HEADER MEMBRANE PROTEIN 01-DEC-23 8X9T TITLE IDENTIFICATION, STRUCTURE AND AGONIST DESIGN OF AN ANDROGEN MEMBRANE TITLE 2 RECEPTOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: GS PROTEIN ALPHA SUBUNIT; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 7 BETA-1; COMPND 8 CHAIN: B; COMPND 9 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 13 GAMMA-2; COMPND 14 CHAIN: G; COMPND 15 SYNONYM: G GAMMA-I; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 4; COMPND 18 MOLECULE: ADHESION G-PROTEIN COUPLED RECEPTOR D1; COMPND 19 CHAIN: R; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 5; COMPND 22 MOLECULE: SCFV16; COMPND 23 CHAIN: S; COMPND 24 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 3 ORGANISM_TAXID: 9913; SOURCE 4 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 8 ORGANISM_COMMON: NORWAY RAT; SOURCE 9 ORGANISM_TAXID: 10116; SOURCE 10 GENE: GNB1; SOURCE 11 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 15 ORGANISM_COMMON: DOMESTIC CATTLE; SOURCE 16 ORGANISM_TAXID: 9913; SOURCE 17 GENE: GNG2; SOURCE 18 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 20 MOL_ID: 4; SOURCE 21 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 22 ORGANISM_COMMON: HUMAN; SOURCE 23 ORGANISM_TAXID: 9606; SOURCE 24 GENE: ADGRD1; SOURCE 25 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 27 MOL_ID: 5; SOURCE 28 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 29 ORGANISM_TAXID: 32630; SOURCE 30 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 31 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS ADHESION GPCR, GPR133, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR Y.Q.PING,Z.YANG REVDAT 1 12-FEB-25 8X9T 0 JRNL AUTH Z.YANG,Y.Q.PING,M.W.WANG,C.ZHANG,S.H.ZHOU,Y.T.XI,K.K.ZHU, JRNL AUTH 2 W.DING,Q.Y.ZHANG,Z.C.SONG,R.J.ZHAO,Z.L.HE,M.X.WANG,L.QI, JRNL AUTH 3 C.ULLMANN,A.RICKEN,T.SCHONEBERG,Z.J.GAN,X.YU,P.XIAO,F.YI, JRNL AUTH 4 I.LIEBSCHER,J.P.SUN JRNL TITL IDENTIFICATION, STRUCTURE, AND AGONIST DESIGN OF AN ANDROGEN JRNL TITL 2 MEMBRANE RECEPTOR. JRNL REF CELL 2025 JRNL REFN ISSN 1097-4172 JRNL PMID 39884271 JRNL DOI 10.1016/J.CELL.2025.01.006 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH Y.Q.PING,P.XIAO,F.YANG,R.J.ZHAO,S.C.GUO,X.YAN,X.WU,C.ZHANG, REMARK 1 AUTH 2 Y.LU,F.ZHAO,F.ZHOU,Y.T.XI,W.YIN,F.Z.LIU,D.F.HE,D.L.ZHANG, REMARK 1 AUTH 3 Z.L.ZHU,Y.JIANG,L.DU,S.Q.FENG,I.LIEBSCHER,H.E.XU,J.P.SUN REMARK 1 TITL STRUCTURAL BASIS FOR THE TETHERED PEPTIDE ACTIVATION OF REMARK 1 TITL 2 ADHESION GPCRS. REMARK 1 REF NATURE V. 604 763 2022 REMARK 1 REFN ESSN 1476-4687 REMARK 1 PMID 35418678 REMARK 1 DOI 10.1038/S41586-021-04077-Y REMARK 2 REMARK 2 RESOLUTION. 2.75 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) : 2.750 REMARK 3 NUMBER OF PARTICLES : 249492 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 8X9T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-DEC-23. REMARK 100 THE DEPOSITION ID IS D_1300042904. 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 : COMPLEX OF GPR133 WITH AGONIST REMARK 245 AND G PROTEIN TRIMER 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 : 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 : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2200.00 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) : 6000.00 REMARK 245 ILLUMINATION MODE : OTHER 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: A, B, G, R, 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 A 8 REMARK 465 GLY A 9 REMARK 465 CYS A 10 REMARK 465 THR A 11 REMARK 465 ILE A 78 REMARK 465 TYR A 79 REMARK 465 HIS A 80 REMARK 465 VAL A 81 REMARK 465 ASN A 82 REMARK 465 GLY A 83 REMARK 465 TYR A 84 REMARK 465 SER A 85 REMARK 465 GLU A 86 REMARK 465 GLU A 87 REMARK 465 GLU A 88 REMARK 465 CYS A 89 REMARK 465 LYS A 90 REMARK 465 GLN A 91 REMARK 465 TYR A 92 REMARK 465 LYS A 93 REMARK 465 ALA A 94 REMARK 465 VAL A 95 REMARK 465 VAL A 96 REMARK 465 TYR A 97 REMARK 465 SER A 98 REMARK 465 ASN A 99 REMARK 465 THR A 100 REMARK 465 ILE A 101 REMARK 465 GLN A 102 REMARK 465 SER A 103 REMARK 465 ILE A 104 REMARK 465 ILE A 105 REMARK 465 ALA A 106 REMARK 465 ILE A 107 REMARK 465 ILE A 108 REMARK 