HEADER MEMBRANE PROTEIN/IMMUNE SYSTEM 27-FEB-25 9M2F TITLE STRUCTURE OF NEUROPEPTIDE FF RECEPTOR 1 COMPLEX WITH NPFF COMPND MOL_ID: 1; COMPND 2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 3 BETA-1; COMPND 4 CHAIN: B; COMPND 5 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 9 GAMMA-2; COMPND 10 CHAIN: G; COMPND 11 SYNONYM: G GAMMA-I; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 3; COMPND 14 MOLECULE: NEUROPEPTIDE FF; COMPND 15 CHAIN: L; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 4; COMPND 18 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I) SUBUNIT ALPHA-1; COMPND 19 CHAIN: A; COMPND 20 SYNONYM: ADENYLATE CYCLASE-INHIBITING G ALPHA PROTEIN; COMPND 21 ENGINEERED: YES; COMPND 22 MUTATION: YES; COMPND 23 MOL_ID: 5; COMPND 24 MOLECULE: NEUROPEPTIDE FF RECEPTOR 1,NEUROPEPTIDE FF RECEPTOR 1, COMPND 25 LGBIT; COMPND 26 CHAIN: R; COMPND 27 SYNONYM: G-PROTEIN COUPLED RECEPTOR 147,RFAMIDE-RELATED PEPTIDE COMPND 28 RECEPTOR OT7T022; COMPND 29 ENGINEERED: YES; COMPND 30 MOL_ID: 6; COMPND 31 MOLECULE: SCFV16; COMPND 32 CHAIN: S; COMPND 33 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 3 ORGANISM_COMMON: NORWAY RAT; SOURCE 4 ORGANISM_TAXID: 10116; SOURCE 5 GENE: GNB1; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 10 ORGANISM_COMMON: DOMESTIC CATTLE; SOURCE 11 ORGANISM_TAXID: 9913; SOURCE 12 GENE: GNG2; SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 15 MOL_ID: 3; SOURCE 16 SYNTHETIC: YES; SOURCE 17 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 18 ORGANISM_TAXID: 32630; SOURCE 19 MOL_ID: 4; SOURCE 20 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 21 ORGANISM_COMMON: HUMAN; SOURCE 22 ORGANISM_TAXID: 9606; SOURCE 23 GENE: GNAI1; SOURCE 24 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 26 MOL_ID: 5; SOURCE 27 ORGANISM_SCIENTIFIC: HOMO SAPIENS, SYNTHETIC CONSTRUCT; SOURCE 28 ORGANISM_COMMON: HUMAN; SOURCE 29 ORGANISM_TAXID: 9606, 32630; SOURCE 30 GENE: NPFFR1, GPR147, NPFF1; SOURCE 31 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 32 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 33 MOL_ID: 6; SOURCE 34 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 35 ORGANISM_TAXID: 32630; SOURCE 36 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 37 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS GPCR, NPFFR1, NPVF, NPFF, MEMBRANE PROTEIN/IMMUNE SYSTEM, MEMBRANE KEYWDS 2 PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR B.X.PAN,Y.JIANG,X.Z.LI REVDAT 1 23-JUL-25 9M2F 0 JRNL AUTH X.Z.LI,B.X.PAN,Y.JIANG JRNL TITL STRUCTURAL BASIS OF PEPTIDE RECOGNITION AND MODULATION FOR JRNL TITL 2 NEUROPEPTIDE FF RECEPTORS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.93 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, PHENIX, CRYOSPARC, REMARK 3 CRYOSPARC, CRYOSPARC, CRYOSPARC, REMARK 3 CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : REAL 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) : 2.930 REMARK 3 NUMBER OF PARTICLES : 35104 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 9M2F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 04-MAR-25. REMARK 100 THE DEPOSITION ID IS D_1300056994. 