HEADER MEMBRANE PROTEIN 20-JUN-23 8JSR TITLE CRYO-EM STRUCTURE OF THE ANAMORELIN-BOUND GHRELIN RECEPTOR AND GQ TITLE 2 COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: GROWTH HORMONE SECRETAGOGUE RECEPTOR TYPE 1; COMPND 3 CHAIN: R; COMPND 4 SYNONYM: GHS-R,GH-RELEASING PEPTIDE RECEPTOR,GHRP,GHRELIN RECEPTOR; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: ENGINEERED G-ALPHA-Q; COMPND 8 CHAIN: A; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 12 BETA-1; COMPND 13 CHAIN: B; COMPND 14 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 15 ENGINEERED: YES; COMPND 16 MOL_ID: 4; COMPND 17 MOLECULE: SCFV16; COMPND 18 CHAIN: C; COMPND 19 ENGINEERED: YES; COMPND 20 MOL_ID: 5; COMPND 21 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 22 GAMMA-2; COMPND 23 CHAIN: G; COMPND 24 SYNONYM: G GAMMA-I; COMPND 25 ENGINEERED: YES; COMPND 26 MOL_ID: 6; COMPND 27 MOLECULE: NB35; COMPND 28 CHAIN: N; COMPND 29 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: GHSR; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; 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_TAXID: 10090; SOURCE 24 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 26 MOL_ID: 5; SOURCE 27 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 28 ORGANISM_COMMON: HUMAN; SOURCE 29 ORGANISM_TAXID: 9606; SOURCE 30 GENE: GNG2; SOURCE 31 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 32 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 33 MOL_ID: 6; SOURCE 34 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 35 ORGANISM_TAXID: 9844; SOURCE 36 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 37 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS GPCR, SBDD, CACHEXIA, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR D.IM,Y.SHIMURA,H.ASADA,S.IWATA REVDAT 2 05-FEB-25 8JSR 1 JRNL REVDAT 1 22-JAN-25 8JSR 0 JRNL AUTH Y.SHIIMURA,D.IM,R.TANY,H.ASADA,R.KISE,E.KURUMIYA, JRNL AUTH 2 H.WAKASUGI-MASUHO,S.YASUDA,K.MATSUI,J.I.KISHIKAWA,T.KATO, JRNL AUTH 3 T.MURATA,M.KOJIMA,S.IWATA,I.MASUHO JRNL TITL THE STRUCTURE AND FUNCTION OF THE GHRELIN RECEPTOR CODING JRNL TITL 2 FOR DRUG ACTIONS. JRNL REF NAT.STRUCT.MOL.BIOL. 2025 JRNL REFN ESSN 1545-9985 JRNL PMID 39833471 JRNL DOI 10.1038/S41594-024-01481-6 REMARK 2 REMARK 2 RESOLUTION. 2.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX 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) : 2.900 REMARK 3 NUMBER OF PARTICLES : 500563 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 8JSR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-JUN-23. REMARK 100 THE DEPOSITION ID IS D_1300038793. 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 : ANAMORELIN-BOUND GHRELIN REMARK 245 RECEPTOR IN COMPLEX WITH GQ REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 10.00 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 : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1800.00 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 : 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: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: R, A, B, C, G, N 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 TRP R 2 REMARK 465 ASN R 3 REMARK 465 ALA R 4 REMARK 465 THR R 5 REMARK 465 PRO R 6 REMARK 465 SER R 7 REMARK 465 GLU R 8 REMARK 465 GLU R 9 REMARK 465 PRO R 10 REMARK 465 GLY R 11 REMARK 465 PHE R 12 REMARK 465 ASN R 13 REMARK 465 LEU R 14 REMARK 465 THR R 15 REMARK 465 LEU R 16 REMARK 465 ALA R 17 REMARK 465 ASP R 18 REMARK 465 LEU R 19 REMARK 465 ASP R 20 REMARK 465 TRP R 21 REMARK 465 ASP R 22 REMARK 465 ALA R 23 REMARK 465 SER R 24 REMARK 465 PRO R 25 REMARK 465 GLY R 26 REMARK 465 ASN R 27 REMARK 465 ASP R 28 REMARK 465 SER R 29 REMARK 465 LEU R 30 REMARK 465 GLY R 31 REMARK 465 ASP R 32 REMARK 465 GLU R 33 REMARK 465 LEU R 34 REMARK 465 LEU R 35 REMARK 465 GLN R 36 REMARK 465 ASN R 188 REMARK 465 GLY R 189 REMARK 465 THR R 190 REMARK 465 ASP R 191 REMARK 465 PRO R 192 REMARK 465 ARG R 242 REMARK 465 ARG R 243 REMARK 465 ARG R 244 REMARK 465 GLY R 245 REMARK 465 ASP R 246 REMARK 465 ALA R 247 REMARK 465 VAL R 248 REMARK 465 VAL R 249 REMARK 465 GLY R 250 REMARK 465 ALA R 251 REMARK 465 SER R 252 REMARK 465 LEU R 253 REMARK 465 ARG R 254 REMARK 465 ASP R 255 REMARK 465 GLN R 256 REMARK 465 GLY R 339 REMARK 465 PHE R 340 REMARK 465 GLU R 341 REMARK 465 PRO R 342 REMARK 465 PHE R 343 REMARK 465 SER R 344 REMARK 465 GLN R 345 REMARK 465 ARG R 346 REMARK 465 LYS R 347 REMARK 465 LEU R 348 REMARK 465 SER R 349 REMARK 465 THR R 350 REMARK 465 LEU R 351 