data_19301 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Redox-linked domain movements in the catalytic cycle of cytochrome P450 reductase ; _BMRB_accession_number 19301 _BMRB_flat_file_name bmr19301.str _Entry_type original _Submission_date 2013-06-17 _Accession_date 2013-06-17 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'NADPH-cytochrome P450 reductase' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Huang Wei-Cheng . . 2 Ellis Jacqueline . . 3 Barsukov Igor L. . 4 Moody Peter 'C. E.' . 5 Raven Emma L. . 6 Robert Gordon 'C. K.' . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 181 "13C chemical shifts" 523 "15N chemical shifts" 181 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-02-13 original author . stop_ _Original_release_date 2014-02-13 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Redox-linked domain movements in the catalytic cycle of cytochrome p450 reductase.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23911089 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Huang Wei-Cheng . . 2 Ellis Jacqueline . . 3 Moody Peter C.E. . 4 Raven Emma L. . 5 Roberts Gordon C.K. . stop_ _Journal_abbreviation Structure _Journal_name_full 'Structure (London, England : 1993)' _Journal_volume 21 _Journal_issue 9 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1581 _Page_last 1589 _Year 2013 _Details . loop_ _Keyword 'cytochrome P450 reductase' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name CPR _Enzyme_commission_number 1.6.2.4 loop_ _Mol_system_component_name _Mol_label CPR $CPR FMN $entity_FMN FAD $entity_FAD stop_ _System_molecular_weight 70827.4 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'This CPR enzyme is required for electron transfer from NADPH to cytochrome P450.' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CPR _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common CPR _Molecular_mass 70827.4 _Mol_thiol_state 'not available' loop_ _Biological_function Oxidoreductase stop_ _Details 'Two cofactors (FMN and FAD) included.' ############################## # Polymer residue sequence # ############################## _Residue_count 614 _Mol_residue_sequence ; VRESSFVEKMKKTGRNIIVF YGSQTGTAEEFANRLSKDAH RYGMRGMSADPEEYDLADLS SLPEIDNALVVFCMATYGEG DPTDNAQDFYDWLQETDVDL SGVKFAVFGLGNKTYEHFNA MGKYVDKRLEQLGAQRIFEL GLGDDDGNLEEDFITWREQF WPAVCEHFGVEATGEESSIR QYELVVHTDIDAAKVYMGEM GRLKSYENQKPPFDAKNPFL AAVTTNRKLNQGTERHLMHL ELDISDSKIRYESGDHVAVY PANDSALVNQLGKILGADLD VVMSLNNLDEESNKKHPFPC PTSYRTALTYYLDITNPPRT NVLYELAQYASEPSEQELLR KMASSSGEGKELYLSWVVEA RRHILAILQDCPSLRPPIDH LCELLPRLQARYYSIASSSK VHPNSVHICAVVVEYETKAG RINKGVATNWLRAKEPAGEN GGRALVPMFVRKSQFRLPFK ATTPVIMVGPGTGVAPFIGF IQERAWLRQQGKEVGETLLY YGCRRSDEDYLYREELAQFH RDGALTQLNVAFSREQSHKV YVQHLLKQDREHLWKLIEGG AHIYVCGDARNMARDVQNTF YDIVAELGAMEHAQAVDYIK KLMTKGRYSLDVWS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 64 VAL 2 65 ARG 3 66 GLU 4 67 SER 5 68 SER 6 69 PHE 7 70 VAL 8 71 GLU 9 72 LYS 10 73 MET 11 74 LYS 12 75 LYS 13 76 THR 14 77 GLY 15 78 ARG 16 79 ASN 17 80 ILE 18 81 ILE 19 82 VAL 20 83 PHE 21 84 TYR 22 85 GLY 23 86 SER 24 87 GLN 25 88 THR 26 89 GLY 27 90 THR 28 91 ALA 29 92 GLU 30 93 GLU 31 94 PHE 32 95 ALA 33 96 ASN 34 97 ARG 35 98 LEU 36 99 SER 37 100 LYS 38 101 ASP 39 102 ALA 40 103 HIS 41 104 ARG 42 105 TYR 43 106 GLY 44 107 MET 45 108 ARG 46 109 GLY 47 110 MET 48 111 SER 49 112 ALA 50 113 ASP 51 114 PRO 52 115 GLU 53 116 GLU 54 117 TYR 55 118 ASP 56 119 LEU 57 120 ALA 58 121 ASP 59 122 LEU 60 123 SER 61 124 SER 62 125 LEU 63 126 PRO 64 127 GLU 65 128 ILE 66 129 ASP 67 130 ASN 68 131 ALA 69 132 LEU 70 133 VAL 71 134 VAL 72 135 PHE 73 136 CYS 74 137 MET 75 138 ALA 76 139 THR 77 140 TYR 78 141 GLY 79 142 GLU 80 143 GLY 81 144 ASP 82 145 PRO 83 146 THR 84 147 ASP 85 148 ASN 86 149 ALA 87 150 GLN 88 151 ASP 89 152 PHE 90 153 TYR 91 154 ASP 92 155 TRP 93 156 LEU 94 157 GLN 95 158 GLU 96 159 THR 97 160 ASP 98 161 VAL 99 162 ASP 100 163 LEU 101 164 SER 102 165 GLY 103 166 VAL 104 167 LYS 105 168 PHE 106 169 ALA 107 170 VAL 108 171 PHE 109 172 GLY 110 173 LEU 111 174 GLY 112 175 ASN 113 176 LYS 114 177 THR 115 178 TYR 116 179 GLU 117 180 HIS 118 181 PHE 119 182 ASN 120 183 ALA 121 184 MET 122 185 GLY 123 186 LYS 124 187 TYR 125 188 VAL 126 189 ASP 127 190 LYS 128 191 ARG 129 192 LEU 130 193 GLU 131 194 GLN 132 195 LEU 133 196 GLY 134 197 ALA 135 198 GLN 136 199 ARG 137 200 ILE 138 201 PHE 139 202 GLU 140 203 LEU 141 204 GLY 142 205 LEU 143 206 GLY 144 207 ASP 145 208 ASP 146 209 ASP 147 210 GLY 148 211 ASN 149 212 LEU 150 213 GLU 151 214 GLU 152 215 ASP 153 216 PHE 154 217 ILE 155 218 THR 156 219 TRP 157 220 ARG 158 221 GLU 159 222 GLN 160 223 PHE 161 224 TRP 162 225 PRO 163 226 ALA 164 227 VAL 165 228 CYS 166 229 GLU 167 230 HIS 168 231 PHE 169 232 GLY 170 233 VAL 171 234 GLU 172 235 ALA 173 236 THR 174 237 GLY 175 238 GLU 176 239 GLU 177 240 SER 178 241 SER 179 242 ILE 180 243 ARG 181 244 GLN 182 245 TYR 183 246 GLU 184 247 LEU 185 248 VAL 186 249 VAL 187 250 HIS 188 251 THR 189 252 ASP 190 253 ILE 191 254 ASP 192 255 ALA 193 256 ALA 194 257 LYS 195 258 VAL 196 259 TYR 197 260 MET 198 261 GLY 199 262 GLU 200 263 MET 201 264 GLY 202 265 ARG 203 266 LEU 204 267 LYS 205 268 SER 206 269 TYR 207 270 GLU 208 271 ASN 209 272 GLN 210 273 LYS 211 274 PRO 212 275 PRO 213 276 PHE 214 277 ASP 215 278 ALA 216 279 LYS 217 280 ASN 218 281 PRO 219 282 PHE 220 283 LEU 221 284 ALA 222 285 ALA 223 286 VAL 224 287 THR 225 288 THR 226 289 ASN 227 290 ARG 228 291 LYS 229 292 LEU 230 293 ASN 231 294 GLN 232 295 GLY 233 296 THR 234 297 GLU 235 298 ARG 236 299 HIS 237 300 LEU 238 301 MET 239 302 HIS 240 303 LEU 241 304 GLU 242 305 LEU 243 306 ASP 244 307 ILE 245 308 SER 246 309 ASP 247 310 SER 248 311 LYS 249 312 ILE 250 313 ARG 251 314 TYR 252 315 GLU 253 316 SER 254 317 GLY 255 318 ASP 256 319 