HEADER MEMBRANE PROTEIN 15-FEB-23 8IED TITLE CRYO-EM STRUCTURE OF GPR156-MINIGO-SCFV16 COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROBABLE G-PROTEIN COUPLED RECEPTOR 156; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(O) SUBUNIT ALPHA; COMPND 7 CHAIN: C; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 11 BETA-1; COMPND 12 CHAIN: D; COMPND 13 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 4; COMPND 16 MOLECULE: SINGLE-CHAIN VARIABLE FRAGMENT SCFV16; COMPND 17 CHAIN: N; COMPND 18 ENGINEERED: YES; COMPND 19 MOL_ID: 5; COMPND 20 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 21 GAMMA-2; COMPND 22 CHAIN: Y; COMPND 23 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: GPR156; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 GENE: GNAO1; SOURCE 14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 16 MOL_ID: 3; SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 18 ORGANISM_COMMON: HUMAN; SOURCE 19 ORGANISM_TAXID: 9606; SOURCE 20 GENE: GNB1; SOURCE 21 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 23 MOL_ID: 4; SOURCE 24 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 25 ORGANISM_TAXID: 10090; SOURCE 26 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 27 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 28 MOL_ID: 5; SOURCE 29 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 30 ORGANISM_COMMON: HUMAN; SOURCE 31 ORGANISM_TAXID: 9606; SOURCE 32 GENE: GNG2; SOURCE 33 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 34 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS MEMBRANE PROTEIN, G-PROTEIN COUPLED RECEPTOR, SIGNAL TRANSDUCTION, KEYWDS 2 PHOSPHOLIPID EXPDTA ELECTRON MICROSCOPY AUTHOR J.SHIN,J.PARK,Y.CHO REVDAT 1 14-FEB-24 8IED 0 JRNL AUTH J.SHIN,J.PARK,J.JEONG,J.H.LAM,X.QIU,D.WU,K.KIM,J.LEE, JRNL AUTH 2 C.V.ROBINSON,J.HYUN,V.KATRITCH,K.KIM,Y.CHO JRNL TITL CRYO-EM STRUCTURE OF GPR156-MINIGO-SCFV16 COMPLEX JRNL REF NAT.STRUCT.MOL.BIOL. 2024 JRNL REFN ESSN 1545-9985 JRNL DOI 10.1038/S41594-024-01224-7 REMARK 2 REMARK 2 RESOLUTION. 3.33 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.330 REMARK 3 NUMBER OF PARTICLES : 205728 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE REMARK 3 CORRECTION REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 8IED COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-FEB-23. REMARK 100 THE DEPOSITION ID IS D_1300035509. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : GPR156-MINIGO-SCFV16 COMPLEX; REMARK 245 GPR156; MINIGO HETEROTRIMERIC REMARK 245 COMPLEX; SCFV16 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.50 REMARK 245 SAMPLE DETAILS : SINGLE-CHAIN VARIABLE FRAGMENT REMARK 245 SCFV16 REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : FEI FALCON IV (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : OTHER REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 6400.00 REMARK 245 ILLUMINATION MODE : OTHER REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : OTHER REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, N, Y REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 1 REMARK 465 GLU A 2 REMARK 465 PRO A 3 REMARK 465 GLU A 4 REMARK 465 ILE A 5 REMARK 465 ASN A 6 REMARK 465 CYS A 7 REMARK 465 SER A 8 REMARK 465 GLU A 9 REMARK 465 LEU A 10 REMARK 465 CYS A 11 REMARK 465 ASP A 12 REMARK 465 SER A 13 REMARK 465 PHE A 14 REMARK 465 PRO A 15 REMARK 465 GLY A 16 REMARK 465 GLN A 17 REMARK 465 GLU A 18 REMARK 465 LEU A 19 REMARK 465 ASP A 20 REMARK 465 ARG A 21 REMARK 465 ARG A 22 REMARK 465 PRO A 23 REMARK 465 LEU A 24 REMARK 465 HIS A 25 REMARK 465 ASP A 26 REMARK 465 LEU A 27 REMARK 465 CYS A 28 REMARK 465 LYS A 29 REMARK 465 THR A 30 REMARK 465 THR A 31 REMARK 465 ILE A 32 REMARK 465 THR A 33 REMARK 465 SER A 34 REMARK 465 SER A 35 REMARK 465 HIS A 36 REMARK 465 HIS A 37 REMARK 465 SER A 38 REMARK 465 SER A 39 REMARK 465 LYS A 40 REMARK 465 THR A 41 REMARK 465 ILE A 42 REMARK 465 SER A 43 REMARK 465 LEU A 111 REMARK 465 VAL A 112 REMARK 465 GLY A 113 REMARK 465 LYS A 156 REMARK 465 ARG A 157 REMARK 465 VAL A 158 REMARK 465 GLU A 319 REMARK 465 GLU A 320 REMARK 465 GLU A 321 REMARK 465 ASN A 322 REMARK 465 GLN A 323 REMARK 465 THR A 324 REMARK 465 ILE A 325 REMARK 465 ARG A 326 REMARK 465 ARG A 327 REMARK 465 MET A 328 REMARK 465 ALA A 329 REMARK 465 LYS A 330 REMARK 465 TYR A 331 REMARK 465 PHE A 332 REMARK 465 SER A 333 REMARK 465 THR A 334 REMARK 465 PRO A 335 REMARK 465 ASN A 336 REMARK 465 LYS A 337 REMARK 465 SER A 338 REMARK 465 PHE A 339 REMARK 465 HIS A 340 REMARK 465 THR A 341 REMARK 465 GLN A 342 REMARK 465 TYR A 343 REMARK 465 GLY A 344 REMARK 465 GLU A 345 REMARK 465 GLU A 346 REMARK 465 GLU A 347 REMARK 465 ASN A 348 REMARK 465 CYS A 349 REMARK 465 HIS A 350 REMARK 465 PRO A 351 REMARK 465 ARG A 352 REMARK 465 GLY A 353 REMARK 465 GLU A 354 REMARK 465 LYS A 355 REMARK 465 SER A 356 REMARK 465 SER A 357 REMARK 465 MET A 358 REMARK 465 GLU A 359 REMARK 465 ARG A 360 REMARK 465 LEU A 361 REMARK 465 LEU A 362 REMARK 465 THR A 363 REMARK 465 GLU A 364 REMARK 465 LYS A 365 REMARK 465 ASN A 366 REMARK 465 ALA A 367 REMARK 465 VAL A 368 REMARK 465 ILE A 369 REMARK 465 GLU A 370 REMARK 465 SER A 371 REMARK 465 LEU A 372 REMARK 465 GLN A 373 REMARK 465 GLU A 374 REMARK 465 GLN A 375 REMARK 465 VAL A 376 REMARK 465 ASN A 377 REMARK 465 ASN A 378 REMARK 465 ALA A 379 REMARK 465 LYS A 380 REMARK 465 GLU A 381 REMARK 465 LYS A 382 REMARK 465 ILE A 383 REMARK 465 VAL A 384 REMARK 465 ARG A 385 REMARK 465 LEU A 386 REMARK 465 MET A 387 REMARK 465 SER A 388 REMARK 465 ALA A 389 REMARK 465 GLU A 390 REMARK 465 CYS A 391 REMARK 465 THR A 392 REMARK 465 TYR A 393 