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 : NPFFR1 COMPLEX WITH GI-PROTEIN REMARK 245 AND NEUROPEPTIDE FF 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 : 7.40 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 : TFS KRIOS REMARK 245 DETECTOR TYPE : FEI FALCON IV (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 5000.00 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) : 5000.00 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: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G, L, A, 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 B -10 REMARK 465 HIS B -9 REMARK 465 HIS B -8 REMARK 465 HIS B -7 REMARK 465 HIS B -6 REMARK 465 HIS B -5 REMARK 465 HIS B -4 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 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 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 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 A 1 REMARK 465 ILE A 55 REMARK 465 ILE A 56 REMARK 465 HIS A 57 REMARK 465 GLU A 58 REMARK 465 ALA 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 ARG A 178 REMARK 465 VAL A 179 REMARK 465 MET R 1 REMARK 465 GLU R 2 REMARK 465 GLY R 3 REMARK 465 GLU R 4 REMARK 465 PRO R 5 REMARK 465 SER R 6 REMARK 465 GLN R 7 REMARK 465 PRO R 8 REMARK 465 PRO R 9 REMARK 465 ASN R 10 REMARK 465 SER R 11 REMARK 465 SER R 12 REMARK 465 TRP R 13 REMARK 465 PRO R 14 REMARK 465 LEU R 15 REMARK 465 SER R 16 REMARK 465 GLN R 17 REMARK 465 ASN R 18 REMARK 465 GLY R 19 REMARK 465 THR R 20 REMARK 465 ASN R 21 REMARK 465 THR R 22 REMARK 465 GLU R 23 REMARK 465 ALA R 24 REMARK 465 THR R 25 REMARK 465 PRO R 26 REMARK 465 ALA R 27 REMARK 465 THR R 28 REMARK 465 ASN R 29 REMARK 465 ALA R 246 REMARK 465 PRO R 247 REMARK 465 GLY R 248 REMARK 465 PRO R 249 REMARK 465 ALA R 250 REMARK 465 PRO R 251 REMARK 465 GLY R 252 REMARK 465 GLY R 253 REMARK 465 GLU R 254 REMARK 465 GLU R 255 REMARK 465 ALA R 256 REMARK 465 ALA R 257 REMARK 465 ASP R 258 REMARK 465 PRO R 259 REMARK 465 ARG R 260 REMARK 465 ALA R 261 REMARK 465 SER R 262 REMARK 465 ARG R 263 REMARK 465 PHE R 340 REMARK 465 GLN R 341 REMARK 465 ALA R 342 REMARK 465 ALA R 343 REMARK 465 PHE R 344 REMARK 465 ARG R 345 REMARK 465 ALA R 346 REMARK 465 ARG R 347 REMARK 465 LEU R 348 REMARK 465 CYS R 349 REMARK 465 PRO R 350 REMARK 465 ARG R 351 REMARK 465 PRO R 352 REMARK 465 SER R 353 REMARK 465 GLY R 354 REMARK 465 SER R 355 REMARK 465 HIS R 356 REMARK 465 LYS R 357 REMARK 465 GLU R 358 REMARK 465 ALA R 359 REMARK 465 TYR R 360 REMARK 465 SER R 361 REMARK 465 GLU R 362 REMARK 465 ARG R 363 REMARK 465 GLY R 364 REMARK 465 SER R 365 REMARK 465 SER R 366 REMARK 465 GLY R 367 REMARK 465 GLY R 368 REMARK 465 GLY R 369 REMARK 465 GLY R 370 REMARK 465 SER R 371 REMARK 465 GLY R 372 REMARK 465 GLY R 373 REMARK 465 GLY R 374 REMARK 465 GLY R 375 REMARK 465 SER R 376 REMARK 465 SER R 377 REMARK 465 GLY R 378 REMARK 465 VAL R 379 REMARK 465 PHE R 380 REMARK 465 THR R 381 REMARK 465 LEU R 382 REMARK 465 GLU R 383 REMARK 465 ASP R 384 REMARK 465 PHE R 385 REMARK 465 VAL R 386 REMARK 465 GLY R 387 REMARK 465 ASP R 388 REMARK 465 TRP R 389 REMARK 465 GLU R 390 REMARK 465 GLN R 391 REMARK 465 THR R 392 REMARK 465 ALA R 393 REMARK 465 ALA R 394 REMARK 465 TYR R 395 REMARK 465 ASN R 396 REMARK 465 LEU R 397 REMARK 465 ASP R 398 REMARK 465 GLN R 399 REMARK 465 VAL R 400 REMARK 465 LEU R 401 REMARK 465 GLU R 402 REMARK 465 GLN R 403 REMARK 465 GLY R 404 REMARK 465 GLY R 405 REMARK 465 VAL R 406 