REMARK 465 LYS R 352 REMARK 465 ASP R 353 REMARK 465 GLU R 354 REMARK 465 SER R 355 REMARK 465 SER R 356 REMARK 465 ARG R 357 REMARK 465 ALA R 358 REMARK 465 TRP R 359 REMARK 465 THR R 360 REMARK 465 GLU R 361 REMARK 465 SER R 362 REMARK 465 SER R 363 REMARK 465 ILE R 364 REMARK 465 ASN R 365 REMARK 465 THR R 366 REMARK 465 VAL R 367 REMARK 465 PHE R 368 REMARK 465 THR R 369 REMARK 465 LEU R 370 REMARK 465 GLU R 371 REMARK 465 ASP R 372 REMARK 465 PHE R 373 REMARK 465 VAL R 374 REMARK 465 GLY R 375 REMARK 465 ASP R 376 REMARK 465 TRP R 377 REMARK 465 GLU R 378 REMARK 465 GLN R 379 REMARK 465 THR R 380 REMARK 465 ALA R 381 REMARK 465 ALA R 382 REMARK 465 TYR R 383 REMARK 465 ASN R 384 REMARK 465 LEU R 385 REMARK 465 ASP R 386 REMARK 465 GLN R 387 REMARK 465 VAL R 388 REMARK 465 LEU R 389 REMARK 465 GLU R 390 REMARK 465 GLN R 391 REMARK 465 GLY R 392 REMARK 465 GLY R 393 REMARK 465 VAL R 394 REMARK 465 SER R 395 REMARK 465 SER R 396 REMARK 465 LEU R 397 REMARK 465 LEU R 398 REMARK 465 GLN R 399 REMARK 465 ASN R 400 REMARK 465 LEU R 401 REMARK 465 ALA R 402 REMARK 465 VAL R 403 REMARK 465 SER R 404 REMARK 465 VAL R 405 REMARK 465 THR R 406 REMARK 465 PRO R 407 REMARK 465 ILE R 408 REMARK 465 GLN R 409 REMARK 465 ARG R 410 REMARK 465 ILE R 411 REMARK 465 VAL R 412 REMARK 465 ARG R 413 REMARK 465 SER R 414 REMARK 465 GLY R 415 REMARK 465 GLU R 416 REMARK 465 ASN R 417 REMARK 465 ALA R 418 REMARK 465 LEU R 419 REMARK 465 LYS R 420 REMARK 465 ILE R 421 REMARK 465 ASP R 422 REMARK 465 ILE R 423 REMARK 465 HIS R 424 REMARK 465 VAL R 425 REMARK 465 ILE R 426 REMARK 465 ILE R 427 REMARK 465 PRO R 428 REMARK 465 TYR R 429 REMARK 465 GLU R 430 REMARK 465 GLY R 431 REMARK 465 LEU R 432 REMARK 465 SER R 433 REMARK 465 ALA R 434 REMARK 465 ASP R 435 REMARK 465 GLN R 436 REMARK 465 MET R 437 REMARK 465 ALA R 438 REMARK 465 GLN R 439 REMARK 465 ILE R 440 REMARK 465 GLU R 441 REMARK 465 GLU R 442 REMARK 465 VAL R 443 REMARK 465 PHE R 444 REMARK 465 LYS R 445 REMARK 465 VAL R 446 REMARK 465 VAL R 447 REMARK 465 TYR R 448 REMARK 465 PRO R 449 REMARK 465 VAL R 450 REMARK 465 ASP R 451 REMARK 465 ASP R 452 REMARK 465 HIS R 453 REMARK 465 HIS R 454 REMARK 465 PHE R 455 REMARK 465 LYS R 456 REMARK 465 VAL R 457 REMARK 465 ILE R 458 REMARK 465 LEU R 459 REMARK 465 PRO R 460 REMARK 465 TYR R 461 REMARK 465 GLY R 462 REMARK 465 THR R 463 REMARK 465 LEU R 464 REMARK 465 VAL R 465 REMARK 465 ILE R 466 REMARK 465 ASP R 467 REMARK 465 GLY R 468 REMARK 465 VAL R 469 REMARK 465 THR R 470 REMARK 465 PRO R 471 REMARK 465 ASN R 472 REMARK 465 MET R 473 REMARK 465 LEU R 474 REMARK 465 ASN R 475 REMARK 465 TYR R 476 REMARK 465 PHE R 477 REMARK 465 GLY R 478 REMARK 465 ARG R 479 REMARK 465 PRO R 480 REMARK 465 TYR R 481 REMARK 465 GLU R 482 REMARK 465 GLY R 483 REMARK 465 ILE R 484 REMARK 465 ALA R 485 REMARK 465 VAL R 486 REMARK 465 PHE R 487 REMARK 465 ASP R 488 REMARK 465 GLY R 489 REMARK 465 LYS R 490 REMARK 465 LYS R 491 REMARK 465 ILE R 492 REMARK 465 THR R 493 REMARK 465 VAL R 494 REMARK 465 THR R 495 REMARK 465 GLY R 496 REMARK 465 THR R 497 REMARK 465 LEU R 498 REMARK 465 TRP R 499 REMARK 465 ASN R 500 REMARK 465 GLY R 501 REMARK 465 ASN R 502 REMARK 465 LYS R 503 REMARK 465 ILE R 504 REMARK 465 ILE R 505 REMARK 465 ASP R 506 REMARK 465 GLU R 507 REMARK 465 ARG R 508 REMARK 465 LEU R 509 REMARK 465 ILE R 510 REMARK 465 THR R 511 REMARK 465 PRO R 512 REMARK 465 ASP R 513 REMARK 465 GLY R 514 REMARK 465 SER R 515 REMARK 465 MET R 516 REMARK 465 LEU R 517 REMARK 465 PHE R 518 REMARK 465 ARG R 519 REMARK 465 VAL R 520 REMARK 465 THR R 521 REMARK 465 ILE R 522 REMARK 465 ASN R 523 REMARK 465 SER R 524 REMARK 465 MET A 1 REMARK 465 VAL A 58 REMARK 465 ASN A 59 REMARK 465 GLY A 60 REMARK 465 TYR A 61 REMARK 465 SER A 62 REMARK 465 GLU A 63 REMARK 465 GLU A 64 REMARK 465 GLU A 65 REMARK 465 CYS A 66 REMARK 465 LYS A 67 REMARK 465 GLN A 68 REMARK 465 TYR A 69 REMARK 465 LYS A 70 REMARK 465 ALA A 71 REMARK 465 VAL A 72 REMARK 465 VAL A 73 REMARK 465 TYR A 74 REMARK 465 SER A 75 REMARK 465 ASN A 76 REMARK 465 THR A 77 REMARK 465 ILE A 78 REMARK 465 GLN A 79 REMARK 465 SER A 80 REMARK 465 ILE A 81 REMARK 465 ILE A 82 REMARK 465 ALA A 83 REMARK 465 ILE A 84 REMARK 465 ILE A 85 REMARK 465 ARG A 86 REMARK 465 ALA A 87 REMARK 465 MET A 88 REMARK 465 GLY A 89 REMARK 465 ARG A 90 REMARK 465 LEU A 91 REMARK 465 LYS A 92 REMARK 465 ILE A 93 REMARK 465 ASP A 94 REMARK 465 PHE A 95 REMARK 465 GLY A 96 REMARK 465 ASP A 97 REMARK 465 SER A 98 REMARK 465 ALA A 99 REMARK 