HIS 257 320 VAL 258 321 ALA 259 322 VAL 260 323 TYR 261 324 PRO 262 325 ALA 263 326 ASN 264 327 ASP 265 328 SER 266 329 ALA 267 330 LEU 268 331 VAL 269 332 ASN 270 333 GLN 271 334 LEU 272 335 GLY 273 336 LYS 274 337 ILE 275 338 LEU 276 339 GLY 277 340 ALA 278 341 ASP 279 342 LEU 280 343 ASP 281 344 VAL 282 345 VAL 283 346 MET 284 347 SER 285 348 LEU 286 349 ASN 287 350 ASN 288 351 LEU 289 352 ASP 290 353 GLU 291 354 GLU 292 355 SER 293 356 ASN 294 357 LYS 295 358 LYS 296 359 HIS 297 360 PRO 298 361 PHE 299 362 PRO 300 363 CYS 301 364 PRO 302 365 THR 303 366 SER 304 367 TYR 305 368 ARG 306 369 THR 307 370 ALA 308 371 LEU 309 372 THR 310 373 TYR 311 374 TYR 312 375 LEU 313 376 ASP 314 377 ILE 315 378 THR 316 379 ASN 317 380 PRO 318 381 PRO 319 382 ARG 320 383 THR 321 384 ASN 322 385 VAL 323 386 LEU 324 387 TYR 325 388 GLU 326 389 LEU 327 390 ALA 328 391 GLN 329 392 TYR 330 393 ALA 331 394 SER 332 395 GLU 333 396 PRO 334 397 SER 335 398 GLU 336 399 GLN 337 400 GLU 338 401 LEU 339 402 LEU 340 403 ARG 341 404 LYS 342 405 MET 343 406 ALA 344 407 SER 345 408 SER 346 409 SER 347 410 GLY 348 411 GLU 349 412 GLY 350 413 LYS 351 414 GLU 352 415 LEU 353 416 TYR 354 417 LEU 355 418 SER 356 419 TRP 357 420 VAL 358 421 VAL 359 422 GLU 360 423 ALA 361 424 ARG 362 425 ARG 363 426 HIS 364 427 ILE 365 428 LEU 366 429 ALA 367 430 ILE 368 431 LEU 369 432 GLN 370 433 ASP 371 434 CYS 372 435 PRO 373 436 SER 374 437 LEU 375 438 ARG 376 439 PRO 377 440 PRO 378 441 ILE 379 442 ASP 380 443 HIS 381 444 LEU 382 445 CYS 383 446 GLU 384 447 LEU 385 448 LEU 386 449 PRO 387 450 ARG 388 451 LEU 389 452 GLN 390 453 ALA 391 454 ARG 392 455 TYR 393 456 TYR 394 457 SER 395 458 ILE 396 459 ALA 397 460 SER 398 461 SER 399 462 SER 400 463 LYS 401 464 VAL 402 465 HIS 403 466 PRO 404 467 ASN 405 468 SER 406 469 VAL 407 470 HIS 408 471 ILE 409 472 CYS 410 473 ALA 411 474 VAL 412 475 VAL 413 476 VAL 414 477 GLU 415 478 TYR 416 479 GLU 417 480 THR 418 481 LYS 419 482 ALA 420 483 GLY 421 484 ARG 422 485 ILE 423 486 ASN 424 487 LYS 425 488 GLY 426 489 VAL 427 490 ALA 428 491 THR 429 492 ASN 430 493 TRP 431 494 LEU 432 495 ARG 433 496 ALA 434 497 LYS 435 498 GLU 436 499 PRO 437 500 ALA 438 501 GLY 439 502 GLU 440 503 ASN 441 504 GLY 442 505 GLY 443 506 ARG 444 507 ALA 445 508 LEU 446 509 VAL 447 510 PRO 448 511 MET 449 512 PHE 450 513 VAL 451 514 ARG 452 515 LYS 453 516 SER 454 517 GLN 455 518 PHE 456 519 ARG 457 520 LEU 458 521 PRO 459 522 PHE 460 523 LYS 461 524 ALA 462 525 THR 463 526 THR 464 527 PRO 465 528 VAL 466 529 ILE 467 530 MET 468 531 VAL 469 532 GLY 470 533 PRO 471 534 GLY 472 535 THR 473 536 GLY 474 537 VAL 475 538 ALA 476 539 PRO 477 540 PHE 478 541 ILE 479 542 GLY 480 543 PHE 481 544 ILE 482 545 GLN 483 546 GLU 484 547 ARG 485 548 ALA 486 549 TRP 487 550 LEU 488 551 ARG 489 552 GLN 490 553 GLN 491 554 GLY 492 555 LYS 493 556 GLU 494 557 VAL 495 558 GLY 496 559 GLU 497 560 THR 498 561 LEU 499 562 LEU 500 563 TYR 501 564 TYR 502 565 GLY 503 566 CYS 504 567 ARG 505 568 ARG 506 569 SER 507 570 ASP 508 571 GLU 509 572 ASP 510 573 TYR 511 574 LEU 512 575 TYR 513 576 ARG 514 577 GLU 515 578 GLU 516 579 LEU 517 580 ALA 518 581 GLN 519 582 PHE 520 583 HIS 521 584 ARG 522 585 ASP 523 586 GLY 524 587 ALA 525 588 LEU 526 589 THR 527 590 GLN 528 591 LEU 529 592 ASN 530 593 VAL 531 594 ALA 532 595 PHE 533 596 SER 534 597 ARG 535 598 GLU 536 599 GLN 537 600 SER 538 601 HIS 539 602 LYS 540 603 VAL 541 604 TYR 542 605 VAL 543 606 GLN 544 607 HIS 545 608 LEU 546 609 LEU 547 610 LYS 548 611 GLN 549 612 ASP 550 613 ARG 551 614 GLU 552 615 HIS 553 616 LEU 554 617 TRP 555 618 LYS 556 619 LEU 557 620 ILE 558 621 GLU 559 622 GLY 560 623 GLY 561 624 ALA 562 625 HIS 563 626 ILE 564 627 TYR 565 628 VAL 566 629 CYS 567 630 GLY 568 631 ASP 569 632 ALA 570 633 ARG 571 634 ASN 572 635 MET 573 636 ALA 574 637 ARG 575 638 ASP 576 639 VAL 577 640 GLN 578 641 ASN 579 642 THR 580 643 PHE 581 644 TYR 582 645 ASP 583 646 ILE 584 647 VAL 585 648 ALA 586 649 GLU 587 650 LEU 588 651 GLY 589 652 ALA 590 653 MET 591 654 GLU 592 655 HIS 593 656 ALA 594 657 GLN 595 658 ALA 596 659 VAL 597 660 ASP 598 661 TYR 599 662 ILE 600 663 LYS 601 664 LYS 602 665 LEU 603 666 MET 604 667 THR 605 668 LYS 606 669 GLY 607 670 ARG 608 671 TYR 609 672 SER 610 673 LEU 611 674 ASP 612 675 VAL 613 676 TRP 614 677 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-04 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 3QE2 "Crystal Structure Of Human Nadph-Cytochrome P450 Reductase" 100.00 618 99.67 99.67 0.00e+00 PDB 3QFC "Crystal Structure Of Human Nadph-Cytochrome P450 (V492e Mutant)" 100.00 618 99.51 99.51 0.00e+00 PDB 3QFR "Crystal Structure Of Human Nadph-Cytochrome P450 Reductase (R457h Mutant)" 100.00 618 99.84 99.84 0.00e+00 PDB 3QFS "Crystal Structure Of Nadph-Cytochrome P450 Reductase (FadNADPH Domain)" 72.64 458 98.21 98.43 0.00e+00 PDB 3QFT "Crystal Structure Of Nadph-Cytochrome P450 Reductase (FadNADPH DOMAIN And R457h Mutant)" 72.64 458 97.98 98.21 0.00e+00 DBJ BAB18572 "NADPH-cytochrome P-450 reductase [Homo sapiens]" 100.00 677 99.67 99.84 0.00e+00 DBJ BAD93111 "Hypothetical protein DKFZp686G04235 variant [Homo sapiens]" 100.00 686 100.00 100.00 0.00e+00 DBJ BAE72975 "hypothetical protein [Macaca fascicularis]" 98.53 605 99.34 99.83 0.00e+00 DBJ BAF83218 "unnamed protein product [Homo sapiens]" 100.00 680 99.67 99.84 0.00e+00 DBJ BAG35442 "unnamed protein product [Homo sapiens]" 100.00 680 99.84 100.00 0.00e+00 EMBL CAH56151 "hypothetical protein [Homo sapiens]" 100.00 680 100.00 100.00 0.00e+00 GB AAB21814 "cytochrome P450 reductase, partial [Homo sapiens]" 100.00 676 99.35 99.35 0.00e+00 GB AAD56649 "OR [Cloning vector pCS512]" 100.00 677 99.02 99.67 0.00e+00 GB AAF07050 "NADPH-cytochrome P450 reductase [Expression vector pCS316]" 100.00 677 99.02 99.67 0.00e+00 