465 ARG A 109 REMARK 465 ALA A 110 REMARK 465 MET A 111 REMARK 465 GLY A 112 REMARK 465 ARG A 113 REMARK 465 LEU A 114 REMARK 465 LYS A 115 REMARK 465 ILE A 116 REMARK 465 ASP A 117 REMARK 465 PHE A 118 REMARK 465 GLY A 119 REMARK 465 ASP A 120 REMARK 465 SER A 121 REMARK 465 ALA A 122 REMARK 465 ARG A 123 REMARK 465 ALA A 124 REMARK 465 ASP A 125 REMARK 465 ASP A 126 REMARK 465 ALA A 127 REMARK 465 ARG A 128 REMARK 465 GLN A 129 REMARK 465 LEU A 130 REMARK 465 PHE A 131 REMARK 465 VAL A 132 REMARK 465 LEU A 133 REMARK 465 ALA A 134 REMARK 465 GLY A 135 REMARK 465 ALA A 136 REMARK 465 ALA A 137 REMARK 465 GLU A 138 REMARK 465 GLU A 139 REMARK 465 GLY A 140 REMARK 465 PHE A 141 REMARK 465 MET A 142 REMARK 465 THR A 143 REMARK 465 ALA A 144 REMARK 465 GLU A 145 REMARK 465 LEU A 146 REMARK 465 ALA A 147 REMARK 465 GLY A 148 REMARK 465 VAL A 149 REMARK 465 ILE A 150 REMARK 465 LYS A 151 REMARK 465 ARG A 152 REMARK 465 LEU A 153 REMARK 465 TRP A 154 REMARK 465 LYS A 155 REMARK 465 ASP A 156 REMARK 465 SER A 157 REMARK 465 GLY A 158 REMARK 465 VAL A 159 REMARK 465 GLN A 160 REMARK 465 ALA A 161 REMARK 465 CYS A 162 REMARK 465 PHE A 163 REMARK 465 ASN A 164 REMARK 465 ARG A 165 REMARK 465 SER A 166 REMARK 465 ARG A 167 REMARK 465 GLU A 168 REMARK 465 TYR A 169 REMARK 465 GLN A 170 REMARK 465 LEU A 171 REMARK 465 ASN A 172 REMARK 465 ASP A 173 REMARK 465 SER A 174 REMARK 465 ALA A 175 REMARK 465 ALA A 176 REMARK 465 TYR A 177 REMARK 465 TYR A 178 REMARK 465 LEU A 179 REMARK 465 ASN A 180 REMARK 465 ASP A 181 REMARK 465 LEU A 182 REMARK 465 ASP A 183 REMARK 465 ARG A 184 REMARK 465 ILE A 185 REMARK 465 ALA A 186 REMARK 465 GLN A 187 REMARK 465 PRO A 188 REMARK 465 ASN A 189 REMARK 465 TYR A 190 REMARK 465 ILE A 191 REMARK 465 PRO A 192 REMARK 465 THR A 193 REMARK 465 GLN A 194 REMARK 465 GLN A 195 REMARK 465 ASP A 196 REMARK 465 VAL A 197 REMARK 465 LEU A 198 REMARK 465 ARG A 199 REMARK 465 THR A 200 REMARK 465 ARG A 201 REMARK 465 VAL A 202 REMARK 465 LYS A 203 REMARK 465 THR A 204 REMARK 465 ASP A 262 REMARK 465 TYR A 263 REMARK 465 GLY B -3 REMARK 465 SER B -2 REMARK 465 LEU B -1 REMARK 465 LEU B 0 REMARK 465 GLN B 1 REMARK 465 SER B 2 REMARK 465 MET G 1 REMARK 465 ALA G 2 REMARK 465 SER G 3 REMARK 465 ASN G 4 REMARK 465 ASN G 5 REMARK 465 THR G 6 REMARK 465 ARG G 62 REMARK 465 GLU G 63 REMARK 465 LYS G 64 REMARK 465 LYS G 65 REMARK 465 PHE G 66 REMARK 465 PHE G 67 REMARK 465 CYS G 68 REMARK 465 ALA G 69 REMARK 465 ILE G 70 REMARK 465 LEU G 71 REMARK 465 HIS R 277 REMARK 465 PRO R 278 REMARK 465 ILE R 279 REMARK 465 ILE R 280 REMARK 465 THR R 281 REMARK 465 ASN R 282 REMARK 465 LEU R 283 REMARK 465 THR R 284 REMARK 465 GLU R 285 REMARK 465 GLU R 286 REMARK 465 ARG R 287 REMARK 465 LYS R 288 REMARK 465 THR R 289 REMARK 465 PHE R 290 REMARK 465 GLN R 291 REMARK 465 SER R 292 REMARK 465 PRO R 293 REMARK 465 GLY R 294 REMARK 465 VAL R 295 REMARK 465 ILE R 296 REMARK 465 LEU R 297 REMARK 465 SER R 298 REMARK 465 TYR R 299 REMARK 465 LEU R 300 REMARK 465 GLN R 301 REMARK 465 ASN R 302 REMARK 465 VAL R 303 REMARK 465 SER R 304 REMARK 465 LEU R 305 REMARK 465 SER R 306 REMARK 465 LEU R 307 REMARK 465 PRO R 308 REMARK 465 SER R 309 REMARK 465 LYS R 310 REMARK 465 SER R 311 REMARK 465 LEU R 312 REMARK 465 SER R 313 REMARK 465 GLU R 314 REMARK 465 GLN R 315 REMARK 465 THR R 316 REMARK 465 ALA R 317 REMARK 465 LEU R 318 REMARK 465 ASN R 319 REMARK 465 LEU R 320 REMARK 465 THR R 321 REMARK 465 LYS R 322 REMARK 465 THR R 323 REMARK 465 PHE R 324 REMARK 465 LEU R 325 REMARK 465 LYS R 326 REMARK 465 ALA R 327 REMARK 465 VAL R 328 REMARK 465 GLY R 329 REMARK 465 GLU R 330 REMARK 465 ILE R 331 REMARK 465 LEU R 332 REMARK 465 LEU R 333 REMARK 465 LEU R 334 REMARK 465 PRO R 335 REMARK 465 GLY R 336 REMARK 465 TRP R 337 REMARK 465 ILE R 338 REMARK 465 ALA R 339 REMARK 465 LEU R 340 REMARK 465 SER R 341 REMARK 465 GLU R 342 REMARK 465 ASP R 343 REMARK 465 SER R 344 REMARK 465 ALA R 345 REMARK 465 VAL R 346 REMARK 465 VAL R 347 REMARK 465 LEU R 348 REMARK 465 SER R 349 REMARK 465 LEU R 350 REMARK 465 ILE R 351 REMARK 465 ASP R 352 REMARK 465 THR R 353 REMARK 465 ILE R 354 REMARK 465 