465 ARG A 100 REMARK 465 ALA A 101 REMARK 465 ASP A 102 REMARK 465 ASP A 103 REMARK 465 ALA A 104 REMARK 465 ARG A 105 REMARK 465 GLN A 106 REMARK 465 LEU A 107 REMARK 465 PHE A 108 REMARK 465 VAL A 109 REMARK 465 LEU A 110 REMARK 465 ALA A 111 REMARK 465 GLY A 112 REMARK 465 ALA A 113 REMARK 465 ALA A 114 REMARK 465 GLU A 115 REMARK 465 GLU A 116 REMARK 465 GLY A 117 REMARK 465 PHE A 118 REMARK 465 MET A 119 REMARK 465 THR A 120 REMARK 465 ALA A 121 REMARK 465 GLU A 122 REMARK 465 LEU A 123 REMARK 465 ALA A 124 REMARK 465 GLY A 125 REMARK 465 VAL A 126 REMARK 465 ILE A 127 REMARK 465 LYS A 128 REMARK 465 ARG A 129 REMARK 465 LEU A 130 REMARK 465 TRP A 131 REMARK 465 LYS A 132 REMARK 465 ASP A 133 REMARK 465 SER A 134 REMARK 465 GLY A 135 REMARK 465 VAL A 136 REMARK 465 GLN A 137 REMARK 465 ALA A 138 REMARK 465 CYS A 139 REMARK 465 PHE A 140 REMARK 465 ASN A 141 REMARK 465 ARG A 142 REMARK 465 SER A 143 REMARK 465 ARG A 144 REMARK 465 GLU A 145 REMARK 465 TYR A 146 REMARK 465 GLN A 147 REMARK 465 LEU A 148 REMARK 465 ASN A 149 REMARK 465 ASP A 150 REMARK 465 SER A 151 REMARK 465 ALA A 152 REMARK 465 ALA A 153 REMARK 465 TYR A 154 REMARK 465 TYR A 155 REMARK 465 LEU A 156 REMARK 465 ASN A 157 REMARK 465 ASP A 158 REMARK 465 LEU A 159 REMARK 465 ASP A 160 REMARK 465 ARG A 161 REMARK 465 ILE A 162 REMARK 465 ALA A 163 REMARK 465 GLN A 164 REMARK 465 PRO A 165 REMARK 465 ASN A 166 REMARK 465 TYR A 167 REMARK 465 ILE A 168 REMARK 465 PRO A 169 REMARK 465 THR A 170 REMARK 465 GLN A 171 REMARK 465 GLN A 172 REMARK 465 ASP A 173 REMARK 465 VAL A 174 REMARK 465 LEU A 175 REMARK 465 ARG A 176 REMARK 465 THR A 177 REMARK 465 MET B -21 REMARK 465 HIS B -20 REMARK 465 HIS B -19 REMARK 465 HIS B -18 REMARK 465 HIS B -17 REMARK 465 HIS B -16 REMARK 465 HIS B -15 REMARK 465 HIS B -14 REMARK 465 HIS B -13 REMARK 465 HIS B -12 REMARK 465 HIS B -11 REMARK 465 LEU B -10 REMARK 465 GLU B -9 REMARK 465 VAL B -8 REMARK 465 LEU B -7 REMARK 465 PHE B -6 REMARK 465 GLN B -5 REMARK 465 GLY B -4 REMARK 465 PRO B -3 REMARK 465 GLY B -2 REMARK 465 SER B -1 REMARK 465 SER B 0 REMARK 465 GLY B 1 REMARK 465 SER B 2 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 GLY B 351 REMARK 465 GLY B 352 REMARK 465 SER B 353 REMARK 465 SER 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 ASP C 1 REMARK 465 SER C 121 REMARK 465 GLY C 122 REMARK 465 GLY C 123 REMARK 465 GLY C 124 REMARK 465 GLY C 125 REMARK 465 SER C 126 REMARK 465 GLY C 127 REMARK 465 GLY C 128 REMARK 465 GLY C 129 REMARK 465 GLY C 130 REMARK 465 SER C 131 REMARK 465 GLY C 132 REMARK 465 GLY C 133 REMARK 465 GLY C 134 REMARK 465 GLY C 135 REMARK 465 SER C 136 REMARK 465 LYS C 248 REMARK 465 ALA C 249 REMARK 465 ALA C 250 REMARK 465 ALA C 251 REMARK 465 HIS C 252 REMARK 465 HIS C 253 REMARK 465 HIS C 254 REMARK 465 HIS C 255 REMARK 465 HIS C 256 REMARK 465 HIS C 257 REMARK 465 HIS C 258 REMARK 465 HIS C 259 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 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 MET N 0 REMARK 465 SER N 127 REMARK 465 SER N 128 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 TRP R 104 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP R 104 CZ3 CH2 REMARK 470 GLN R 105 CG CD OE1 NE2 REMARK 470 ARG R 107 CG CD NE CZ NH1 NH2 REMARK 470 GLU R 185 CG CD OE1 OE2 REMARK 470 HIS R 186 CG ND1 CD2 CE1 NE2 REMARK 470 GLU R 187 CG CD OE1 OE2 REMARK 470 TRP R 193 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP R 193 CZ3 CH2 REMARK 470 ASP R 194 CG OD1 OD2 REMARK 470 GLU R 197 CG CD OE1 OE2 REMARK 470 GLU R 202 CG CD OE1 OE2 REMARK 470 ARG R 206 CG CD NE CZ NH1 NH2 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 O GLY C 8 OG1 THR C 115 2.18 REMARK 500 REMARK 500 REMARK: NULL 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 CYS R 198 CA - CB - SG ANGL. DEV. = 6.7 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 ARG R 75 53.32 -92.17 REMARK 500 LYS R 328 -7.68 71.30 REMARK 500 LEU A 360 -60.87 -94.89 REMARK 500 ARG B 68 -31.68 -132.43 REMARK 500 THR B 223 64.47 39.26 REMARK 500 SER B 334 37.59 70.13 REMARK 500 VAL C 48 -60.44 -121.08 REMARK 500 TYR C 173 60.07 60.00 REMARK 500 MET C 192 -13.73 74.55 REMARK 500 PHE N 108 -64.03 -94.02 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-36627 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF THE ANAMORELIN-BOUND GHRELIN RECEPTOR AND GQ REMARK 900 COMPLEX DBREF 8JSR R 2 366 UNP Q92847 GHSR_HUMAN 2 366 DBREF 8JSR A 1 361 PDB 8JSR 8JSR 1 361 DBREF 8JSR B 