GB AAF07052 "human NADPH-cytochrome P450 reductase [Expression vector pSB229]" 100.00 677 99.02 99.67 0.00e+00 GB AAF09458 "hOR [Shuttle vector pCS513]" 100.00 677 99.02 99.67 0.00e+00 REF NP_000932 "NADPH--cytochrome P450 reductase [Homo sapiens]" 100.00 680 100.00 100.00 0.00e+00 REF NP_001248085 "NADPH--cytochrome P450 reductase [Macaca mulatta]" 100.00 680 99.51 100.00 0.00e+00 REF XP_001155755 "PREDICTED: NADPH--cytochrome P450 reductase isoform X1 [Pan troglodytes]" 100.00 680 99.67 100.00 0.00e+00 REF XP_003276705 "PREDICTED: NADPH--cytochrome P450 reductase [Nomascus leucogenys]" 100.00 680 99.19 99.67 0.00e+00 REF XP_003808966 "PREDICTED: NADPH--cytochrome P450 reductase isoform X2 [Pan paniscus]" 100.00 680 99.67 100.00 0.00e+00 SP P16435 "RecName: Full=NADPH--cytochrome P450 reductase; Short=CPR; Short=P450R" 100.00 677 100.00 100.00 0.00e+00 stop_ save_ ############# # Ligands # ############# save_FMN _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'FLAVIN MONONUCLEOTIDE' _BMRB_code FMN _PDB_code FMN _Molecular_mass 456.344 _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 N1 N1 N . 0 . ? C2 C2 C . 0 . ? O2 O2 O . 0 . ? N3 N3 N . 0 . ? C4 C4 C . 0 . ? O4 O4 O . 0 . ? C4A C4A C . 0 . ? N5 N5 N . 0 . ? C5A C5A C . 0 . ? C6 C6 C . 0 . ? C7 C7 C . 0 . ? C7M C7M C . 0 . ? C8 C8 C . 0 . ? C8M C8M C . 0 . ? C9 C9 C . 0 . ? C9A C9A C . 0 . ? N10 N10 N . 0 . ? C10 C10 C . 0 . ? C1' C1' C . 0 . ? C2' C2' C . 0 . ? O2' O2' O . 0 . ? C3' C3' C . 0 . ? O3' O3' O . 0 . ? C4' C4' C . 0 . ? O4' O4' O . 0 . ? C5' C5' C . 0 . ? O5' O5' O . 0 . ? P P P . 0 . ? O1P O1P O . 0 . ? O2P O2P O . 0 . ? O3P O3P O . 0 . ? HN3 HN3 H . 0 . ? H6 H6 H . 0 . ? HM71 HM71 H . 0 . ? HM72 HM72 H . 0 . ? HM73 HM73 H . 0 . ? HM81 HM81 H . 0 . ? HM82 HM82 H . 0 . ? HM83 HM83 H . 0 . ? H9 H9 H . 0 . ? H1'1 H1'1 H . 0 . ? H1'2 H1'2 H . 0 . ? H2' H2' H . 0 . ? HO2' HO2' H . 0 . ? H3' H3' H . 0 . ? HO3' HO3' H . 0 . ? H4' H4' H . 0 . ? HO4' HO4' H . 0 . ? H5'1 H5'1 H . 0 . ? H5'2 H5'2 H . 0 . ? HOP2 HOP2 H . 0 . ? HOP3 HOP3 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N1 C2 ? ? DOUB N1 C10 ? ? DOUB C2 O2 ? ? SING C2 N3 ? ? SING N3 C4 ? ? SING N3 HN3 ? ? DOUB C4 O4 ? ? SING C4 C4A ? ? DOUB C4A N5 ? ? SING C4A C10 ? ? SING N5 C5A ? ? DOUB C5A C6 ? ? SING C5A C9A ? ? SING C6 C7 ? ? SING C6 H6 ? ? SING C7 C7M ? ? DOUB C7 C8 ? ? SING C7M HM71 ? ? SING C7M HM72 ? ? SING C7M HM73 ? ? SING C8 C8M ? ? SING C8 C9 ? ? SING C8M HM81 ? ? SING C8M HM82 ? ? SING C8M HM83 ? ? DOUB C9 C9A ? ? SING C9 H9 ? ? SING C9A N10 ? ? SING N10 C10 ? ? SING N10 C1' ? ? SING C1' C2' ? ? SING C1' H1'1 ? ? SING C1' H1'2 ? ? SING C2' O2' ? ? SING C2' C3' ? ? SING C2' H2' ? ? SING O2' HO2' ? ? SING C3' O3' ? ? SING C3' C4' ? ? SING C3' H3' ? ? SING O3' HO3' ? ? SING C4' O4' ? ? SING C4' C5' ? ? SING C4' H4' ? ? SING O4' HO4' ? ? SING C5' O5' ? ? SING C5' H5'1 ? ? SING C5' H5'2 ? ? SING O5' P ? ? DOUB P O1P ? ? SING P O2P ? ? SING P O3P ? ? SING O2P HOP2 ? ? SING O3P HOP3 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ save_FAD _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'FLAVIN-ADENINE DINUCLEOTIDE' _BMRB_code FAD _PDB_code FAD _Molecular_mass 785.550 _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 PA PA P . 0 . ? O1A O1A O . 0 . ? O2A O2A O . 0 . ? O5B O5B O . 0 . ? C5B C5B C . 0 . ? C4B C4B C . 0 . ? O4B O4B O . 0 . ? C3B C3B C . 0 . ? O3B O3B O . 0 . ? C2B C2B C . 0 . ? O2B O2B O . 0 . ? C1B C1B C . 0 . ? N9A N9A N . 0 . ? C8A C8A C . 0 . ? N7A N7A N . 0 . ? C5A C5A C . 0 . ? C6A C6A C . 0 . ? N6A N6A N . 0 . ? N1A N1A N . 0 . ? C2A C2A C . 0 . ? N3A N3A N . 0 . ? C4A C4A C . 0 . ? N1 N1 N . 0 . ? C2 C2 C . 0 . ? O2 O2 O . 0 . ? N3 N3 N . 0 . ? C4 C4 C . 0 . ? O4 O4 O . 0 . ? C4X C4X C . 0 . ? N5 N5 N . 0 . ? C5X C5X C . 0 . ? C6 C6 C . 0 . ? C7 C7 C . 0 . ? C7M C7M C . 0 . ? C8 C8 C . 0 . ? C8M C8M C . 0 . ? C9 C9 C . 0 . ? C9A C9A C . 0 . ? N10 N10 N . 0 . ? C10 C10 C . 0 . ? C1' C1' C . 0 . ? C2' C2' C . 0 . ? O2' O2' O . 0 . ? C3' C3' C . 0 . ? O3' O3' O . 0 . ? C4' C4' C . 0 . ? O4' O4' O . 0 . ? C5' C5' C . 0 . ? O5' O5' O . 0 . ? P P P . 0 . ? O1P O1P O . 0 . ? O2P O2P O . 0 . ? O3P O3P O . 0 . ? HOA2 HOA2 H . 0 . ? H51A H51A H . 0 . ? H52A H52A H . 0 . ? H4B H4B H . 0 . ? H3B H3B H . 0 . ? HO3A HO3A H . 0 . ? H2B H2B H . 0 . ? HO2A HO2A H . 0 . ? H1B H1B H . 0 . ? H8A H8A H . 0 . ? H61A H61A H . 0 . ? H62A H62A H . 0 . ? H2A H2A H . 0 . ? HN3 HN3 H . 0 . ? H6 H6 H . 0 . ? HM71 HM71 H . 0 . ? HM72 HM72 H . 0 . ? HM73 HM73 H . 0 . ? HM81 HM81 H . 0 . ? HM82 HM82 H . 0 . ? HM83 HM83 H . 0 . ? H9 H9 H . 0 . ? H1'1 H1'1 H . 0 . ? H1'2 H1'2 H . 0 . ? H2' H2' H . 0 . ? HO2' HO2' H . 0 . ? H3' H3' H . 0 . ? HO3' HO3' H . 0 . ? H4' H4' H . 0 . ? HO4' HO4' H . 0 . ? H5'1 H5'1 H . 0 . ? H5'2 H5'2 H . 0 . ? HOP2 HOP2 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 PA O1A ? ? SING PA O2A ? ? SING PA O5B ? ? SING PA O3P ? ? SING O2A HOA2 ? ? SING O5B C5B ? ? SING C5B C4B ? ? SING C5B H51A ? ? SING C5B H52A ? ? SING C4B O4B ? ? SING C4B C3B ? ? SING C4B H4B ? ? SING O4B C1B ? ? SING C3B O3B ? ? SING C3B C2B ? ? SING C3B H3B ? ? SING O3B HO3A ? ? SING C2B O2B ? ? SING C2B C1B ? ? SING C2B H2B ? ? SING O2B HO2A ? ? SING C1B N9A ? ? SING C1B H1B ? ? SING N9A C8A ? ? SING N9A C4A ? ? DOUB C8A N7A ? ? SING C8A H8A ? ? SING N7A C5A ? ? SING C5A C6A ? ? DOUB C5A C4A ? ? SING C6A N6A ? ? DOUB C6A N1A ? ? SING N6A H61A ? ? SING N6A H62A ? ? SING N1A C2A ? ? DOUB C2A N3A ? ? SING C2A H2A ? ? SING N3A C4A ? ? SING N1 C2 ? ? DOUB N1 C10 ? ? DOUB C2 O2 ? ? SING C2 N3 ? ? SING N3 C4 ? ? SING N3 HN3 ? ? DOUB C4 O4 ? ? SING C4 C4X ? ? DOUB C4X N5 ? ? SING C4X C10 ? ? SING N5 C5X ? ? DOUB C5X C6 ? ? SING C5X C9A ? ? SING C6 C7 ? ? SING C6 H6 ? ? SING C7 C7M ? ? DOUB C7 C8 ? ? SING C7M HM71 ? ? SING C7M HM72 ? ? SING C7M HM73 ? ? SING C8 C8M ? ? SING C8 C9 ? ? SING C8M HM81 ? ? SING C8M HM82 ? ? SING C8M HM83 ? ? DOUB C9 C9A ? ? SING C9 H9 ? ? SING C9A N10 ? ? SING N10 C10 ? ? SING N10 C1' ? ? SING C1' C2' ? ? SING C1' H1'1 ? ? SING C1' H1'2 ? ? SING C2' O2' ? ? SING C2' C3' ? ? SING C2' H2' ? ? SING O2' HO2' ? ? SING C3' O3' ? ? SING C3' C4' ? ? SING C3' H3' ? ? SING O3' HO3' ? ? SING C4' O4' ? ? SING C4' C5' ? ? SING C4' H4' ? ? SING O4' HO4' ? ? SING C5' O5' ? ? SING C5' H5'1 ? ? SING C5' H5'2 ? ? SING O5' P ? ? DOUB P O1P ? ? SING P O2P ? ? SING P O3P ? ? SING O2P HOP2 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Details $CPR Human 9606 Eukaryota Metazoa Homo sapiens 'Human fibroblast CPR lacking the N-terminal 63 a.a. membrane-anchoring region.' 