU CB C 30.413 0.2 1 8 5 5 GLU N N 123.111 0.2 1 9 6 6 LYS H H 8.241 0.02 1 10 6 6 LYS C C 176.181 0.2 1 11 6 6 LYS CA C 56.333 0.2 1 12 6 6 LYS CB C 33.078 0.2 1 13 6 6 LYS N N 122.263 0.2 1 14 7 7 VAL H H 8.183 0.02 1 15 7 7 VAL C C 175.957 0.2 1 16 7 7 VAL CA C 62.331 0.2 1 17 7 7 VAL CB C 32.684 0.2 1 18 7 7 VAL N N 123.03 0.2 1 19 8 8 ILE H H 8.204 0.02 1 20 8 8 ILE C C 175.511 0.2 1 21 8 8 ILE CA C 60.851 0.2 1 22 8 8 ILE CB C 38.718 0.2 1 23 8 8 ILE N N 125.056 0.2 1 24 9 9 ASP H H 8.269 0.02 1 25 9 9 ASP C C 175.679 0.2 1 26 9 9 ASP CA C 54.257 0.2 1 27 9 9 ASP CB C 41.404 0.2 1 28 9 9 ASP N N 124.444 0.2 1 29 10 10 HIS H H 8.124 0.02 1 30 10 10 HIS C C 174.773 0.2 1 31 10 10 HIS CA C 56.485 0.2 1 32 10 10 HIS CB C 30.725 0.2 1 33 10 10 HIS N N 119.93 0.2 1 34 11 11 TYR H H 8.1 0.02 1 35 11 11 TYR C C 175.357 0.2 1 36 11 11 TYR CA C 57.959 0.2 1 37 11 11 TYR CB C 38.752 0.2 1 38 11 11 TYR N N 121.649 0.2 1 39 12 12 GLU H H 8.149 0.02 1 40 12 12 GLU C C 175.38 0.2 1 41 12 12 GLU CA C 56.094 0.2 1 42 12 12 GLU CB C 30.599 0.2 1 43 12 12 GLU N N 122.646 0.2 1 44 13 13 ASN H H 8.34 0.02 1 45 13 13 ASN CA C 51.426 0.2 1 46 13 13 ASN CB C 38.824 0.2 1 47 13 13 ASN N N 120.922 0.2 1 48 14 14 PRO C C 176.933 0.2 1 49 14 14 PRO CA C 63.477 0.2 1 50 14 14 PRO CB C 32.062 0.2 1 51 15 15 ARG H H 8.318 0.02 1 52 15 15 ARG C C 176.087 0.2 1 53 15 15 ARG CA C 56.117 0.2 1 54 15 15 ARG CB C 30.664 0.2 1 55 15 15 ARG N N 120.124 0.2 1 56 16 16 ASN H H 8.334 0.02 1 57 16 16 ASN N N 119.518 0.2 1 58 17 17 VAL C C 176.495 0.2 1 59 17 17 VAL CA C 62.622 0.2 1 60 17 17 VAL CB C 32.54 0.2 1 61 18 18 GLY H H 8.425 0.02 1 62 18 18 GLY C C 173.858 0.2 1 63 18 18 GLY CA C 45.231 0.2 1 64 18 18 GLY N N 112.053 0.2 1 65 19 19 SER H H 8.017 0.02 1 66 19 19 SER C C 174.166 0.2 1 67 19 19 SER CA C 58.136 0.2 1 68 19 19 SER CB C 63.915 0.2 1 69 19 19 SER N N 115.404 0.2 1 70 20 20 PHE H H 8.285 0.02 1 71 20 20 PHE C C 175.282 0.2 1 72 20 20 PHE CA C 57.632 0.2 1 73 20 20 PHE CB C 39.562 0.2 1 74 20 20 PHE N N 121.904 0.2 1 75 21 21 ASP H H 8.26 0.02 1 76 21 21 ASP C C 175.642 0.2 1 77 21 21 ASP CA C 54.343 0.2 1 78 21 21 ASP CB C 41.231 0.2 1 79 21 21 ASP N N 121.496 0.2 1 80 22 22 ASN H H 8.284 0.02 1 81 22 22 ASN C C 