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 8JSR B 356 366 PDB 8JSR 8JSR 356 366 DBREF 8JSR C 1 259 PDB 8JSR 8JSR 1 259 DBREF 8JSR G 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 8JSR N 0 128 PDB 8JSR 8JSR 0 128 SEQADV 8JSR VAL R 367 UNP Q92847 EXPRESSION TAG SEQADV 8JSR PHE R 368 UNP Q92847 EXPRESSION TAG SEQADV 8JSR THR R 369 UNP Q92847 EXPRESSION TAG SEQADV 8JSR LEU R 370 UNP Q92847 EXPRESSION TAG SEQADV 8JSR GLU R 371 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ASP R 372 UNP Q92847 EXPRESSION TAG SEQADV 8JSR PHE R 373 UNP Q92847 EXPRESSION TAG SEQADV 8JSR VAL R 374 UNP Q92847 EXPRESSION TAG SEQADV 8JSR GLY R 375 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ASP R 376 UNP Q92847 EXPRESSION TAG SEQADV 8JSR TRP R 377 UNP Q92847 EXPRESSION TAG SEQADV 8JSR GLU R 378 UNP Q92847 EXPRESSION TAG SEQADV 8JSR GLN R 379 UNP Q92847 EXPRESSION TAG SEQADV 8JSR THR R 380 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ALA R 381 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ALA R 382 UNP Q92847 EXPRESSION TAG SEQADV 8JSR TYR R 383 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ASN R 384 UNP Q92847 EXPRESSION TAG SEQADV 8JSR LEU R 385 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ASP R 386 UNP Q92847 EXPRESSION TAG SEQADV 8JSR GLN R 387 UNP Q92847 EXPRESSION TAG SEQADV 8JSR VAL R 388 UNP Q92847 EXPRESSION TAG SEQADV 8JSR LEU R 389 UNP Q92847 EXPRESSION TAG SEQADV 8JSR GLU R 390 UNP Q92847 EXPRESSION TAG SEQADV 8JSR GLN R 391 UNP Q92847 EXPRESSION TAG SEQADV 8JSR GLY R 392 UNP Q92847 EXPRESSION TAG SEQADV 8JSR GLY R 393 UNP Q92847 EXPRESSION TAG SEQADV 8JSR VAL R 394 UNP Q92847 EXPRESSION TAG SEQADV 8JSR SER R 395 UNP Q92847 EXPRESSION TAG SEQADV 8JSR SER R 396 UNP Q92847 EXPRESSION TAG SEQADV 8JSR LEU R 397 UNP Q92847 EXPRESSION TAG SEQADV 8JSR LEU R 398 UNP Q92847 EXPRESSION TAG SEQADV 8JSR GLN R 399 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ASN R 400 UNP Q92847 EXPRESSION TAG SEQADV 8JSR LEU R 401 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ALA R 402 UNP Q92847 EXPRESSION TAG SEQADV 8JSR VAL R 403 UNP Q92847 EXPRESSION TAG SEQADV 8JSR SER R 404 UNP Q92847 EXPRESSION TAG SEQADV 8JSR VAL R 405 UNP Q92847 EXPRESSION TAG SEQADV 8JSR THR R 406 UNP Q92847 EXPRESSION TAG SEQADV 8JSR PRO R 407 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ILE R 408 UNP Q92847 EXPRESSION TAG SEQADV 8JSR GLN R 409 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ARG R 410 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ILE R 411 UNP Q92847 EXPRESSION TAG SEQADV 8JSR VAL R 412 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ARG R 413 UNP Q92847 EXPRESSION TAG SEQADV 8JSR SER R 414 UNP Q92847 EXPRESSION TAG SEQADV 8JSR GLY R 415 UNP Q92847 EXPRESSION TAG SEQADV 8JSR GLU R 416 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ASN R 417 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ALA R 418 UNP Q92847 EXPRESSION TAG SEQADV 8JSR LEU R 419 UNP Q92847 EXPRESSION TAG SEQADV 8JSR LYS R 420 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ILE R 421 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ASP R 422 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ILE R 423 UNP Q92847 EXPRESSION TAG SEQADV 8JSR HIS R 424 UNP Q92847 EXPRESSION TAG SEQADV 8JSR VAL R 425 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ILE R 426 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ILE R 427 UNP Q92847 EXPRESSION TAG SEQADV 8JSR PRO R 428 UNP Q92847 EXPRESSION TAG SEQADV 8JSR TYR R 429 UNP Q92847 EXPRESSION TAG SEQADV 8JSR GLU R 430 UNP Q92847 EXPRESSION TAG SEQADV 8JSR GLY R 431 UNP Q92847 EXPRESSION TAG SEQADV 8JSR LEU R 432 UNP Q92847 EXPRESSION TAG SEQADV 8JSR SER R 433 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ALA R 434 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ASP R 435 UNP Q92847 EXPRESSION TAG SEQADV 8JSR GLN R 436 UNP Q92847 EXPRESSION TAG SEQADV 8JSR MET R 437 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ALA R 438 UNP Q92847 EXPRESSION TAG SEQADV 8JSR GLN R 439 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ILE R 440 UNP Q92847 EXPRESSION TAG SEQADV 8JSR GLU R 441 UNP Q92847 EXPRESSION TAG SEQADV 8JSR GLU R 442 UNP Q92847 EXPRESSION TAG SEQADV 8JSR VAL R 443 UNP Q92847 EXPRESSION TAG SEQADV 8JSR PHE R 444 UNP Q92847 EXPRESSION TAG SEQADV 8JSR LYS R 445 UNP Q92847 EXPRESSION TAG SEQADV 8JSR VAL R 446 UNP Q92847 EXPRESSION TAG SEQADV 8JSR VAL R 447 UNP Q92847 EXPRESSION TAG SEQADV 8JSR TYR R 448 UNP Q92847 EXPRESSION TAG SEQADV 