HEADER MEMBRANE PROTEIN 01-AUG-24 9IZH TITLE CRYO-EM STRUCTURE OF LPA1-G13 COMPLEX WITH LPA COMPND MOL_ID: 1; COMPND 2 MOLECULE: SOLUBLE CYTOCHROME B562,LYSOPHOSPHATIDIC ACID RECEPTOR 1, COMPND 3 LGBIT TAG; COMPND 4 CHAIN: R; COMPND 5 SYNONYM: CYTOCHROME B-562,LPA RECEPTOR 1,LPA-1,LYSOPHOSPHATIDIC ACID COMPND 6 RECEPTOR EDG-2; COMPND 7 ENGINEERED: YES; COMPND 8 OTHER_DETAILS: N-TERMINAL HA SIGNAL SEQUENCE, FLAG TAG C-TERMINAL COMPND 9 LGBIT; COMPND 10 MOL_ID: 2; COMPND 11 MOLECULE: G PROTEIN SUBUNIT 13 (GI2-MINI-G13 CHIMERA); COMPND 12 CHAIN: A; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 3; COMPND 15 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 16 BETA-1; COMPND 17 CHAIN: B; COMPND 18 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 19 ENGINEERED: YES; COMPND 20 MOL_ID: 4; COMPND 21 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 22 GAMMA-2; COMPND 23 CHAIN: C; COMPND 24 SYNONYM: G GAMMA-I; COMPND 25 ENGINEERED: YES; COMPND 26 MOL_ID: 5; COMPND 27 MOLECULE: SCFV16; COMPND 28 CHAIN: S; COMPND 29 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI, HOMO SAPIENS, SYNTHETIC SOURCE 3 CONSTRUCT; SOURCE 4 ORGANISM_COMMON: HUMAN; SOURCE 5 ORGANISM_TAXID: 562, 9606, 32630; SOURCE 6 GENE: CYBC, LPAR1, EDG2, LPA1; SOURCE 7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 16 ORGANISM_COMMON: HUMAN; SOURCE 17 ORGANISM_TAXID: 9606; SOURCE 18 GENE: GNB1; SOURCE 19 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 21 MOL_ID: 4; SOURCE 22 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 23 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 24 ORGANISM_TAXID: 10090; SOURCE 25 GENE: GNG2; SOURCE 26 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 27 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 28 MOL_ID: 5; SOURCE 29 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 30 ORGANISM_TAXID: 32630; SOURCE 31 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 32 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS GPCR, SIGNALING PROTEIN, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR S.SUZUKI,K.NISHIKAWA,A.KAMEGAWA,Y.HIROAKI,H.SUZUKI,Y.FUJIYOSHI REVDAT 1 01-JAN-25 9IZH 0 JRNL AUTH S.SUZUKI,A.KAMEGAWA,Y.HIROAKI,K.TANAKA,K.NISHIKAWA,H.SUZUKI, JRNL AUTH 2 N.NUMOTO,D.SASAKI,A.OSHIMA,Y.FUJIYOSHI JRNL TITL STRUCTURAL INSIGHTS INTO THE ENGAGEMENT OF LYSOPHOSPHATIDIC JRNL TITL 2 ACID RECEPTOR 1 WITH DIFFERENT G PROTEINS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.04 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) : 3.040 REMARK 3 NUMBER OF PARTICLES : 727119 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 9IZH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-AUG-24. REMARK 100 THE DEPOSITION ID IS D_1300049952. 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 : MULTIPROTEIN COMPLEX REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 15.00 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : NULL 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 : JEOL CRYO ARM 300 REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (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 : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 7100.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN 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: PENTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: R, A, B, C, S 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 R -128 REMARK 465 LYS R -127 REMARK 465 THR R -126 REMARK 465 ILE R -125 REMARK 465 ILE R -124 REMARK 465 ALA R -123 REMARK 465 LEU R -122 REMARK 465 SER R -121 REMARK 465 TYR R -120 REMARK 465 ILE R -119 REMARK 465 PHE R -118 REMARK 465 CYS R -117 REMARK 465 LEU R -116 REMARK 465 VAL R -115 REMARK 465 PHE R -114 REMARK 465 ALA R -113 REMARK 465 ASP R -112 REMARK 465 TYR R -111 REMARK 465 LYS R -110 REMARK 465 ASP R -109 REMARK 465 ASP R -108 REMARK 465 ASP R -107 REMARK 465 ASP R -106 REMARK 465 LYS R -105 REMARK 465 ALA