REMARK 465 ASP A 394 REMARK 465 LEU A 395 REMARK 465 PRO A 396 REMARK 465 GLU A 397 REMARK 465 GLY A 398 REMARK 465 ALA A 399 REMARK 465 ALA A 400 REMARK 465 PRO A 401 REMARK 465 PRO A 402 REMARK 465 ALA A 403 REMARK 465 SER A 404 REMARK 465 SER A 405 REMARK 465 PRO A 406 REMARK 465 ASN A 407 REMARK 465 LYS A 408 REMARK 465 ASP A 409 REMARK 465 VAL A 410 REMARK 465 GLN A 411 REMARK 465 ALA A 412 REMARK 465 VAL A 413 REMARK 465 ALA A 414 REMARK 465 SER A 415 REMARK 465 VAL A 416 REMARK 465 HIS A 417 REMARK 465 THR A 418 REMARK 465 LEU A 419 REMARK 465 ALA A 420 REMARK 465 ALA A 421 REMARK 465 ALA A 422 REMARK 465 GLN A 423 REMARK 465 GLY A 424 REMARK 465 PRO A 425 REMARK 465 SER A 426 REMARK 465 GLY A 427 REMARK 465 HIS A 428 REMARK 465 LEU A 429 REMARK 465 SER A 430 REMARK 465 ASP A 431 REMARK 465 PHE A 432 REMARK 465 GLN A 433 REMARK 465 ASN A 434 REMARK 465 ASP A 435 REMARK 465 PRO A 436 REMARK 465 GLY A 437 REMARK 465 MET A 438 REMARK 465 ALA A 439 REMARK 465 ALA A 440 REMARK 465 ARG A 441 REMARK 465 ASP A 442 REMARK 465 SER A 443 REMARK 465 GLN A 444 REMARK 465 CYS A 445 REMARK 465 THR A 446 REMARK 465 SER A 447 REMARK 465 GLY A 448 REMARK 465 PRO A 449 REMARK 465 SER A 450 REMARK 465 SER A 451 REMARK 465 TYR A 452 REMARK 465 ALA A 453 REMARK 465 GLN A 454 REMARK 465 SER A 455 REMARK 465 LEU A 456 REMARK 465 GLU A 457 REMARK 465 GLY A 458 REMARK 465 PRO A 459 REMARK 465 GLY A 460 REMARK 465 LYS A 461 REMARK 465 ASP A 462 REMARK 465 SER A 463 REMARK 465 SER A 464 REMARK 465 PHE A 465 REMARK 465 SER A 466 REMARK 465 PRO A 467 REMARK 465 GLY A 468 REMARK 465 LYS A 469 REMARK 465 GLU A 470 REMARK 465 GLU A 471 REMARK 465 LYS A 472 REMARK 465 ILE A 473 REMARK 465 SER A 474 REMARK 465 ASP A 475 REMARK 465 SER A 476 REMARK 465 LYS A 477 REMARK 465 ASP A 478 REMARK 465 PHE A 479 REMARK 465 SER A 480 REMARK 465 ASP A 481 REMARK 465 HIS A 482 REMARK 465 LEU A 483 REMARK 465 ASP A 484 REMARK 465 SER A 485 REMARK 465 GLY A 486 REMARK 465 CYS A 487 REMARK 465 SER A 488 REMARK 465 GLN A 489 REMARK 465 LYS A 490 REMARK 465 PRO A 491 REMARK 465 TRP A 492 REMARK 465 THR A 493 REMARK 465 GLU A 494 REMARK 465 GLN A 495 REMARK 465 SER A 496 REMARK 465 LEU A 497 REMARK 465 GLY A 498 REMARK 465 PRO A 499 REMARK 465 GLU A 500 REMARK 465 ARG A 501 REMARK 465 GLY A 502 REMARK 465 ASP A 503 REMARK 465 GLN A 504 REMARK 465 VAL A 505 REMARK 465 PRO A 506 REMARK 465 MET A 507 REMARK 465 ASN A 508 REMARK 465 PRO A 509 REMARK 465 SER A 510 REMARK 465 GLN A 511 REMARK 465 SER A 512 REMARK 465 LEU A 513 REMARK 465 LEU A 514 REMARK 465 PRO A 515 REMARK 465 GLU A 516 REMARK 465 ARG A 517 REMARK 465 GLY A 518 REMARK 465 GLY A 519 REMARK 465 SER A 520 REMARK 465 ASP A 521 REMARK 465 PRO A 522 REMARK 465 GLN A 523 REMARK 465 ARG A 524 REMARK 465 GLN A 525 REMARK 465 ARG A 526 REMARK 465 HIS A 527 REMARK 465 LEU A 528 REMARK 465 GLU A 529 REMARK 465 ASN A 530 REMARK 465 SER A 531 REMARK 465 GLU A 532 REMARK 465 GLU A 533 REMARK 465 PRO A 534 REMARK 465 PRO A 535 REMARK 465 GLU A 536 REMARK 465 ARG A 537 REMARK 465 ARG A 538 REMARK 465 SER A 539 REMARK 465 ARG A 540 REMARK 465 VAL A 541 REMARK 465 SER A 542 REMARK 465 SER A 543 REMARK 465 VAL A 544 REMARK 465 ILE A 545 REMARK 465 ARG A 546 REMARK 465 GLU A 547 REMARK 465 LYS A 548 REMARK 465 LEU A 549 REMARK 465 GLN A 550 REMARK 465 GLU A 551 REMARK 465 VAL A 552 REMARK 465 LEU A 553 REMARK 465 GLN A 554 REMARK 465 ASP A 555 REMARK 465 LEU A 556 REMARK 465 GLY A 557 REMARK 465 SER A 558 REMARK 465 GLY A 559 REMARK 465 SER A 560 REMARK 465 GLY A 561 REMARK 465 SER A 562 REMARK 465 GLY A 563 REMARK 465 ARG A 564 REMARK 465 GLY A 565 REMARK 465 ARG A 566 REMARK 465 GLY A 567 REMARK 465 GLY A 568 REMARK 465 SER A 569 REMARK 465 GLU A 570 REMARK 465 ASN A 571 REMARK 465 LEU A 572 REMARK 465 TYR A 573 REMARK 465 PHE A 574 REMARK 465 GLN A 575 REMARK 465 GLY A 576 REMARK 465 GLY A 577 REMARK 465 SER A 578 REMARK 465 GLY A 579 REMARK 465 SER A 580 REMARK 465 GLY A 581 REMARK 465 GLY A 582 REMARK 465 ASP A 583 REMARK 465 TYR A 584 REMARK 465 LYS A 585 REMARK 465 ASP A 586 REMARK 465 ASP A 587 REMARK 465 ASP A 588 REMARK 465 ASP A 589 REMARK 465 LYS A 590 REMARK 465 ASP A 591 REMARK 465 TYR A 592 REMARK 465 LYS A 593 REMARK 465 ASP A 594 REMARK 465 ASP A 595 REMARK 465 ASP A 596 REMARK 465 ASP A 597 REMARK 465 LYS A 598 REMARK 465 MET B 1 REMARK 465 GLU B 2 REMARK 465 PRO B 3 REMARK 465 GLU B 4 REMARK 465 ILE B 5 REMARK 465 ASN B 6 REMARK 465 CYS B 7 REMARK 465 SER B 8 REMARK 465 GLU B 9 REMARK 465 LEU B 10 REMARK 465 CYS B 11 REMARK 465 ASP B 12 REMARK 465 SER B 13 REMARK 465 PHE B 14 REMARK 465 PRO B 15 REMARK 465 GLY B 16 REMARK 465 GLN B 17 REMARK 465 GLU B 18 REMARK 465 LEU B 19 REMARK 465 ASP B 20 REMARK 465 ARG B 21 REMARK 465 ARG B 22 REMARK 465 PRO B 23 REMARK 465 LEU B 24 REMARK 465 HIS B 25 REMARK 465 ASP B 26 REMARK 465 LEU B 27 REMARK 465 CYS B 28 REMARK 465 LYS B 29 REMARK 465 THR B 30 REMARK 465 THR B 31 REMARK 465 ILE B 32 REMARK 465 THR B 33 REMARK 465 SER B 34 REMARK 465 SER B 35 REMARK 465 HIS B 36 REMARK 465 HIS B 37 REMARK 465 SER B 38 REMARK 465 SER B 39 REMARK 465 LYS B 40 REMARK 465 THR B 41 REMARK 465 ILE B 42 REMARK 465 SER B 43 REMARK 465 VAL B 112 REMARK 465 GLY B 113 REMARK 465 SER B 114 REMARK 465 ASN B 336 REMARK 465 LYS B 337 REMARK 465 SER B 338 REMARK 465 PHE B 339 REMARK 465 HIS B 340 REMARK 465 THR B 341 REMARK 465 GLN B 342 REMARK 465 TYR B 343 REMARK 465 GLY B 344 REMARK 465 GLU B 345 REMARK 465 GLU B 346 REMARK 465 GLU B 347 REMARK 465 ASN B 348 REMARK 465 CYS B 349 REMARK 465 HIS B 350 REMARK 465 PRO B 351 REMARK 465 ARG B 352 REMARK 465 GLY B 353 REMARK 465 GLU B 354 REMARK 