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 _Details $CPR 'recombinant technology' . Escherichia coli 'BL21 Star' pCS22 'Reference: Ellis, J., et. al. Journal of Biological Chemistry, 2009. 284(52): p.36628' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '[2H, 13C, 15N]-labeled CPR' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CPR 0.5 mM '[U-100% 13C; U-100% 15N; U-80% 2H]' 'FLAVIN MONONUCLEOTIDE' 0.5 mM '[U-100% 13C; U-100% 15N; U-80% 2H]' 'FLAVIN-ADENINE DINUCLEOTIDE' 0.5 mM '[U-100% 13C; U-100% 15N; U-80% 2H]' BES 30 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 2.1 loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' collection 'data analysis' processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details 'equipped with CryoProbes' save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details 'equipped with CryoProbes' 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_1H-15N_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N TOCSY' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _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_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HN(COCA)CB_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(COCA)CB' _Sample_label $sample_1 save_ save_3D_C(CO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details '30 mM BES, pH 6.5' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 12 . mM pH 6.5 . pH pressure 1 . atm temperature 273 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details ; Proton chemical shifts were referenced to external 2,2-dimethyl-2-silapentanesulfonic acid. ; 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 '3D 1H-15N TOCSY' '3D HNCA' '3D HN(CO)CA' '3D HNCACB' '3D HNCO' '3D C(CO)NH' '2D 1H-15N HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name CPR _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 64 1 VAL H H 7.98 . . 2 64 1 VAL C C 176.05 . . 3 64 1 VAL CA C 61.67 . . 4 64 1 VAL CB C 31.64 . . 5 64 1 VAL N N 121.63 . . 6 65 2 ARG H H 8.30 . . 7 65 2 ARG C C 176.56 . . 8 65 2 ARG CA C 55.53 . . 9 65 2 ARG CB C 29.63 . . 10 65 2 ARG N N 125.34 . . 11 66 3 GLU H H 8.43 . . 12 66 3 GLU C C 176.44 . . 13 66 3 GLU CA C 56.85 . . 14 66 3 GLU CB C 28.99 . . 15 66 3 GLU N N 122.19 . . 16 67 4 SER H H 7.95 . . 17 67 4 SER C C 174.31 . . 18 67 4 SER CA C 57.99 . . 19 67 4 SER CB C 63.27 . . 20 67 4 SER N N 114.46 . . 21 68 5 SER H H 8.14 . . 22 68 5 SER C C 177.16 . . 23 68 5 SER CA C 56.25 . . 24 68 5 SER CB C 63.35 . . 25 68 5 SER N N 116.38 . . 26 69 6 PHE H H 7.86 . . 27 69 6 PHE C C 176.00 . . 28 69 6 PHE CA C 59.04 . . 29 69 6 PHE CB C 34.73 . . 30 69 6 PHE N N 124.14 . . 31 70 7 VAL H H 6.81 . . 32 70 7 VAL C C 177.77 . . 33 70 7 VAL CA C 65.58 . . 34 70 7 VAL N N 124.12 . . 35 71 8 GLU H H 7.07 . . 36 71 8 GLU C C 179.37 . . 37 71 8 GLU CA C 58.37 . . 38 71 8 GLU N N 119.50 . . 39 72 9 LYS H H 7.46 . . 40 72 9 LYS C C 179.76 . . 41 72 9 LYS CA C 59.45 . . 42 72 9 LYS CB C 31.50 . . 43 72 9 LYS N N 119.37 . . 44 73 10 MET H H 8.16 . . 45 73 10 MET C C 178.56 . . 46 73 10 MET CA C 59.74 . . 47 73 10 MET N N 121.19 . . 48 74 11 LYS H H 8.13 . . 49 74 11 LYS C C 180.05 . . 50 74 11 LYS CA C 59.37 . . 51 74 11 LYS CB C 32.17 . . 52 74 11 LYS N N 118.83 . . 53 75 12 LYS H H 7.91 . . 54 75 12 LYS C C 178.03 . . 55 75 12 LYS CA C 58.44 . . 56 75 12 LYS CB C 32.41 . . 57 75 12 LYS N N 118.11 . . 58 76 13 THR H H 7.33 . . 59 76 13 THR C C 175.33 . . 60 76 13 THR CA C 60.56 . . 61 76 13 THR CB C 66.46 . . 62 76 13 THR N N 104.63 . . 63 77 14 GLY H H 7.45 . . 64 77 14 GLY C C 174.93 . . 65 77 14 GLY CA C 46.66 . . 66 77 14 GLY N N 112.30 . . 67 78 15 ARG H H 8.20 . . 68 78 15 ARG C C 174.44 . . 69 78 15 ARG CA C 54.80 . . 70 78 15 ARG CB C 31.00 . . 71 78 15 ARG N N 119.21 . . 72 79 16 ASN H H 8.43 . . 73 79 16 ASN C C 175.23 . . 74 79 16 ASN CA C 53.02 . . 75 79 16 ASN N N 116.11 . . 76 80 17 ILE H H 7.51 . . 77 80 17 ILE C C 174.08 . . 78 80 17 ILE CA C 58.57 . . 79 80 17 ILE CB C 39.34 . . 80 80 17 ILE N N 119.34 . . 81 81 18 ILE H H 8.20 . . 82 81 18 ILE C C 171.87 . . 83 81 18 ILE CA C 56.78 . . 84 81 18 ILE CB C 39.30 . . 85 81 18 ILE N N 126.34 . . 86 82 19 VAL H H 8.26 . . 87 82 19 VAL C C 175.98 . . 88 82 19 VAL CA C 58.27 . . 89 82 19 VAL CB C 31.33 . . 90 82 19 VAL N N 126.60 . . 91 83 20 PHE H H 8.62 . . 92 83 20 PHE C C 176.07 . . 93 83 20 PHE CA C 56.36 . . 94 83 20 PHE CB C 41.39 . . 95 83 20 PHE N N 124.20 . . 96 84 21 TYR H H 7.26 . . 97 84 21 TYR C C 173.35 . . 98 84 21 TYR CA C 52.00 . . 99 84 21 TYR CB C 39.32 . . 100 84 21 TYR N N 114.88 . . 101 85 22 GLY H H 8.99 . . 102 85 22 GLY C C 172.55 . . 103 85 22 GLY CA C 45.89 . . 104 85 22 GLY N N 111.97 . . 105 86 23 SER H H 7.77 . . 106 86 23 SER C C 174.73 . . 107 86 23 SER CA C 55.88 . . 108 86 23 SER CB C 68.25 . . 109 86 23 SER N N 116.08 . . 110 87 24 GLN H H 10.61 . . 111 87 24 GLN N N 131.45 . . 112 88 25 THR C C 179.51 . . 113 88 25 THR CA C 60.49 . . 114 89 26 GLY H H 7.32 . . 115 89 26 GLY C C 173.64 . . 116 89 26 GLY CA C 44.49 . . 