R -104 REMARK 465 ASP R -103 REMARK 465 LEU R -102 REMARK 465 GLU R -101 REMARK 465 ASP R -100 REMARK 465 ASN R -99 REMARK 465 TRP R -98 REMARK 465 GLU R -97 REMARK 465 THR R -96 REMARK 465 LEU R -95 REMARK 465 ASN R -94 REMARK 465 ASP R -93 REMARK 465 ASN R -92 REMARK 465 LEU R -91 REMARK 465 LYS R -90 REMARK 465 VAL R -89 REMARK 465 ILE R -88 REMARK 465 GLU R -87 REMARK 465 LYS R -86 REMARK 465 ALA R -85 REMARK 465 ASP R -84 REMARK 465 ASN R -83 REMARK 465 ALA R -82 REMARK 465 ALA R -81 REMARK 465 GLN R -80 REMARK 465 VAL R -79 REMARK 465 LYS R -78 REMARK 465 ASP R -77 REMARK 465 ALA R -76 REMARK 465 LEU R -75 REMARK 465 THR R -74 REMARK 465 LYS R -73 REMARK 465 MET R -72 REMARK 465 ARG R -71 REMARK 465 ALA R -70 REMARK 465 ALA R -69 REMARK 465 ALA R -68 REMARK 465 LEU R -67 REMARK 465 ASP R -66 REMARK 465 ALA R -65 REMARK 465 GLN R -64 REMARK 465 LYS R -63 REMARK 465 ALA R -62 REMARK 465 THR R -61 REMARK 465 PRO R -60 REMARK 465 PRO R -59 REMARK 465 LYS R -58 REMARK 465 LEU R -57 REMARK 465 GLU R -56 REMARK 465 ASP R -55 REMARK 465 LYS R -54 REMARK 465 SER R -53 REMARK 465 PRO R -52 REMARK 465 ASP R -51 REMARK 465 SER R -50 REMARK 465 PRO R -49 REMARK 465 GLU R -48 REMARK 465 MET R -47 REMARK 465 LYS R -46 REMARK 465 ASP R -45 REMARK 465 PHE R -44 REMARK 465 ARG R -43 REMARK 465 HIS R -42 REMARK 465 GLY R -41 REMARK 465 PHE R -40 REMARK 465 ASP R -39 REMARK 465 ILE R -38 REMARK 465 LEU R -37 REMARK 465 VAL R -36 REMARK 465 GLY R -35 REMARK 465 GLN R -34 REMARK 465 ILE R -33 REMARK 465 ASP R -32 REMARK 465 ASP R -31 REMARK 465 ALA R -30 REMARK 465 LEU R -29 REMARK 465 LYS R -28 REMARK 465 LEU R -27 REMARK 465 ALA R -26 REMARK 465 ASN R -25 REMARK 465 GLU R -24 REMARK 465 GLY R -23 REMARK 465 LYS R -22 REMARK 465 VAL R -21 REMARK 465 LYS R -20 REMARK 465 GLU R -19 REMARK 465 ALA R -18 REMARK 465 GLN R -17 REMARK 465 ALA R -16 REMARK 465 ALA R -15 REMARK 465 ALA R -14 REMARK 465 GLU R -13 REMARK 465 GLN R -12 REMARK 465 LEU R -11 REMARK 465 LYS R -10 REMARK 465 THR R -9 REMARK 465 THR R -8 REMARK 465 ARG R -7 REMARK 465 ASN R -6 REMARK 465 ALA R -5 REMARK 465 TYR R -4 REMARK 465 ILE R -3 REMARK 465 GLN R -2 REMARK 465 LYS R -1 REMARK 465 TYR R 0 REMARK 465 LEU R 1 REMARK 465 ALA R 2 REMARK 465 ALA R 3 REMARK 465 ILE R 4 REMARK 465 SER R 5 REMARK 465 THR R 6 REMARK 465 SER R 7 REMARK 465 ILE R 8 REMARK 465 PRO R 9 REMARK 465 VAL R 10 REMARK 465 ILE R 11 REMARK 465 SER R 12 REMARK 465 GLN R 13 REMARK 465 PRO R 14 REMARK 465 GLN R 15 REMARK 465 PHE R 16 REMARK 465 THR R 17 REMARK 465 ALA R 18 REMARK 465 MET R 19 REMARK 465 ASN R 20 REMARK 465 GLU R 21 REMARK 465 PRO R 22 REMARK 465 GLN R 23 REMARK 465 CYS R 24 REMARK 465 PHE R 25 REMARK 465 TYR R 26 REMARK 465 ASN R 27 REMARK 465 GLU R 28 REMARK 465 CYS R 328 REMARK 465 GLN R 329 REMARK 465 ARG R 330 REMARK 465 SER R 331 REMARK 465 GLU R 332 REMARK 465 ASN R 333 REMARK 465 PRO R 334 REMARK 465 THR R 335 REMARK 465 GLY R 336 REMARK 465 PRO R 337 REMARK 465 THR R 338 REMARK 465 GLU R 339 REMARK 465 GLY R 340 REMARK 465 SER R 341 REMARK 465 ASP R 342 REMARK 465 ARG R 343 REMARK 465 SER R 344 REMARK 465 ALA R 345 REMARK 465 SER R 346 REMARK 465 SER R 347 REMARK 465 LEU R 348 REMARK 465 ASN R 349 REMARK 465 HIS R 350 REMARK 465 THR R 351 REMARK 465 ILE R 352 REMARK 465 LEU R 353 REMARK 465 ALA R 354 REMARK 465 GLY R 355 REMARK 465 VAL R 356 REMARK 465 HIS R 357 REMARK 465 SER R 358 REMARK 465 ASN R 359 REMARK 465 ASP R 360 REMARK 465 HIS R 361 REMARK 465 SER R 362 REMARK 465 VAL R 363 REMARK 465 VAL R 364 REMARK 465 VAL R 365 REMARK 465 PHE R 366 REMARK 465 THR R 367 REMARK 465 LEU R 368 REMARK 465 GLU R 369 REMARK 465 ASP R 370 REMARK 465 PHE R 371 REMARK 465 VAL R 372 REMARK 465 GLY R 373 REMARK 465 ASP R 374 REMARK 465 TRP R 375 REMARK 465 GLU R 376 REMARK 465 GLN R 377 REMARK 465 THR R 378 REMARK 465 ALA R 379 REMARK 465 ALA R 380 REMARK 465 TYR R 381 REMARK 465 ASN R 382 REMARK 465 LEU R 383 REMARK 465 ASP R 384 REMARK 