465 LYS B 355 REMARK 465 SER B 356 REMARK 465 SER B 357 REMARK 465 MET B 358 REMARK 465 GLU B 359 REMARK 465 ARG B 360 REMARK 465 LEU B 361 REMARK 465 LEU B 362 REMARK 465 THR B 363 REMARK 465 GLU B 364 REMARK 465 LYS B 365 REMARK 465 ASN B 366 REMARK 465 ALA B 367 REMARK 465 VAL B 368 REMARK 465 ILE B 369 REMARK 465 GLU B 370 REMARK 465 SER B 371 REMARK 465 LEU B 372 REMARK 465 GLN B 373 REMARK 465 GLU B 374 REMARK 465 GLN B 375 REMARK 465 VAL B 376 REMARK 465 ASN B 377 REMARK 465 ASN B 378 REMARK 465 ALA B 379 REMARK 465 LYS B 380 REMARK 465 GLU B 381 REMARK 465 LYS B 382 REMARK 465 ILE B 383 REMARK 465 VAL B 384 REMARK 465 ARG B 385 REMARK 465 LEU B 386 REMARK 465 MET B 387 REMARK 465 SER B 388 REMARK 465 ALA B 389 REMARK 465 GLU B 390 REMARK 465 CYS B 391 REMARK 465 THR B 392 REMARK 465 TYR B 393 REMARK 465 ASP B 394 REMARK 465 LEU B 395 REMARK 465 PRO B 396 REMARK 465 GLU B 397 REMARK 465 GLY B 398 REMARK 465 ALA B 399 REMARK 465 ALA B 400 REMARK 465 PRO B 401 REMARK 465 PRO B 402 REMARK 465 ALA B 403 REMARK 465 SER B 404 REMARK 465 SER B 405 REMARK 465 PRO B 406 REMARK 465 ASN B 407 REMARK 465 LYS B 408 REMARK 465 ASP B 409 REMARK 465 VAL B 410 REMARK 465 GLN B 411 REMARK 465 ALA B 412 REMARK 465 VAL B 413 REMARK 465 ALA B 414 REMARK 465 SER B 415 REMARK 465 VAL B 416 REMARK 465 HIS B 417 REMARK 465 THR B 418 REMARK 465 LEU B 419 REMARK 465 ALA B 420 REMARK 465 ALA B 421 REMARK 465 ALA B 422 REMARK 465 GLN B 423 REMARK 465 GLY B 424 REMARK 465 PRO B 425 REMARK 465 SER B 426 REMARK 465 GLY B 427 REMARK 465 HIS B 428 REMARK 465 LEU B 429 REMARK 465 SER B 430 REMARK 465 ASP B 431 REMARK 465 PHE B 432 REMARK 465 GLN B 433 REMARK 465 ASN B 434 REMARK 465 ASP B 435 REMARK 465 PRO B 436 REMARK 465 GLY B 437 REMARK 465 MET B 438 REMARK 465 ALA B 439 REMARK 465 ALA B 440 REMARK 465 ARG B 441 REMARK 465 ASP B 442 REMARK 465 SER B 443 REMARK 465 GLN B 444 REMARK 465 CYS B 445 REMARK 465 THR B 446 REMARK 465 SER B 447 REMARK 465 GLY B 448 REMARK 465 PRO B 449 REMARK 465 SER B 450 REMARK 465 SER B 451 REMARK 465 TYR B 452 REMARK 465 ALA B 453 REMARK 465 GLN B 454 REMARK 465 SER B 455 REMARK 465 LEU B 456 REMARK 465 GLU B 457 REMARK 465 GLY B 458 REMARK 465 PRO B 459 REMARK 465 GLY B 460 REMARK 465 LYS B 461 REMARK 465 ASP B 462 REMARK 465 SER B 463 REMARK 465 SER B 464 REMARK 465 PHE B 465 REMARK 465 SER B 466 REMARK 465 PRO B 467 REMARK 465 GLY B 468 REMARK 465 LYS B 469 REMARK 465 GLU B 470 REMARK 465 GLU B 471 REMARK 465 LYS B 472 REMARK 465 ILE B 473 REMARK 465 SER B 474 REMARK 465 ASP B 475 REMARK 465 SER B 476 REMARK 465 LYS B 477 REMARK 465 ASP B 478 REMARK 465 PHE B 479 REMARK 465 SER B 480 REMARK 465 ASP B 481 REMARK 465 HIS B 482 REMARK 465 LEU B 483 REMARK 465 ASP B 484 REMARK 465 SER B 485 REMARK 465 GLY B 486 REMARK 465 CYS B 487 REMARK 465 SER B 488 REMARK 465 GLN B 489 REMARK 465 LYS B 490 REMARK 465 PRO B 491 REMARK 465 TRP B 492 REMARK 465 THR B 493 REMARK 465 GLU B 494 REMARK 465 GLN B 495 REMARK 465 SER B 496 REMARK 465 LEU B 497 REMARK 465 GLY B 498 REMARK 465 PRO B 499 REMARK 465 GLU B 500 REMARK 465 ARG B 501 REMARK 465 GLY B 502 REMARK 465 ASP B 503 REMARK 465 GLN B 504 REMARK 465 VAL B 505 REMARK 465 PRO B 506 REMARK 465 MET B 507 REMARK 465 ASN B 508 REMARK 465 PRO B 509 REMARK 465 SER B 510 REMARK 465 GLN B 511 REMARK 465 SER B 512 REMARK 465 LEU B 513 REMARK 465 LEU B 514 REMARK 465 PRO B 515 REMARK 465 GLU B 516 REMARK 465 ARG B 517 REMARK 465 GLY B 518 REMARK 465 GLY B 519 REMARK 465 SER B 520 REMARK 465 ASP B 521 REMARK 465 PRO B 522 REMARK 465 GLN B 523 REMARK 465 ARG B 524 REMARK 465 GLN B 525 REMARK 465 ARG B 526 REMARK 465 HIS B 527 REMARK 465 LEU B 528 REMARK 465 GLU B 529 REMARK 465 ASN B 530 REMARK 465 SER B 531 REMARK 465 GLU B 532 REMARK 465 GLU B 533 REMARK 465 PRO B 534 REMARK 465 PRO B 535 REMARK 465 GLU B 536 REMARK 465 ARG B 537 REMARK 465 ARG B 538 REMARK 465 SER B 539 REMARK 465 ARG B 540 REMARK 465 VAL B 541 REMARK 465 SER B 542 REMARK 465 SER B 543 REMARK 465 VAL B 544 REMARK 465 ILE B 545 REMARK 465 ARG B 546 REMARK 465 GLU B 547 REMARK 465 LYS B 548 REMARK 465 LEU B 549 REMARK 465 GLN B 550 REMARK 465 GLU B 551 REMARK 465 VAL B 552 REMARK 465 LEU B 553 REMARK 465 GLN B 554 REMARK 465 ASP B 555 REMARK 465 LEU B 556 REMARK 465 GLY B 557 REMARK 465 SER B 558 REMARK 465 GLY B 559 REMARK 465 SER B 560 REMARK 465 GLY B 561 REMARK 465 SER B 562 REMARK 465 GLY B 563 REMARK 465 ARG B 564 REMARK 465 GLY B 565 REMARK 465 ARG B 566 REMARK 465 GLY B 567 REMARK 465 GLY B 568 REMARK 465 SER B 569 REMARK 465 GLU B 570 REMARK 465 ASN B 571 REMARK 465 LEU B 572 REMARK 465 TYR B 573 REMARK 465 PHE B 574 REMARK 465 GLN B 575 REMARK 465 GLY B 576 REMARK 465 GLY B 577 REMARK 465 SER B 578 REMARK 465 GLY B 579 REMARK 465 SER B 580 REMARK 465 GLY B 581 REMARK 465 GLY B 582 REMARK 465 ASP B 583 REMARK 465 TYR B 584 REMARK 465 LYS B 585 REMARK 465 ASP B 586 REMARK 465 ASP B 587 REMARK 465 ASP B 588 REMARK 465 ASP B 589 REMARK 465 LYS B 590 REMARK 465 ASP B 591 REMARK 465 TYR B 592 REMARK 465 LYS B 593 REMARK 465 ASP B 594 REMARK 465 ASP B 595 REMARK 465 ASP B 596 REMARK 465 ASP B 597 REMARK 465 LYS B 598 REMARK 465 MET C 1 REMARK 465 GLY C 2 REMARK 465 CYS C 3 REMARK 465 HIS C 57 REMARK 465 GLY C 58 REMARK 465 GLY C 59 REMARK 465 SER C 60 REMARK 465 GLY C 61 REMARK 465 GLY C 62 REMARK 465 SER C 63 REMARK 465 GLY C 64 REMARK 465 GLY C 65 REMARK 465 THR C 66 REMARK 465 MET D -17 REMARK 465 HIS D -16 REMARK 465 HIS D -15 REMARK 465 HIS D -14 REMARK 465 HIS D -13 REMARK 465 HIS D -12 REMARK 465 HIS D -11 REMARK 465 LEU D -10 REMARK 465 GLU D -9 REMARK 465 VAL D -8 REMARK 465 LEU D -7 REMARK 465 PHE D -6 