8JSR PRO R 449 UNP Q92847 EXPRESSION TAG SEQADV 8JSR VAL R 450 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ASP R 451 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ASP R 452 UNP Q92847 EXPRESSION TAG SEQADV 8JSR HIS R 453 UNP Q92847 EXPRESSION TAG SEQADV 8JSR HIS R 454 UNP Q92847 EXPRESSION TAG SEQADV 8JSR PHE R 455 UNP Q92847 EXPRESSION TAG SEQADV 8JSR LYS R 456 UNP Q92847 EXPRESSION TAG SEQADV 8JSR VAL R 457 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ILE R 458 UNP Q92847 EXPRESSION TAG SEQADV 8JSR LEU R 459 UNP Q92847 EXPRESSION TAG SEQADV 8JSR PRO R 460 UNP Q92847 EXPRESSION TAG SEQADV 8JSR TYR R 461 UNP Q92847 EXPRESSION TAG SEQADV 8JSR GLY R 462 UNP Q92847 EXPRESSION TAG SEQADV 8JSR THR R 463 UNP Q92847 EXPRESSION TAG SEQADV 8JSR LEU R 464 UNP Q92847 EXPRESSION TAG SEQADV 8JSR VAL R 465 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ILE R 466 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ASP R 467 UNP Q92847 EXPRESSION TAG SEQADV 8JSR GLY R 468 UNP Q92847 EXPRESSION TAG SEQADV 8JSR VAL R 469 UNP Q92847 EXPRESSION TAG SEQADV 8JSR THR R 470 UNP Q92847 EXPRESSION TAG SEQADV 8JSR PRO R 471 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ASN R 472 UNP Q92847 EXPRESSION TAG SEQADV 8JSR MET R 473 UNP Q92847 EXPRESSION TAG SEQADV 8JSR LEU R 474 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ASN R 475 UNP Q92847 EXPRESSION TAG SEQADV 8JSR TYR R 476 UNP Q92847 EXPRESSION TAG SEQADV 8JSR PHE R 477 UNP Q92847 EXPRESSION TAG SEQADV 8JSR GLY R 478 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ARG R 479 UNP Q92847 EXPRESSION TAG SEQADV 8JSR PRO R 480 UNP Q92847 EXPRESSION TAG SEQADV 8JSR TYR R 481 UNP Q92847 EXPRESSION TAG SEQADV 8JSR GLU R 482 UNP Q92847 EXPRESSION TAG SEQADV 8JSR GLY R 483 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ILE R 484 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ALA R 485 UNP Q92847 EXPRESSION TAG SEQADV 8JSR VAL R 486 UNP Q92847 EXPRESSION TAG SEQADV 8JSR PHE R 487 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ASP R 488 UNP Q92847 EXPRESSION TAG SEQADV 8JSR GLY R 489 UNP Q92847 EXPRESSION TAG SEQADV 8JSR LYS R 490 UNP Q92847 EXPRESSION TAG SEQADV 8JSR LYS R 491 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ILE R 492 UNP Q92847 EXPRESSION TAG SEQADV 8JSR THR R 493 UNP Q92847 EXPRESSION TAG SEQADV 8JSR VAL R 494 UNP Q92847 EXPRESSION TAG SEQADV 8JSR THR R 495 UNP Q92847 EXPRESSION TAG SEQADV 8JSR GLY R 496 UNP Q92847 EXPRESSION TAG SEQADV 8JSR THR R 497 UNP Q92847 EXPRESSION TAG SEQADV 8JSR LEU R 498 UNP Q92847 EXPRESSION TAG SEQADV 8JSR TRP R 499 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ASN R 500 UNP Q92847 EXPRESSION TAG SEQADV 8JSR GLY R 501 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ASN R 502 UNP Q92847 EXPRESSION TAG SEQADV 8JSR LYS R 503 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ILE R 504 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ILE R 505 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ASP R 506 UNP Q92847 EXPRESSION TAG SEQADV 8JSR GLU R 507 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ARG R 508 UNP Q92847 EXPRESSION TAG SEQADV 8JSR LEU R 509 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ILE R 510 UNP Q92847 EXPRESSION TAG SEQADV 8JSR THR R 511 UNP Q92847 EXPRESSION TAG SEQADV 8JSR PRO R 512 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ASP R 513 UNP Q92847 EXPRESSION TAG SEQADV 8JSR GLY R 514 UNP Q92847 EXPRESSION TAG SEQADV 8JSR SER R 515 UNP Q92847 EXPRESSION TAG SEQADV 8JSR MET R 516 UNP Q92847 EXPRESSION TAG SEQADV 8JSR LEU R 517 UNP Q92847 EXPRESSION TAG SEQADV 8JSR PHE R 518 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ARG R 519 UNP Q92847 EXPRESSION TAG SEQADV 8JSR VAL R 520 UNP Q92847 EXPRESSION TAG SEQADV 8JSR THR R 521 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ILE R 522 UNP Q92847 EXPRESSION TAG SEQADV 8JSR ASN R 523 UNP Q92847 EXPRESSION TAG SEQADV 8JSR SER R 524 UNP Q92847 EXPRESSION TAG SEQADV 8JSR MET B -21 UNP P62873 INITIATING METHIONINE SEQADV 8JSR HIS B -20 UNP P62873 EXPRESSION TAG SEQADV 8JSR HIS B -19 UNP P62873 EXPRESSION TAG SEQADV 8JSR HIS B -18 UNP P62873 EXPRESSION TAG SEQADV 8JSR HIS B -17 UNP P62873 EXPRESSION TAG SEQADV 8JSR HIS B -16 UNP P62873 EXPRESSION TAG SEQADV 8JSR HIS B -15 UNP P62873 EXPRESSION TAG SEQADV 8JSR HIS B -14 UNP P62873 EXPRESSION TAG SEQADV 8JSR HIS B -13 UNP P62873 EXPRESSION TAG SEQADV 8JSR HIS B -12 UNP P62873 EXPRESSION TAG SEQADV 8JSR HIS B -11 UNP P62873 EXPRESSION