ASP R 355 REMARK 465 THR R 356 REMARK 465 VAL R 357 REMARK 465 MET R 358 REMARK 465 GLY R 359 REMARK 465 HIS R 360 REMARK 465 VAL R 361 REMARK 465 SER R 362 REMARK 465 SER R 363 REMARK 465 ASN R 364 REMARK 465 LEU R 365 REMARK 465 HIS R 366 REMARK 465 GLY R 367 REMARK 465 SER R 368 REMARK 465 THR R 369 REMARK 465 PRO R 370 REMARK 465 GLN R 371 REMARK 465 VAL R 372 REMARK 465 THR R 373 REMARK 465 VAL R 374 REMARK 465 GLU R 375 REMARK 465 GLY R 376 REMARK 465 SER R 377 REMARK 465 SER R 378 REMARK 465 ALA R 379 REMARK 465 MET R 380 REMARK 465 ALA R 381 REMARK 465 GLU R 382 REMARK 465 PHE R 383 REMARK 465 SER R 384 REMARK 465 VAL R 385 REMARK 465 ALA R 386 REMARK 465 LYS R 387 REMARK 465 ILE R 388 REMARK 465 LEU R 389 REMARK 465 PRO R 390 REMARK 465 LYS R 391 REMARK 465 THR R 392 REMARK 465 VAL R 393 REMARK 465 ASN R 394 REMARK 465 SER R 395 REMARK 465 SER R 396 REMARK 465 HIS R 397 REMARK 465 TYR R 398 REMARK 465 ARG R 399 REMARK 465 PHE R 400 REMARK 465 PRO R 401 REMARK 465 ALA R 402 REMARK 465 HIS R 403 REMARK 465 GLY R 404 REMARK 465 GLN R 405 REMARK 465 SER R 406 REMARK 465 PHE R 407 REMARK 465 ILE R 408 REMARK 465 GLN R 409 REMARK 465 ILE R 410 REMARK 465 PRO R 411 REMARK 465 HIS R 412 REMARK 465 GLU R 413 REMARK 465 ALA R 414 REMARK 465 PHE R 415 REMARK 465 HIS R 416 REMARK 465 ARG R 417 REMARK 465 HIS R 418 REMARK 465 ALA R 419 REMARK 465 TRP R 420 REMARK 465 SER R 421 REMARK 465 THR R 422 REMARK 465 VAL R 423 REMARK 465 VAL R 424 REMARK 465 GLY R 425 REMARK 465 LEU R 426 REMARK 465 LEU R 427 REMARK 465 TYR R 428 REMARK 465 HIS R 429 REMARK 465 SER R 430 REMARK 465 MET R 431 REMARK 465 HIS R 432 REMARK 465 TYR R 433 REMARK 465 TYR R 434 REMARK 465 LEU R 435 REMARK 465 ASN R 436 REMARK 465 ASN R 437 REMARK 465 ILE R 438 REMARK 465 TRP R 439 REMARK 465 PRO R 440 REMARK 465 ALA R 441 REMARK 465 HIS R 442 REMARK 465 THR R 443 REMARK 465 LYS R 444 REMARK 465 ILE R 445 REMARK 465 ALA R 446 REMARK 465 GLU R 447 REMARK 465 ALA R 448 REMARK 465 MET R 449 REMARK 465 HIS R 450 REMARK 465 HIS R 451 REMARK 465 GLN R 452 REMARK 465 ASP R 453 REMARK 465 CYS R 454 REMARK 465 LEU R 455 REMARK 465 LEU R 456 REMARK 465 PHE R 457 REMARK 465 ALA R 458 REMARK 465 THR R 459 REMARK 465 SER R 460 REMARK 465 HIS R 461 REMARK 465 LEU R 462 REMARK 465 ILE R 463 REMARK 465 SER R 464 REMARK 465 LEU R 465 REMARK 465 GLU R 466 REMARK 465 VAL R 467 REMARK 465 SER R 468 REMARK 465 PRO R 469 REMARK 465 PRO R 470 REMARK 465 PRO R 471 REMARK 465 THR R 472 REMARK 465 LEU R 473 REMARK 465 SER R 474 REMARK 465 GLN R 475 REMARK 465 ASN R 476 REMARK 465 LEU R 477 REMARK 465 SER R 478 REMARK 465 GLY R 479 REMARK 465 SER R 480 REMARK 465 PRO R 481 REMARK 465 LEU R 482 REMARK 465 ILE R 483 REMARK 465 THR R 484 REMARK 465 VAL R 485 REMARK 465 HIS R 486 REMARK 465 LEU R 487 REMARK 465 LYS R 488 REMARK 465 HIS R 489 REMARK 465 ARG R 490 REMARK 465 LEU R 491 REMARK 465 THR R 492 REMARK 465 ARG R 493 REMARK 465 LYS R 494 REMARK 465 GLN R 495 REMARK 465 HIS R 496 REMARK 465 SER R 497 REMARK 465 GLU R 498 REMARK 465 ALA R 499 REMARK 465 THR R 500 REMARK 465 ASN R 501 REMARK 465 SER R 502 REMARK 465 SER R 503 REMARK 465 ASN R 504 REMARK 465 ARG R 505 REMARK 465 VAL R 506 REMARK 465 PHE R 507 REMARK 465 VAL R 508 REMARK 465 TYR R 509 REMARK 465 CYS R 510 REMARK 465 ALA R 511 REMARK 465 PHE R 512 REMARK 465 LEU R 513 REMARK 465 ASP R 514 REMARK 465 PHE R 515 REMARK 465 SER R 516 REMARK 465 SER R 517 REMARK 465 GLY R 518 REMARK 465 GLU R 519 REMARK 465 GLY R 520 REMARK 465 VAL R 521 REMARK 465 TRP R 522 REMARK 465 SER R 523 REMARK 465 ASN R 524 REMARK 465 HIS R 525 REMARK 465 GLY R 526 REMARK 465 CYS R 527 REMARK 465 ALA R 528 REMARK 465 LEU R 529 REMARK 465 THR R 530 REMARK 465 ARG R 531 REMARK 465 GLY R 532 REMARK 465 ASN R 533 REMARK 465 LEU R 534 REMARK 465 THR R 535 REMARK 465 TYR R 536 REMARK 465 SER R 537 REMARK 465 VAL R 538 REMARK 465 CYS R 539 REMARK 465 ARG R 540 REMARK 465 CYS R 541 REMARK 465 THR R 542 REMARK 465 HIS R 543 REMARK 465 LEU R 544 REMARK 465 THR R 545 REMARK 465 ASN R 546 REMARK 465 PHE R 547 REMARK 465 ALA R 548 REMARK 465 ILE R 549 REMARK 465 LEU R 550 REMARK 465 MET R 551 REMARK 