REMARK 465 GLN D -5 REMARK 465 GLY D -4 REMARK 465 PRO D -3 REMARK 465 GLY D -2 REMARK 465 SER D -1 REMARK 465 SER D 0 REMARK 465 GLY D 1 REMARK 465 SER D 2 REMARK 465 ASP N 1 REMARK 465 SER N 120A REMARK 465 GLY N 120B REMARK 465 GLY N 120C REMARK 465 GLY N 120D REMARK 465 GLY N 120E REMARK 465 SER N 120F REMARK 465 GLY N 120G REMARK 465 GLY N 120H REMARK 465 GLY N 120I REMARK 465 GLY N 120J REMARK 465 SER N 120K REMARK 465 GLY N 120L REMARK 465 GLY N 120M REMARK 465 GLY N 120N REMARK 465 GLY N 120O REMARK 465 SER N 120P REMARK 465 LYS N 236 REMARK 465 ALA N 237 REMARK 465 ALA N 238 REMARK 465 ALA N 239 REMARK 465 HIS N 240 REMARK 465 HIS N 241 REMARK 465 HIS N 242 REMARK 465 HIS N 243 REMARK 465 HIS N 244 REMARK 465 HIS N 245 REMARK 465 HIS N 246 REMARK 465 HIS N 247 REMARK 465 MET Y 1 REMARK 465 ALA Y 2 REMARK 465 SER Y 3 REMARK 465 ASN Y 4 REMARK 465 ASN Y 5 REMARK 465 THR Y 6 REMARK 465 ALA Y 7 REMARK 465 GLU Y 63 REMARK 465 LYS Y 64 REMARK 465 LYS Y 65 REMARK 465 PHE Y 66 REMARK 465 PHE Y 67 REMARK 465 CYS Y 68 REMARK 465 ALA Y 69 REMARK 465 ILE Y 70 REMARK 465 LEU Y 71 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLN A 151 CG CD OE1 NE2 REMARK 470 ARG A 152 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 155 CG OD1 OD2 REMARK 470 LYS C 10 CG CD CE NZ REMARK 470 ASP C 42 CG OD1 OD2 REMARK 470 ASN C 43 CG OD1 ND2 REMARK 470 LYS C 51 CG CD CE NZ REMARK 470 ARG C 90 CG CD NE CZ NH1 NH2 REMARK 470 LYS C 94 CG CD CE NZ REMARK 470 ASP C 111 CG OD1 OD2 REMARK 470 MET C 123 CG SD CE REMARK 470 LYS C 132 CG CD CE NZ REMARK 470 LYS C 154 CG CD CE NZ REMARK 470 LYS C 155 CG CD CE NZ REMARK 470 GLU C 164 CG CD OE1 OE2 REMARK 470 GLU C 172 CG CD OE1 OE2 REMARK 470 GLU D 3 CG CD OE1 OE2 REMARK 470 LEU D 4 CG CD1 CD2 REMARK 470 ASP D 5 CG OD1 OD2 REMARK 470 GLN D 6 CG CD OE1 NE2 REMARK 470 LEU D 7 CG CD1 CD2 REMARK 470 ARG D 8 CG CD NE CZ NH1 NH2 REMARK 470 GLN D 9 CG CD OE1 NE2 REMARK 470 GLU D 10 CG CD OE1 OE2 REMARK 470 GLU D 12 CG CD OE1 OE2 REMARK 470 ARG D 19 CG CD NE CZ NH1 NH2 REMARK 470 ARG D 46 CG CD NE CZ NH1 NH2 REMARK 470 ARG D 214 CG CD NE CZ NH1 NH2 REMARK 470 GLU D 215 CG CD OE1 OE2 REMARK 470 MET D 217 CG SD CE REMARK 470 THR D 221 OG1 CG2 REMARK 470 SER D 245 OG REMARK 470 SER D 265 OG REMARK 470 ASP D 267 CG OD1 OD2 REMARK 470 ILE D 270 CG1 CG2 CD1 REMARK 470 ASP D 303 CG OD1 OD2 REMARK 470 SER D 331 OG REMARK 470 GLU N 6 CG CD OE1 OE2 REMARK 470 GLN N 13 CG CD OE1 NE2 REMARK 470 GLU N 42 CG CD OE1 OE2 REMARK 470 LYS N 43 CG CD CE NZ REMARK 470 LYS N 76 CG CD CE NZ REMARK 470 GLU N 89 CG CD OE1 OE2 REMARK 470 THR N 91 OG1 CG2 REMARK 470 VAL N 119 CG1 CG2 REMARK 470 VAL N 127 CG1 CG2 REMARK 470 THR N 132 OG1 CG2 REMARK 470 SER N 134 OG REMARK 470 VAL N 137 CG1 CG2 REMARK 470 GLU N 141 CG CD OE1 OE2 REMARK 470 THR N 198 OG1 CG2 REMARK 470 ARG N 206 CG CD NE CZ NH1 NH2 REMARK 470 GLU N 208 CG CD OE1 OE2 REMARK 470 GLU N 210 CG CD OE1 OE2 REMARK 470 THR N 226 OG1 CG2 REMARK 470 GLU N 234 CG CD OE1 OE2 REMARK 470 SER Y 8 OG REMARK 470 ILE Y 9 CG1 CG2 CD1 REMARK 470 ARG Y 13 CG CD NE CZ NH1 NH2 REMARK 470 LYS Y 14 CG CD CE NZ REMARK 470 VAL Y 16 CG1 CG2 REMARK 470 ARG Y 27 CG CD NE CZ NH1 NH2 REMARK 470 LYS Y 29 CG CD CE NZ REMARK 470 LYS Y 32 CG CD CE NZ REMARK 470 ASP Y 48 CG OD1 OD2 REMARK 470 VAL Y 54 CG1 CG2 REMARK 470 GLU Y 58 CG CD OE1 OE2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OE2 GLU D 260 OG1 THR D 263 2.17 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER A 84 74.31 53.07 REMARK 500 THR A 246 52.12 -92.24 REMARK 500 LEU A 281 52.08 -93.66 REMARK 500 CYS B 74 51.40 -91.87 REMARK 500 VAL B 110 -58.69 -121.49 REMARK 500 ASP B 155 -156.58 54.03 REMARK 500 THR B 246 35.80 -98.58 REMARK 500 GLU B 320 -60.57 -90.66 REMARK 500 LYS C 77 -116.10 54.40 REMARK 500 ARG C 93 49.19 -84.76 REMARK 500 PHE C 100 50.99 -93.58 REMARK 500 LEU C 158 -10.93 72.66 REMARK 500 ALA D 26 53.51 -93.24 REMARK 500 THR D 29 -165.78 -77.86 REMARK 500 GLN D 32 19.11 54.75 REMARK 500 ARG D 129 50.03 -91.00 REMARK 500 ASP D 163 38.21 -97.85 REMARK 500 HIS D 183 71.94 58.12 REMARK 500 PRO D 194 45.55 -76.56 REMARK 500 ASP D 291 36.79 -93.86 REMARK 500 PHE D 292 40.92 70.41 REMARK 500 PRO N 14 78.30 -69.12 REMARK 500 VAL N 48 -63.58 -121.12 REMARK 500 ALA N 131 -157.53 51.86 REMARK 500 GLU N 141 -174.48 -172.60 REMARK 500 ARG N 179 -100.52 52.77 REMARK 500 MET N 180 -35.53 -132.20 REMARK 500 HIS N 220 22.63 -140.29 REMARK 500 LEU N 221 -72.64 -77.91 REMARK 500 PRO Y 55 49.55 -87.16 REMARK 500 ASN Y 59 71.20 52.54 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 PC1 A 601 REMARK 610 PC1 B 601 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-35380 RELATED DB: EMDB REMARK 900 STRUCTURE OF GLOBALLY REFINED GPCR-G COMPLEX DBREF 8IED A 1 557 UNP Q8NFN8 GP156_HUMAN 1 557 DBREF 8IED B 1 557 UNP Q8NFN8 GP156_HUMAN 1 557 DBREF 8IED C 1 56 PDB 8IED 8IED 1 56 DBREF 8IED C 66 228 UNP P09471 GNAO_HUMAN 182 354 DBREF 8IED D 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 8IED N 1 247 PDB 8IED 8IED 1 247 DBREF 8IED Y 1 71 UNP P59768 GBG2_HUMAN 1 71 SEQADV 8IED SER A 558 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED GLY A 559 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED SER A 560 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED GLY A 561 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED SER A 562 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED GLY A 563 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED ARG A 564 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED GLY A 565 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED ARG A 566 