174.969 0.2 1 82 22 22 ASN CA C 53.436 0.2 1 83 22 22 ASN CB C 38.918 0.2 1 84 22 22 ASN N N 119.078 0.2 1 85 23 23 ASN H H 8.445 0.02 1 86 23 23 ASN C C 175.013 0.2 1 87 23 23 ASN CA C 53.644 0.2 1 88 23 23 ASN CB C 39.039 0.2 1 89 23 23 ASN N N 119.288 0.2 1 90 24 24 ASP H H 8.277 0.02 1 91 24 24 ASP C C 176.489 0.2 1 92 24 24 ASP CA C 54.801 0.2 1 93 24 24 ASP CB C 41.09 0.2 1 94 24 24 ASP N N 120.749 0.2 1 95 25 25 GLU H H 8.36 0.02 1 96 25 25 GLU C C 176.447 0.2 1 97 25 25 GLU CA C 57.058 0.2 1 98 25 25 GLU CB C 30.09 0.2 1 99 25 25 GLU N N 120.923 0.2 1 100 26 26 ASN H H 8.433 0.02 1 101 26 26 ASN C C 175.385 0.2 1 102 26 26 ASN CA C 53.524 0.2 1 103 26 26 ASN CB C 38.872 0.2 1 104 26 26 ASN N N 119.223 0.2 1 105 27 27 VAL H H 7.987 0.02 1 106 27 27 VAL C C 176.824 0.2 1 107 27 27 VAL CA C 62.72 0.2 1 108 27 27 VAL CB C 32.497 0.2 1 109 27 27 VAL N N 119.954 0.2 1 110 28 28 GLY H H 8.431 0.02 1 111 28 28 GLY C C 174.43 0.2 1 112 28 28 GLY CA C 45.419 0.2 1 113 28 28 GLY N N 111.932 0.2 1 114 29 29 SER H H 8.226 0.02 1 115 29 29 SER C C 175.234 0.2 1 116 29 29 SER CA C 58.751 0.2 1 117 29 29 SER CB C 63.86 0.2 1 118 29 29 SER N N 115.789 0.2 1 119 30 30 GLY H H 8.461 0.02 1 120 30 30 GLY C C 174.04 0.2 1 121 30 30 GLY CA C 45.422 0.2 1 122 30 30 GLY N N 110.714 0.2 1 123 31 31 MET H H 8.127 0.02 1 124 31 31 MET C C 176.202 0.2 1 125 31 31 MET CA C 55.482 0.2 1 126 31 31 MET CB C 32.932 0.2 1 127 31 31 MET N N 119.95 0.2 1 128 32 32 VAL H H 8.164 0.02 1 129 32 32 VAL C C 176.528 0.2 1 130 32 32 VAL CA C 62.544 0.2 1 131 32 32 VAL CB C 32.639 0.2 1 132 32 32 VAL N N 121.823 0.2 1 133 33 33 GLY H H 8.449 0.02 1 134 33 33 GLY C C 173.255 0.2 1 135 33 33 GLY CA C 44.934 0.2 1 136 33 33 GLY N N 112.866 0.2 1 137 34 34 ALA H H 8.069 0.02 1 138 34 34 ALA CA C 50.482 0.2 1 139 34 34 ALA CB C 18.296 0.2 1 140 34 34 ALA N N 124.801 0.2 1 141 35 35 PRO C C 176.742 0.2 1 142 35 35 PRO CA C 63.004 0.2 1 143 35 35 PRO CB C 32.004 0.2 1 144 36 36 ALA H H 8.452 0.02 1 145 36 36 ALA C C 177.761 0.2 1 146 36 36 ALA CA C 52.477 0.2 1 147 36 36 ALA CB C 19.16 0.2 1 148 36 36 ALA N N 124.487 0.2 1 149 37 37 CYS H H 8.33 0.02 1 150 37 37 CYS CA C 58.637 0.2 1 151 37 37 CYS CB C 28.278 0.2 1 152 37 37 CYS N N 118.385 