TAG SEQADV 8JSR LEU B -10 UNP P62873 EXPRESSION TAG SEQADV 8JSR GLU B -9 UNP P62873 EXPRESSION TAG SEQADV 8JSR VAL B -8 UNP P62873 EXPRESSION TAG SEQADV 8JSR LEU B -7 UNP P62873 EXPRESSION TAG SEQADV 8JSR PHE B -6 UNP P62873 EXPRESSION TAG SEQADV 8JSR GLN B -5 UNP P62873 EXPRESSION TAG SEQADV 8JSR GLY B -4 UNP P62873 EXPRESSION TAG SEQADV 8JSR PRO B -3 UNP P62873 EXPRESSION TAG SEQADV 8JSR GLY B -2 UNP P62873 EXPRESSION TAG SEQADV 8JSR SER B -1 UNP P62873 EXPRESSION TAG SEQADV 8JSR SER B 0 UNP P62873 EXPRESSION TAG SEQADV 8JSR GLY B 1 UNP P62873 EXPRESSION TAG SEQADV 8JSR GLY B 341 UNP P62873 LINKER SEQADV 8JSR SER B 342 UNP P62873 LINKER SEQADV 8JSR SER B 343 UNP P62873 LINKER SEQADV 8JSR GLY B 344 UNP P62873 LINKER SEQADV 8JSR GLY B 345 UNP P62873 LINKER SEQADV 8JSR GLY B 346 UNP P62873 LINKER SEQADV 8JSR GLY B 347 UNP P62873 LINKER SEQADV 8JSR SER B 348 UNP P62873 LINKER SEQADV 8JSR GLY B 349 UNP P62873 LINKER SEQADV 8JSR GLY B 350 UNP P62873 LINKER SEQADV 8JSR GLY B 351 UNP P62873 LINKER SEQADV 8JSR GLY B 352 UNP P62873 LINKER SEQADV 8JSR SER B 353 UNP P62873 LINKER SEQADV 8JSR SER B 354 UNP P62873 LINKER SEQADV 8JSR GLY B 355 UNP P62873 LINKER SEQRES 1 R 523 TRP ASN ALA THR PRO SER GLU GLU PRO GLY PHE ASN LEU SEQRES 2 R 523 THR LEU ALA ASP LEU ASP TRP ASP ALA SER PRO GLY ASN SEQRES 3 R 523 ASP SER LEU GLY ASP GLU LEU LEU GLN LEU PHE PRO ALA SEQRES 4 R 523 PRO LEU LEU ALA GLY VAL THR ALA THR CYS VAL ALA LEU SEQRES 5 R 523 PHE VAL VAL GLY ILE ALA GLY ASN LEU LEU THR MET LEU SEQRES 6 R 523 VAL VAL SER ARG PHE ARG GLU LEU ARG THR THR THR ASN SEQRES 7 R 523 LEU TYR LEU SER SER MET ALA PHE SER ASP LEU LEU ILE SEQRES 8 R 523 PHE LEU CYS MET PRO LEU ASP LEU VAL ARG LEU TRP GLN SEQRES 9 R 523 TYR ARG PRO TRP ASN PHE GLY ASP LEU LEU CYS LYS LEU SEQRES 10 R 523 PHE GLN PHE VAL SER GLU SER CYS THR TYR ALA THR VAL SEQRES 11 R 523 LEU THR ILE THR ALA LEU SER VAL GLU ARG TYR PHE ALA SEQRES 12 R 523 ILE CYS PHE PRO LEU ARG ALA LYS VAL VAL VAL THR LYS SEQRES 13 R 523 GLY ARG VAL LYS LEU VAL ILE PHE VAL ILE TRP ALA VAL SEQRES 14 R 523 ALA PHE CYS SER ALA GLY PRO ILE PHE VAL LEU VAL GLY SEQRES 15 R 523 VAL GLU HIS GLU ASN GLY THR ASP PRO TRP ASP THR ASN SEQRES 16 R 523 GLU CYS ARG PRO THR GLU PHE ALA VAL ARG SER GLY LEU SEQRES 17 R 523 LEU THR VAL MET VAL TRP VAL SER SER ILE PHE PHE PHE SEQRES 18 R 523 LEU PRO VAL PHE CYS LEU THR VAL LEU TYR SER LEU ILE SEQRES 19 R 523 GLY ARG LYS LEU TRP ARG ARG ARG ARG GLY ASP ALA VAL SEQRES 20 R 523 VAL GLY ALA SER LEU ARG ASP GLN ASN HIS LYS GLN THR SEQRES 21 R 523 VAL LYS MET LEU ALA VAL VAL VAL PHE ALA PHE ILE LEU SEQRES 22 R 523 CYS TRP LEU PRO PHE HIS VAL GLY ARG TYR LEU PHE SER SEQRES 23 R 523 LYS SER PHE GLU PRO GLY SER LEU GLU ILE ALA GLN ILE SEQRES 24 R 523 SER GLN TYR CYS ASN LEU VAL SER PHE VAL LEU PHE TYR SEQRES 25 R 523 LEU SER ALA ALA ILE ASN PRO ILE LEU TYR ASN ILE MET SEQRES 26 R 523 SER LYS LYS TYR ARG VAL ALA VAL PHE ARG LEU LEU GLY SEQRES 27 R 523 PHE GLU PRO PHE SER GLN ARG LYS LEU SER THR LEU LYS SEQRES 28 R 523 ASP GLU SER SER ARG ALA TRP THR GLU SER SER ILE ASN SEQRES 29 R 523 THR VAL PHE THR LEU GLU ASP PHE VAL GLY ASP TRP GLU SEQRES 30 R 523 GLN THR ALA ALA TYR ASN LEU ASP GLN VAL LEU GLU GLN SEQRES 31 R 523 GLY GLY VAL SER SER LEU LEU GLN ASN LEU ALA VAL SER SEQRES 32 R 523 VAL THR PRO ILE GLN ARG ILE VAL ARG SER GLY GLU ASN SEQRES 33 R 523 ALA LEU LYS ILE ASP ILE HIS VAL ILE ILE PRO TYR GLU SEQRES 34 R 523 GLY LEU SER ALA ASP GLN MET ALA GLN ILE GLU GLU VAL SEQRES 35 R 523 PHE LYS VAL VAL TYR PRO VAL ASP ASP HIS HIS PHE LYS SEQRES 36 R 523 VAL ILE LEU PRO TYR GLY THR LEU VAL ILE ASP GLY VAL SEQRES 37 R 523 THR PRO ASN MET LEU ASN TYR PHE GLY ARG PRO TYR GLU SEQRES 38 R 523 GLY ILE ALA VAL PHE ASP GLY LYS LYS ILE THR VAL THR SEQRES 39 R 523 GLY THR LEU TRP ASN GLY ASN LYS ILE ILE ASP GLU ARG SEQRES 40 R 523 LEU ILE THR PRO ASP GLY SER MET LEU PHE ARG VAL THR SEQRES 41 R 523 ILE ASN SER 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 ARG THR LEU 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 LYS GLU PHE SEQRES 25 A 361 VAL ASP ILE SER THR ALA SER GLY ASP GLY ARG HIS ILE 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 LYS ASP ILE ILE LEU SEQRES 28 A 361 GLN MET ASN LEU ARG GLU TYR ASN LEU VAL SEQRES 1 B 388 MET HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS LEU GLU SEQRES 2 B 388 VAL LEU PHE GLN GLY PRO GLY SER SER GLY SER GLU LEU SEQRES 3 B 388 ASP GLN LEU ARG GLN GLU ALA GLU GLN LEU LYS ASN GLN SEQRES 4 B 388 ILE ARG ASP ALA ARG LYS