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED GLY A 567 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED GLY A 568 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED SER A 569 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED GLU A 570 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED ASN A 571 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED LEU A 572 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED TYR A 573 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED PHE A 574 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED GLN A 575 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED GLY A 576 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED GLY A 577 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED SER A 578 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED GLY A 579 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED SER A 580 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED GLY A 581 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED GLY A 582 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED ASP A 583 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED TYR A 584 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED LYS A 585 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED ASP A 586 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED ASP A 587 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED ASP A 588 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED ASP A 589 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED LYS A 590 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED ASP A 591 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED TYR A 592 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED LYS A 593 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED ASP A 594 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED ASP A 595 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED ASP A 596 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED ASP A 597 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED LYS A 598 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED SER B 558 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED GLY B 559 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED SER B 560 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED GLY B 561 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED SER B 562 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED GLY B 563 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED ARG B 564 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED GLY B 565 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED ARG B 566 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED GLY B 567 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED GLY B 568 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED SER B 569 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED GLU B 570 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED ASN B 571 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED LEU B 572 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED TYR B 573 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED PHE B 574 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED GLN B 575 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED GLY B 576 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED GLY B 577 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED SER B 578 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED GLY B 579 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED SER B 580 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED GLY B 581 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED GLY B 582 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED ASP B 583 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED TYR B 584 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED LYS B 585 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED ASP B 586 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED ASP B 587 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED ASP B 588 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED ASP B 589 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED LYS B 590 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED ASP B 591 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED TYR B 592 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED LYS B 593 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED ASP B 594 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED ASP B 595 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED ASP B 596 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED ASP B 597 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED LYS B 598 UNP Q8NFN8 EXPRESSION TAG SEQADV 8IED HIS C 57 PDB LINKER SEQADV 8IED GLY C 58 PDB LINKER SEQADV 8IED GLY C 59 PDB LINKER SEQADV 8IED SER C 60 PDB LINKER SEQADV 8IED GLY C 61 PDB LINKER SEQADV 8IED GLY C 62 PDB LINKER SEQADV 8IED SER C 63 PDB LINKER SEQADV 8IED GLY C 64 PDB LINKER SEQADV 8IED GLY C 65 PDB LINKER SEQADV 8IED ASP C 111 UNP P09471 ALA 227 CONFLICT SEQADV 8IED ASP C 114 UNP P09471 GLY 230 CONFLICT SEQADV 8IED C UNP P09471 ASP 232 DELETION SEQADV 8IED C UNP P09471 GLN 233 DELETION SEQADV 8IED C UNP P09471 VAL 234 DELETION SEQADV 8IED C UNP P09471 LEU 235 DELETION SEQADV 8IED C UNP P09471 HIS 236 DELETION SEQADV 8IED C UNP P09471 GLU 237 DELETION SEQADV 8IED C UNP P09471 ASP 238 DELETION SEQADV 8IED C UNP P09471 GLU 239 DELETION SEQADV 8IED C UNP P09471 THR 240 DELETION SEQADV 8IED C UNP P09471 THR 241 