117 89 26 GLY N N 109.86 . . 118 90 27 THR H H 9.45 . . 119 90 27 THR C C 175.63 . . 120 90 27 THR CA C 54.27 . . 121 90 27 THR N N 127.74 . . 122 91 28 ALA H H 10.19 . . 123 91 28 ALA C C 179.50 . . 124 91 28 ALA CA C 54.61 . . 125 91 28 ALA N N 121.71 . . 126 92 29 GLU H H 6.44 . . 127 92 29 GLU C C 177.26 . . 128 92 29 GLU CA C 58.44 . . 129 92 29 GLU CB C 27.92 . . 130 92 29 GLU N N 115.21 . . 131 93 30 GLU H H 7.60 . . 132 93 30 GLU C C 180.70 . . 133 93 30 GLU CA C 58.78 . . 134 93 30 GLU CB C 27.44 . . 135 93 30 GLU N N 121.09 . . 136 94 31 PHE H H 7.77 . . 137 94 31 PHE C C 177.46 . . 138 94 31 PHE CA C 57.01 . . 139 94 31 PHE CB C 40.47 . . 140 94 31 PHE N N 118.96 . . 141 95 32 ALA H H 8.31 . . 142 95 32 ALA C C 179.64 . . 143 95 32 ALA CA C 54.87 . . 144 95 32 ALA CB C 18.69 . . 145 95 32 ALA N N 122.32 . . 146 96 33 ASN H H 8.23 . . 147 96 33 ASN C C 178.51 . . 148 96 33 ASN CA C 55.79 . . 149 96 33 ASN CB C 37.92 . . 150 96 33 ASN N N 117.99 . . 151 97 34 ARG H H 8.45 . . 152 97 34 ARG CA C 57.19 . . 153 97 34 ARG CB C 28.86 . . 154 97 34 ARG N N 121.85 . . 155 98 35 LEU C C 179.06 . . 156 98 35 LEU CA C 57.28 . . 157 99 36 SER H H 8.15 . . 158 99 36 SER C C 177.29 . . 159 99 36 SER CA C 62.08 . . 160 99 36 SER N N 112.08 . . 161 100 37 LYS H H 7.76 . . 162 100 37 LYS C C 179.29 . . 163 100 37 LYS CA C 59.03 . . 164 100 37 LYS CB C 31.59 . . 165 100 37 LYS N N 121.14 . . 166 101 38 ASP H H 8.03 . . 167 101 38 ASP C C 177.21 . . 168 101 38 ASP CA C 55.97 . . 169 101 38 ASP CB C 41.63 . . 170 101 38 ASP N N 120.48 . . 171 102 39 ALA H H 6.92 . . 172 102 39 ALA C C 178.45 . . 173 102 39 ALA CA C 54.84 . . 174 102 39 ALA CB C 17.67 . . 175 102 39 ALA N N 117.76 . . 176 103 40 HIS H H 7.18 . . 177 103 40 HIS C C 178.11 . . 178 103 40 HIS CA C 58.41 . . 179 103 40 HIS CB C 29.40 . . 180 103 40 HIS N N 114.93 . . 181 104 41 ARG H H 7.41 . . 182 104 41 ARG C C 175.57 . . 183 104 41 ARG CA C 57.12 . . 184 104 41 ARG CB C 28.20 . . 185 104 41 ARG N N 119.60 . . 186 105 42 TYR H H 6.86 . . 187 105 42 TYR C C 174.64 . . 188 105 42 TYR CA C 56.14 . . 189 105 42 TYR CB C 37.37 . . 190 105 42 TYR N N 116.72 . . 191 106 43 GLY H H 7.17 . . 192 106 43 GLY C C 174.21 . . 193 106 43 GLY CA C 45.27 . . 194 106 43 GLY N N 104.70 . . 195 107 44 MET H H 7.21 . . 196 107 44 MET C C 173.55 . . 197 107 44 MET CA C 53.97 . . 198 107 44 MET CB C 34.62 . . 199 107 44 MET N N 118.17 . . 200 108 45 ARG H H 7.78 . . 201 108 45 ARG C C 175.11 . . 202 108 45 ARG CA C 55.56 . . 203 108 45 ARG CB C 33.32 . . 204 108 45 ARG N N 117.23 . . 205 109 46 GLY H H 8.83 . . 206 109 46 GLY C C 173.07 . . 207 109 46 GLY CA C 43.58 . . 208 109 46 GLY N N 112.09 . . 209 110 47 MET H H 7.91 . . 210 110 47 MET C C 173.05 . . 211 110 47 MET CA C 54.36 . . 212 110 47 MET CB C 35.63 . . 213 110 47 MET N N 115.37 . . 214 111 48 SER H H 8.55 . . 215 111 48 SER C C 174.45 . . 216 111 48 SER CA C 55.27 . . 217 111 48 SER CB C 64.77 . . 218 111 48 SER N N 117.99 . . 219 112 49 ALA H H 8.62 . . 220 112 49 ALA C C 172.53 . . 221 112 49 ALA CA C 50.71 . . 222 112 49 ALA CB C 22.66 . . 223 112 49 ALA N N 124.61 . . 224 113 50 ASP H H 8.51 . . 225 113 50 ASP C C 176.53 . . 226 113 50 ASP CA C 49.29 . . 227 113 50 ASP CB C 40.85 . . 228 113 50 ASP N N 123.57 . . 229 115 52 GLU C C 177.95 . . 230 115 52 GLU CA C 58.40 . . 231 116 53 GLU H H 7.41 . . 232 116 53 GLU C C 174.92 . . 233 116 53 GLU CA C 55.62 . . 234 116 53 GLU CB C 29.21 . . 235 116 53 GLU N N 114.28 . . 236 117 54 TYR H H 7.59 . . 237 117 54 TYR C C 172.06 . . 238 117 54 TYR CA C 57.02 . . 239 117 54 TYR CB C 42.57 . . 240 117 54 TYR N N 117.93 . . 241 118 55 ASP H H 8.50 . . 242 118 55 ASP C C 177.25 . . 243 118 55 ASP CA C 51.84 . . 244 118 55 ASP CB C 40.63 . . 245 118 55 ASP N N 118.04 . . 246 119 56 LEU H H 8.78 . . 247 119 56 LEU C C 176.75 . . 248 119 56 LEU CA C 55.75 . . 249 119 56 LEU CB C 36.34 . . 250 119 56 LEU N N 130.21 . . 251 120 57 ALA H H 7.57 . . 252 120 57 ALA C C 180.17 . . 253 120 57 ALA CA C 54.37 . . 254 120 57 ALA CB C 16.95 . . 255 120 57 ALA N N 121.77 . . 256 121 58 ASP H H 7.73 . . 257 121 58 ASP C C 177.30 . . 258 121 58 ASP CA C 55.47 . . 259 121 58 ASP CB C 39.29 . . 260 121 58 ASP N N 116.47 . . 261 122 59 LEU H H 8.26 . . 262 122 59 LEU C C 177.98 . . 263 122 59 LEU CA C 57.93 . . 264 122 59 LEU CB C 42.62 . . 265 122 59 LEU N N 122.10 . . 266 123 60 SER H H 7.44 . . 267 123 60 SER C C 174.96 . . 268 123 60 SER CA C 60.53 . . 269 123 60 SER CB C 62.54 . . 270 123 60 SER N N 108.62 . . 271 124 61 SER H H 7.81 . . 272 124 61 SER C C 173.58 . . 273 124 61 SER CA C 58.63 . . 274 124 61 SER CB C 63.27 . . 275 124 61 SER N N 116.62 . . 276 125 62 LEU H H 7.40 . . 277 125 62 LEU C C 174.28 . . 278 125 62 LEU CA C 58.64 . . 279 125 62 LEU CB C 39.50 . . 280 125 62 LEU N N 124.64 . . 281 126 63 PRO C C 176.78 . . 282 126 63 PRO CA C 64.22 . . 283 127 64 GLU H H 7.59 . . 284 127 64 GLU C C 177.01 . . 285 127 64 GLU CA C 57.40 . . 286 127 64 GLU N N 116.49 . . 287 128 65 ILE H H 8.29 . . 288 128 65 ILE C C 175.27 . . 289 128 65 ILE CA C 59.94 . . 290 128 65 ILE CB C 37.36 . . 291 128 65 ILE N N 122.56 . . 292 129 66 ASP H H 8.43 . . 293 129 66 ASP C C 176.55 . . 294 129 66 ASP CA C 55.22 . . 295 129 66 ASP CB C 40.02 . . 296 129 66 ASP N N 128.47 . . 297 130 67 ASN H H 8.80 . . 298 130 67 ASN C C 173.11 . . 299 130 67 ASN CA C 53.17 . . 300 130 67 ASN CB C 34.87 . . 301 130 67 ASN N N 117.33 . . 302 131 68 ALA H H 6.98 . . 303 131 68 ALA C C 179.04 . . 304 131 68 ALA CA C 51.99 . . 305 131 68 ALA CB C 20.11 . . 306 131 68 ALA N N 118.46 . . 307 132 69 LEU H H 8.38 . . 308 132 69 LEU C C 172.95 . . 309 132 69 LEU CA C 54.31 . . 310 132 69 LEU CB C 45.03 . . 311 132 69 LEU N N 122.29 . . 312 133 70 VAL H H 8.55 . . 313 133 70 VAL C C 172.24 . . 