465 GLN R 385 REMARK 465 VAL R 386 REMARK 465 LEU R 387 REMARK 465 GLU R 388 REMARK 465 GLN R 389 REMARK 465 GLY R 390 REMARK 465 GLY R 391 REMARK 465 VAL R 392 REMARK 465 SER R 393 REMARK 465 SER R 394 REMARK 465 LEU R 395 REMARK 465 LEU R 396 REMARK 465 GLN R 397 REMARK 465 ASN R 398 REMARK 465 LEU R 399 REMARK 465 ALA R 400 REMARK 465 VAL R 401 REMARK 465 SER R 402 REMARK 465 VAL R 403 REMARK 465 THR R 404 REMARK 465 PRO R 405 REMARK 465 ILE R 406 REMARK 465 GLN R 407 REMARK 465 ARG R 408 REMARK 465 ILE R 409 REMARK 465 VAL R 410 REMARK 465 ARG R 411 REMARK 465 SER R 412 REMARK 465 GLY R 413 REMARK 465 GLU R 414 REMARK 465 ASN R 415 REMARK 465 ALA R 416 REMARK 465 LEU R 417 REMARK 465 LYS R 418 REMARK 465 ILE R 419 REMARK 465 ASP R 420 REMARK 465 ILE R 421 REMARK 465 HIS R 422 REMARK 465 VAL R 423 REMARK 465 ILE R 424 REMARK 465 ILE R 425 REMARK 465 PRO R 426 REMARK 465 TYR R 427 REMARK 465 GLU R 428 REMARK 465 GLY R 429 REMARK 465 LEU R 430 REMARK 465 SER R 431 REMARK 465 ALA R 432 REMARK 465 ASP R 433 REMARK 465 GLN R 434 REMARK 465 MET R 435 REMARK 465 ALA R 436 REMARK 465 GLN R 437 REMARK 465 ILE R 438 REMARK 465 GLU R 439 REMARK 465 GLU R 440 REMARK 465 VAL R 441 REMARK 465 PHE R 442 REMARK 465 LYS R 443 REMARK 465 VAL R 444 REMARK 465 VAL R 445 REMARK 465 TYR R 446 REMARK 465 PRO R 447 REMARK 465 VAL R 448 REMARK 465 ASP R 449 REMARK 465 ASP R 450 REMARK 465 HIS R 451 REMARK 465 HIS R 452 REMARK 465 PHE R 453 REMARK 465 LYS R 454 REMARK 465 VAL R 455 REMARK 465 ILE R 456 REMARK 465 LEU R 457 REMARK 465 PRO R 458 REMARK 465 TYR R 459 REMARK 465 GLY R 460 REMARK 465 THR R 461 REMARK 465 LEU R 462 REMARK 465 VAL R 463 REMARK 465 ILE R 464 REMARK 465 ASP R 465 REMARK 465 GLY R 466 REMARK 465 VAL R 467 REMARK 465 THR R 468 REMARK 465 PRO R 469 REMARK 465 ASN R 470 REMARK 465 MET R 471 REMARK 465 LEU R 472 REMARK 465 ASN R 473 REMARK 465 TYR R 474 REMARK 465 PHE R 475 REMARK 465 GLY R 476 REMARK 465 ARG R 477 REMARK 465 PRO R 478 REMARK 465 TYR R 479 REMARK 465 GLU R 480 REMARK 465 GLY R 481 REMARK 465 ILE R 482 REMARK 465 ALA R 483 REMARK 465 VAL R 484 REMARK 465 PHE R 485 REMARK 465 ASP R 486 REMARK 465 GLY R 487 REMARK 465 LYS R 488 REMARK 465 LYS R 489 REMARK 465 ILE R 490 REMARK 465 THR R 491 REMARK 465 VAL R 492 REMARK 465 THR R 493 REMARK 465 GLY R 494 REMARK 465 THR R 495 REMARK 465 LEU R 496 REMARK 465 TRP R 497 REMARK 465 ASN R 498 REMARK 465 GLY R 499 REMARK 465 ASN R 500 REMARK 465 LYS R 501 REMARK 465 ILE R 502 REMARK 465 ILE R 503 REMARK 465 ASP R 504 REMARK 465 GLU R 505 REMARK 465 ARG R 506 REMARK 465 LEU R 507 REMARK 465 ILE R 508 REMARK 465 THR R 509 REMARK 465 PRO R 510 REMARK 465 ASP R 511 REMARK 465 GLY R 512 REMARK 465 SER R 513 REMARK 465 MET R 514 REMARK 465 LEU R 515 REMARK 465 PHE R 516 REMARK 465 ARG R 517 REMARK 465 VAL R 518 REMARK 465 THR R 519 REMARK 465 ILE R 520 REMARK 465 ASN R 521 REMARK 465 SER R 522 REMARK 465 SER A 3 REMARK 465 THR A 4 REMARK 465 VAL A 5 REMARK 465 SER A 6 REMARK 465 ALA A 7 REMARK 465 ILE A 56 REMARK 465 HIS A 57 REMARK 465 GLY A 58 REMARK 465 GLY A 59 REMARK 465 SER A 60 REMARK 465 GLY A 61 REMARK 465 GLY A 62 REMARK 465 SER A 63 REMARK 465 GLY A 64 REMARK 465 GLY A 65 REMARK 465 THR A 66 REMARK 465 MET B -15 REMARK 465 HIS B -14 REMARK 465 HIS B -13 REMARK 465 HIS B -12 REMARK 465 HIS B -11 REMARK 465 HIS B -10 REMARK 465 HIS B -9 REMARK 465 HIS B -8 REMARK 465 HIS B -7 REMARK 465 GLU B -6 REMARK 465 ASN B -5 REMARK 465 LEU B -4 REMARK 465 TYR B -3 REMARK 465 PHE B -2 REMARK 465 GLN B -1 REMARK 465 GLY B 0 REMARK 465 SER B 1 REMARK 465 GLY B 341 REMARK 465 GLY B 342 REMARK 465 SER B 343 REMARK 465 GLY B 344 REMARK 465 GLY B 345 REMARK 465 GLY B 346 REMARK 465 GLY B 347 REMARK 465 SER B 348 REMARK 465 GLY B 349 REMARK 465 GLY B 350 REMARK 465 SER B 351 REMARK 465 SER B 352 REMARK 465 SER B 353 REMARK 465 GLY B 354 REMARK 465 GLY B 355 REMARK 465 VAL B 356 REMARK 465 SER B 357 REMARK 465 GLY B 358 REMARK 