465 GLN R 552 REMARK 465 VAL R 553 REMARK 465 VAL R 554 REMARK 465 PRO R 555 REMARK 465 LEU R 556 REMARK 465 GLU R 557 REMARK 465 LEU R 558 REMARK 465 ALA R 559 REMARK 465 ARG R 560 REMARK 465 GLY R 561 REMARK 465 HIS R 562 REMARK 465 GLN R 563 REMARK 465 VAL R 564 REMARK 465 ALA R 565 REMARK 465 LEU R 566 REMARK 465 SER R 567 REMARK 465 TYR R 746 REMARK 465 LYS R 747 REMARK 465 ILE R 748 REMARK 465 HIS R 749 REMARK 465 GLY R 750 REMARK 465 ASP R 751 REMARK 465 PRO R 752 REMARK 465 SER R 828 REMARK 465 SER R 829 REMARK 465 SER R 830 REMARK 465 ALA R 831 REMARK 465 ARG R 832 REMARK 465 THR R 833 REMARK 465 SER R 834 REMARK 465 ASN R 835 REMARK 465 ALA R 836 REMARK 465 LYS R 837 REMARK 465 PRO R 838 REMARK 465 PHE R 839 REMARK 465 HIS R 840 REMARK 465 SER R 841 REMARK 465 ASP R 842 REMARK 465 LEU R 843 REMARK 465 MET R 844 REMARK 465 ASN R 845 REMARK 465 GLY R 846 REMARK 465 THR R 847 REMARK 465 ARG R 848 REMARK 465 PRO R 849 REMARK 465 GLY R 850 REMARK 465 MET R 851 REMARK 465 ALA R 852 REMARK 465 SER R 853 REMARK 465 THR R 854 REMARK 465 LYS R 855 REMARK 465 LEU R 856 REMARK 465 SER R 857 REMARK 465 PRO R 858 REMARK 465 TRP R 859 REMARK 465 ASP R 860 REMARK 465 LYS R 861 REMARK 465 SER R 862 REMARK 465 SER R 863 REMARK 465 HIS R 864 REMARK 465 SER R 865 REMARK 465 ALA R 866 REMARK 465 HIS R 867 REMARK 465 ARG R 868 REMARK 465 VAL R 869 REMARK 465 ASP R 870 REMARK 465 LEU R 871 REMARK 465 SER R 872 REMARK 465 ALA R 873 REMARK 465 VAL R 874 REMARK 465 MET S 1 REMARK 465 ALA S 120A REMARK 465 GLY S 120B REMARK 465 GLY S 120C REMARK 465 GLY S 120D REMARK 465 GLY S 120E REMARK 465 SER S 120F REMARK 465 GLY S 120G REMARK 465 GLY S 120H REMARK 465 GLY S 120I REMARK 465 GLY S 120J REMARK 465 SER S 120K REMARK 465 GLY S 120L REMARK 465 GLY S 120M REMARK 465 GLY S 120N REMARK 465 GLY S 120O REMARK 465 SER S 120P REMARK 465 LEU S 236 REMARK 465 GLU S 237 REMARK 465 GLU S 238 REMARK 465 ASN S 239 REMARK 465 LEU S 240 REMARK 465 TYR S 241 REMARK 465 PHE S 242 REMARK 465 GLN S 243 REMARK 465 GLY S 244 REMARK 465 ALA S 245 REMARK 465 SER S 246 REMARK 465 HIS S 247 REMARK 465 HIS S 248 REMARK 465 HIS S 249 REMARK 465 HIS S 250 REMARK 465 HIS S 251 REMARK 465 HIS S 252 REMARK 465 HIS S 253 REMARK 465 HIS S 254 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 LYS A 28 CG CD CE NZ REMARK 470 LYS A 32 CG CD CE NZ REMARK 470 GLN A 35 CG CD OE1 NE2 REMARK 470 ARG A 38 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 49 CG OD1 OD2 REMARK 470 LYS A 58 CG CD CE NZ REMARK 470 ARG A 61 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 209 CG CD OE1 OE2 REMARK 470 ASP A 215 CG OD1 OD2 REMARK 470 LYS A 216 CG CD CE NZ REMARK 470 ASP A 229 CG OD1 OD2 REMARK 470 GLU A 230 CG CD OE1 OE2 REMARK 470 ASP A 240 CG OD1 OD2 REMARK 470 LYS A 305 CG CD CE NZ REMARK 470 LYS A 307 CG CD CE NZ REMARK 470 GLU A 309 CG CD OE1 OE2 REMARK 470 ASP A 310 CG OD1 OD2 REMARK 470 GLU A 314 CG CD OE1 OE2 REMARK 470 ARG A 317 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 322 CG CD OE1 OE2 REMARK 470 ASP A 323 CG OD1 OD2 REMARK 470 GLU A 327 CG CD OE1 OE2 REMARK 470 GLU A 330 CG CD OE1 OE2 REMARK 470 ASP A 331 CG OD1 OD2 REMARK 470 ARG A 336 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 356 CG CD NE CZ NH1 NH2 REMARK 470 THR A 364 OG1 CG2 REMARK 470 THR A 369 OG1 CG2 REMARK 470 GLU A 370 CG CD OE1 OE2 REMARK 470 ASP B 5 CG OD1 OD2 REMARK 470 LEU B 7 CG CD1 CD2 REMARK 470 ARG B 8 CG CD NE CZ NH1 NH2 REMARK 470 GLN B 9 CG CD OE1 NE2 REMARK 470 GLU B 10 CG CD OE1 OE2 REMARK 470 GLU B 12 CG CD OE1 OE2 REMARK 470 GLN B 13 CG CD OE1 NE2 REMARK 470 LEU B 14 CG CD1 CD2 REMARK 470 LYS B 15 CG CD CE NZ REMARK 470 ASN B 16 CG OD1 ND2 REMARK 470 GLN B 17 CG CD OE1 NE2 REMARK 470 ARG B 19 CG CD NE CZ NH1 NH2 REMARK 470 ASP B 20 CG OD1 OD2 REMARK 470 LYS B 23 CG CD CE NZ REMARK 470 ASP B 27 CG OD1 OD2 REMARK 470 ILE B 33 CG1 CG2 CD1 REMARK 470 ASN B 35 CG OD1 ND2 REMARK 470 ASN B 36 CG OD1 ND2 REMARK 470 ARG B 42 CG CD NE CZ NH1 NH2 REMARK 470 GLN B 44 CG CD OE1 NE2 REMARK 470 ARG B 46 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 96 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 