314 133 70 VAL CA C 56.81 . . 315 133 70 VAL CB C 33.50 . . 316 133 70 VAL N N 123.16 . . 317 134 71 VAL H H 8.56 . . 318 134 71 VAL C C 173.92 . . 319 134 71 VAL CA C 58.14 . . 320 134 71 VAL CB C 33.84 . . 321 134 71 VAL N N 126.20 . . 322 135 72 PHE H H 8.54 . . 323 135 72 PHE C C 175.11 . . 324 135 72 PHE CA C 55.93 . . 325 135 72 PHE CB C 40.81 . . 326 135 72 PHE N N 122.48 . . 327 136 73 CYS H H 9.01 . . 328 136 73 CYS C C 174.34 . . 329 136 73 CYS CA C 57.09 . . 330 136 73 CYS CB C 27.84 . . 331 136 73 CYS N N 123.20 . . 332 137 74 MET H H 8.20 . . 333 137 74 MET C C 174.98 . . 334 137 74 MET CA C 52.22 . . 335 137 74 MET CB C 34.10 . . 336 137 74 MET N N 118.58 . . 337 138 75 ALA H H 9.23 . . 338 138 75 ALA CA C 51.17 . . 339 138 75 ALA CB C 20.33 . . 340 138 75 ALA N N 132.62 . . 341 139 76 THR C C 175.66 . . 342 139 76 THR CA C 62.53 . . 343 140 77 TYR H H 8.61 . . 344 140 77 TYR C C 173.59 . . 345 140 77 TYR CA C 56.39 . . 346 140 77 TYR CB C 30.57 . . 347 140 77 TYR N N 132.83 . . 348 142 79 GLU C C 177.19 . . 349 142 79 GLU CA C 54.86 . . 350 143 80 GLY H H 7.48 . . 351 143 80 GLY C C 173.50 . . 352 143 80 GLY CA C 44.43 . . 353 143 80 GLY N N 107.03 . . 354 144 81 ASP H H 7.71 . . 355 144 81 ASP CA C 53.30 . . 356 144 81 ASP N N 121.79 . . 357 146 83 THR H H 7.38 . . 358 146 83 THR C C 175.62 . . 359 146 83 THR CA C 61.19 . . 360 146 83 THR CB C 68.88 . . 361 146 83 THR N N 108.25 . . 362 147 84 ASP H H 8.58 . . 363 147 84 ASP C C 179.62 . . 364 147 84 ASP CA C 57.48 . . 365 147 84 ASP CB C 38.99 . . 366 147 84 ASP N N 123.42 . . 367 148 85 ASN H H 9.11 . . 368 148 85 ASN C C 173.99 . . 369 148 85 ASN CA C 54.14 . . 370 148 85 ASN CB C 36.88 . . 371 148 85 ASN N N 117.35 . . 372 149 86 ALA H H 7.56 . . 373 149 86 ALA C C 176.20 . . 374 149 86 ALA CA C 49.73 . . 375 149 86 ALA N N 120.71 . . 376 150 87 GLN H H 7.36 . . 377 150 87 GLN C C 177.11 . . 378 150 87 GLN CA C 59.16 . . 379 150 87 GLN CB C 28.40 . . 380 150 87 GLN N N 122.96 . . 381 151 88 ASP H H 8.76 . . 382 151 88 ASP C C 179.79 . . 383 151 88 ASP CA C 57.42 . . 384 151 88 ASP CB C 38.86 . . 385 151 88 ASP N N 119.57 . . 386 152 89 PHE H H 8.19 . . 387 152 89 PHE C C 175.86 . . 388 152 89 PHE CA C 57.81 . . 389 152 89 PHE N N 122.50 . . 390 153 90 TYR H H 8.43 . . 391 153 90 TYR C C 177.00 . . 392 153 90 TYR CA C 60.70 . . 393 153 90 TYR N N 121.00 . . 394 154 91 ASP H H 8.64 . . 395 154 91 ASP C C 178.93 . . 396 154 91 ASP CA C 57.27 . . 397 154 91 ASP CB C 39.37 . . 398 154 91 ASP N N 119.55 . . 399 155 92 TRP H H 8.18 . . 400 155 92 TRP C C 177.51 . . 401 155 92 TRP CA C 61.44 . . 402 155 92 TRP CB C 26.92 . . 403 155 92 TRP N N 122.61 . . 404 156 93 LEU H H 8.56 . . 405 156 93 LEU C C 179.03 . . 406 156 93 LEU CA C 56.19 . . 407 156 93 LEU CB C 41.59 . . 408 156 93 LEU N N 119.19 . . 409 157 94 GLN H H 7.38 . . 410 157 94 GLN C C 177.43 . . 411 157 94 GLN CA C 57.78 . . 412 157 94 GLN CB C 29.29 . . 413 157 94 GLN N N 115.44 . . 414 158 95 GLU H H 7.01 . . 415 158 95 GLU C C 176.79 . . 416 158 95 GLU CA C 55.69 . . 417 158 95 GLU CB C 30.72 . . 418 158 95 GLU N N 116.15 . . 419 159 96 THR H H 7.41 . . 420 159 96 THR C C 171.33 . . 421 159 96 THR CA C 62.68 . . 422 159 96 THR CB C 67.37 . . 423 159 96 THR N N 116.31 . . 424 160 97 ASP H H 7.39 . . 425 160 97 ASP C C 176.51 . . 426 160 97 ASP CA C 52.03 . . 427 160 97 ASP CB C 40.76 . . 428 160 97 ASP N N 122.92 . . 429 161 98 VAL H H 7.73 . . 430 161 98 VAL C C 173.15 . . 431 161 98 VAL CA C 62.29 . . 432 161 98 VAL CB C 31.53 . . 433 161 98 VAL N N 120.81 . . 434 162 99 ASP H H 7.80 . . 435 162 99 ASP C C 177.42 . . 436 162 99 ASP CA C 52.81 . . 437 162 99 ASP CB C 40.67 . . 438 162 99 ASP N N 120.89 . . 439 163 100 LEU H H 8.61 . . 440 163 100 LEU C C 175.40 . . 441 163 100 LEU CA C 52.61 . . 442 163 100 LEU CB C 40.10 . . 443 163 100 LEU N N 126.13 . . 444 164 101 SER H H 8.27 . . 445 164 101 SER C C 175.82 . . 446 164 101 SER CA C 61.12 . . 447 164 101 SER CB C 62.15 . . 448 164 101 SER N N 116.57 . . 449 165 102 GLY H H 8.98 . . 450 165 102 GLY C C 174.67 . . 451 165 102 GLY CA C 44.45 . . 452 165 102 GLY N N 113.43 . . 453 166 103 VAL H H 8.21 . . 454 166 103 VAL C C 174.19 . . 455 166 103 VAL CA C 62.89 . . 456 166 103 VAL CB C 30.29 . . 457 166 103 VAL N N 123.78 . . 458 167 104 LYS H H 9.21 . . 459 167 104 LYS C C 175.31 . . 460 167 104 LYS CA C 54.21 . . 461 167 104 LYS CB C 33.26 . . 462 167 104 LYS N N 131.19 . . 463 168 105 PHE H H 8.52 . . 464 168 105 PHE C C 173.57 . . 465 168 105 PHE CA C 55.16 . . 466 168 105 PHE CB C 45.90 . . 467 168 105 PHE N N 118.75 . . 468 169 106 ALA H H 8.29 . . 469 169 106 ALA C C 176.06 . . 470 169 106 ALA CA C 51.78 . . 471 169 106 ALA CB C 23.85 . . 472 169 106 ALA N N 118.87 . . 473 170 107 VAL H H 9.68 . . 474 170 107 VAL C C 172.75 . . 475 170 107 VAL CA C 60.65 . . 476 170 107 VAL CB C 34.65 . . 477 170 107 VAL N N 121.76 . . 478 171 108 PHE H H 8.96 . . 479 171 108 PHE C C 173.82 . . 480 171 108 PHE CA C 57.45 . . 481 171 108 PHE CB C 40.02 . . 482 171 108 PHE N N 126.11 . . 483 172 109 GLY H H 8.55 . . 484 172 109 GLY C C 170.52 . . 485 172 109 GLY CA C 43.92 . . 486 172 109 GLY N N 117.18 . . 487 173 110 LEU H H 7.67 . . 488 173 110 LEU C C 173.78 . . 489 173 110 LEU CA C 56.15 . . 490 173 110 LEU N N 125.05 . . 491 174 111 GLY H H 6.97 . . 492 174 111 GLY C C 174.11 . . 493 174 111 GLY CA C 45.20 . . 494 174 111 GLY N N 107.71 . . 495 175 112 ASN H H 8.99 . . 496 175 112 ASN C C 175.73 . . 497 175 112 ASN CA C 53.23 . . 498 175 112 ASN CB C 39.12 . . 499 175 112 ASN N N 119.98 . . 500 176 113 LYS H H 8.79 . . 501 176 113 LYS C C 176.79 . . 502 176 113 LYS CA C 58.17 . . 503 176 113 LYS CB C 31.03 . . 504 176 113 LYS N N 127.60 . . 505 177 114 THR H H 8.72 . . 506 177 114 THR C C 174.62 . . 507 177 114 THR CA C 63.33 . . 