465 TRP B 359 REMARK 465 ARG B 360 REMARK 465 LEU B 361 REMARK 465 PHE B 362 REMARK 465 LYS B 363 REMARK 465 LYS B 364 REMARK 465 ILE B 365 REMARK 465 SER B 366 REMARK 465 ALA C 2 REMARK 465 SER C 3 REMARK 465 ASN C 4 REMARK 465 ASN C 5 REMARK 465 LYS C 65 REMARK 465 PHE C 66 REMARK 465 PHE C 67 REMARK 465 CYS C 68 REMARK 465 ALA C 69 REMARK 465 ILE C 70 REMARK 465 LEU C 71 REMARK 465 ASP S 1 REMARK 465 GLY S 121A REMARK 465 GLY S 121B REMARK 465 GLY S 121C REMARK 465 GLY S 121D REMARK 465 SER S 121E REMARK 465 GLY S 121F REMARK 465 GLY S 121G REMARK 465 GLY S 121H REMARK 465 GLY S 121I REMARK 465 SER S 121J REMARK 465 GLY S 121K REMARK 465 GLY S 121L REMARK 465 GLY S 121M REMARK 465 GLY S 121N REMARK 465 LYS S 236 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 ARG R 78 CG CD NE CZ NH1 NH2 REMARK 470 ARG R 238 CG CD NE CZ NH1 NH2 REMARK 470 SER R 244 OG REMARK 470 ASN R 249 CG OD1 ND2 REMARK 470 GLN R 286 CG CD OE1 NE2 REMARK 470 ASP R 288 CG OD1 OD2 REMARK 470 LYS R 316 CG CD CE NZ REMARK 470 GLU R 317 CG CD OE1 OE2 REMARK 470 CYS R 327 CB SG REMARK 470 ASP A 9 CG OD1 OD2 REMARK 470 ARG A 15 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 93 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 95 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 132 CG CD NE CZ NH1 NH2 REMARK 470 LEU A 148 CG CD1 CD2 REMARK 470 LEU A 149 CG CD1 CD2 REMARK 470 GLU A 150 CG CD OE1 OE2 REMARK 470 GLU A 151 CG CD OE1 OE2 REMARK 470 LYS A 159 CG CD CE NZ REMARK 470 ASP A 160 CG OD1 OD2 REMARK 470 GLU A 164 CG CD OE1 OE2 REMARK 470 GLU A 166 CG CD OE1 OE2 REMARK 470 ARG A 173 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 174 CG OD1 OD2 REMARK 470 LYS A 177 CG CD CE NZ REMARK 470 GLN A 191 CG CD OE1 NE2 REMARK 470 GLN A 192 CG CD OE1 NE2 REMARK 470 ASP B 312 CG OD1 OD2 REMARK 470 ARG C 62 CG CD NE CZ NH1 NH2 REMARK 470 GLU S 6 CG CD OE1 OE2 REMARK 470 GLU S 42 CG CD OE1 OE2 REMARK 470 ASP S 62 CG OD1 OD2 REMARK 470 LYS S 76 CG CD CE NZ REMARK 470 GLU S 89 CG CD OE1 OE2 REMARK 470 SER S 121 OG REMARK 470 SER S 124 OG REMARK 470 THR S 132 OG1 CG2 REMARK 470 SER S 134 OG REMARK 470 GLU S 141 CG CD OE1 OE2 REMARK 470 ARG S 148 CG CD NE CZ NH1 NH2 REMARK 470 SER S 152 OG REMARK 470 ARG S 206 CG CD NE CZ NH1 NH2 REMARK 470 GLU S 208 CG CD OE1 OE2 REMARK 470 GLU S 234 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 OG SER B 331 OD1 ASP B 333 2.11 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 ARG R 158 32.40 -95.05 REMARK 500 MET R 239 52.38 -92.33 REMARK 500 PRO R 246 65.63 -68.48 REMARK 500 ARG R 248 -146.80 68.21 REMARK 500 ASN R 249 -159.97 72.42 REMARK 500 GLN R 286 53.22 -91.84 REMARK 500 GLN A 154 -8.65 74.30 REMARK 500 ALA A 202 30.18 -87.10 REMARK 500 ASN A 204 -8.95 73.22 REMARK 500 LEU B 190 148.43 -170.31 REMARK 500 ARG B 197 -10.28 -142.54 REMARK 500 CYS B 204 49.65 -81.91 REMARK 500 PHE B 292 -0.34 75.78 REMARK 500 ALA S 131 56.87 -96.82 REMARK 500 MET S 180 -10.21 72.14 REMARK 500 THR S 198 -39.66 -132.24 REMARK 500 PRO S 224 76.14 -64.38 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-61033 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF LPA1-G13 COMPLEX WITH LPA DBREF 9IZH R -104 0 UNP P0ABE7 C562_ECOLX 23 127 DBREF 9IZH R 2 364 UNP Q92633 LPAR1_HUMAN 2 364 DBREF 9IZH R 365 522 PDB 9IZH 9IZH 365 522 DBREF 9IZH A 3 230 PDB 9IZH 9IZH 3 230 DBREF 9IZH B 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 9IZH C 2 71 UNP P63213 GBG2_MOUSE 2 71 DBREF 9IZH S 1 236 PDB 9IZH 9IZH 1 236 SEQADV 9IZH MET R -128 UNP P0ABE7 INITIATING METHIONINE SEQADV 9IZH LYS R -127 UNP P0ABE7 EXPRESSION TAG SEQADV 9IZH THR R -126 UNP P0ABE7 EXPRESSION TAG SEQADV 9IZH ILE R -125 UNP P0ABE7 EXPRESSION TAG SEQADV 9IZH ILE R -124 UNP P0ABE7 EXPRESSION TAG SEQADV 9IZH ALA R -123 UNP P0ABE7 EXPRESSION TAG SEQADV 9IZH LEU R -122 UNP P0ABE7 EXPRESSION TAG SEQADV 9IZH SER R -121 UNP P0ABE7 EXPRESSION TAG SEQADV 9IZH TYR R -120 UNP P0ABE7 EXPRESSION TAG SEQADV 