REMARK 465 SER R 407 REMARK 465 SER R 408 REMARK 465 LEU R 409 REMARK 465 LEU R 410 REMARK 465 GLN R 411 REMARK 465 ASN R 412 REMARK 465 LEU R 413 REMARK 465 ALA R 414 REMARK 465 VAL R 415 REMARK 465 SER R 416 REMARK 465 VAL R 417 REMARK 465 THR R 418 REMARK 465 PRO R 419 REMARK 465 ILE R 420 REMARK 465 GLN R 421 REMARK 465 ARG R 422 REMARK 465 ILE R 423 REMARK 465 VAL R 424 REMARK 465 ARG R 425 REMARK 465 SER R 426 REMARK 465 GLY R 427 REMARK 465 GLU R 428 REMARK 465 ASN R 429 REMARK 465 ALA R 430 REMARK 465 LEU R 431 REMARK 465 LYS R 432 REMARK 465 ILE R 433 REMARK 465 ASP R 434 REMARK 465 ILE R 435 REMARK 465 HIS R 436 REMARK 465 VAL R 437 REMARK 465 ILE R 438 REMARK 465 ILE R 439 REMARK 465 PRO R 440 REMARK 465 TYR R 441 REMARK 465 GLU R 442 REMARK 465 GLY R 443 REMARK 465 LEU R 444 REMARK 465 SER R 445 REMARK 465 ALA R 446 REMARK 465 ASP R 447 REMARK 465 GLN R 448 REMARK 465 MET R 449 REMARK 465 ALA R 450 REMARK 465 GLN R 451 REMARK 465 ILE R 452 REMARK 465 GLU R 453 REMARK 465 GLU R 454 REMARK 465 VAL R 455 REMARK 465 PHE R 456 REMARK 465 LYS R 457 REMARK 465 VAL R 458 REMARK 465 VAL R 459 REMARK 465 TYR R 460 REMARK 465 PRO R 461 REMARK 465 VAL R 462 REMARK 465 ASP R 463 REMARK 465 ASP R 464 REMARK 465 HIS R 465 REMARK 465 HIS R 466 REMARK 465 PHE R 467 REMARK 465 LYS R 468 REMARK 465 VAL R 469 REMARK 465 ILE R 470 REMARK 465 LEU R 471 REMARK 465 PRO R 472 REMARK 465 TYR R 473 REMARK 465 GLY R 474 REMARK 465 THR R 475 REMARK 465 LEU R 476 REMARK 465 VAL R 477 REMARK 465 ILE R 478 REMARK 465 ASP R 479 REMARK 465 GLY R 480 REMARK 465 VAL R 481 REMARK 465 THR R 482 REMARK 465 PRO R 483 REMARK 465 ASN R 484 REMARK 465 MET R 485 REMARK 465 LEU R 486 REMARK 465 ASN R 487 REMARK 465 TYR R 488 REMARK 465 PHE R 489 REMARK 465 GLY R 490 REMARK 465 ARG R 491 REMARK 465 PRO R 492 REMARK 465 TYR R 493 REMARK 465 GLU R 494 REMARK 465 GLY R 495 REMARK 465 ILE R 496 REMARK 465 ALA R 497 REMARK 465 VAL R 498 REMARK 465 PHE R 499 REMARK 465 ASP R 500 REMARK 465 GLY R 501 REMARK 465 LYS R 502 REMARK 465 LYS R 503 REMARK 465 ILE R 504 REMARK 465 THR R 505 REMARK 465 VAL R 506 REMARK 465 THR R 507 REMARK 465 GLY R 508 REMARK 465 THR R 509 REMARK 465 LEU R 510 REMARK 465 TRP R 511 REMARK 465 ASN R 512 REMARK 465 GLY R 513 REMARK 465 ASN R 514 REMARK 465 LYS R 515 REMARK 465 ILE R 516 REMARK 465 ILE R 517 REMARK 465 ASP R 518 REMARK 465 GLU R 519 REMARK 465 ARG R 520 REMARK 465 LEU R 521 REMARK 465 ILE R 522 REMARK 465 THR R 523 REMARK 465 PRO R 524 REMARK 465 ASP R 525 REMARK 465 GLY R 526 REMARK 465 SER R 527 REMARK 465 MET R 528 REMARK 465 LEU R 529 REMARK 465 PHE R 530 REMARK 465 ARG R 531 REMARK 465 VAL R 532 REMARK 465 THR R 533 REMARK 465 ILE R 534 REMARK 465 ASN R 535 REMARK 465 SER R 536 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 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 LEU L 2 CG CD1 CD2 REMARK 470 PHE L 3 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG L 7 CG CD NE CZ NH1 NH2 REMARK 470 LEU A 234 CD2 REMARK 470 GLU A 236 CG CD OE1 OE2 REMARK 470 ASP A 237 CG OD1 OD2 REMARK 470 GLU A 238 CG CD OE1 OE2 REMARK 470 GLU A 239 CB CG CD OE1 OE2 REMARK 470 MET A 240 SD CE REMARK 470 GLU A 245 CG CD OE1 OE2 REMARK 470 THR R 31 OG1 CG2 REMARK 470 PHE R 32 CG CD1 CD2 CE1 CE2 CZ REMARK 470 SER R 33 OG REMARK 470 SER R 34 OG REMARK 470 