DELETION SEQADV 8IED ALA C 206 UNP P09471 ILE 332 CONFLICT SEQADV 8IED ILE C 209 UNP P09471 VAL 335 CONFLICT SEQADV 8IED MET D -17 UNP P62873 INITIATING METHIONINE SEQADV 8IED HIS D -16 UNP P62873 EXPRESSION TAG SEQADV 8IED HIS D -15 UNP P62873 EXPRESSION TAG SEQADV 8IED HIS D -14 UNP P62873 EXPRESSION TAG SEQADV 8IED HIS D -13 UNP P62873 EXPRESSION TAG SEQADV 8IED HIS D -12 UNP P62873 EXPRESSION TAG SEQADV 8IED HIS D -11 UNP P62873 EXPRESSION TAG SEQADV 8IED LEU D -10 UNP P62873 EXPRESSION TAG SEQADV 8IED GLU D -9 UNP P62873 EXPRESSION TAG SEQADV 8IED VAL D -8 UNP P62873 EXPRESSION TAG SEQADV 8IED LEU D -7 UNP P62873 EXPRESSION TAG SEQADV 8IED PHE D -6 UNP P62873 EXPRESSION TAG SEQADV 8IED GLN D -5 UNP P62873 EXPRESSION TAG SEQADV 8IED GLY D -4 UNP P62873 EXPRESSION TAG SEQADV 8IED PRO D -3 UNP P62873 EXPRESSION TAG SEQADV 8IED GLY D -2 UNP P62873 EXPRESSION TAG SEQADV 8IED SER D -1 UNP P62873 EXPRESSION TAG SEQADV 8IED SER D 0 UNP P62873 EXPRESSION TAG SEQADV 8IED GLY D 1 UNP P62873 EXPRESSION TAG SEQRES 1 A 598 MET GLU PRO GLU ILE ASN CYS SER GLU LEU CYS ASP SER SEQRES 2 A 598 PHE PRO GLY GLN GLU LEU ASP ARG ARG PRO LEU HIS ASP SEQRES 3 A 598 LEU CYS LYS THR THR ILE THR SER SER HIS HIS SER SER SEQRES 4 A 598 LYS THR ILE SER SER LEU SER PRO VAL LEU LEU GLY ILE SEQRES 5 A 598 VAL TRP THR PHE LEU SER CYS GLY LEU LEU LEU ILE LEU SEQRES 6 A 598 PHE PHE LEU ALA PHE THR ILE HIS CYS ARG LYS ASN ARG SEQRES 7 A 598 ILE VAL LYS MET SER SER PRO ASN LEU ASN ILE VAL THR SEQRES 8 A 598 LEU LEU GLY SER CYS LEU THR TYR SER SER ALA TYR LEU SEQRES 9 A 598 PHE GLY ILE GLN ASP VAL LEU VAL GLY SER SER MET GLU SEQRES 10 A 598 THR LEU ILE GLN THR ARG LEU SER MET LEU CYS ILE GLY SEQRES 11 A 598 THR SER LEU VAL PHE GLY PRO ILE LEU GLY LYS SER TRP SEQRES 12 A 598 ARG LEU TYR LYS VAL PHE THR GLN ARG VAL PRO ASP LYS SEQRES 13 A 598 ARG VAL ILE ILE LYS ASP LEU GLN LEU LEU GLY LEU VAL SEQRES 14 A 598 ALA ALA LEU LEU MET ALA ASP VAL ILE LEU LEU MET THR SEQRES 15 A 598 TRP VAL LEU THR ASP PRO ILE GLN CYS LEU GLN ILE LEU SEQRES 16 A 598 SER VAL SER MET THR VAL THR GLY LYS ASP VAL SER CYS SEQRES 17 A 598 THR SER THR SER THR HIS PHE CYS ALA SER ARG TYR SER SEQRES 18 A 598 ASP VAL TRP ILE ALA LEU ILE TRP GLY CYS LYS GLY LEU SEQRES 19 A 598 LEU LEU LEU TYR GLY ALA TYR LEU ALA GLY LEU THR GLY SEQRES 20 A 598 HIS VAL SER SER PRO PRO VAL ASN GLN SER LEU THR ILE SEQRES 21 A 598 MET VAL GLY VAL ASN LEU LEU VAL LEU ALA ALA GLY LEU SEQRES 22 A 598 LEU PHE VAL VAL THR ARG TYR LEU HIS SER TRP PRO ASN SEQRES 23 A 598 LEU VAL PHE GLY LEU THR SER GLY GLY ILE PHE VAL CYS SEQRES 24 A 598 THR THR THR ILE ASN CYS PHE ILE PHE ILE PRO GLN LEU SEQRES 25 A 598 LYS GLN TRP LYS ALA PHE GLU GLU GLU ASN GLN THR ILE SEQRES 26 A 598 ARG ARG MET ALA LYS TYR PHE SER THR PRO ASN LYS SER SEQRES 27 A 598 PHE HIS THR GLN TYR GLY GLU GLU GLU ASN CYS HIS PRO SEQRES 28 A 598 ARG GLY GLU LYS SER SER MET GLU ARG LEU LEU THR GLU SEQRES 29 A 598 LYS ASN ALA VAL ILE GLU SER LEU GLN GLU GLN VAL ASN SEQRES 30 A 598 ASN ALA LYS GLU LYS ILE VAL ARG LEU MET SER ALA GLU SEQRES 31 A 598 CYS THR TYR ASP LEU PRO GLU GLY ALA ALA PRO PRO ALA SEQRES 32 A 598 SER SER PRO ASN LYS ASP VAL GLN ALA VAL ALA SER VAL SEQRES 33 A 598 HIS THR LEU ALA ALA ALA GLN GLY PRO SER GLY HIS LEU SEQRES 34 A 598 SER ASP PHE GLN ASN ASP PRO GLY MET ALA ALA ARG ASP SEQRES 35 A 598 SER GLN CYS THR SER GLY PRO SER SER TYR ALA GLN SER SEQRES 36 A 598 LEU GLU GLY PRO GLY LYS ASP SER SER PHE SER PRO GLY SEQRES 37 A 598 LYS GLU GLU LYS ILE SER ASP SER LYS ASP PHE SER ASP SEQRES 38 A 598 HIS LEU ASP SER GLY CYS SER GLN LYS PRO TRP THR GLU SEQRES 39 A 598 GLN SER LEU GLY PRO GLU ARG GLY ASP GLN VAL PRO MET SEQRES 40 A 598 ASN PRO SER GLN SER LEU LEU PRO GLU ARG GLY GLY SER SEQRES 41 A 598 ASP PRO GLN ARG GLN ARG HIS LEU GLU ASN SER GLU GLU SEQRES 42 A 598 PRO PRO GLU ARG ARG SER ARG VAL SER SER VAL ILE ARG SEQRES 43 A 598 GLU LYS LEU GLN GLU VAL LEU GLN ASP LEU GLY SER GLY SEQRES 44 A 598 SER GLY SER GLY ARG GLY ARG GLY GLY SER GLU ASN LEU SEQRES 45 A 598 TYR PHE GLN GLY GLY SER GLY SER GLY GLY ASP TYR LYS SEQRES 46 A 598 ASP ASP ASP ASP LYS ASP TYR LYS ASP ASP ASP ASP LYS SEQRES 1 B 598 MET GLU PRO GLU ILE ASN CYS SER GLU LEU CYS ASP SER SEQRES 2 B 598 PHE PRO GLY GLN GLU LEU ASP ARG ARG PRO LEU HIS ASP SEQRES 3 B 598 LEU CYS LYS THR THR ILE THR SER SER HIS HIS SER SER SEQRES 4 B 598 LYS THR ILE SER SER LEU SER PRO VAL LEU LEU GLY ILE SEQRES 5 B 598 VAL TRP THR PHE LEU SER CYS GLY LEU LEU LEU ILE LEU SEQRES 6 B 598 PHE PHE LEU ALA PHE THR ILE HIS CYS ARG LYS ASN ARG SEQRES 7 B 598 ILE VAL LYS MET SER SER PRO ASN LEU ASN ILE VAL THR SEQRES 8 B 598 LEU LEU GLY SER CYS LEU THR TYR SER SER ALA TYR LEU SEQRES 9 B 598 PHE GLY ILE GLN ASP VAL LEU VAL GLY SER SER MET GLU SEQRES 10 B 598 THR LEU ILE GLN THR ARG LEU SER MET LEU CYS ILE GLY SEQRES 11 B 598 THR SER LEU VAL PHE GLY PRO ILE LEU GLY LYS SER TRP SEQRES 12 B 598 ARG LEU TYR LYS VAL PHE THR GLN ARG VAL PRO ASP LYS SEQRES 13 B 598 ARG VAL ILE ILE LYS ASP LEU GLN LEU LEU GLY LEU VAL SEQRES 14 B 598 ALA ALA LEU LEU MET ALA ASP VAL ILE LEU LEU MET THR SEQRES 15 B 598 TRP VAL LEU THR ASP PRO ILE GLN CYS LEU GLN ILE LEU SEQRES 16 B 598 SER VAL SER MET THR VAL THR GLY LYS ASP VAL SER CYS SEQRES 17 B 598 THR SER THR SER THR HIS PHE CYS ALA SER ARG TYR SER SEQRES 18 B 598 ASP VAL TRP ILE ALA LEU ILE TRP GLY CYS LYS GLY LEU SEQRES 19 B 598 LEU LEU LEU TYR GLY ALA TYR LEU ALA GLY LEU THR GLY SEQRES 20 B 598 HIS VAL SER SER PRO PRO VAL ASN GLN SER LEU THR ILE SEQRES 21 B 598 MET VAL GLY VAL ASN LEU LEU VAL LEU ALA ALA GLY LEU SEQRES 22 B 598 LEU PHE VAL VAL THR ARG TYR LEU HIS SER TRP PRO ASN SEQRES 