9IZH ILE R -119 UNP P0ABE7 EXPRESSION TAG SEQADV 9IZH PHE R -118 UNP P0ABE7 EXPRESSION TAG SEQADV 9IZH CYS R -117 UNP P0ABE7 EXPRESSION TAG SEQADV 9IZH LEU R -116 UNP P0ABE7 EXPRESSION TAG SEQADV 9IZH VAL R -115 UNP P0ABE7 EXPRESSION TAG SEQADV 9IZH PHE R -114 UNP P0ABE7 EXPRESSION TAG SEQADV 9IZH ALA R -113 UNP P0ABE7 EXPRESSION TAG SEQADV 9IZH ASP R -112 UNP P0ABE7 EXPRESSION TAG SEQADV 9IZH TYR R -111 UNP P0ABE7 EXPRESSION TAG SEQADV 9IZH LYS R -110 UNP P0ABE7 EXPRESSION TAG SEQADV 9IZH ASP R -109 UNP P0ABE7 EXPRESSION TAG SEQADV 9IZH ASP R -108 UNP P0ABE7 EXPRESSION TAG SEQADV 9IZH ASP R -107 UNP P0ABE7 EXPRESSION TAG SEQADV 9IZH ASP R -106 UNP P0ABE7 EXPRESSION TAG SEQADV 9IZH LYS R -105 UNP P0ABE7 EXPRESSION TAG SEQADV 9IZH TRP R -98 UNP P0ABE7 MET 29 CONFLICT SEQADV 9IZH ILE R -3 UNP P0ABE7 HIS 124 CONFLICT SEQADV 9IZH LEU R 1 UNP P0ABE7 LINKER SEQADV 9IZH MET B -15 UNP P62873 INITIATING METHIONINE SEQADV 9IZH HIS B -14 UNP P62873 EXPRESSION TAG SEQADV 9IZH HIS B -13 UNP P62873 EXPRESSION TAG SEQADV 9IZH HIS B -12 UNP P62873 EXPRESSION TAG SEQADV 9IZH HIS B -11 UNP P62873 EXPRESSION TAG SEQADV 9IZH HIS B -10 UNP P62873 EXPRESSION TAG SEQADV 9IZH HIS B -9 UNP P62873 EXPRESSION TAG SEQADV 9IZH HIS B -8 UNP P62873 EXPRESSION TAG SEQADV 9IZH HIS B -7 UNP P62873 EXPRESSION TAG SEQADV 9IZH GLU B -6 UNP P62873 EXPRESSION TAG SEQADV 9IZH ASN B -5 UNP P62873 EXPRESSION TAG SEQADV 9IZH LEU B -4 UNP P62873 EXPRESSION TAG SEQADV 9IZH TYR B -3 UNP P62873 EXPRESSION TAG SEQADV 9IZH PHE B -2 UNP P62873 EXPRESSION TAG SEQADV 9IZH GLN B -1 UNP P62873 EXPRESSION TAG SEQADV 9IZH GLY B 0 UNP P62873 EXPRESSION TAG SEQADV 9IZH SER B 1 UNP P62873 EXPRESSION TAG SEQADV 9IZH GLY B 341 UNP P62873 EXPRESSION TAG SEQADV 9IZH GLY B 342 UNP P62873 EXPRESSION TAG SEQADV 9IZH SER B 343 UNP P62873 EXPRESSION TAG SEQADV 9IZH GLY B 344 UNP P62873 EXPRESSION TAG SEQADV 9IZH GLY B 345 UNP P62873 EXPRESSION TAG SEQADV 9IZH GLY B 346 UNP P62873 EXPRESSION TAG SEQADV 9IZH GLY B 347 UNP P62873 EXPRESSION TAG SEQADV 9IZH SER B 348 UNP P62873 EXPRESSION TAG SEQADV 9IZH GLY B 349 UNP P62873 EXPRESSION TAG SEQADV 9IZH GLY B 350 UNP P62873 EXPRESSION TAG SEQADV 9IZH SER B 351 UNP P62873 EXPRESSION TAG SEQADV 9IZH SER B 352 UNP P62873 EXPRESSION TAG SEQADV 9IZH SER B 353 UNP P62873 EXPRESSION TAG SEQADV 9IZH GLY B 354 UNP P62873 EXPRESSION TAG SEQADV 9IZH GLY B 355 UNP P62873 EXPRESSION TAG SEQADV 9IZH VAL B 356 UNP P62873 EXPRESSION TAG SEQADV 9IZH SER B 357 UNP P62873 EXPRESSION TAG SEQADV 9IZH GLY B 358 UNP P62873 EXPRESSION TAG SEQADV 9IZH TRP B 359 UNP P62873 EXPRESSION TAG SEQADV 9IZH ARG B 360 UNP P62873 EXPRESSION TAG SEQADV 9IZH LEU B 361 UNP P62873 EXPRESSION TAG SEQADV 9IZH PHE B 362 UNP P62873 EXPRESSION TAG SEQADV 9IZH LYS B 363 UNP P62873 EXPRESSION TAG SEQADV 9IZH LYS B 364 UNP P62873 EXPRESSION TAG SEQADV 9IZH ILE B 365 UNP P62873 EXPRESSION TAG SEQADV 9IZH SER B 366 UNP P62873 EXPRESSION TAG SEQRES 1 R 651 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU SEQRES 2 R 651 VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP LYS ALA ASP SEQRES 3 R 651 LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS SEQRES 4 R 651 VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP SEQRES 5 R 651 ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN SEQRES 6 R 651 LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SEQRES 7 R 651 SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE SEQRES 8 R 651 LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN SEQRES 9 R 651 GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN SEQRES 10 R 651 LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU SEQRES 11 R 651 ALA ALA ILE SER THR SER ILE PRO VAL ILE SER GLN PRO SEQRES 12 R 651 GLN PHE THR ALA MET ASN GLU PRO GLN CYS PHE TYR ASN SEQRES 13 R 651 GLU SER ILE ALA PHE PHE TYR ASN ARG SER GLY LYS HIS SEQRES 14 R 651 LEU ALA THR GLU TRP ASN THR VAL SER LYS LEU VAL MET SEQRES 15 R 651 GLY LEU