TYR R 35 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TYR R 36 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 HIS R 38 CG ND1 CD2 CE1 NE2 REMARK 470 VAL R 102 CG1 CG2 REMARK 470 TRP R 109 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP R 109 CZ3 CH2 REMARK 470 PHE R 111 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG R 184 CG CD NE CZ NH1 NH2 REMARK 470 GLU R 186 CG CD OE1 OE2 REMARK 470 ARG R 194 CG CD NE CZ NH1 NH2 REMARK 470 ASN R 195 CG OD1 ND2 REMARK 470 ARG R 196 CG CD NE CZ NH1 NH2 REMARK 470 SER R 197 OG REMARK 470 TYR R 198 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU R 303 CG CD1 CD2 REMARK 470 HIS R 304 CG ND1 CD2 CE1 NE2 REMARK 470 GLU S 42 CG CD OE1 OE2 REMARK 470 SER S 52 OG REMARK 470 ASP S 73 CG OD1 OD2 REMARK 470 GLU S 89 CG CD OE1 OE2 REMARK 470 GLU S 153 CG CD OE1 OE2 REMARK 470 ASP S 201 CG OD1 OD2 REMARK 470 GLU S 246 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 A 6 OD1 ASP A 9 2.07 REMARK 500 O VAL A 342 ND2 ASN A 346 2.13 REMARK 500 O PHE R 319 OG SER R 322 2.18 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 ASP B 205 1.99 -69.92 REMARK 500 LYS G 46 -6.04 67.94 REMARK 500 GLU A 43 52.30 -92.25 REMARK 500 LYS A 192 62.29 39.94 REMARK 500 GLU A 239 -4.88 75.66 REMARK 500 PHE R 32 -131.45 52.02 REMARK 500 SER R 33 162.37 64.59 REMARK 500 HIS R 75 6.09 -69.74 REMARK 500 THR R 76 -165.54 -79.34 REMARK 500 THR R 78 -8.88 -57.44 REMARK 500 ASN R 113 -8.27 72.29 REMARK 500 HIS R 147 74.15 -114.80 REMARK 500 THR R 183 -140.38 55.48 REMARK 500 LYS R 210 -108.19 54.44 REMARK 500 TYR R 309 -62.13 -94.89 REMARK 500 GLU R 334 -0.93 68.31 REMARK 500 ALA S 136 -158.65 53.95 REMARK 500 MET S 192 -11.11 71.78 REMARK 500 THR S 210 -39.66 -130.55 REMARK 500 GLU S 222 -6.30 69.46 REMARK 500 HIS S 232 26.92 -141.61 REMARK 500 PRO S 236 72.75 -65.11 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-63584 RELATED DB: EMDB REMARK 900 STRUCTURE OF NEUROPEPTIDE FF RECEPTOR 1 COMPLEX WITH NPVF DBREF 9M2F B 2 340 UNP P54311 GBB1_RAT 2 340 DBREF 9M2F G 1 71 UNP P63212 GBG2_BOVIN 1 71 DBREF 9M2F L 2 9 PDB 9M2F 9M2F 2 9 DBREF 9M2F A 1 354 UNP P63096 GNAI1_HUMAN 1 354 DBREF 9M2F R 1 363 UNP Q9GZQ6 NPFF1_HUMAN 1 363 DBREF 9M2F R 380 536 PDB 9M2F 9M2F 380 536 DBREF 9M2F S 2 247 PDB 9M2F 9M2F 2 247 SEQADV 9M2F MET B -10 UNP P54311 INITIATING METHIONINE SEQADV 9M2F HIS B -9 UNP P54311 EXPRESSION TAG SEQADV 9M2F HIS B -8 UNP P54311 EXPRESSION TAG SEQADV 9M2F HIS B -7 UNP P54311 EXPRESSION TAG SEQADV 9M2F HIS B -6 UNP P54311 EXPRESSION TAG SEQADV 9M2F HIS B -5 UNP P54311 EXPRESSION TAG SEQADV 9M2F HIS B -4 UNP P54311 EXPRESSION TAG SEQADV 9M2F GLY B -3 UNP P54311 EXPRESSION TAG SEQADV 9M2F SER B -2 UNP P54311 EXPRESSION TAG SEQADV 9M2F LEU B -1 UNP P54311 EXPRESSION TAG SEQADV 9M2F LEU B 0 UNP P54311 EXPRESSION TAG SEQADV 9M2F GLN B 1 UNP P54311 EXPRESSION TAG SEQADV 9M2F GLY B 341 UNP P54311 EXPRESSION TAG SEQADV 9M2F SER B 342 UNP P54311 EXPRESSION TAG SEQADV 9M2F SER B 343 UNP P54311 EXPRESSION TAG SEQADV 9M2F GLY B 344 UNP P54311 EXPRESSION TAG SEQADV 9M2F GLY B 345 UNP P54311 EXPRESSION TAG SEQADV 9M2F GLY B 346 UNP P54311 EXPRESSION TAG SEQADV 9M2F GLY B 347 UNP P54311 EXPRESSION TAG SEQADV 9M2F SER B 348 UNP P54311 EXPRESSION TAG SEQADV 9M2F GLY B 349 UNP P54311 EXPRESSION TAG SEQADV 9M2F GLY B 350 