129 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 130 CG CD OE1 OE2 REMARK 470 GLU B 172 CG CD OE1 OE2 REMARK 470 ARG B 197 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 214 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 215 CG CD OE1 OE2 REMARK 470 THR B 243 OG1 CG2 REMARK 470 ASP B 267 CG OD1 OD2 REMARK 470 ASN B 268 CG OD1 ND2 REMARK 470 ILE B 270 CG1 CG2 CD1 REMARK 470 ASP B 312 CG OD1 OD2 REMARK 470 GLN G 11 CG CD OE1 NE2 REMARK 470 ARG G 13 CG CD NE CZ NH1 NH2 REMARK 470 LYS G 14 CG CD CE NZ REMARK 470 VAL G 16 CG1 CG2 REMARK 470 GLU G 17 CG CD OE1 OE2 REMARK 470 LYS G 20 CG CD CE NZ REMARK 470 MET G 21 CG SD CE REMARK 470 ASP G 26 CG OD1 OD2 REMARK 470 LYS G 29 CG CD CE NZ REMARK 470 GLU G 42 CG CD OE1 OE2 REMARK 470 GLU G 47 CG CD OE1 OE2 REMARK 470 TYR R 571 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG R 598 CG CD NE CZ NH1 NH2 REMARK 470 SER R 622 OG REMARK 470 ARG R 624 CG CD NE CZ NH1 NH2 REMARK 470 GLU R 626 CG CD OE1 OE2 REMARK 470 LYS R 663 CG CD CE NZ REMARK 470 GLU R 668 CG CD OE1 OE2 REMARK 470 SER R 670 OG REMARK 470 LYS R 671 CG CD CE NZ REMARK 470 ARG R 673 CG CD NE CZ NH1 NH2 REMARK 470 ASN R 702 CG OD1 ND2 REMARK 470 ASN R 703 CG OD1 ND2 REMARK 470 PHE R 755 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS R 756 CG CD CE NZ REMARK 470 LYS R 760 CG CD CE NZ REMARK 470 ASN R 781 CG OD1 ND2 REMARK 470 GLN R 788 CG CD OE1 NE2 REMARK 470 LYS R 818 CG CD CE NZ REMARK 470 GLU S 42 CG CD OE1 OE2 REMARK 470 GLU S 46 CG CD OE1 OE2 REMARK 470 ILE S 51 CG1 CG2 CD1 REMARK 470 ASP S 62 CG OD1 OD2 REMARK 470 MET S 83 CG SD CE REMARK 470 GLU S 89 CG CD OE1 OE2 REMARK 470 VAL S 127 CG1 CG2 REMARK 470 VAL S 137 CG1 CG2 REMARK 470 GLU S 141 CG CD OE1 OE2 REMARK 470 GLN S 174 CG CD OE1 NE2 REMARK 470 ARG S 206 CG CD NE CZ NH1 NH2 REMARK 470 GLU S 210 CG CD OE1 OE2 REMARK 470 GLU S 222 CG CD OE1 OE2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 LEU R 706 CA - CB - CG ANGL. DEV. = 14.1 DEGREES 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 ASN A 50 58.59 -96.48 REMARK 500 MET A 60 34.50 39.92 REMARK 500 SER A 275 -5.08 68.34 REMARK 500 SER A 366 -8.30 71.26 REMARK 500 ASP A 368 115.18 -161.68 REMARK 500 THR B 87 -1.24 66.50 REMARK 500 ASP B 153 -167.22 -161.78 REMARK 500 THR B 196 -4.67 71.57 REMARK 500 ASP B 246 46.79 -82.27 REMARK 500 CYS B 271 -168.46 -79.66 REMARK 500 LEU B 308 57.34 -95.81 REMARK 500 HIS G 44 51.26 -92.13 REMARK 500 LYS G 46 45.99 -87.37 REMARK 500 PRO G 49 42.27 -78.19 REMARK 500 PHE R 682 -38.05 -38.36 REMARK 500 THR R 700 -149.17 52.54 REMARK 500 SER R 701 -144.70 52.47 REMARK 500 SER R 710 -166.79 -167.92 REMARK 500 TRP R 773 46.73 -90.88 REMARK 500 ASN R 781 -169.40 -127.62 REMARK 500 MET R 790 -59.61 177.84 REMARK 500 SER R 811 -6.27 71.31 REMARK 500 MET S 180 -13.89 73.11 REMARK 500 SER S 181 88.43 -154.22 REMARK 500 ASN S 182 117.10 -167.01 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-38184 RELATED DB: EMDB REMARK 900 AP503-GPR133-GS-SCFV16 COMPLEX DBREF 8X9T A 8 394 PDB 8X9T 8X9T 8 394 DBREF 8X9T B 2 340 UNP P54311 GBB1_RAT 2 340 DBREF 8X9T G 1 71 UNP P63212 GBG2_BOVIN 1 71 DBREF 8X9T R 277 874 UNP Q6QNK2 AGRD1_HUMAN 277 874 DBREF 8X9T S 1 254 PDB 8X9T 8X9T 1 254 SEQADV 8X9T GLY B -3 UNP P54311 EXPRESSION TAG SEQADV 8X9T SER B -2 UNP P54311 EXPRESSION TAG SEQADV 8X9T LEU B -1 UNP P54311 EXPRESSION TAG SEQADV 8X9T LEU B 0 UNP P54311 EXPRESSION TAG SEQADV 8X9T GLN B 1 UNP P54311 EXPRESSION TAG SEQRES 1 A 361 MET GLY CYS THR LEU SER ALA GLU ASP LYS ALA ALA VAL SEQRES 2 A 361 GLU ARG SER LYS MET ILE GLU LYS GLN LEU GLN LYS ASP SEQRES 3 A 361 LYS GLN VAL TYR ARG ALA THR HIS ARG LEU LEU LEU LEU SEQRES 4 A 361 GLY ALA ASP ASN SER GLY LYS SER THR ILE VAL LYS GLN SEQRES 5 A 361 MET ARG ILE TYR HIS VAL ASN GLY TYR SER GLU GLU GLU SEQRES 6 A 361 CYS LYS GLN TYR LYS ALA VAL VAL TYR SER ASN THR ILE SEQRES 7 A 361 GLN SER ILE ILE ALA ILE ILE ARG ALA MET GLY ARG LEU SEQRES 8 A 361 LYS ILE ASP PHE GLY ASP SER ALA ARG ALA ASP ASP ALA SEQRES 9 A 361 ARG GLN LEU PHE VAL LEU ALA GLY ALA ALA GLU GLU GLY SEQRES 10 A 361 PHE MET THR ALA GLU LEU ALA GLY VAL ILE LYS ARG LEU SEQRES 11 A 