23 B 598 LEU VAL PHE GLY LEU THR SER GLY GLY ILE PHE VAL CYS SEQRES 24 B 598 THR THR THR ILE ASN CYS PHE ILE PHE ILE PRO GLN LEU SEQRES 25 B 598 LYS GLN TRP LYS ALA PHE GLU GLU GLU ASN GLN THR ILE SEQRES 26 B 598 ARG ARG MET ALA LYS TYR PHE SER THR PRO ASN LYS SER SEQRES 27 B 598 PHE HIS THR GLN TYR GLY GLU GLU GLU ASN CYS HIS PRO SEQRES 28 B 598 ARG GLY GLU LYS SER SER MET GLU ARG LEU LEU THR GLU SEQRES 29 B 598 LYS ASN ALA VAL ILE GLU SER LEU GLN GLU GLN VAL ASN SEQRES 30 B 598 ASN ALA LYS GLU LYS ILE VAL ARG LEU MET SER ALA GLU SEQRES 31 B 598 CYS THR TYR ASP LEU PRO GLU GLY ALA ALA PRO PRO ALA SEQRES 32 B 598 SER SER PRO ASN LYS ASP VAL GLN ALA VAL ALA SER VAL SEQRES 33 B 598 HIS THR LEU ALA ALA ALA GLN GLY PRO SER GLY HIS LEU SEQRES 34 B 598 SER ASP PHE GLN ASN ASP PRO GLY MET ALA ALA ARG ASP SEQRES 35 B 598 SER GLN CYS THR SER GLY PRO SER SER TYR ALA GLN SER SEQRES 36 B 598 LEU GLU GLY PRO GLY LYS ASP SER SER PHE SER PRO GLY SEQRES 37 B 598 LYS GLU GLU LYS ILE SER ASP SER LYS ASP PHE SER ASP SEQRES 38 B 598 HIS LEU ASP SER GLY CYS SER GLN LYS PRO TRP THR GLU SEQRES 39 B 598 GLN SER LEU GLY PRO GLU ARG GLY ASP GLN VAL PRO MET SEQRES 40 B 598 ASN PRO SER GLN SER LEU LEU PRO GLU ARG GLY GLY SER SEQRES 41 B 598 ASP PRO GLN ARG GLN ARG HIS LEU GLU ASN SER GLU GLU SEQRES 42 B 598 PRO PRO GLU ARG ARG SER ARG VAL SER SER VAL ILE ARG SEQRES 43 B 598 GLU LYS LEU GLN GLU VAL LEU GLN ASP LEU GLY SER GLY SEQRES 44 B 598 SER GLY SER GLY ARG GLY ARG GLY GLY SER GLU ASN LEU SEQRES 45 B 598 TYR PHE GLN GLY GLY SER GLY SER GLY GLY ASP TYR LYS SEQRES 46 B 598 ASP ASP ASP ASP LYS ASP TYR LYS ASP ASP ASP ASP LYS SEQRES 1 C 228 MET GLY CYS THR LEU SER ALA GLU ASP LYS ALA ALA VAL SEQRES 2 C 228 GLU ARG SER LYS MET ILE GLU LYS ASN LEU LYS GLU ASP SEQRES 3 C 228 GLY ILE SER ALA ALA LYS ASP VAL LYS LEU LEU LEU LEU SEQRES 4 C 228 GLY ALA ASP ASN SER GLY LYS SER THR ILE VAL LYS GLN SEQRES 5 C 228 MET LYS ILE ILE HIS GLY GLY SER GLY GLY SER GLY GLY SEQRES 6 C 228 THR THR GLY ILE VAL GLU THR HIS PHE THR PHE LYS ASN SEQRES 7 C 228 LEU HIS PHE ARG LEU PHE ASP VAL GLY GLY GLN ARG SER SEQRES 8 C 228 GLU ARG LYS LYS TRP ILE HIS CYS PHE GLU ASP VAL THR SEQRES 9 C 228 ALA ILE ILE PHE CYS VAL ASP LEU SER ASP TYR ASN ARG SEQRES 10 C 228 MET HIS GLU SER LEU MET LEU PHE ASP SER ILE CYS ASN SEQRES 11 C 228 ASN LYS PHE PHE ILE ASP THR SER ILE ILE LEU PHE LEU SEQRES 12 C 228 ASN LYS LYS ASP LEU PHE GLY GLU LYS ILE LYS LYS SER SEQRES 13 C 228 PRO LEU THR ILE CYS PHE PRO GLU TYR THR GLY PRO ASN SEQRES 14 C 228 THR TYR GLU ASP ALA ALA ALA TYR ILE GLN ALA GLN PHE SEQRES 15 C 228 GLU SER LYS ASN ARG SER PRO ASN LYS GLU ILE TYR CYS SEQRES 16 C 228 HIS MET THR CYS ALA THR ASP THR ASN ASN ALA GLN VAL SEQRES 17 C 228 ILE PHE ASP ALA VAL THR ASP ILE ILE ILE ALA ASN ASN SEQRES 18 C 228 LEU ARG GLY CYS GLY LEU TYR SEQRES 1 D 358 MET HIS HIS HIS HIS HIS HIS LEU GLU VAL LEU PHE GLN SEQRES 2 D 358 GLY PRO GLY SER SER GLY SER GLU LEU ASP GLN LEU ARG SEQRES 3 D 358 GLN GLU ALA GLU GLN LEU LYS ASN GLN ILE ARG ASP ALA SEQRES 4 D 358 ARG LYS ALA CYS ALA ASP ALA THR LEU SER GLN ILE THR SEQRES 5 D 358 ASN ASN ILE ASP PRO VAL GLY ARG ILE GLN MET ARG THR SEQRES 6 D 358 ARG ARG THR LEU ARG GLY HIS LEU ALA LYS ILE TYR ALA SEQRES 7 D 358 MET HIS TRP GLY THR ASP SER ARG LEU LEU VAL SER ALA SEQRES 8 D 358 SER GLN ASP GLY LYS LEU ILE ILE TRP ASP SER TYR THR SEQRES 9 D 358 THR ASN LYS VAL HIS ALA ILE PRO LEU ARG SER SER TRP SEQRES 10 D 358 VAL MET THR CYS ALA TYR ALA PRO SER GLY ASN TYR VAL SEQRES 11 D 358 ALA CYS GLY GLY LEU ASP ASN ILE CYS SER ILE TYR ASN SEQRES 12 D 358 LEU LYS THR ARG GLU GLY ASN VAL ARG VAL SER ARG GLU SEQRES 13 D 358 LEU ALA GLY HIS THR GLY TYR LEU SER CYS CYS ARG PHE SEQRES 14 D 358 LEU ASP ASP ASN GLN ILE VAL THR SER SER GLY ASP THR SEQRES 15 D 358 THR CYS ALA LEU TRP ASP ILE GLU THR GLY GLN GLN THR SEQRES 16 D 358 THR THR PHE THR GLY HIS THR GLY ASP VAL MET SER LEU SEQRES 17 D 358 SER LEU ALA PRO ASP THR ARG LEU PHE VAL SER GLY ALA SEQRES 18 D 358 CYS ASP ALA SER ALA LYS LEU TRP ASP VAL ARG GLU GLY SEQRES 19 D 358 MET CYS ARG GLN THR PHE THR GLY HIS GLU SER ASP ILE SEQRES 20 D 358 ASN ALA ILE CYS PHE PHE PRO ASN GLY ASN ALA PHE ALA SEQRES 21 D 358 THR GLY SER ASP ASP ALA THR CYS ARG LEU PHE ASP LEU SEQRES 22 D 358 ARG ALA ASP GLN GLU LEU MET THR TYR SER HIS ASP ASN SEQRES 23 D 358 ILE ILE CYS GLY ILE THR SER VAL SER PHE SER LYS SER SEQRES 24 D 358 GLY ARG LEU LEU LEU ALA GLY TYR ASP ASP PHE ASN CYS SEQRES 25 D 358 ASN VAL TRP ASP ALA LEU LYS ALA ASP ARG ALA GLY VAL SEQRES 26 D 358 LEU ALA GLY HIS ASP ASN ARG VAL SER CYS LEU GLY VAL SEQRES 27 D 358 THR ASP ASP GLY MET ALA VAL ALA THR GLY SER TRP ASP SEQRES 28 D 358 SER PHE LEU LYS ILE TRP ASN SEQRES 1 N 259 ASP VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 N 259 PRO GLY GLY SER ARG LYS LEU SER CYS SER ALA SER GLY SEQRES 3 N 259 PHE ALA PHE SER SER PHE GLY MET HIS TRP VAL ARG GLN SEQRES 4 N 259 ALA PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SEQRES 5 N 259 SER GLY SER GLY THR ILE TYR TYR ALA ASP THR VAL LYS SEQRES 6 N 259 GLY ARG PHE THR ILE SER ARG ASP ASP PRO LYS ASN THR SEQRES 7 N 259 LEU PHE LEU GLN MET THR SER LEU THR SER GLU ASP THR SEQRES 8 N 259 ALA MET TYR TYR CYS VAL ARG SER ILE TYR TYR TYR GLY SEQRES 9 N 259 SER SER PRO PHE ASP PHE TRP GLY GLN GLY THR THR LEU SEQRES 10 N 259 THR VAL SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SEQRES 11 N 259 SER GLY GLY GLY GLY SER ASP ILE VAL MET THR GLN ALA SEQRES 12 N 259 THR SER SER VAL PRO VAL ILE PRO GLY GLU SER VAL SER SEQRES 13 N 259 ILE SER CYS ARG SER SER LYS SER LEU LEU HIS SER ASN SEQRES 14 N 259 GLY ASN THR TYR LEU TYR TRP