UNP P54311 EXPRESSION TAG SEQADV 9M2F GLY B 351 UNP P54311 EXPRESSION TAG SEQADV 9M2F GLY B 352 UNP P54311 EXPRESSION TAG SEQADV 9M2F SER B 353 UNP P54311 EXPRESSION TAG SEQADV 9M2F SER B 354 UNP P54311 EXPRESSION TAG SEQADV 9M2F GLY B 355 UNP P54311 EXPRESSION TAG SEQADV 9M2F ALA A 203 UNP P63096 GLY 203 ENGINEERED MUTATION SEQADV 9M2F SER A 326 UNP P63096 ALA 326 ENGINEERED MUTATION SEQADV 9M2F GLY R 364 UNP Q9GZQ6 LINKER SEQADV 9M2F SER R 365 UNP Q9GZQ6 LINKER SEQADV 9M2F SER R 366 UNP Q9GZQ6 LINKER SEQADV 9M2F GLY R 367 UNP Q9GZQ6 LINKER SEQADV 9M2F GLY R 368 UNP Q9GZQ6 LINKER SEQADV 9M2F GLY R 369 UNP Q9GZQ6 LINKER SEQADV 9M2F GLY R 370 UNP Q9GZQ6 LINKER SEQADV 9M2F SER R 371 UNP Q9GZQ6 LINKER SEQADV 9M2F GLY R 372 UNP Q9GZQ6 LINKER SEQADV 9M2F GLY R 373 UNP Q9GZQ6 LINKER SEQADV 9M2F GLY R 374 UNP Q9GZQ6 LINKER SEQADV 9M2F GLY R 375 UNP Q9GZQ6 LINKER SEQADV 9M2F SER R 376 UNP Q9GZQ6 LINKER SEQADV 9M2F SER R 377 UNP Q9GZQ6 LINKER SEQADV 9M2F GLY R 378 UNP Q9GZQ6 LINKER SEQADV 9M2F VAL R 379 UNP Q9GZQ6 LINKER SEQRES 1 B 366 MET HIS HIS HIS HIS HIS HIS GLY SER LEU LEU GLN SER SEQRES 2 B 366 GLU LEU ASP GLN LEU ARG GLN GLU ALA GLU GLN LEU LYS SEQRES 3 B 366 ASN GLN ILE ARG ASP ALA ARG LYS ALA CYS ALA ASP ALA SEQRES 4 B 366 THR LEU SER GLN ILE THR ASN ASN ILE ASP PRO VAL GLY SEQRES 5 B 366 ARG ILE GLN MET ARG THR ARG ARG THR LEU ARG GLY HIS SEQRES 6 B 366 LEU ALA LYS ILE TYR ALA MET HIS TRP GLY THR ASP SER SEQRES 7 B 366 ARG LEU LEU VAL SER ALA SER GLN ASP GLY LYS LEU ILE SEQRES 8 B 366 ILE TRP ASP SER TYR THR THR ASN LYS VAL HIS ALA ILE SEQRES 9 B 366 PRO LEU ARG SER SER TRP VAL MET THR CYS ALA TYR ALA SEQRES 10 B 366 PRO SER GLY ASN TYR VAL ALA CYS GLY GLY LEU ASP ASN SEQRES 11 B 366 ILE CYS SER ILE TYR ASN LEU LYS THR ARG GLU GLY ASN SEQRES 12 B 366 VAL ARG VAL SER ARG GLU LEU ALA GLY HIS THR GLY TYR SEQRES 13 B 366 LEU SER CYS CYS ARG PHE LEU ASP ASP ASN GLN ILE VAL SEQRES 14 B 366 THR SER SER GLY ASP THR THR CYS ALA LEU TRP ASP ILE SEQRES 15 B 366 GLU THR GLY GLN GLN THR THR THR PHE THR GLY HIS THR SEQRES 16 B 366 GLY ASP VAL MET SER LEU SER LEU ALA PRO ASP THR ARG SEQRES 17 B 366 LEU PHE VAL SER GLY ALA CYS ASP ALA SER ALA LYS LEU SEQRES 18 B 366 TRP ASP VAL ARG GLU GLY MET CYS ARG GLN THR PHE THR SEQRES 19 B 366 GLY HIS GLU SER ASP ILE ASN ALA ILE CYS PHE PHE PRO SEQRES 20 B 366 ASN GLY ASN ALA PHE ALA THR GLY SER ASP ASP ALA THR SEQRES 21 B 366 CYS ARG LEU PHE ASP LEU ARG ALA ASP GLN GLU LEU MET SEQRES 22 B 366 THR TYR SER HIS ASP ASN ILE ILE CYS GLY ILE THR SER SEQRES 23 B 366 VAL SER PHE SER LYS SER GLY ARG LEU LEU LEU ALA GLY SEQRES 24 B 366 TYR ASP ASP PHE ASN CYS ASN VAL TRP ASP ALA LEU LYS SEQRES 25 B 366 ALA ASP ARG ALA GLY VAL LEU ALA GLY HIS ASP ASN ARG SEQRES 26 B 366 VAL SER CYS LEU GLY VAL THR ASP ASP GLY MET ALA VAL SEQRES 27 B 366 ALA THR GLY SER TRP ASP SER PHE LEU LYS ILE TRP ASN SEQRES 28 B 366 GLY SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER SEQRES 29 B 366 SER GLY 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 L 8 LEU PHE GLN PRO GLN ARG PHE NH2 SEQRES 1 A 354 MET GLY CYS THR LEU SER ALA GLU ASP LYS ALA ALA VAL SEQRES 2 A 354 GLU ARG SER LYS MET ILE ASP ARG ASN LEU ARG GLU ASP SEQRES 3 A 354 GLY GLU LYS ALA ALA ARG GLU VAL LYS LEU LEU LEU LEU SEQRES 4 A 354 GLY ALA GLY GLU SER GLY LYS SER THR ILE VAL