ALA CYS ALA ASP ALA THR LEU SEQRES 5 B 388 SER GLN ILE THR ASN ASN ILE ASP PRO VAL GLY ARG ILE SEQRES 6 B 388 GLN MET ARG THR ARG ARG THR LEU ARG GLY HIS LEU ALA SEQRES 7 B 388 LYS ILE TYR ALA MET HIS TRP GLY THR ASP SER ARG LEU SEQRES 8 B 388 LEU VAL SER ALA SER GLN ASP GLY LYS LEU ILE ILE TRP SEQRES 9 B 388 ASP SER TYR THR THR ASN LYS VAL HIS ALA ILE PRO LEU SEQRES 10 B 388 ARG SER SER TRP VAL MET THR CYS ALA TYR ALA PRO SER SEQRES 11 B 388 GLY ASN TYR VAL ALA CYS GLY GLY LEU ASP ASN ILE CYS SEQRES 12 B 388 SER ILE TYR ASN LEU LYS THR ARG GLU GLY ASN VAL ARG SEQRES 13 B 388 VAL SER ARG GLU LEU ALA GLY HIS THR GLY TYR LEU SER SEQRES 14 B 388 CYS CYS ARG PHE LEU ASP ASP ASN GLN ILE VAL THR SER SEQRES 15 B 388 SER GLY ASP THR THR CYS ALA LEU TRP ASP ILE GLU THR SEQRES 16 B 388 GLY GLN GLN THR THR THR PHE THR GLY HIS THR GLY ASP SEQRES 17 B 388 VAL MET SER LEU SER LEU ALA PRO ASP THR ARG LEU PHE SEQRES 18 B 388 VAL SER GLY ALA CYS ASP ALA SER ALA LYS LEU TRP ASP SEQRES 19 B 388 VAL ARG GLU GLY MET CYS ARG GLN THR PHE THR GLY HIS SEQRES 20 B 388 GLU SER ASP ILE ASN ALA ILE CYS PHE PHE PRO ASN GLY SEQRES 21 B 388 ASN ALA PHE ALA THR GLY SER ASP ASP ALA THR CYS ARG SEQRES 22 B 388 LEU PHE ASP LEU ARG ALA ASP GLN GLU LEU MET THR TYR SEQRES 23 B 388 SER HIS ASP ASN ILE ILE CYS GLY ILE THR SER VAL SER SEQRES 24 B 388 PHE SER LYS SER GLY ARG LEU LEU LEU ALA GLY TYR ASP SEQRES 25 B 388 ASP PHE ASN CYS ASN VAL TRP ASP ALA LEU LYS ALA ASP SEQRES 26 B 388 ARG ALA GLY VAL LEU ALA GLY HIS ASP ASN ARG VAL SER SEQRES 27 B 388 CYS LEU GLY VAL THR ASP ASP GLY MET ALA VAL ALA THR SEQRES 28 B 388 GLY SER TRP ASP SER PHE LEU LYS ILE TRP ASN GLY SER SEQRES 29 B 388 SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER SER GLY SEQRES 30 B 388 VAL SER GLY TRP ARG LEU PHE LYS LYS ILE SER SEQRES 1 C 259 ASP VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 C 259 PRO GLY GLY SER ARG LYS LEU SER CYS SER ALA SER GLY SEQRES 3 C 259 PHE ALA PHE SER SER PHE GLY MET HIS TRP VAL ARG GLN SEQRES 4 C 259 ALA PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SEQRES 5 C 259 SER GLY SER GLY THR ILE TYR TYR ALA ASP THR VAL LYS SEQRES 6 C 259 GLY ARG PHE THR ILE SER ARG ASP ASP PRO LYS ASN THR SEQRES 7 C 259 LEU PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR SEQRES 8 C 259 ALA MET TYR TYR CYS VAL ARG SER ILE TYR TYR TYR GLY SEQRES 9 C 259 SER SER PRO PHE ASP PHE TRP GLY GLN GLY THR THR LEU SEQRES 10 C 259 THR VAL SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SEQRES 11 C 259 SER GLY GLY GLY GLY SER ASP ILE VAL MET THR GLN ALA SEQRES 12 C 259 THR SER SER VAL PRO VAL THR PRO GLY GLU SER VAL SER SEQRES 13 C 259 ILE SER CYS ARG SER SER LYS SER LEU LEU HIS SER ASN SEQRES 14 C 259 GLY ASN THR TYR LEU TYR TRP PHE LEU GLN ARG PRO GLY SEQRES 15 C 259 GLN SER PRO GLN LEU LEU ILE TYR ARG MET SER ASN LEU SEQRES 16 C 259 ALA SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SER SEQRES 17 C 259 GLY THR ALA PHE THR LEU THR ILE SER ARG LEU GLU ALA SEQRES 18 C 259 GLU ASP VAL GLY VAL TYR TYR CYS MET GLN HIS LEU GLU SEQRES 19 C 259 TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU LEU SEQRES 20 C 259 LYS ALA ALA ALA HIS HIS HIS HIS HIS HIS HIS HIS 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 N 129 MET GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL SEQRES 2 N 129 GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER SEQRES 3 N 129 GLY PHE THR PHE SER ASN TYR LYS MET ASN TRP VAL ARG SEQRES 4 N 129 GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ASP ILE SEQRES 5 N 129 SER GLN SER GLY ALA SER ILE SER TYR THR GLY SER VAL SEQRES 6 N 129 LYS GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SEQRES 7 N 129 THR LEU TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP SEQRES 8 N 129 THR ALA VAL TYR TYR CYS ALA ARG CYS PRO ALA PRO PHE SEQRES 9 N 129 THR ARG ASP CYS PHE ASP VAL THR SER THR THR TYR ALA SEQRES 10 N 129 TYR ARG GLY GLN GLY THR GLN VAL THR VAL SER SER HET UYI R 601 40 HETNAM UYI 2-AZANYL-N-[(2R)-1-[(3R)-3-[DIMETHYLAMINO(METHYL) HETNAM 2 UYI CARBAMOYL]-3-(PHENYLMETHYL)PIPERIDIN-1-YL]-3-(1H- HETNAM 3 UYI INDOL-3-YL)-1-OXIDANYLIDENE-PROPAN-2-YL]-2-METHYL- HETNAM 4 UYI PROPANAMIDE FORMUL 7 UYI C31 H42 N6 O3 HELIX 1 AA1 PRO R 39 PHE R 71 1 33 HELIX 2 AA2 THR R 76 CYS R 95 1 20 HELIX 3 AA3 CYS R 95 GLN R 105 1 11 HELIX 4 AA4 GLY R 112 PHE R 147 1 36 HELIX 5 AA5 PHE R 147 VAL R 155 1 9 HELIX 6 AA6 THR R 156 ALA R 175 1 20 HELIX 7 AA7 PRO R 177 LEU R 181 1 5 HELIX 8 AA8 THR R 201 GLY R 208 1 8 HELIX 9 AA9 GLY