361 TRP LYS ASP SER GLY VAL GLN ALA CYS PHE ASN ARG SER SEQRES 12 A 361 ARG GLU TYR GLN LEU ASN ASP SER ALA ALA TYR TYR LEU SEQRES 13 A 361 ASN ASP LEU ASP ARG ILE ALA GLN PRO ASN TYR ILE PRO SEQRES 14 A 361 THR GLN GLN ASP VAL LEU ARG THR ARG VAL LYS THR SER SEQRES 15 A 361 GLY ILE PHE GLU THR LYS PHE GLN VAL ASP LYS VAL ASN SEQRES 16 A 361 PHE HIS MET PHE ASP VAL GLY ALA GLN ARG ASP GLU ARG SEQRES 17 A 361 ARG LYS TRP ILE GLN CYS PHE ASN ASP VAL THR ALA ILE SEQRES 18 A 361 ILE PHE VAL VAL ASP SER SER ASP TYR ASN ARG LEU GLN SEQRES 19 A 361 GLU ALA LEU ASN ASP PHE LYS SER ILE TRP ASN ASN ARG SEQRES 20 A 361 TRP LEU ARG THR ILE SER VAL ILE LEU PHE LEU ASN LYS SEQRES 21 A 361 GLN ASP LEU LEU ALA GLU LYS VAL LEU ALA GLY LYS SER SEQRES 22 A 361 LYS ILE GLU ASP TYR PHE PRO GLU PHE ALA ARG TYR THR SEQRES 23 A 361 THR PRO GLU ASP ALA THR PRO GLU PRO GLY GLU ASP PRO SEQRES 24 A 361 ARG VAL THR ARG ALA LYS TYR PHE ILE ARG ASP GLU PHE SEQRES 25 A 361 LEU ARG ILE SER THR ALA SER GLY ASP GLY ARG HIS TYR SEQRES 26 A 361 CYS TYR PRO HIS PHE THR CYS SER VAL ASP THR GLU ASN SEQRES 27 A 361 ALA ARG ARG ILE PHE ASN ASP CYS ARG ASP ILE ILE GLN SEQRES 28 A 361 ARG MET HIS LEU ARG GLN TYR GLU LEU LEU SEQRES 1 B 344 GLY SER LEU LEU GLN SER GLU LEU ASP GLN LEU ARG GLN SEQRES 2 B 344 GLU ALA GLU GLN LEU LYS ASN GLN ILE ARG ASP ALA ARG SEQRES 3 B 344 LYS ALA CYS ALA ASP ALA THR LEU SER GLN ILE THR ASN SEQRES 4 B 344 ASN ILE ASP PRO VAL GLY ARG ILE GLN MET ARG THR ARG SEQRES 5 B 344 ARG THR LEU ARG GLY HIS LEU ALA LYS ILE TYR ALA MET SEQRES 6 B 344 HIS TRP GLY THR ASP SER ARG LEU LEU VAL SER ALA SER SEQRES 7 B 344 GLN ASP GLY LYS LEU ILE ILE TRP ASP SER TYR THR THR SEQRES 8 B 344 ASN LYS VAL HIS ALA ILE PRO LEU ARG SER SER TRP VAL SEQRES 9 B 344 MET THR CYS ALA TYR ALA PRO SER GLY ASN TYR VAL ALA SEQRES 10 B 344 CYS GLY GLY LEU ASP ASN ILE CYS SER ILE TYR ASN LEU SEQRES 11 B 344 LYS THR ARG GLU GLY ASN VAL ARG VAL SER ARG GLU LEU SEQRES 12 B 344 ALA GLY HIS THR GLY TYR LEU SER CYS CYS ARG PHE LEU SEQRES 13 B 344 ASP ASP ASN GLN ILE VAL THR SER SER GLY ASP THR THR SEQRES 14 B 344 CYS ALA LEU TRP ASP ILE GLU THR GLY GLN GLN THR THR SEQRES 15 B 344 THR PHE THR GLY HIS THR GLY ASP VAL MET SER LEU SER SEQRES 16 B 344 LEU ALA PRO ASP THR ARG LEU PHE VAL SER GLY ALA CYS SEQRES 17 B 344 ASP ALA SER ALA LYS LEU TRP ASP VAL ARG GLU GLY MET SEQRES 18 B 344 CYS ARG GLN THR PHE THR GLY HIS GLU SER ASP ILE ASN SEQRES 19 B 344 ALA ILE CYS PHE PHE PRO ASN GLY ASN ALA PHE ALA THR SEQRES 20 B 344 GLY SER ASP ASP ALA THR CYS ARG LEU PHE ASP LEU ARG SEQRES 21 B 344 ALA ASP GLN GLU LEU MET THR TYR SER HIS ASP ASN ILE SEQRES 22 B 344 ILE CYS GLY ILE THR SER VAL SER PHE SER LYS SER GLY SEQRES 23 B 344 ARG LEU LEU LEU ALA GLY TYR ASP ASP PHE ASN CYS ASN SEQRES 24 B 344 VAL TRP ASP ALA LEU LYS ALA ASP ARG ALA GLY VAL LEU SEQRES 25 B 344 ALA GLY HIS ASP ASN ARG VAL SER CYS LEU GLY VAL THR SEQRES 26 B 344 ASP ASP GLY MET ALA VAL ALA THR GLY SER TRP ASP SER SEQRES 27 B 344 PHE LEU LYS ILE TRP ASN SEQRES 1 G 71 MET ALA SER ASN ASN THR ALA SER ILE ALA GLN ALA ARG SEQRES 2 G 71 LYS LEU VAL GLU GLN LEU LYS MET GLU ALA ASN ILE ASP SEQRES 3 G 71 ARG ILE LYS VAL SER LYS ALA ALA ALA ASP LEU MET ALA SEQRES 4 G 71 TYR CYS GLU ALA HIS ALA LYS GLU ASP PRO LEU LEU THR SEQRES 5 G 71 PRO VAL PRO ALA SER GLU ASN PRO PHE ARG GLU LYS LYS SEQRES 6 G 71 PHE PHE CYS ALA ILE LEU SEQRES 1 R 598 HIS PRO ILE ILE THR ASN LEU THR GLU GLU ARG LYS THR SEQRES 2 R 598 PHE GLN SER PRO GLY VAL ILE LEU SER TYR LEU GLN ASN SEQRES 3 R 598 VAL SER LEU SER LEU PRO SER LYS SER LEU SER GLU GLN SEQRES 4 R 598 THR ALA LEU ASN LEU THR LYS THR PHE LEU LYS ALA VAL SEQRES 5 R 598 GLY GLU ILE LEU LEU LEU PRO GLY TRP ILE ALA LEU SER SEQRES 6 R 598 GLU ASP SER ALA VAL VAL LEU SER LEU ILE ASP THR ILE SEQRES 7 R 598 ASP THR VAL MET GLY HIS VAL SER SER ASN LEU HIS GLY SEQRES 8 R 598 SER THR PRO GLN VAL THR VAL GLU GLY SER SER ALA MET SEQRES 9 R 598 ALA GLU PHE SER VAL ALA LYS ILE LEU PRO LYS THR VAL SEQRES 10 R 598 ASN SER SER HIS TYR ARG PHE PRO ALA HIS GLY GLN SER SEQRES 11 R 598 PHE ILE GLN ILE PRO HIS GLU ALA PHE HIS ARG HIS ALA SEQRES 12 R 598 TRP SER