LYS GLN SEQRES 5 A 354 MET LYS ILE ILE HIS GLU ALA GLY TYR SER GLU GLU GLU SEQRES 6 A 354 CYS LYS GLN TYR LYS ALA VAL VAL TYR SER ASN THR ILE SEQRES 7 A 354 GLN SER ILE ILE ALA ILE ILE ARG ALA MET GLY ARG LEU SEQRES 8 A 354 LYS ILE ASP PHE GLY ASP SER ALA ARG ALA ASP ASP ALA SEQRES 9 A 354 ARG GLN LEU PHE VAL LEU ALA GLY ALA ALA GLU GLU GLY SEQRES 10 A 354 PHE MET THR ALA GLU LEU ALA GLY VAL ILE LYS ARG LEU SEQRES 11 A 354 TRP LYS ASP SER GLY VAL GLN ALA CYS PHE ASN ARG SER SEQRES 12 A 354 ARG GLU TYR GLN LEU ASN ASP SER ALA ALA TYR TYR LEU SEQRES 13 A 354 ASN ASP LEU ASP ARG ILE ALA GLN PRO ASN TYR ILE PRO SEQRES 14 A 354 THR GLN GLN ASP VAL LEU ARG THR ARG VAL LYS THR THR SEQRES 15 A 354 GLY ILE VAL GLU THR HIS PHE THR PHE LYS ASP LEU HIS SEQRES 16 A 354 PHE LYS MET PHE ASP VAL GLY ALA GLN ARG SER GLU ARG SEQRES 17 A 354 LYS LYS TRP ILE HIS CYS PHE GLU GLY VAL THR ALA ILE SEQRES 18 A 354 ILE PHE CYS VAL ALA LEU SER ASP TYR ASP LEU VAL LEU SEQRES 19 A 354 ALA GLU ASP GLU GLU MET ASN ARG MET HIS GLU SER MET SEQRES 20 A 354 LYS LEU PHE ASP SER ILE CYS ASN ASN LYS TRP PHE THR SEQRES 21 A 354 ASP THR SER ILE ILE LEU PHE LEU ASN LYS LYS ASP LEU SEQRES 22 A 354 PHE GLU GLU LYS ILE LYS LYS SER PRO LEU THR ILE CYS SEQRES 23 A 354 TYR PRO GLU TYR ALA GLY SER ASN THR TYR GLU GLU ALA SEQRES 24 A 354 ALA ALA TYR ILE GLN CYS GLN PHE GLU ASP LEU ASN LYS SEQRES 25 A 354 ARG LYS ASP THR LYS GLU ILE TYR THR HIS PHE THR CYS SEQRES 26 A 354 SER THR ASP THR LYS ASN VAL GLN PHE VAL PHE ASP ALA SEQRES 27 A 354 VAL THR ASP VAL ILE ILE LYS ASN ASN LEU LYS ASP CYS SEQRES 28 A 354 GLY LEU PHE SEQRES 1 R 536 MET GLU GLY GLU PRO SER GLN PRO PRO ASN SER SER TRP SEQRES 2 R 536 PRO LEU SER GLN ASN GLY THR ASN THR GLU ALA THR PRO SEQRES 3 R 536 ALA THR ASN LEU THR PHE SER SER TYR TYR GLN HIS THR SEQRES 4 R 536 SER PRO VAL ALA ALA MET PHE ILE VAL ALA TYR ALA LEU SEQRES 5 R 536 ILE PHE LEU LEU CYS MET VAL GLY ASN THR LEU VAL CYS SEQRES 6 R 536 PHE ILE VAL LEU LYS ASN ARG HIS MET HIS THR VAL THR SEQRES 7 R 536 ASN MET PHE ILE LEU ASN LEU ALA VAL SER ASP LEU LEU SEQRES 8 R 536 VAL GLY ILE PHE CYS MET PRO THR THR LEU VAL ASP ASN SEQRES 9 R 536 LEU ILE THR GLY TRP PRO PHE ASP ASN ALA THR CYS LYS SEQRES 10 R 536 MET SER GLY LEU VAL GLN GLY MET SER VAL SER ALA SER SEQRES 11 R 536 VAL PHE THR LEU VAL ALA ILE ALA VAL GLU ARG PHE ARG SEQRES 12 R 536 CYS ILE VAL HIS PRO PHE ARG GLU LYS LEU THR LEU ARG SEQRES 13 R 536 LYS ALA LEU VAL THR ILE ALA VAL ILE TRP ALA LEU ALA SEQRES 14 R 536 LEU LEU ILE MET CYS PRO SER ALA VAL THR LEU THR VAL SEQRES 15 R 536 THR ARG GLU GLU HIS HIS PHE MET VAL ASP ALA ARG ASN SEQRES 16 R 536 ARG SER TYR PRO LEU TYR SER CYS TRP GLU ALA TRP PRO SEQRES 17 R 536 GLU LYS GLY MET ARG ARG VAL TYR THR THR VAL LEU PHE SEQRES 18 R 536 SER HIS ILE TYR LEU ALA PRO LEU ALA LEU ILE VAL VAL SEQRES 19 R 536 MET TYR ALA ARG ILE ALA ARG LYS LEU CYS GLN ALA PRO SEQRES 20 R 536 GLY PRO ALA PRO GLY GLY GLU GLU ALA ALA ASP PRO ARG SEQRES 21 R 536 ALA SER ARG ARG ARG ALA ARG VAL VAL HIS MET LEU VAL SEQRES 22 R 536 MET VAL ALA LEU PHE PHE THR LEU SER TRP LEU PRO LEU SEQRES 23 R 536 TRP ALA LEU LEU LEU LEU ILE ASP TYR GLY GLN LEU SER SEQRES 24 R 536 ALA PRO GLN LEU HIS LEU VAL THR VAL TYR ALA PHE PRO SEQRES 25 R 536 PHE ALA HIS TRP LEU ALA PHE PHE ASN SER SER ALA ASN SEQRES 26 R 536 PRO ILE