508 177 114 THR N N 113.12 . . 509 178 115 TYR H H 7.32 . . 510 178 115 TYR C C 175.53 . . 511 178 115 TYR CA C 57.65 . . 512 178 115 TYR CB C 37.14 . . 513 178 115 TYR N N 120.72 . . 514 181 118 PHE C C 176.32 . . 515 181 118 PHE CA C 55.72 . . 516 182 119 ASN H H 9.70 . . 517 182 119 ASN C C 179.39 . . 518 182 119 ASN CA C 54.63 . . 519 182 119 ASN CB C 38.81 . . 520 182 119 ASN N N 127.77 . . 521 185 122 GLY H H 8.27 . . 522 185 122 GLY C C 174.07 . . 523 185 122 GLY CA C 46.38 . . 524 185 122 GLY N N 107.76 . . 525 186 123 LYS H H 7.77 . . 526 186 123 LYS C C 178.76 . . 527 186 123 LYS CA C 59.28 . . 528 186 123 LYS CB C 32.08 . . 529 186 123 LYS N N 116.98 . . 530 187 124 TYR H H 8.02 . . 531 187 124 TYR C C 176.58 . . 532 187 124 TYR CA C 61.68 . . 533 187 124 TYR CB C 37.36 . . 534 187 124 TYR N N 120.60 . . 535 188 125 VAL H H 8.38 . . 536 188 125 VAL C C 176.18 . . 537 188 125 VAL CA C 66.61 . . 538 188 125 VAL CB C 30.98 . . 539 188 125 VAL N N 118.63 . . 540 189 126 ASP H H 7.56 . . 541 189 126 ASP C C 176.42 . . 542 189 126 ASP CA C 57.39 . . 543 189 126 ASP CB C 44.18 . . 544 189 126 ASP N N 115.75 . . 545 190 127 LYS H H 7.33 . . 546 190 127 LYS C C 179.53 . . 547 190 127 LYS CA C 57.59 . . 548 190 127 LYS CB C 31.22 . . 549 190 127 LYS N N 116.33 . . 550 191 128 ARG H H 8.70 . . 551 191 128 ARG C C 178.19 . . 552 191 128 ARG CA C 56.16 . . 553 191 128 ARG CB C 28.21 . . 554 191 128 ARG N N 120.97 . . 555 192 129 LEU H H 7.78 . . 556 192 129 LEU C C 178.45 . . 557 192 129 LEU CA C 57.61 . . 558 192 129 LEU CB C 37.85 . . 559 192 129 LEU N N 116.83 . . 560 193 130 GLU H H 6.35 . . 561 193 130 GLU C C 180.61 . . 562 193 130 GLU CA C 58.04 . . 563 193 130 GLU CB C 28.93 . . 564 193 130 GLU N N 117.56 . . 565 194 131 GLN H H 8.00 . . 566 194 131 GLN C C 178.43 . . 567 194 131 GLN CA C 58.53 . . 568 194 131 GLN CB C 27.52 . . 569 194 131 GLN N N 122.54 . . 570 195 132 LEU H H 7.54 . . 571 195 132 LEU C C 176.15 . . 572 195 132 LEU CA C 54.74 . . 573 195 132 LEU N N 117.90 . . 574 196 133 GLY H H 7.67 . . 575 196 133 GLY C C 174.09 . . 576 196 133 GLY CA C 44.08 . . 577 196 133 GLY N N 106.83 . . 578 197 134 ALA H H 7.79 . . 579 197 134 ALA C C 175.92 . . 580 197 134 ALA CA C 51.62 . . 581 197 134 ALA CB C 19.24 . . 582 197 134 ALA N N 123.29 . . 583 198 135 GLN H H 9.27 . . 584 198 135 GLN C C 173.32 . . 585 198 135 GLN CA C 53.89 . . 586 198 135 GLN CB C 29.84 . . 587 198 135 GLN N N 121.47 . . 588 199 136 ARG H H 8.56 . . 589 199 136 ARG C C 177.98 . . 590 199 136 ARG CA C 55.04 . . 591 199 136 ARG N N 130.88 . . 592 200 137 ILE H H 8.88 . . 593 200 137 ILE CA C 59.26 . . 594 200 137 ILE N N 125.01 . . 595 201 138 PHE C C 171.57 . . 596 201 138 PHE CA C 57.40 . . 597 202 139 GLU H H 5.76 . . 598 202 139 GLU C C 172.96 . . 599 202 139 GLU CA C 55.44 . . 600 202 139 GLU CB C 29.54 . . 601 202 139 GLU N N 123.88 . . 602 203 140 LEU H H 7.97 . . 603 203 140 LEU C C 177.89 . . 604 203 140 LEU CA C 54.83 . . 605 203 140 LEU CB C 40.99 . . 606 203 140 LEU N N 123.96 . . 607 204 141 GLY H H 8.79 . . 608 204 141 GLY C C 171.45 . . 609 204 141 GLY CA C 44.65 . . 610 204 141 GLY N N 117.26 . . 611 205 142 LEU H H 8.53 . . 612 205 142 LEU C C 175.53 . . 613 205 142 LEU CA C 51.10 . . 614 205 142 LEU CB C 40.99 . . 615 205 142 LEU N N 127.01 . . 616 206 143 GLY H H 8.44 . . 617 206 143 GLY C C 173.60 . . 618 206 143 GLY CA C 45.77 . . 619 206 143 GLY N N 112.67 . . 620 207 144 ASP H H 9.56 . . 621 207 144 ASP C C 176.86 . . 622 207 144 ASP CA C 51.95 . . 623 207 144 ASP CB C 42.56 . . 624 207 144 ASP N N 125.31 . . 625 208 145 ASP H H 10.16 . . 626 208 145 ASP C C 176.22 . . 627 208 145 ASP CA C 54.26 . . 628 208 145 ASP CB C 41.13 . . 629 208 145 ASP N N 125.56 . . 630 209 146 ASP H H 8.34 . . 631 209 146 ASP C C 176.19 . . 632 209 146 ASP CA C 55.28 . . 633 209 146 ASP N N 117.55 . . 634 210 147 GLY H H 7.16 . . 635 210 147 GLY C C 173.67 . . 636 210 147 GLY CA C 44.66 . . 637 210 147 GLY N N 107.68 . . 638 211 148 ASN H H 9.48 . . 639 211 148 ASN C C 179.93 . . 640 211 148 ASN CA C 54.62 . . 641 211 148 ASN CB C 40.06 . . 642 211 148 ASN N N 127.86 . . 643 212 149 LEU H H 8.20 . . 644 212 149 LEU CA C 61.25 . . 645 212 149 LEU N N 122.74 . . 646 218 155 THR C C 175.65 . . 647 218 155 THR CA C 66.97 . . 648 219 156 TRP H H 7.61 . . 649 219 156 TRP C C 177.66 . . 650 219 156 TRP CA C 62.15 . . 651 219 156 TRP CB C 28.91 . . 652 219 156 TRP N N 124.57 . . 653 221 158 GLU C C 177.48 . . 654 221 158 GLU CA C 57.27 . . 655 222 159 GLN H H 6.80 . . 656 222 159 GLN C C 176.22 . . 657 222 159 GLN CA C 55.76 . . 658 222 159 GLN CB C 30.08 . . 659 222 159 GLN N N 115.13 . . 660 223 160 PHE H H 8.01 . . 661 223 160 PHE C C 175.80 . . 662 223 160 PHE CA C 58.55 . . 663 223 160 PHE CB C 37.69 . . 664 223 160 PHE N N 125.44 . . 665 224 161 TRP H H 6.60 . . 666 224 161 TRP C C 177.24 . . 667 224 161 TRP CA C 60.75 . . 668 224 161 TRP CB C 25.76 . . 669 224 161 TRP N N 116.26 . . 670 225 162 PRO C C 178.73 . . 671 225 162 PRO CA C 65.90 . . 672 226 163 ALA H H 6.59 . . 673 226 163 ALA C C 180.94 . . 674 226 163 ALA CA C 54.71 . . 675 226 163 ALA CB C 17.15 . . 676 226 163 ALA N N 120.87 . . 677 227 164 VAL H H 7.64 . . 678 227 164 VAL C C 178.29 . . 679 227 164 VAL CA C 66.34 . . 680 227 164 VAL CB C 30.51 . . 681 227 164 VAL N N 122.74 . . 682 228 165 CYS H H 8.31 . . 683 228 165 CYS C C 177.51 . . 684 228 165 CYS CA C 63.61 . . 685 228 165 CYS CB C 26.06 . . 686 228 165 CYS N N 117.89 . . 687 229 166 GLU H H 7.94 . . 688 229 166 GLU C C 178.63 . . 689 229 166 GLU CA C 58.30 . . 690 229 166 GLU CB C 28.34 . . 691 229 166 GLU N N 119.04 . . 692 230 167 HIS H H 7.85 . . 693 230 167 HIS C C 177.17 . . 694 230 167 HIS CA C 59.75 . . 695 230 167 HIS N N 118.22 . . 696 231 168 PHE H H 8.10 . . 