0.2 1 153 38 38 GLY C C 173.751 0.2 1 154 38 38 GLY CA C 45.341 0.2 1 155 39 39 ASP H H 8.2 0.02 1 156 39 39 ASP C C 176.69 0.2 1 157 39 39 ASP CA C 54.541 0.2 1 158 39 39 ASP CB C 41.162 0.2 1 159 39 39 ASP N N 120.786 0.2 1 160 40 40 VAL H H 8.061 0.02 1 161 40 40 VAL C C 176.568 0.2 1 162 40 40 VAL CA C 62.853 0.2 1 163 40 40 VAL CB C 32.49 0.2 1 164 40 40 VAL N N 120.133 0.2 1 165 41 41 MET H H 8.327 0.02 1 166 41 41 MET C C 176.462 0.2 1 167 41 41 MET CA C 56.097 0.2 1 168 41 41 MET CB C 32.823 0.2 1 169 41 41 MET N N 122.459 0.2 1 170 42 42 LYS H H 8.096 0.02 1 171 42 42 LYS C C 176.383 0.2 1 172 42 42 LYS CA C 56.449 0.2 1 173 42 42 LYS CB C 32.902 0.2 1 174 42 42 LYS N N 121.893 0.2 1 175 43 43 LEU H H 8.059 0.02 1 176 43 43 LEU C C 177.091 0.2 1 177 43 43 LEU CA C 55.24 0.2 1 178 43 43 LEU CB C 42.389 0.2 1 179 43 43 LEU N N 122.532 0.2 1 180 44 44 GLN H H 8.285 0.02 1 181 44 44 GLN C C 175.536 0.2 1 182 44 44 GLN CA C 55.56 0.2 1 183 44 44 GLN CB C 29.423 0.2 1 184 44 44 GLN N N 121.381 0.2 1 185 45 45 ILE H H 8.075 0.02 1 186 45 45 ILE C C 175.76 0.2 1 187 45 45 ILE CA C 60.958 0.2 1 188 45 45 ILE CB C 38.828 0.2 1 189 45 45 ILE N N 122.549 0.2 1 190 46 46 LYS H H 8.383 0.02 1 191 46 46 LYS CA C 55.967 0.2 1 192 46 46 LYS CB C 33.257 0.2 1 193 46 46 LYS N N 126.254 0.2 1 194 47 47 VAL C C 175.788 0.2 1 195 47 47 VAL CA C 61.98 0.2 1 196 48 48 ASN H H 8.494 0.02 1 197 48 48 ASN CA C 53.125 0.2 1 198 48 48 ASN CB C 38.95 0.2 1 199 48 48 ASN N N 122.312 0.2 1 200 50 50 GLU C C 176.988 0.2 1 201 50 50 GLU CA C 56.958 0.2 1 202 51 51 GLY H H 8.367 0.02 1 203 51 51 GLY C C 173.925 0.2 1 204 51 51 GLY CA C 45.444 0.2 1 205 51 51 GLY N N 109.16 0.2 1 206 52 52 ILE H H 7.852 0.02 1 207 52 52 ILE C C 176.198 0.2 1 208 52 52 ILE CA C 60.965 0.2 1 209 52 52 ILE CB C 38.624 0.2 1 210 52 52 ILE N N 120.385 0.2 1 211 53 53 ILE H H 8.222 0.02 1 212 53 53 ILE C C 176.161 0.2 1 213 53 53 ILE CA C 60.99 0.2 1 214 53 53 ILE CB C 38.513 0.2 1 215 53 53 ILE N N 125.728 0.2 1 216 54 54 GLU H H 8.487 0.02 1 217 54 54 GLU CA C 56.625 0.2 1 218 54 54 GLU CB C 30.481 0.2 1 219 54 54 GLU N N 125.92 0.2 1 220 55 55 ASP C C 176.425 0.2 1 221 55 55 ASP CA C 54.445 0.2 1 222 55 55 ASP CB C 41.501 0.2 1 223 56 56 