ILE TYR GLY TYR PHE ASN GLU ASN PHE ARG ARG SEQRES 27 R 536 GLY PHE GLN ALA ALA PHE ARG ALA ARG LEU CYS PRO ARG SEQRES 28 R 536 PRO SER GLY SER HIS LYS GLU ALA TYR SER GLU ARG GLY SEQRES 29 R 536 SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER SER SEQRES 30 R 536 GLY VAL PHE THR LEU GLU ASP PHE VAL GLY ASP TRP GLU SEQRES 31 R 536 GLN THR ALA ALA TYR ASN LEU ASP GLN VAL LEU GLU GLN SEQRES 32 R 536 GLY GLY VAL SER SER LEU LEU GLN ASN LEU ALA VAL SER SEQRES 33 R 536 VAL THR PRO ILE GLN ARG ILE VAL ARG SER GLY GLU ASN SEQRES 34 R 536 ALA LEU LYS ILE ASP ILE HIS VAL ILE ILE PRO TYR GLU SEQRES 35 R 536 GLY LEU SER ALA ASP GLN MET ALA GLN ILE GLU GLU VAL SEQRES 36 R 536 PHE LYS VAL VAL TYR PRO VAL ASP ASP HIS HIS PHE LYS SEQRES 37 R 536 VAL ILE LEU PRO TYR GLY THR LEU VAL ILE ASP GLY VAL SEQRES 38 R 536 THR PRO ASN MET LEU ASN TYR PHE GLY ARG PRO TYR GLU SEQRES 39 R 536 GLY ILE ALA VAL PHE ASP GLY LYS LYS ILE THR VAL THR SEQRES 40 R 536 GLY THR LEU TRP ASN GLY ASN LYS ILE ILE ASP GLU ARG SEQRES 41 R 536 LEU ILE THR PRO ASP GLY SER MET LEU PHE ARG VAL THR SEQRES 42 R 536 ILE ASN SER SEQRES 1 S 247 VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN PRO SEQRES 2 S 247 GLY GLY SER ARG LYS LEU SER CYS SER ALA SER GLY PHE SEQRES 3 S 247 ALA PHE SER SER PHE GLY MET HIS TRP VAL ARG GLN ALA SEQRES 4 S 247 PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SER SEQRES 5 S 247 GLY SER GLY THR ILE TYR TYR ALA ASP THR VAL LYS GLY SEQRES 6 S 247 ARG PHE THR ILE SER ARG ASP ASP PRO LYS ASN THR LEU SEQRES 7 S 247 PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR ALA SEQRES 8 S 247 MET TYR TYR CYS VAL ARG SER ILE TYR TYR TYR GLY SER SEQRES 9 S 247 SER PRO PHE ASP PHE TRP GLY GLN GLY THR THR LEU THR SEQRES 10 S 247 VAL SER ALA GLY GLY GLY GLY SER GLY GLY GLY GLY SER SEQRES 11 S 247 GLY GLY GLY GLY SER ALA ASP ILE VAL MET THR GLN ALA SEQRES 12 S 247 THR SER SER VAL PRO VAL THR PRO GLY GLU SER VAL SER SEQRES 13 S 247 ILE SER CYS ARG SER SER LYS SER LEU LEU HIS SER ASN SEQRES 14 S 247 GLY ASN THR TYR LEU TYR TRP PHE LEU GLN ARG PRO GLY SEQRES 15 S 247 GLN SER PRO GLN LEU LEU ILE TYR ARG MET SER ASN LEU SEQRES 16 S 247 ALA SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SER SEQRES 17 S 247 GLY THR ALA PHE THR LEU THR ILE SER ARG LEU GLU ALA SEQRES 18 S 247 GLU ASP VAL GLY VAL TYR TYR CYS MET GLN HIS LEU GLU SEQRES 19 S 247 TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU LEU HET NH2 L 9 1 HETNAM NH2 AMINO GROUP FORMUL 3 NH2 H2 N HELIX 1 AA1 SER B 2 ALA B 26 1 25 HELIX 2 AA2 THR B 29 THR B 34 1 6 HELIX 3 AA3 SER G 8 ASN G 24 1 17 HELIX 4 AA4 LYS G 29 HIS G 44 1 16 HELIX 5 AA5 SER A 6 ARG A 32 1 27 HELIX 6 AA6 GLY A 45 LYS A 54 1 10 HELIX 7 AA7 GLU A 207 GLU A 216 5 10 HELIX 8 AA8 SER A 228 TYR A 230 5 3 HELIX 9 AA9 ASN A 241 ASN A 255 1 15 HELIX 10 AB1 ASN A 256 THR A 260 5 5 HELIX 11 AB2 LYS A 270 LYS A 279 1 10 HELIX 12 AB3 THR A 295 LEU A 310 1 16 HELIX 13 AB4 THR A 327 CYS A 351 1 25 HELIX 14 AB5 SER R 40 ASN R 71 1 32 HELIX 15 AB6 THR R 76 PHE R 95 1 20 HELIX 16 AB7 CYS R 96 ILE R 106 1 11 HELIX 17 AB8 ALA R 114 HIS R 147 1 34 HELIX 18 AB9 LEU R 155 CYS R 174 1 20 HELIX 19 AC1 GLY R 211 LEU R 226 1 16 HELIX 20 AC2 LEU R 226 LEU R 243 1 18 HELIX 21 AC3 ALA R 266 TYR R 295 1 30 HELIX 22 AC4 PRO R 301 GLY R 330 1 30 HELIX 23 AC5 ALA S 28 PHE