R 208 ARG R 241 1 34 HELIX 10 AB1 HIS R 258 SER R 289 1 32 HELIX 11 AB2 GLU R 296 ILE R 325 1 30 HELIX 12 AB3 LYS R 329 LEU R 338 1 10 HELIX 13 AB4 SER A 6 THR A 33 1 28 HELIX 14 AB5 GLY A 45 ARG A 54 1 10 HELIX 15 AB6 ILE A 55 HIS A 57 5 3 HELIX 16 AB7 LYS A 210 ASN A 216 5 7 HELIX 17 AB8 ARG A 232 ASN A 246 1 15 HELIX 18 AB9 LYS A 260 GLY A 271 1 12 HELIX 19 AC1 LYS A 274 TYR A 278 5 5 HELIX 20 AC2 PHE A 279 ALA A 283 5 5 HELIX 21 AC3 ASP A 298 SER A 319 1 22 HELIX 22 AC4 GLU A 337 TYR A 358 1 22 HELIX 23 AC5 LEU B 4 CYS B 25 1 22 HELIX 24 AC6 THR B 29 THR B 34 1 6 HELIX 25 AC7 ALA C 28 PHE C 32 5 5 HELIX 26 AC8 ASP C 62 LYS C 65 5 4 HELIX 27 AC9 ARG C 87 THR C 91 5 5 HELIX 28 AD1 GLU C 220 VAL C 224 5 5 HELIX 29 AD2 ALA G 7 ASN G 24 1 18 HELIX 30 AD3 LYS G 29 HIS G 44 1 16 HELIX 31 AD4 ALA G 45 ASP G 48 5 4 HELIX 32 AD5 THR N 28 TYR N 32 5 5 HELIX 33 AD6 LYS N 87 THR N 91 5 5 SHEET 1 AA1 2 VAL R 182 HIS R 186 0 SHEET 2 AA1 2 ASN R 196 PRO R 200 -1 O ARG R 199 N GLY R 183 SHEET 1 AA2 6 ILE A 184 GLN A 190 0 SHEET 2 AA2 6 ASN A 195 VAL A 201 -1 O ASP A 200 N PHE A 185 SHEET 3 AA2 6 LEU A 34 GLY A 40 1 N LEU A 36 O HIS A 197 SHEET 4 AA2 6 ALA A 220 ASP A 226 1 O ILE A 222 N LEU A 37 SHEET 5 AA2 6 SER A 253 ASN A 259 1 O ILE A 255 N ILE A 221 SHEET 6 AA2 6 CYS A 326 PHE A 330 1 O HIS A 329 N LEU A 258 SHEET 1 AA3 4 ARG B 46 LEU B 51 0 SHEET 2 AA3 4 LEU B 336 ASN B 340 -1 O LEU B 336 N LEU B 51 SHEET 3 AA3 4 VAL B 327 SER B 331 -1 N VAL B 327 O TRP B 339 SHEET 4 AA3 4 VAL B 315 VAL B 320 -1 N GLY B 319 O ALA B 328 SHEET 1 AA4 4 ILE B 58 TRP B 63 0 SHEET 2 AA4 4 LEU B 70 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 ASN B 88 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 GLY B 115 N MET B 101 SHEET 3 AA5 4 CYS B 121 ASN B 125 -1 O TYR B 124 N VAL B 112 SHEET 4 AA5 4 ARG B 134 LEU B 139 -1 O SER B 136 N ILE B 123 SHEET 1 AA6 4 LEU B 146 PHE B 151 0 SHEET 2 AA6 4 GLN B 156 SER B 161 -1 O SER B 160 N SER B 147 SHEET 3 AA6 4 CYS B 166 ASP B 170 -1 O TRP B 169 N ILE B 157 SHEET 4 AA6 4 GLN B 175 PHE B 180 -1 O PHE B 180 N CYS B 166 SHEET 1 AA7 4 VAL B 187 LEU B 192 0 SHEET 2 AA7 4 LEU B 198 ALA B 203 -1 O GLY B 202 N MET B 188 SHEET 3 AA7 4 ALA B 208 ASP B 212 -1 O TRP B 211 N PHE B 199 SHEET 4 AA7 4 MET B 217 THR B 221 -1 O ARG B 219 N LEU B 210 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 CYS B 250 ASP B 254 -1 O PHE B 253 N PHE B 241 SHEET 4 AA8 4 GLN B 259 TYR B 264 -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 LEU B 286 N SER B 277 SHEET 3 AA9 4 CYS B 294 ASP B 298 -1 O TRP B 297 N LEU B 285 SHEET 4 AA9 4 ASP B 303 LEU B 308 -1 O LEU B 308 N CYS B 294 SHEET 1 AB1 4 GLN C 3 SER C 7 0 SHEET 2 AB1 4 ARG C 18 SER C 25 -1 O SER C 23 N VAL C 5 SHEET 3 AB1 4 THR C 78 MET C 83 -1 O MET C 83 N ARG C 18 SHEET 4 AB1 4 THR C 69 ASP C 73 -1 N SER C 71 O PHE C 80 SHEET 1 AB2 6 LEU C 11 VAL C 12 0 SHEET 2 AB2 6 THR C 115 VAL C 119 1 O THR C 118 N VAL C 12 SHEET 3 AB2 6 ALA C 92 SER C 99 -1 N TYR C 94 O THR C 115 SHEET 4 AB2 6 GLY C 33 GLN C 39 -1 N VAL C 37 O TYR C 95 SHEET 5 AB2 6 LEU C 45 ILE C 51 -1 O GLU C 46 N ARG C 38 SHEET 6 AB2 6 ILE C 58 TYR C 60 -1 O TYR C 59 N TYR C 50 SHEET 1 AB3 4 MET C 140 THR C 141 0 SHEET 2 AB3 4 VAL C 155 SER C 161 -1 O ARG C 160 N THR C 141 SHEET 3 AB3 4 ALA C 211 ILE C 216 -1 O LEU C 214 N ILE C 157 SHEET 4 AB3 4 PHE C 203 GLY C 207 -1 N SER C 204 O THR C 215 SHEET 1 AB4 6 SER C 146 PRO C 148 0 SHEET 2 AB4 6 THR C 243 GLU C 246 1 O GLU C 246 N VAL C 147 SHEET 3 AB4 6 GLY C 225 GLN C 231 -1 N GLY C 225 O LEU C 245 SHEET 4 AB4 6 LEU C 174 GLN C 179 -1 N TYR C 175 O MET C 230 SHEET 5 AB4 6 GLN C 186 TYR C 190 -1 O LEU C 188 N TRP C 176 SHEET 6 AB4 6 ASN C 194 LEU C 195 -1 O ASN C 194 N TYR C 190 SHEET 1 AB5 4 GLN N 3 GLU N 6 0 SHEET 2 AB5 4 SER N 17 SER N 25 -1 O SER N 25 N GLN N 3 SHEET 3 AB5 4 THR N 78 ASN N 84 -1 O MET N 83 N LEU N 18 SHEET 4 AB5 4 PHE N 68 ASP N 73 -1 N SER N 71 O TYR N 80 SHEET 1 AB6 6 GLY N 10 LEU N 11 0 SHEET 2 AB6 6 THR N 122 THR N 125 1 O THR N 125 N GLY N 10 SHEET 3 AB6 6 ALA N 92 ARG N 98 -1 N ALA N 92 O VAL N 124 SHEET 4 AB6 6 MET N 34 GLN N 39 -1 N VAL N 37 O TYR N 95 SHEET 5 AB6 6 LEU N 45 ILE N 51 -1 O GLU N 46 N ARG N 38 SHEET 6 AB6 6 ILE N 58 TYR N 60 -1 O SER N 59 N ASP N 50 SSBOND 1 CYS R 116 CYS R 198 1555 1555 2.04 SSBOND 2 CYS C 22 CYS C 96 1555 1555 2.04 SSBOND 3 CYS N 22 CYS N 96 1555 1555 2.03 SSBOND 4 CYS N 99 CYS N 107 1555 1555 2.02 CISPEP 1 TYR C 235 PRO C 236 0 3.83 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