ALA H H 8.372 0.02 1 224 56 56 ALA C C 178.376 0.2 1 225 56 56 ALA CA C 53.275 0.2 1 226 56 56 ALA CB C 18.901 0.2 1 227 56 56 ALA N N 125.648 0.2 1 228 57 57 ARG H H 8.22 0.02 1 229 57 57 ARG C C 176.753 0.2 1 230 57 57 ARG CA C 57.195 0.2 1 231 57 57 ARG CB C 30.302 0.2 1 232 57 57 ARG N N 118.408 0.2 1 233 58 58 PHE H H 7.908 0.02 1 234 58 58 PHE C C 175.785 0.2 1 235 58 58 PHE CA C 57.665 0.2 1 236 58 58 PHE CB C 39.237 0.2 1 237 58 58 PHE N N 118.615 0.2 1 238 59 59 LYS H H 7.907 0.02 1 239 59 59 LYS C C 176.387 0.2 1 240 59 59 LYS CA C 56.579 0.2 1 241 59 59 LYS CB C 33.072 0.2 1 242 59 59 LYS N N 121.503 0.2 1 243 60 60 THR H H 7.955 0.02 1 244 60 60 THR C C 174.168 0.2 1 245 60 60 THR CA C 61.916 0.2 1 246 60 60 THR CB C 69.896 0.2 1 247 60 60 THR N N 114.236 0.2 1 248 61 61 TYR H H 8.198 0.02 1 249 61 61 TYR C C 176.327 0.2 1 250 61 61 TYR N N 121.842 0.2 1 251 62 62 GLY H H 8.307 0.02 1 252 62 62 GLY N N 110.385 0.2 1 253 71 71 SER C C 174.363 0.2 1 254 71 71 SER CA C 58.712 0.2 1 255 71 71 SER CB C 63.76 0.2 1 256 72 72 LEU H H 8.112 0.02 1 257 72 72 LEU CA C 55.54 0.2 1 258 72 72 LEU CB C 42.314 0.2 1 259 72 72 LEU N N 123.672 0.2 1 260 76 76 TRP HE1 H 10.171 0.02 1 261 76 76 TRP NE1 N 129.412 0.2 1 262 80 80 LYS C C 176.613 0.2 1 263 80 80 LYS CA C 56.156 0.2 1 264 81 81 SER H H 8.374 0.02 1 265 81 81 SER C C 174.723 0.2 1 266 81 81 SER CA C 58.403 0.2 1 267 81 81 SER CB C 63.819 0.2 1 268 81 81 SER N N 117.419 0.2 1 269 82 82 LEU H H 8.36 0.02 1 270 82 82 LEU C C 177.304 0.2 1 271 82 82 LEU CA C 55.768 0.2 1 272 82 82 LEU CB C 42.122 0.2 1 273 82 82 LEU N N 124.169 0.2 1 274 83 83 ASP H H 8.215 0.02 1 275 83 83 ASP C C 176.718 0.2 1 276 83 83 ASP CA C 54.742 0.2 1 277 83 83 ASP CB C 41.074 0.2 1 278 83 83 ASP N N 120.343 0.2 1 279 84 84 GLU H H 8.23 0.02 1 280 84 84 GLU C C 176.755 0.2 1 281 84 84 GLU CA C 57.173 0.2 1 282 84 84 GLU CB C 30.18 0.2 1 283 84 84 GLU N N 121.475 0.2 1 284 85 85 ALA H H 8.226 0.02 1 285 85 85 ALA C C 178.14 0.2 1 286 85 85 ALA CA C 53.099 0.2 1 287 85 85 ALA CB C 18.897 0.2 1 288 85 85 ALA N N 123.755 0.2 1 289 86 86 GLN H H 8.104 0.02 1 290 86 86 GLN C C 175.833 0.2 1 291 86 86 GLN CA C 55.885 0.2 1 292 86 86 GLN CB C 29.355 0.2 1 293 86 86 GLN N N 