S 32 5 5 HELIX 24 AC6 SER S 53 GLY S 56 5 4 HELIX 25 AC7 ARG S 87 THR S 91 5 5 SHEET 1 AA1 4 ARG B 46 ARG B 52 0 SHEET 2 AA1 4 PHE B 335 ASN B 340 -1 O ILE B 338 N ARG B 48 SHEET 3 AA1 4 VAL B 327 SER B 331 -1 N VAL B 327 O TRP B 339 SHEET 4 AA1 4 VAL B 315 VAL B 320 -1 N GLY B 319 O ALA B 328 SHEET 1 AA2 4 ALA B 60 TRP B 63 0 SHEET 2 AA2 4 LEU B 69 ALA B 73 -1 O VAL B 71 N HIS B 62 SHEET 3 AA2 4 LYS B 78 ASP B 83 -1 O TRP B 82 N LEU B 70 SHEET 4 AA2 4 ASN B 88 PRO B 94 -1 O ILE B 93 N LEU B 79 SHEET 1 AA3 4 VAL B 100 TYR B 105 0 SHEET 2 AA3 4 TYR B 111 GLY B 116 -1 O ALA B 113 N ALA B 104 SHEET 3 AA3 4 ILE B 120 ASN B 125 -1 O TYR B 124 N VAL B 112 SHEET 4 AA3 4 ARG B 134 ALA B 140 -1 O ARG B 134 N ASN B 125 SHEET 1 AA4 4 LEU B 146 ASP B 153 0 SHEET 2 AA4 4 GLN B 156 SER B 161 -1 O SER B 160 N CYS B 148 SHEET 3 AA4 4 THR B 165 ASP B 170 -1 O ALA B 167 N THR B 159 SHEET 4 AA4 4 GLN B 175 THR B 181 -1 O PHE B 180 N CYS B 166 SHEET 1 AA5 4 VAL B 187 LEU B 192 0 SHEET 2 AA5 4 LEU B 198 ALA B 203 -1 O GLY B 202 N MET B 188 SHEET 3 AA5 4 ALA B 208 ASP B 212 -1 O TRP B 211 N PHE B 199 SHEET 4 AA5 4 CYS B 218 PHE B 222 -1 O GLN B 220 N LEU B 210 SHEET 1 AA6 4 ILE B 229 PHE B 234 0 SHEET 2 AA6 4 ALA B 240 SER B 245 -1 O GLY B 244 N ALA B 231 SHEET 3 AA6 4 CYS B 250 ASP B 254 -1 O PHE B 253 N PHE B 241 SHEET 4 AA6 4 GLN B 259 TYR B 264 -1 O TYR B 264 N CYS B 250 SHEET 1 AA7 4 ILE B 273 PHE B 278 0 SHEET 2 AA7 4 LEU B 284 TYR B 289 -1 O LEU B 286 N SER B 277 SHEET 3 AA7 4 CYS B 294 ASP B 298 -1 O TRP B 297 N LEU B 285 SHEET 4 AA7 4 ARG B 304 LEU B 308 -1 O ALA B 305 N VAL B 296 SHEET 1 AA8 6 VAL A 185 THR A 190 0 SHEET 2 AA8 6 HIS A 195 ASP A 200 -1 O MET A 198 N THR A 187 SHEET 3 AA8 6 VAL A 34 GLY A 40 1 N VAL A 34 O HIS A 195 SHEET 4 AA8 6 ALA A 220 ALA A 226 1 O ILE A 222 N LEU A 37 SHEET 5 AA8 6 ILE A 264 ASN A 269 1 O PHE A 267 N PHE A 223 SHEET 6 AA8 6 ILE A 319 PHE A 323 1 O HIS A 322 N LEU A 268 SHEET 1 AA9 4 GLN S 3 SER S 7 0 SHEET 2 AA9 4 ARG S 18 SER S 25 -1 O SER S 21 N SER S 7 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 THR S 69 O GLN S 82 SHEET 1 AB1 6 GLY S 10 VAL S 12 0 SHEET 2 AB1 6 THR S 115 VAL S 119 1 O THR S 118 N GLY S 10 SHEET 3 AB1 6 MET S 93 TYR S 95 -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 VAL S 48 N TRP S 36 SHEET 6 AB1 6 ILE S 58 TYR S 60 -1 O TYR S 59 N TYR S 50 SHEET 1 AB2 6 GLY S 10 VAL S 12 0 SHEET 2 AB2 6 THR S 115 VAL S 119 1 O THR S 118 N GLY S 10 SHEET 3 AB2 6 MET S 93 TYR S 95 -1 N TYR S 94 O THR S 115 SHEET 4 AB2 6 GLY S 33 GLN S 39 -1 N VAL S 37 O TYR S 95 SHEET 5 AB2 6 VAL S 97 SER S 99 -1 O VAL S 97 N HIS S 35 SHEET 6 AB2 6 PHE S 110 TRP S 111 -1 O PHE S 110 N ARG S 98 SHEET 1 AB3 6 SER S 146 PRO S 148 0 SHEET 2 AB3 6 THR S 243 GLU S 246 1 O GLU S 246 N VAL S 147 SHEET 3 AB3 6 GLY S 225 GLN S 231 -1 N GLY S 225 O LEU S 245 SHEET 4 AB3 6 LEU S 174 GLN S 179 -1 N GLN S 179 O VAL S 226 SHEET 5 AB3 6 GLN S 186 TYR S 190 -1 O GLN S 186 N LEU S 178 SHEET 6 AB3 6 ASN S 194 LEU S 195 -1 O ASN S 194 N TYR S 190 SHEET 1 AB4 3 VAL S 155 ARG S 160 0 SHEET 2 AB4 3 ALA S 211 ILE S 216 -1 O PHE S 212 N CYS S 159 SHEET 3 AB4 3 PHE S 203 GLY S 205 -1 N SER S 204 O THR S 215 SSBOND 1 CYS R 116 CYS R 203 1555 1555 2.03 LINK C PHE L 8 N NH2 L 9 1555 1555 1.33 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