THR VAL VAL GLY LEU LEU TYR HIS SER MET HIS SEQRES 13 R 598 TYR TYR LEU ASN ASN ILE TRP PRO ALA HIS THR LYS ILE SEQRES 14 R 598 ALA GLU ALA MET HIS HIS GLN ASP CYS LEU LEU PHE ALA SEQRES 15 R 598 THR SER HIS LEU ILE SER LEU GLU VAL SER PRO PRO PRO SEQRES 16 R 598 THR LEU SER GLN ASN LEU SER GLY SER PRO LEU ILE THR SEQRES 17 R 598 VAL HIS LEU LYS HIS ARG LEU THR ARG LYS GLN HIS SER SEQRES 18 R 598 GLU ALA THR ASN SER SER ASN ARG VAL PHE VAL TYR CYS SEQRES 19 R 598 ALA PHE LEU ASP PHE SER SER GLY GLU GLY VAL TRP SER SEQRES 20 R 598 ASN HIS GLY CYS ALA LEU THR ARG GLY ASN LEU THR TYR SEQRES 21 R 598 SER VAL CYS ARG CYS THR HIS LEU THR ASN PHE ALA ILE SEQRES 22 R 598 LEU MET GLN VAL VAL PRO LEU GLU LEU ALA ARG GLY HIS SEQRES 23 R 598 GLN VAL ALA LEU SER SER ILE SER TYR VAL GLY CYS SER SEQRES 24 R 598 LEU SER VAL LEU CYS LEU VAL ALA THR LEU VAL THR PHE SEQRES 25 R 598 ALA VAL LEU SER SER VAL SER THR ILE ARG ASN GLN ARG SEQRES 26 R 598 TYR HIS ILE HIS ALA ASN LEU SER PHE ALA VAL LEU VAL SEQRES 27 R 598 ALA GLN VAL LEU LEU LEU ILE SER PHE ARG LEU GLU PRO SEQRES 28 R 598 GLY THR THR PRO CYS GLN VAL MET ALA VAL LEU LEU HIS SEQRES 29 R 598 TYR PHE PHE LEU SER ALA PHE ALA TRP MET LEU VAL GLU SEQRES 30 R 598 GLY LEU HIS LEU TYR SER MET VAL ILE LYS VAL PHE GLY SEQRES 31 R 598 SER GLU ASP SER LYS HIS ARG TYR TYR TYR GLY MET GLY SEQRES 32 R 598 TRP GLY PHE PRO LEU LEU ILE CYS ILE ILE SER LEU SER SEQRES 33 R 598 PHE ALA MET ASP SER TYR GLY THR SER ASN ASN CYS TRP SEQRES 34 R 598 LEU SER LEU ALA SER GLY ALA ILE TRP ALA PHE VAL ALA SEQRES 35 R 598 PRO ALA LEU PHE VAL ILE VAL VAL ASN ILE GLY ILE LEU SEQRES 36 R 598 ILE ALA VAL THR ARG VAL ILE SER GLN ILE SER ALA ASP SEQRES 37 R 598 ASN TYR LYS ILE HIS GLY ASP PRO SER ALA PHE LYS LEU SEQRES 38 R 598 THR ALA LYS ALA VAL ALA VAL LEU LEU PRO ILE LEU GLY SEQRES 39 R 598 THR SER TRP VAL PHE GLY VAL LEU ALA VAL ASN GLY CYS SEQRES 40 R 598 ALA VAL VAL PHE GLN TYR MET PHE ALA THR LEU ASN SER SEQRES 41 R 598 LEU GLN GLY LEU PHE ILE PHE LEU PHE HIS CYS LEU LEU SEQRES 42 R 598 ASN SER GLU VAL ARG ALA ALA PHE LYS HIS LYS THR LYS SEQRES 43 R 598 VAL TRP SER LEU THR SER SER SER ALA ARG THR SER ASN SEQRES 44 R 598 ALA LYS PRO PHE HIS SER ASP LEU MET ASN GLY THR ARG SEQRES 45 R 598 PRO GLY MET ALA SER THR LYS LEU SER PRO TRP ASP LYS SEQRES 46 R 598 SER SER HIS SER ALA HIS ARG VAL ASP LEU SER ALA VAL SEQRES 1 S 267 MET VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 S 267 PRO GLY GLY SER ARG LYS LEU SER CYS SER ALA SER GLY SEQRES 3 S 267 PHE ALA PHE SER SER PHE GLY MET HIS TRP VAL ARG GLN SEQRES 4 S 267 ALA PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SEQRES 5 S 267 SER GLY SER GLY THR ILE TYR TYR ALA ASP THR VAL LYS SEQRES 6 S 267 GLY ARG PHE THR ILE SER ARG ASP ASP PRO LYS ASN THR SEQRES 7 S 267 LEU PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR SEQRES 8 S 267 ALA MET TYR TYR CYS VAL ARG SER ILE TYR TYR TYR GLY SEQRES 9 S 267 SER SER PRO PHE ASP PHE TRP GLY GLN GLY THR THR LEU SEQRES 10 S 267 THR VAL SER ALA GLY GLY GLY GLY SER GLY GLY GLY GLY SEQRES 11 S 267 SER GLY GLY GLY GLY SER SER ASP ILE VAL MET THR GLN SEQRES 12 S 267 ALA THR SER SER VAL PRO VAL THR PRO GLY GLU SER VAL SEQRES 13 S 267 SER ILE SER CYS ARG SER SER LYS SER LEU LEU HIS SER SEQRES 14 S 267 ASN GLY ASN THR TYR LEU TYR TRP PHE LEU GLN ARG PRO SEQRES 15 S 267 GLY GLN SER PRO GLN LEU LEU ILE TYR ARG MET SER ASN SEQRES 16 S 267 LEU ALA SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SEQRES 17 S 267 SER GLY THR ALA PHE THR LEU THR ILE SER ARG LEU GLU SEQRES 18 S 267 ALA GLU ASP VAL GLY VAL TYR TYR CYS MET GLN HIS LEU SEQRES 19 S 267 GLU TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU SEQRES 20 S 267 LEU LEU GLU GLU ASN LEU TYR PHE GLN GLY ALA SER HIS SEQRES 21 S 267 HIS HIS HIS HIS HIS HIS HIS HET YNH R 901 31 HETNAM YNH METHYL 3-[2-(2,4-DIMETHYLPHENOXY)ETHANOYLAMINO]-4-(4- HETNAM 2 YNH ETHYLPIPERAZIN-1-YL)BENZOATE FORMUL 6 YNH C24 H31 N3 O4 HELIX 1 AA1 SER A 13 ARG A 38 1 26 HELIX 2 AA2 GLY A 52 GLN A 59 1 8 HELIX 3 AA3 TRP A 234 ASN A 239 5 6 HELIX 4 AA4 ARG A 265 LYS A 274 1 10 HELIX 5 AA5 LYS A 293 LEU A 302 1 10 HELIX 6 AA6 LYS A 307 