GLY ILE THR VAL CYS ILE PHE ILE MET LEU ALA SEQRES 16 R 651 ASN LEU LEU VAL MET VAL ALA ILE TYR VAL ASN ARG ARG SEQRES 17 R 651 PHE HIS PHE PRO ILE TYR TYR LEU MET ALA ASN LEU ALA SEQRES 18 R 651 ALA ALA ASP PHE PHE ALA GLY LEU ALA TYR PHE TYR LEU SEQRES 19 R 651 MET PHE ASN THR GLY PRO ASN THR ARG ARG LEU THR VAL SEQRES 20 R 651 SER THR TRP LEU LEU ARG GLN GLY LEU ILE ASP THR SER SEQRES 21 R 651 LEU THR ALA SER VAL ALA ASN LEU LEU ALA ILE ALA ILE SEQRES 22 R 651 GLU ARG HIS ILE THR VAL PHE ARG MET GLN LEU HIS THR SEQRES 23 R 651 ARG MET SER ASN ARG ARG VAL VAL VAL VAL ILE VAL VAL SEQRES 24 R 651 ILE TRP THR MET ALA ILE VAL MET GLY ALA ILE PRO SER SEQRES 25 R 651 VAL GLY TRP ASN CYS ILE CYS ASP ILE GLU ASN CYS SER SEQRES 26 R 651 ASN MET ALA PRO LEU TYR SER ASP SER TYR LEU VAL PHE SEQRES 27 R 651 TRP ALA ILE PHE ASN LEU VAL THR PHE VAL VAL MET VAL SEQRES 28 R 651 VAL LEU TYR ALA HIS ILE PHE GLY TYR VAL ARG GLN ARG SEQRES 29 R 651 THR MET ARG MET SER ARG HIS SER SER GLY PRO ARG ARG SEQRES 30 R 651 ASN ARG ASP THR MET MET SER LEU LEU LYS THR VAL VAL SEQRES 31 R 651 ILE VAL LEU GLY ALA PHE ILE ILE CYS TRP THR PRO GLY SEQRES 32 R 651 LEU VAL LEU LEU LEU LEU ASP VAL CYS CYS PRO GLN CYS SEQRES 33 R 651 ASP VAL LEU ALA TYR GLU LYS PHE PHE LEU LEU LEU ALA SEQRES 34 R 651 GLU PHE ASN SER ALA MET ASN PRO ILE ILE TYR SER TYR SEQRES 35 R 651 ARG ASP LYS GLU MET SER ALA THR PHE ARG GLN ILE LEU SEQRES 36 R 651 CYS CYS GLN ARG SER GLU ASN PRO THR GLY PRO THR GLU SEQRES 37 R 651 GLY SER ASP ARG SER ALA SER SER LEU ASN HIS THR ILE SEQRES 38 R 651 LEU ALA GLY VAL HIS SER ASN ASP HIS SER VAL VAL VAL SEQRES 39 R 651 PHE THR LEU GLU ASP PHE VAL GLY ASP TRP GLU GLN THR SEQRES 40 R 651 ALA ALA TYR ASN LEU ASP GLN VAL LEU GLU GLN GLY GLY SEQRES 41 R 651 VAL SER SER LEU LEU GLN ASN LEU ALA VAL SER VAL THR SEQRES 42 R 651 PRO ILE GLN ARG ILE VAL ARG SER GLY GLU ASN ALA LEU SEQRES 43 R 651 LYS ILE ASP ILE HIS VAL ILE ILE PRO TYR GLU GLY LEU SEQRES 44 R 651 SER ALA ASP GLN MET ALA GLN ILE GLU GLU VAL PHE LYS SEQRES 45 R 651 VAL VAL TYR PRO VAL ASP ASP HIS HIS PHE LYS VAL ILE SEQRES 46 R 651 LEU PRO TYR GLY THR LEU VAL ILE ASP GLY VAL THR PRO SEQRES 47 R 651 ASN MET LEU ASN TYR PHE GLY ARG PRO TYR GLU GLY ILE SEQRES 48 R 651 ALA VAL PHE ASP GLY LYS LYS ILE THR VAL THR GLY THR SEQRES 49 R 651 LEU TRP ASN GLY ASN LYS ILE ILE ASP GLU ARG LEU ILE SEQRES 50 R 651 THR PRO ASP GLY SER MET LEU PHE ARG VAL THR ILE ASN SEQRES 51 R 651 SER SEQRES 1 A 228 SER THR VAL SER ALA GLU ASP LYS ALA ALA ALA GLU ARG SEQRES 2 A 228 SER LYS GLU ILE ASP LYS CYS LEU SER ARG GLU LYS THR SEQRES 3 A 228 TYR VAL LYS ARG LEU VAL LYS ILE LEU LEU LEU GLY ALA SEQRES 4 A 228 ASP ASN SER GLY LYS SER THR PHE LEU LYS GLN MET ARG SEQRES 5 A 228 ILE ILE HIS GLY GLY SER GLY GLY SER GLY GLY THR LYS SEQRES 6 A 228 GLY ILE HIS GLU TYR ASP PHE GLU ILE LYS ASN VAL PRO SEQRES 7 A 228 PHE LYS MET VAL ASP VAL GLY GLY GLN ARG SER GLU ARG SEQRES 8 A 228 LYS ARG TRP PHE GLU CYS PHE ASP SER VAL THR SER ILE SEQRES 9 A 228 LEU PHE LEU VAL ASP SER SER ASP PHE ASN ARG LEU THR SEQRES 10 A 228 GLU SER LEU ASN ASP PHE GLU THR ILE VAL ASN ASN ARG SEQRES 11 A 228 VAL PHE SER ASN VAL SER ILE ILE LEU PHE LEU ASN LYS SEQRES 12 A 228 THR ASP LEU LEU GLU GLU LYS VAL GLN ILE VAL SER ILE SEQRES 13 A 228 LYS ASP TYR PHE LEU GLU PHE GLU GLY ASP PRO HIS CYS SEQRES 14 A 228 LEU ARG ASP VAL GLN LYS PHE LEU VAL GLU CYS PHE ARG SEQRES 15 A 228 ASN LYS ARG ARG ASP GLN GLN GLN LYS PRO LEU TYR HIS SEQRES 16 A 228 HIS PHE THR THR ALA ILE ASN THR GLU ASN ALA ARG LEU SEQRES 17 A 228 ILE PHE ARG ASP VAL LYS ASP THR ILE LEU HIS ASP ASN SEQRES 18 A 228 LEU LYS GLN LEU MET LEU GLN SEQRES 1 B 382 MET HIS HIS HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR SEQRES 2 B 382 PHE GLN GLY SER SER GLU LEU ASP GLN LEU ARG GLN GLU SEQRES 3 B 382 ALA GLU GLN LEU LYS ASN GLN ILE ARG ASP ALA ARG LYS SEQRES 4 B 382 ALA CYS ALA ASP ALA THR LEU SER GLN ILE THR ASN ASN SEQRES 5 B 382 ILE