118.232 0.2 1 294 87 87 ALA H H 8.083 0.02 1 295 87 87 ALA C C 177.711 0.2 1 296 87 87 ALA CA C 52.711 0.2 1 297 87 87 ALA CB C 19.111 0.2 1 298 87 87 ALA N N 124.454 0.2 1 299 88 88 ILE H H 7.999 0.02 1 300 88 88 ILE C C 176.223 0.2 1 301 88 88 ILE CA C 61.172 0.2 1 302 88 88 ILE CB C 38.632 0.2 1 303 88 88 ILE N N 119.979 0.2 1 304 89 89 LYS H H 8.287 0.02 1 305 89 89 LYS CA C 56.074 0.2 1 306 89 89 LYS CB C 33.195 0.2 1 307 89 89 LYS N N 125.439 0.2 1 308 90 90 ASN C C 175.454 0.2 1 309 90 90 ASN CA C 53.513 0.2 1 310 90 90 ASN CB C 38.869 0.2 1 311 91 91 THR H H 8.11 0.02 1 312 91 91 THR C C 174.21 0.2 1 313 91 91 THR CA C 61.901 0.2 1 314 91 91 THR CB C 69.609 0.2 1 315 91 91 THR N N 114.011 0.2 1 316 92 92 ASP H H 8.316 0.02 1 317 92 92 ASP C C 176.018 0.2 1 318 92 92 ASP CA C 54.669 0.2 1 319 92 92 ASP CB C 41.044 0.2 1 320 92 92 ASP N N 122.876 0.2 1 321 93 93 ILE H H 7.943 0.02 1 322 93 93 ILE C C 175.785 0.2 1 323 93 93 ILE CA C 60.986 0.2 1 324 93 93 ILE CB C 38.773 0.2 1 325 93 93 ILE N N 120.749 0.2 1 326 94 94 ALA H H 8.301 0.02 1 327 94 94 ALA C C 177.506 0.2 1 328 94 94 ALA CA C 52.445 0.2 1 329 94 94 ALA CB C 19.251 0.2 1 330 94 94 ALA N N 128.245 0.2 1 331 95 95 GLU H H 8.259 0.02 1 332 95 95 GLU CA C 56.476 0.2 1 333 95 95 GLU CB C 30.503 0.2 1 334 95 95 GLU N N 120.571 0.2 1 335 110 110 ALA C C 178.088 0.2 1 336 111 111 GLU H H 8.454 0.02 1 337 111 111 GLU N N 119.784 0.2 1 338 112 112 ASP C C 176.478 0.2 1 339 112 112 ASP CA C 54.902 0.2 1 340 112 112 ASP CB C 40.827 0.2 1 341 113 113 ALA H H 7.991 0.02 1 342 113 113 ALA C C 178.289 0.2 1 343 113 113 ALA CA C 53.166 0.2 1 344 113 113 ALA CB C 19.085 0.2 1 345 113 113 ALA N N 123.745 0.2 1 346 114 114 ILE H H 7.934 0.02 1 347 114 114 ILE CA C 61.76 0.2 1 348 114 114 ILE CB C 38.236 0.2 1 349 114 114 ILE N N 119.432 0.2 1 350 126 126 GLU C C 175.857 0.2 1 351 126 126 GLU CA C 56.397 0.2 1 352 126 126 GLU CB C 30.344 0.2 1 353 127 127 ALA H H 8.163 0.02 1 354 127 127 ALA C C 176.458 0.2 1 355 127 127 ALA CA C 52.457 0.2 1 356 127 127 ALA CB C 19.159 0.2 1 357 127 127 ALA N N 125.66 0.2 1 358 128 128 LYS H H 7.858 0.02 1 359 128 128 LYS CA C 57.565 0.2 1 360 128 128 LYS CB C 33.793 0.2 1 361 128 128 LYS N N 126.159 0.2 1 stop_ save_