PHE LEU GLN ARG PRO GLY SEQRES 15 N 259 GLN SER PRO GLN LEU LEU ILE TYR ARG MET SER ASN LEU SEQRES 16 N 259 ALA SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SER SEQRES 17 N 259 GLY THR ALA PHE THR LEU THR ILE SER ARG LEU GLU ALA SEQRES 18 N 259 GLU ASP VAL GLY VAL TYR TYR CYS MET GLN HIS LEU GLU SEQRES 19 N 259 TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU LEU SEQRES 20 N 259 LYS ALA ALA ALA HIS HIS HIS HIS HIS HIS HIS HIS SEQRES 1 Y 71 MET ALA SER ASN ASN THR ALA SER ILE ALA GLN ALA ARG SEQRES 2 Y 71 LYS LEU VAL GLU GLN LEU LYS MET GLU ALA ASN ILE ASP SEQRES 3 Y 71 ARG ILE LYS VAL SER LYS ALA ALA ALA ASP LEU MET ALA SEQRES 4 Y 71 TYR CYS GLU ALA HIS ALA LYS GLU ASP PRO LEU LEU THR SEQRES 5 Y 71 PRO VAL PRO ALA SER GLU ASN PRO PHE ARG GLU LYS LYS SEQRES 6 Y 71 PHE PHE CYS ALA ILE LEU HET PC1 A 601 52 HET PC1 B 601 52 HETNAM PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE HETSYN PC1 3-SN-PHOSPHATIDYLCHOLINE FORMUL 7 PC1 2(C44 H88 N O8 P) HELIX 1 AA1 SER A 46 CYS A 74 1 29 HELIX 2 AA2 ASN A 77 MET A 82 1 6 HELIX 3 AA3 SER A 84 PHE A 105 1 22 HELIX 4 AA4 SER A 115 GLN A 151 1 37 HELIX 5 AA5 LYS A 161 ASP A 187 1 27 HELIX 6 AA6 TYR A 220 THR A 246 1 27 HELIX 7 AA7 SER A 257 TYR A 280 1 24 HELIX 8 AA8 TRP A 284 ALA A 317 1 34 HELIX 9 AA9 SER B 46 CYS B 74 1 29 HELIX 10 AB1 ASN B 77 SER B 83 1 7 HELIX 11 AB2 SER B 84 PHE B 105 1 22 HELIX 12 AB3 MET B 116 THR B 150 1 35 HELIX 13 AB4 LYS B 161 ASP B 187 1 27 HELIX 14 AB5 TYR B 220 THR B 246 1 27 HELIX 15 AB6 GLN B 256 LEU B 281 1 26 HELIX 16 AB7 TRP B 284 TRP B 315 1 32 HELIX 17 AB8 LYS B 316 GLU B 319 5 4 HELIX 18 AB9 THR B 324 MET B 328 5 5 HELIX 19 AC1 ALA B 329 SER B 333 5 5 HELIX 20 AC2 SER C 6 ALA C 31 1 26 HELIX 21 AC3 TRP C 96 ASP C 102 5 7 HELIX 22 AC4 ARG C 117 CYS C 129 1 13 HELIX 23 AC5 ASN C 130 ILE C 135 5 6 HELIX 24 AC6 LYS C 145 ILE C 153 1 9 HELIX 25 AC7 THR C 170 SER C 184 1 15 HELIX 26 AC8 ASN C 205 CYS C 225 1 21 HELIX 27 AC9 LEU D 4 CYS D 25 1 22 HELIX 28 AD1 ALA N 28 PHE N 32 5 5 HELIX 29 AD2 SER N 53 GLY N 56 5 4 HELIX 30 AD3 THR N 87 THR N 91 5 5 HELIX 31 AD4 ILE Y 9 ASN Y 24 1 16 HELIX 32 AD5 ALA Y 34 HIS Y 44 1 11 SHEET 1 AA1 4 VAL A 206 CYS A 216 0 SHEET 2 AA1 4 CYS A 191 VAL A 201 -1 N SER A 198 O THR A 209 SHEET 3 AA1 4 GLN B 190 VAL B 201 -1 O MET B 199 N LEU A 195 SHEET 4 AA1 4 VAL B 206 ALA B 217 -1 O THR B 209 N SER B 198 SHEET 1 AA2 7 LYS C 54 ILE C 55 0 SHEET 2 AA2 7 GLU C 71 PHE C 76 -1 O HIS C 73 N LYS C 54 SHEET 3 AA2 7 LEU C 79 PHE C 84 -1 O PHE C 81 N PHE C 74 SHEET 4 AA2 7 ASP C 33 GLY C 40 1 N VAL C 34 O HIS C 80 SHEET 5 AA2 7 ALA C 105 ASP C 111 1 O ILE C 107 N LEU C 39 SHEET 6 AA2 7 SER C 138 ASN C 144 1 O SER C 138 N ILE C 106 SHEET 7 AA2 7 ILE C 193 MET C 197 1 O TYR C 194 N ILE C 139 SHEET 1 AA3 4 ARG D 49 LEU D 51 0 SHEET 2 AA3 4 LEU D 336 TRP D 339 -1 O LEU D 336 N LEU D 51 SHEET 3 AA3 4 VAL D 327 SER D 331 -1 N THR D 329 O LYS D 337 SHEET 4 AA3 4 VAL D 315 VAL D 320 -1 N GLY D 319 O ALA D 328 SHEET 1 AA4 4 ILE D 58 TRP D 63 0 SHEET 2 AA4 4 LEU D 69 SER D 74 -1 O VAL D 71 N HIS D 62 SHEET 3 AA4 4 LYS D 78 ASP D 83 -1 O TRP D 82 N LEU D 70 SHEET 4 AA4 4 ASN D 88 PRO D 94 -1 O ASN D 88 N ASP D 83 SHEET 1 AA5 4 VAL D 100 TYR D 105 0 SHEET 2 AA5 4 TYR D 111 GLY D 116 -1 O GLY D 115 N MET D 101 SHEET 3 AA5 4 ILE D 120 ASN D 125 -1 O TYR D 124 N VAL D 112 SHEET 4 AA5 4 ARG D 134 ALA D 140 -1 O ARG D 137 N ILE D 123 SHEET 1 AA6 4 LEU D 146 PHE D 151 0 SHEET 2 AA6 4 GLN D 156 SER D 161 -1 O SER D 160 N SER D 147 SHEET 3 AA6 4 THR D 165 ASP D 170 -1 O TRP D 169 N ILE D 157 SHEET 4 AA6 4 GLN D 175 THR D 181 -1 O PHE D 180 N CYS D 166 SHEET 1 AA7 4 SER D 191 LEU D 192 0 SHEET 2 AA7 4 LEU D 198 ALA D 203 -1 O VAL D 200 N SER D 191 SHEET 3 AA7 4 SER D 207 ASP D 212 -1 O TRP D 211 N PHE D 199 SHEET 4 AA7 4 CYS D 218 PHE D 222 -1 O ARG D 219 N LEU D 210 SHEET 1 AA8 4 ILE D 229 PHE D 234 0 SHEET 2 AA8 4 ALA D 240 SER D 245 -1 O ALA D 242 N CYS D 233 SHEET 3 AA8 4 THR D 249 ASP D 254 -1 O PHE D 253 N PHE D 241 SHEET 4 AA8 4 GLN D 259 SER D 265 -1 O TYR D 264 N CYS D 250 SHEET 1 AA9 4 VAL D 276 PHE D 278 0 SHEET 2 AA9 4 LEU D 284 TYR D 289 -1 O LEU D 286 N SER D 277 SHEET 3 AA9 4 ASN D 293 ASP D 298 -1 O TRP D 297 N LEU D 285 SHEET 4 AA9 4 GLY D 306 ALA D 309 -1 O GLY D 306 N VAL D 296 SHEET 1 AB1 4 GLN N 3 SER N 7 0 SHEET 2 AB1 4 SER N 17 SER N 25 -1 O SER N 21 N SER N 7 SHEET 3 AB1 4 THR N 78 THR N 84 -1 O LEU N 79 N CYS N 22 SHEET 4 AB1 4 PHE N 68 ASP N 73 -1 N SER N 71 O PHE N 80 SHEET 1 AB2 6 GLY N 10 VAL N 12 0 SHEET 2 AB2 6 THR N 115 VAL N 119 1 O THR N 118 N GLY N 10 SHEET 3 AB2 6 MET N 93 ARG N 98 -1 N TYR N 94 O THR N 115 SHEET 4 AB2 6 HIS N 35 GLN N 39 -1 N VAL N 37 O TYR N 95 SHEET 5 AB2 6 LEU N 45 ILE N 51 -1 O VAL N 48 N TRP N 36 SHEET 6 AB2 6 ILE N 58 TYR N 60 -1 O TYR N 59 N TYR N 50 SHEET 1 AB3 4 GLY N 10 VAL N 12 0 SHEET 2 AB3 4 THR N 115 VAL N 119 1 O THR N 118 N GLY N 10 SHEET 3 AB3 4 MET N 93 ARG N 98 -1 N TYR N 94 O THR N 115 SHEET 4 AB3 4 PHE N 110 TRP N 111 -1 O PHE N 110 N ARG N 98 SHEET 1 AB4 3 SER N 142 CYS N 147 0 SHEET 2 AB4 3 ALA N 199 SER N 205 -1 O ILE N 204 N VAL N 143 SHEET 3 AB4 3 PHE N 191 SER N 196 -1 N SER N 196 O ALA N 199 SHEET 1 AB5 5 ASN N 182 LEU N 183 0 SHEET 2 AB5 5 GLN N 174 TYR N 178 -1 N TYR N 178 O ASN N 182 SHEET 3 AB5 5 TRP N 164 GLN N 167 -1 N TRP N 164 O LEU N 176 SHEET 4 AB5 5 VAL N 214 TYR N 216 -1 O VAL N 214 N GLN N 167 SHEET 5 AB5 5 THR N 231 LYS N 232 -1 O THR N 231 N TYR N 215 SSBOND 1 CYS A 191 CYS A 216 1555 1555 2.03 SSBOND 2 CYS B 191 CYS B 216 1555 1555 2.03 SSBOND 3 CYS N 147 CYS N 217 1555 1555 2.03 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000