697 231 168 PHE C C 175.74 . . 698 231 168 PHE CA C 57.97 . . 699 231 168 PHE CB C 39.02 . . 700 231 168 PHE N N 112.51 . . 701 232 169 GLY H H 7.81 . . 702 232 169 GLY C C 175.07 . . 703 232 169 GLY CA C 46.65 . . 704 232 169 GLY N N 111.37 . . 705 233 170 VAL H H 7.62 . . 706 233 170 VAL C C 174.49 . . 707 233 170 VAL CA C 59.41 . . 708 233 170 VAL CB C 33.22 . . 709 233 170 VAL N N 113.52 . . 710 234 171 GLU H H 7.91 . . 711 234 171 GLU C C 175.11 . . 712 234 171 GLU CA C 54.40 . . 713 234 171 GLU CB C 31.71 . . 714 234 171 GLU N N 119.15 . . 715 235 172 ALA H H 8.40 . . 716 235 172 ALA C C 178.41 . . 717 235 172 ALA CA C 51.48 . . 718 235 172 ALA CB C 17.89 . . 719 235 172 ALA N N 123.90 . . 720 236 173 THR H H 8.10 . . 721 236 173 THR C C 175.56 . . 722 236 173 THR CA C 61.26 . . 723 236 173 THR CB C 69.23 . . 724 236 173 THR N N 114.26 . . 725 237 174 GLY H H 8.11 . . 726 237 174 GLY C C 173.66 . . 727 237 174 GLY CA C 44.53 . . 728 237 174 GLY N N 110.52 . . 729 238 175 GLU H H 7.90 . . 730 238 175 GLU C C 176.17 . . 731 238 175 GLU CA C 55.37 . . 732 238 175 GLU CB C 29.86 . . 733 238 175 GLU N N 120.77 . . 734 239 176 GLU H H 8.47 . . 735 239 176 GLU C C 175.91 . . 736 239 176 GLU CA C 55.83 . . 737 239 176 GLU CB C 29.20 . . 738 239 176 GLU N N 123.47 . . 739 240 177 SER H H 8.14 . . 740 240 177 SER C C 173.82 . . 741 240 177 SER CA C 57.34 . . 742 240 177 SER CB C 63.74 . . 743 240 177 SER N N 118.20 . . 744 241 178 SER H H 8.41 . . 745 241 178 SER C C 174.17 . . 746 241 178 SER CA C 57.52 . . 747 241 178 SER CB C 62.61 . . 748 241 178 SER N N 118.61 . . 749 242 179 ILE H H 8.41 . . 750 242 179 ILE C C 176.11 . . 751 242 179 ILE CA C 59.88 . . 752 242 179 ILE CB C 39.17 . . 753 242 179 ILE N N 125.24 . . 754 243 180 ARG H H 8.15 . . 755 243 180 ARG CA C 54.37 . . 756 243 180 ARG CB C 29.64 . . 757 243 180 ARG N N 124.79 . . 758 244 181 GLN C C 173.90 . . 759 244 181 GLN CA C 54.76 . . 760 245 182 TYR H H 7.68 . . 761 245 182 TYR C C 173.78 . . 762 245 182 TYR CA C 55.31 . . 763 245 182 TYR CB C 41.88 . . 764 245 182 TYR N N 115.20 . . 765 246 183 GLU H H 8.78 . . 766 246 183 GLU C C 174.74 . . 767 246 183 GLU CA C 53.06 . . 768 246 183 GLU CB C 31.85 . . 769 246 183 GLU N N 118.38 . . 770 247 184 LEU H H 8.40 . . 771 247 184 LEU C C 176.45 . . 772 247 184 LEU CA C 54.52 . . 773 247 184 LEU CB C 42.71 . . 774 247 184 LEU N N 126.42 . . 775 248 185 VAL H H 8.98 . . 776 248 185 VAL C C 173.87 . . 777 248 185 VAL CA C 61.28 . . 778 248 185 VAL CB C 33.47 . . 779 248 185 VAL N N 129.34 . . 780 249 186 VAL H H 8.22 . . 781 249 186 VAL C C 175.98 . . 782 249 186 VAL CA C 61.90 . . 783 249 186 VAL CB C 31.52 . . 784 249 186 VAL N N 125.54 . . 785 250 187 HIS H H 8.43 . . 786 250 187 HIS CA C 54.14 . . 787 250 187 HIS CB C 29.02 . . 788 250 187 HIS N N 128.07 . . 789 252 189 ASP C C 174.67 . . 790 252 189 ASP CA C 53.52 . . 791 252 189 ASP CB C 40.00 . . 792 253 190 ILE H H 7.61 . . 793 253 190 ILE C C 173.62 . . 794 253 190 ILE CA C 59.63 . . 795 253 190 ILE CB C 39.12 . . 796 253 190 ILE N N 120.93 . . 797 254 191 ASP H H 7.91 . . 798 254 191 ASP C C 176.78 . . 799 254 191 ASP CA C 53.62 . . 800 254 191 ASP CB C 41.44 . . 801 254 191 ASP N N 127.39 . . 802 255 192 ALA H H 8.51 . . 803 255 192 ALA C C 179.32 . . 804 255 192 ALA CA C 54.34 . . 805 255 192 ALA CB C 17.60 . . 806 255 192 ALA N N 128.48 . . 807 256 193 ALA H H 8.39 . . 808 256 193 ALA C C 178.11 . . 809 256 193 ALA CA C 53.35 . . 810 256 193 ALA N N 119.29 . . 811 257 194 LYS H H 7.74 . . 812 257 194 LYS C C 174.27 . . 813 257 194 LYS CA C 55.07 . . 814 257 194 LYS CB C 31.87 . . 815 257 194 LYS N N 115.67 . . 816 258 195 VAL H H 6.70 . . 817 258 195 VAL C C 176.13 . . 818 258 195 VAL CA C 61.49 . . 819 258 195 VAL CB C 33.14 . . 820 258 195 VAL N N 117.85 . . 821 336 273 LYS C C 177.86 . . 822 336 273 LYS CA C 58.19 . . 823 337 274 ILE H H 8.29 . . 824 337 274 ILE C C 176.07 . . 825 337 274 ILE CA C 59.70 . . 826 337 274 ILE CB C 38.44 . . 827 337 274 ILE N N 118.15 . . 828 338 275 LEU H H 8.12 . . 829 338 275 LEU C C 177.69 . . 830 338 275 LEU CA C 54.26 . . 831 338 275 LEU N N 124.55 . . 832 339 276 GLY H H 7.69 . . 833 339 276 GLY C C 174.11 . . 834 339 276 GLY CA C 45.78 . . 835 339 276 GLY N N 110.00 . . 836 340 277 ALA H H 7.67 . . 837 340 277 ALA C C 175.56 . . 838 340 277 ALA CA C 50.19 . . 839 340 277 ALA CB C 21.10 . . 840 340 277 ALA N N 120.65 . . 841 341 278 ASP H H 7.96 . . 842 341 278 ASP C C 177.30 . . 843 341 278 ASP CA C 52.44 . . 844 341 278 ASP CB C 39.66 . . 845 341 278 ASP N N 120.88 . . 846 342 279 LEU H H 8.54 . . 847 342 279 LEU C C 176.94 . . 848 342 279 LEU CA C 55.29 . . 849 342 279 LEU CB C 41.21 . . 850 342 279 LEU N N 122.95 . . 851 343 280 ASP H H 8.39 . . 852 343 280 ASP C C 175.83 . . 853 343 280 ASP CA C 54.92 . . 854 343 280 ASP CB C 40.35 . . 855 343 280 ASP N N 116.46 . . 856 344 281 VAL H H 6.83 . . 857 344 281 VAL C C 173.19 . . 858 344 281 VAL CA C 63.97 . . 859 344 281 VAL CB C 32.25 . . 860 344 281 VAL N N 123.98 . . 861 345 282 VAL H H 8.14 . . 862 345 282 VAL CA C 61.94 . . 863 345 282 VAL CB C 30.81 . . 864 345 282 VAL N N 126.62 . . 865 621 558 GLU C C 178.27 . . 866 621 558 GLU CA C 57.14 . . 867 622 559 GLY H H 8.01 . . 868 622 559 GLY C C 179.10 . . 869 622 559 GLY CA C 47.59 . . 870 622 559 GLY N N 103.33 . . 871 623 560 GLY H H 8.96 . . 872 623 560 GLY CA C 47.60 . . 873 623 560 GLY N N 108.69 . . 874 651 588 GLY C C 172.73 . . 875 651 588 GLY CA C 44.85 . . 876 652 589 ALA H H 6.75 . . 877 652 589 ALA C C 175.05 . . 878 652 589 ALA CA C 51.73 . . 879 652 589 ALA CB C 15.34 . . 880 652 589 ALA N N 122.02 . . 881 653 590 MET H H 8.36 . . 882 653 590 MET C C 174.85 . . 883 653 590 MET CA C 53.36 . . 884 653 590 MET CB C 36.24 . . 885 653 590 MET N N 116.78 . . stop_ save_