ASP PRO VAL GLY ARG ILE GLN MET ARG THR ARG ARG SEQRES 6 B 382 THR LEU ARG GLY HIS LEU ALA LYS ILE TYR ALA MET HIS SEQRES 7 B 382 TRP GLY THR ASP SER ARG LEU LEU VAL SER ALA SER GLN SEQRES 8 B 382 ASP GLY LYS LEU ILE ILE TRP ASP SER TYR THR THR ASN SEQRES 9 B 382 LYS VAL HIS ALA ILE PRO LEU ARG SER SER TRP VAL MET SEQRES 10 B 382 THR CYS ALA TYR ALA PRO SER GLY ASN TYR VAL ALA CYS SEQRES 11 B 382 GLY GLY LEU ASP ASN ILE CYS SER ILE TYR ASN LEU LYS SEQRES 12 B 382 THR ARG GLU GLY ASN VAL ARG VAL SER ARG GLU LEU ALA SEQRES 13 B 382 GLY HIS THR GLY TYR LEU SER CYS CYS ARG PHE LEU ASP SEQRES 14 B 382 ASP ASN GLN ILE VAL THR SER SER GLY ASP THR THR CYS SEQRES 15 B 382 ALA LEU TRP ASP ILE GLU THR GLY GLN GLN THR THR THR SEQRES 16 B 382 PHE THR GLY HIS THR GLY ASP VAL MET SER LEU SER LEU SEQRES 17 B 382 ALA PRO ASP THR ARG LEU PHE VAL SER GLY ALA CYS ASP SEQRES 18 B 382 ALA SER ALA LYS LEU TRP ASP VAL ARG GLU GLY MET CYS SEQRES 19 B 382 ARG GLN THR PHE THR GLY HIS GLU SER ASP ILE ASN ALA SEQRES 20 B 382 ILE CYS PHE PHE PRO ASN GLY ASN ALA PHE ALA THR GLY SEQRES 21 B 382 SER ASP ASP ALA THR CYS ARG LEU PHE ASP LEU ARG ALA SEQRES 22 B 382 ASP GLN GLU LEU MET THR TYR SER HIS ASP ASN ILE ILE SEQRES 23 B 382 CYS GLY ILE THR SER VAL SER PHE SER LYS SER GLY ARG SEQRES 24 B 382 LEU LEU LEU ALA GLY TYR ASP ASP PHE ASN CYS ASN VAL SEQRES 25 B 382 TRP ASP ALA LEU LYS ALA ASP ARG ALA GLY VAL LEU ALA SEQRES 26 B 382 GLY HIS ASP ASN ARG VAL SER CYS LEU GLY VAL THR ASP SEQRES 27 B 382 ASP GLY MET ALA VAL ALA THR GLY SER TRP ASP SER PHE SEQRES 28 B 382 LEU LYS ILE TRP ASN GLY GLY SER GLY GLY GLY GLY SER SEQRES 29 B 382 GLY GLY SER SER SER GLY GLY VAL SER GLY TRP ARG LEU SEQRES 30 B 382 PHE LYS LYS ILE SER SEQRES 1 C 70 ALA SER ASN ASN THR ALA SER ILE ALA GLN ALA ARG LYS SEQRES 2 C 70 LEU VAL GLU GLN LEU LYS MET GLU ALA ASN ILE ASP ARG SEQRES 3 C 70 ILE LYS VAL SER LYS ALA ALA ALA ASP LEU MET ALA TYR SEQRES 4 C 70 CYS GLU ALA HIS ALA LYS GLU ASP PRO LEU LEU THR PRO SEQRES 5 C 70 VAL PRO ALA SER GLU ASN PRO PHE ARG GLU LYS LYS PHE SEQRES 6 C 70 PHE CYS ALA ILE LEU SEQRES 1 S 248 ASP VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 S 248 PRO GLY GLY SER ARG LYS LEU SER CYS SER ALA SER GLY SEQRES 3 S 248 PHE ALA PHE SER SER PHE GLY MET HIS TRP VAL ARG GLN SEQRES 4 S 248 ALA PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SEQRES 5 S 248 SER GLY SER GLY THR ILE TYR TYR ALA ASP THR VAL LYS SEQRES 6 S 248 GLY ARG PHE THR ILE SER ARG ASP ASP PRO LYS ASN THR SEQRES 7 S 248 LEU PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR SEQRES 8 S 248 ALA MET TYR TYR CYS VAL ARG SER ILE TYR TYR TYR GLY SEQRES 9 S 248 SER SER PRO PHE ASP PHE TRP GLY GLN GLY THR THR LEU SEQRES 10 S 248 THR VAL SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SEQRES 11 S 248 SER GLY GLY GLY GLY SER ASP ILE VAL MET THR GLN ALA SEQRES 12 S 248 THR SER SER VAL PRO VAL THR PRO GLY GLU SER VAL SER SEQRES 13 S 248 ILE SER CYS ARG SER SER LYS SER LEU LEU HIS SER ASN SEQRES 14 S 248 GLY ASN THR TYR LEU TYR TRP PHE LEU GLN ARG PRO GLY SEQRES 15 S 248 GLN SER PRO GLN LEU LEU ILE TYR ARG MET SER ASN LEU SEQRES 16 S 248 ALA SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SER SEQRES 17 S 248 GLY THR ALA PHE THR LEU THR ILE SER ARG LEU GLU ALA SEQRES 18 S 248 GLU ASP VAL GLY VAL TYR TYR CYS MET GLN HIS LEU GLU SEQRES 19 S 248 TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU LEU SEQRES 20 S 248 LYS HET NKP R 601 29 HETNAM NKP (2R)-2-HYDROXY-3-(PHOSPHONOOXY)PROPYL (9E)-OCTADEC-9- HETNAM 2 NKP ENOATE HETSYN NKP 18:1 LPA; OLEOYL LYSOPHOSPHATIDIC ACID FORMUL 6 NKP C21 H41 O7 P HELIX 1 AA1 SER R 29 SER R 37 1 9 HELIX 2 AA2 ASN R 46 ASN R 77 1 32 HELIX 3 AA3 ARG R 78 HIS R 81 5 4 HELIX 4 AA4 PHE R 82 ASN R 108 1 27 HELIX 5 AA5 THR R 117 THR R 149 1 33 HELIX 6 AA6 LEU R 155 MET R 159 5 5 HELIX 7 AA7 ASN R 161 ILE R 181 1 21 HELIX 8 AA8 PRO R 182 VAL R 184 5 3 HELIX 9 AA9 SER R 203 MET R 239 1 37 HELIX 10 AB1 ASN