PHE A 312 1 6 HELIX 7 AA7 ASP A 331 ALA A 351 1 21 HELIX 8 AA8 GLU A 370 TYR A 391 1 22 HELIX 9 AA9 LEU B 4 CYS B 25 1 22 HELIX 10 AB1 THR B 29 THR B 34 1 6 HELIX 11 AB2 SER G 8 ALA G 23 1 16 HELIX 12 AB3 LYS G 29 HIS G 44 1 16 HELIX 13 AB4 ALA G 45 ASP G 48 5 4 HELIX 14 AB5 ILE R 569 SER R 592 1 24 HELIX 15 AB6 ASN R 599 ALA R 615 1 17 HELIX 16 AB7 GLN R 616 ARG R 624 1 9 HELIX 17 AB8 THR R 629 ILE R 662 1 34 HELIX 18 AB9 LYS R 671 GLY R 679 1 9 HELIX 19 AC1 GLY R 681 PHE R 693 1 13 HELIX 20 AC2 ILE R 713 LEU R 721 1 9 HELIX 21 AC3 VAL R 725 ASP R 744 1 20 HELIX 22 AC4 ALA R 754 LEU R 769 1 16 HELIX 23 AC5 PHE R 787 CYS R 807 1 21 HELIX 24 AC6 GLU R 812 THR R 827 1 16 HELIX 25 AC7 ARG S 87 THR S 91 5 5 SHEET 1 AA1 3 ILE A 207 THR A 210 0 SHEET 2 AA1 3 VAL A 217 VAL A 224 -1 O MET A 221 N THR A 210 SHEET 3 AA1 3 GLN A 213 VAL A 214 -1 N VAL A 214 O VAL A 217 SHEET 1 AA2 6 ILE A 207 THR A 210 0 SHEET 2 AA2 6 VAL A 217 VAL A 224 -1 O MET A 221 N THR A 210 SHEET 3 AA2 6 HIS A 41 GLY A 47 1 N LEU A 43 O PHE A 222 SHEET 4 AA2 6 ALA A 243 ASP A 249 1 O VAL A 247 N LEU A 46 SHEET 5 AA2 6 SER A 286 ASN A 292 1 O PHE A 290 N PHE A 246 SHEET 6 AA2 6 CYS A 359 PHE A 363 1 O TYR A 360 N VAL A 287 SHEET 1 AA3 4 THR B 47 ARG B 52 0 SHEET 2 AA3 4 PHE B 335 TRP B 339 -1 O LEU B 336 N LEU B 51 SHEET 3 AA3 4 VAL B 327 SER B 331 -1 N THR B 329 O LYS B 337 SHEET 4 AA3 4 VAL B 315 VAL B 320 -1 N CYS B 317 O GLY B 330 SHEET 1 AA4 4 ILE B 58 TRP B 63 0 SHEET 2 AA4 4 LEU B 69 SER B 74 -1 O VAL B 71 N HIS B 62 SHEET 3 AA4 4 LYS B 78 ASP B 83 -1 O TRP B 82 N LEU B 70 SHEET 4 AA4 4 LYS B 89 PRO B 94 -1 O ILE B 93 N LEU B 79 SHEET 1 AA5 4 VAL B 100 TYR B 105 0 SHEET 2 AA5 4 TYR B 111 GLY B 116 -1 O ALA B 113 N ALA B 104 SHEET 3 AA5 4 ILE B 120 ASN B 125 -1 O TYR B 124 N VAL B 112 SHEET 4 AA5 4 ARG B 134 ALA B 140 -1 O SER B 136 N ILE B 123 SHEET 1 AA6 4 LEU B 146 PHE B 151 0 SHEET 2 AA6 4 ILE B 157 SER B 161 -1 O VAL B 158 N ARG B 150 SHEET 3 AA6 4 THR B 165 LEU B 168 -1 O ALA B 167 N THR B 159 SHEET 4 AA6 4 THR B 178 THR B 181 -1 O THR B 178 N LEU B 168 SHEET 1 AA7 4 VAL B 187 LEU B 192 0 SHEET 2 AA7 4 LEU B 198 ALA B 203 -1 O VAL B 200 N SER B 191 SHEET 3 AA7 4 ALA B 208 ASP B 212 -1 O TRP B 211 N PHE B 199 SHEET 4 AA7 4 CYS B 218 PHE B 222 -1 O PHE B 222 N ALA B 208 SHEET 1 AA8 4 ILE B 229 PHE B 234 0 SHEET 2 AA8 4 ALA B 240 SER B 245 -1 O ALA B 242 N CYS B 233 SHEET 3 AA8 4 THR B 249 ASP B 254 -1 O PHE B 253 N PHE B 241 SHEET 4 AA8 4 GLN B 259 SER B 265 -1 O LEU B 261 N LEU B 252 SHEET 1 AA9 4 ILE B 273 PHE B 278 0 SHEET 2 AA9 4 LEU B 284 TYR B 289 -1 O GLY B 288 N SER B 275 SHEET 3 AA9 4 CYS B 294 ASP B 298 -1 O TRP B 297 N LEU B 285 SHEET 4 AA9 4 ARG B 304 LEU B 308 -1 O ALA B 305 N VAL B 296 SHEET 1 AB1 4 GLN S 3 SER S 7 0 SHEET 2 AB1 4 ARG S 18 SER S 25 -1 O SER S 23 N VAL S 5 SHEET 3 AB1 4 THR S 78 MET S 83 -1 O LEU S 81 N LEU S 20 SHEET 4 AB1 4 PHE S 68 ASP S 73 -1 N THR S 69 O GLN S 82 SHEET 1 AB2 6 LEU S 11 VAL S 12 0 SHEET 2 AB2 6 THR S 115 VAL S 119 1 O THR S 118 N VAL S 12 SHEET 3 AB2 6 ALA S 92 SER S 99 -1 N ALA S 92 O LEU S 117 SHEET 4 AB2 6 GLY S 33 GLN S 39 -1 N GLY S 33 O SER S 99 SHEET 5 AB2 6 LEU S 45 ILE S 51 -1 O VAL S 48 N TRP S 36 SHEET 6 AB2 6 ILE S 58 TYR S 60 -1 O TYR S 59 N TYR S 50 SHEET 1 AB3 4 LEU S 11 VAL S 12 0 SHEET 2 AB3 4 THR S 115 VAL S 119 1 O THR S 118 N VAL S 12 SHEET 3 AB3 4 ALA S 92 SER S 99 -1 N ALA S 92 O LEU S 117 SHEET 4 AB3 4 PHE S 110 TRP S 111 -1 O PHE S 110 N ARG S 98 SHEET 1 AB4 4 MET S 128 THR S 129 0 SHEET 2 AB4 4 VAL S 143 SER S 149 -1 O ARG S 148 N THR S 129 SHEET 3 AB4 4 ALA S 199 ILE S 204 -1 O PHE S 200 N CYS S 147 SHEET 4 AB4 4 PHE S 191 SER S 196 -1 N SER S 194 O THR S 201 SHEET 1 AB5 5 SER S 134 PRO S 136 0 SHEET 2 AB5 5 THR S 231 GLU S 234 1 O LYS S 232 N VAL S 135 SHEET 3 AB5 5 GLY S 213 GLN S 219 -1 N GLY S 213 O LEU S 233 SHEET 4 AB5 5 LEU S 162 GLN S 167 -1 N PHE S 165 O TYR S 216 SHEET 5 AB5 5 GLN S 174 ILE S 177 -1 O GLN S 174 N LEU S 166 SSBOND 1 CYS R 632 CYS R 704 1555 1555 2.03 SSBOND 2 CYS S 147 CYS S 217 1555 1555 2.03 CISPEP 1 TYR S 223 PRO S 224 0 1.71 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