R 249 LEU R 256 1 8 HELIX 11 AB2 LEU R 256 CYS R 284 1 29 HELIX 12 AB3 TYR R 292 PHE R 302 1 11 HELIX 13 AB4 PHE R 302 ASN R 307 1 6 HELIX 14 AB5 ASP R 315 LEU R 326 1 12 HELIX 15 AB6 ASP A 9 LYS A 31 1 23 HELIX 16 AB7 GLY A 45 GLN A 52 1 8 HELIX 17 AB8 GLY A 87 GLU A 92 5 6 HELIX 18 AB9 ASP A 114 ASN A 130 1 17 HELIX 19 AC1 LYS A 145 VAL A 153 1 9 HELIX 20 AC2 CYS A 171 ASN A 185 1 15 HELIX 21 AC3 GLU A 206 LEU A 227 1 22 HELIX 22 AC4 GLU B 3 ALA B 26 1 24 HELIX 23 AC5 THR B 29 THR B 34 1 6 HELIX 24 AC6 SER C 8 ASN C 24 1 17 HELIX 25 AC7 LYS C 29 HIS C 44 1 16 HELIX 26 AC8 ALA C 45 ASP C 48 5 4 HELIX 27 AC9 ALA S 28 PHE S 32 5 5 HELIX 28 AD1 GLU S 208 VAL S 212 5 5 SHEET 1 AA1 6 HIS A 70 ILE A 76 0 SHEET 2 AA1 6 VAL A 79 ASP A 85 -1 O PHE A 81 N PHE A 74 SHEET 3 AA1 6 VAL A 34 LEU A 39 1 N ILE A 36 O VAL A 84 SHEET 4 AA1 6 SER A 105 ASP A 111 1 O LEU A 107 N LEU A 37 SHEET 5 AA1 6 SER A 138 ASN A 144 1 O ILE A 140 N ILE A 106 SHEET 6 AA1 6 LEU A 195 HIS A 198 1 O TYR A 196 N ILE A 139 SHEET 1 AA2 4 THR B 47 LEU B 51 0 SHEET 2 AA2 4 LEU B 336 TRP B 339 -1 O ILE B 338 N ARG B 48 SHEET 3 AA2 4 VAL B 327 SER B 331 -1 N VAL B 327 O TRP B 339 SHEET 4 AA2 4 VAL B 315 VAL B 320 -1 N GLY B 319 O ALA B 328 SHEET 1 AA3 4 ILE B 58 TRP B 63 0 SHEET 2 AA3 4 LEU B 69 SER B 74 -1 O ALA B 73 N ALA B 60 SHEET 3 AA3 4 LYS B 78 ASP B 83 -1 O TRP B 82 N LEU B 70 SHEET 4 AA3 4 ASN B 88 PRO B 94 -1 O ILE B 93 N LEU B 79 SHEET 1 AA4 4 VAL B 100 TYR B 105 0 SHEET 2 AA4 4 TYR B 111 GLY B 116 -1 O ALA B 113 N ALA B 104 SHEET 3 AA4 4 CYS B 121 ASN B 125 -1 O TYR B 124 N VAL B 112 SHEET 4 AA4 4 ARG B 134 LEU B 139 -1 O SER B 136 N ILE B 123 SHEET 1 AA5 4 LEU B 146 ASP B 153 0 SHEET 2 AA5 4 GLN B 156 SER B 161 -1 O GLN B 156 N LEU B 152 SHEET 3 AA5 4 THR B 165 ASP B 170 -1 O ALA B 167 N THR B 159 SHEET 4 AA5 4 GLN B 175 PHE B 180 -1 O PHE B 180 N CYS B 166 SHEET 1 AA6 4 SER B 191 LEU B 192 0 SHEET 2 AA6 4 LEU B 198 GLY B 202 -1 O VAL B 200 N SER B 191 SHEET 3 AA6 4 SER B 207 ASP B 212 -1 O TRP B 211 N PHE B 199 SHEET 4 AA6 4 GLN B 220 THR B 223 -1 O PHE B 222 N ALA B 208 SHEET 1 AA7 4 ILE B 229 PHE B 234 0 SHEET 2 AA7 4 ALA B 240 SER B 245 -1 O ALA B 242 N CYS B 233 SHEET 3 AA7 4 CYS B 250 ASP B 254 -1 O ARG B 251 N THR B 243 SHEET 4 AA7 4 GLU B 260 TYR B 264 -1 O LEU B 261 N LEU B 252 SHEET 1 AA8 4 ILE B 273 PHE B 278 0 SHEET 2 AA8 4 LEU B 284 TYR B 289 -1 O LEU B 286 N SER B 277 SHEET 3 AA8 4 CYS B 294 ASP B 298 -1 O ASN B 295 N ALA B 287 SHEET 4 AA8 4 ARG B 304 VAL B 307 -1 O ALA B 305 N VAL B 296 SHEET 1 AA9 4 LEU S 4 SER S 7 0 SHEET 2 AA9 4 ARG S 18 ALA S 24 -1 O SER S 23 N VAL S 5 SHEET 3 AA9 4 THR S 78 MET S 83 -1 O LEU S 81 N LEU S 20 SHEET 4 AA9 4 PHE S 68 ASP S 73 -1 N SER S 71 O PHE S 80 SHEET 1 AB1 6 LEU S 11 VAL S 12 0 SHEET 2 AB1 6 THR S 115 VAL S 119 1 O THR S 118 N VAL S 12 SHEET 3 AB1 6 ALA S 92 SER S 99 -1 N TYR S 94 O THR S 115 SHEET 4 AB1 6 GLY S 33 GLN S 39 -1 N VAL S 37 O TYR S 95 SHEET 5 AB1 6 LEU S 45 ILE S 51 -1 O GLU S 46 N ARG S 38 SHEET 6 AB1 6 ILE S 58 TYR S 60 -1 O TYR S 59 N TYR S 50 SHEET 1 AB2 4 LEU S 11 VAL S 12 0 SHEET 2 AB2 4 THR S 115 VAL S 119 1 O THR S 118 N VAL S 12 SHEET 3 AB2 4 ALA S 92 SER S 99 -1 N TYR S 94 O THR S 115 SHEET 4 AB2 4 PHE S 110 TRP S 111 -1 O PHE S 110 N ARG S 98 SHEET 1 AB3 4 MET S 128 THR S 129 0 SHEET 2 AB3 4 VAL S 143 SER S 149 -1 O ARG S 148 N THR S 129 SHEET 3 AB3 4 ALA S 199 ILE S 204 -1 O ILE S 204 N VAL S 143 SHEET 4 AB3 4 PHE S 191 GLY S 195 -1 N SER S 192 O THR S 203 SHEET 1 AB4 6 SER S 134 VAL S 135 0 SHEET 2 AB4 6 LYS S 232 LEU S 233 1 O LYS S 232 N VAL S 135 SHEET 3 AB4 6 GLY S 213 GLN S 219 -1 N GLY S 213 O LEU S 233 SHEET 4 AB4 6 LEU S 162 GLN S 167 -1 N GLN S 167 O VAL S 214 SHEET 5 AB4 6 GLN S 174 TYR S 178 -1 O LEU S 176 N TRP S 164 SHEET 6 AB4 6 ASN S 182 LEU S 183 -1 O ASN S 182 N TYR S 178 SSBOND 1 CYS R 188 CYS R 195 1555 1555 2.03 SSBOND 2 CYS R 284 CYS R 287 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