HEADER MEMBRANE PROTEIN 18-OCT-24 9K3H TITLE CRYO-EM STRUCTURE OF THE UNLIGANDED HUMAN MELANOCORTIN RECEPTOR 5 TITLE 2 (MC5R)-GS COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: MELANOCORTIN RECEPTOR 5,MELANOCORTIN RECEPTOR 5, COMPND 3 MELANOCORTIN RECEPTOR 5,LGBIT SUBUNIT; COMPND 4 CHAIN: R; COMPND 5 SYNONYM: MC5-R,MC-2; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I) SUBUNIT ALPHA-1, COMPND 9 GUANINE NUCLEOTIDE-BINDING PROTEIN G(S) SUBUNIT ALPHA ISOFORMS SHORT; COMPND 10 CHAIN: A; COMPND 11 SYNONYM: ADENYLATE CYCLASE-INHIBITING G ALPHA PROTEIN,ADENYLATE COMPND 12 CYCLASE-STIMULATING G ALPHA PROTEIN; COMPND 13 EC: 3.6.5.-; COMPND 14 ENGINEERED: YES; COMPND 15 MUTATION: YES; COMPND 16 MOL_ID: 3; COMPND 17 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 18 BETA-1,GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 19 BETA-1,GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 20 BETA-1,HIBIT; COMPND 21 CHAIN: B; COMPND 22 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 23 ENGINEERED: YES; COMPND 24 MOL_ID: 4; COMPND 25 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 26 GAMMA-2; COMPND 27 CHAIN: G; COMPND 28 SYNONYM: G GAMMA-I; COMPND 29 ENGINEERED: YES; COMPND 30 MOL_ID: 5; COMPND 31 MOLECULE: SCFV16; COMPND 32 CHAIN: S; COMPND 33 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, SYNTHETIC CONSTRUCT; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 326; SOURCE 5 GENE: MC5R; 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 GENE: GNAI1, GNAS, GNAS1, GSP; SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS, SYNTHETIC CONSTRUCT; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606, 32630; SOURCE 19 GENE: GNB1; SOURCE 20 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 24 ORGANISM_COMMON: DOMESTIC CATTLE; SOURCE 25 ORGANISM_TAXID: 9913; SOURCE 26 GENE: GNG2; SOURCE 27 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 29 MOL_ID: 5; SOURCE 30 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 31 ORGANISM_TAXID: 32630; SOURCE 32 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 33 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS HUMAN MELANOCORTIN RECEPTOR 5, G PROTEIN-COUPLED RECEPTOR, KEYWDS 2 UNLIGANDED, CONSTITUTIVE ACTIVITY, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR W.B.FENG,Q.T.ZHOU,C.ZHENG,D.H.YANG,M.W.WANG REVDAT 1 06-AUG-25 9K3H 0 JRNL AUTH W.FENG,Q.ZHOU,C.ZHENG,D.YANG,M.W.WANG JRNL TITL STRUCTURAL BASIS FOR THE CONSTITUTIVE ACTIVITY OF THE JRNL TITL 2 MELANOCORTIN RECEPTOR FAMILY. JRNL REF STRUCTURE V. 33 1074 2025 JRNL REFN ISSN 0969-2126 JRNL PMID 40157361 JRNL DOI 10.1016/J.STR.2025.03.004 REMARK 2 REMARK 2 RESOLUTION. 2.86 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) : 2.860 REMARK 3 NUMBER OF PARTICLES : 116135 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 9K3H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 22-OCT-24. REMARK 100 THE DEPOSITION ID IS D_1300051554. 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 : CRYO-EM STRUCTURE OF UNLIGANDED REMARK 245 HUMAN MELANOCORTIN RECEPTOR 5 REMARK 245 IN COMPLEX WITH G PROTEIN 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 : 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) : 8000.00 REMARK 245 ILLUMINATION MODE : SPOT SCAN REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: R, A, B, G, S REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET R 1 REMARK 465 ASN R 2 REMARK 465 SER R 3 REMARK 465 SER R 4 REMARK 465 PHE R 5 REMARK 465 HIS R 6 REMARK 465 LEU R 7 REMARK 465 HIS R 8 REMARK 465 PHE R 9 REMARK 465 LEU R 10 REMARK 465 ASP R 11 REMARK 465 LEU R 12 REMARK 465 ASN R 13 REMARK 465 LEU R 14 REMARK 465 ASN R 15 REMARK 465 ALA R 16 REMARK 465 THR R 17 REMARK 465 GLU R 18 REMARK 465 GLY R 19 REMARK 465 ASN R 20 REMARK 465 LEU R 21 REMARK 465 SER R 22 REMARK 465 GLY R 23 REMARK 465 PRO R 24 REMARK 465 ASN R 25 REMARK 465 VAL R 26 REMARK 465 LYS R 27 REMARK 465 ASN R 28 REMARK 465 LYS R 29 REMARK 465 SER R 30 REMARK 465 SER R 31 REMARK 465 PRO R 32 REMARK 465 CYS R 33 REMARK 465 GLU R 34 REMARK 465 ASP R 35 REMARK 465 MET R 36 REMARK 465 GLY R 37 REMARK 465 SER R 227 REMARK 465 ALA R 228 REMARK 465 ARG R 229 REMARK 465 GLN R 230 REMARK 465 ARG R 313 REMARK 465 GLY R 314 REMARK 465 PHE R 315 REMARK 465 ARG R 316 REMARK 465 ILE R 317 REMARK 465 ALA R 318 REMARK 465 CYS R 319 REMARK 465 SER R 320 REMARK 465 PHE R 321 REMARK 465 PRO R 322 REMARK 465 ARG R 323 REMARK 465 ARG R 324 REMARK 465 ASP R 325 REMARK 465 GLY R 326 REMARK 465 SER R 327 REMARK 465 SER R 328 REMARK 465 GLY R 329 REMARK 465 GLY R 330 REMARK 465 GLY R 331 REMARK 465 GLY R 332 REMARK 465 SER R 333 REMARK 465 GLY R 334 REMARK 465 GLY R 335 REMARK 465 GLY R 336 REMARK 465 GLY R 337 REMARK 465 SER R 338 REMARK 465 SER R 339 REMARK 465 GLY R 340 REMARK 465 VAL R 341 REMARK 465 PHE R 342 REMARK 465 THR R 343 REMARK 465 LEU R 344 REMARK 465 GLU R 345 REMARK 465 ASP R 346 REMARK 465 PHE R 347 REMARK 465 VAL R 348 REMARK 465 GLY R 349 REMARK 465 ASP R 350 REMARK 465 TRP R 351 REMARK 465 GLU R 352 REMARK 465 GLN R 353 REMARK 465 THR R 354 REMARK 465 ALA R 355 REMARK 465 ALA R 356 REMARK 465 TYR R 357 REMARK 465 ASN R 358 REMARK 465 LEU R 359 REMARK 465 ASP R 360 REMARK 465 GLN R 361 REMARK 465 VAL R 362 REMARK 465 LEU R 363 REMARK 465 GLU R 364 REMARK 465 GLN R 365 REMARK 465 GLY R 366 REMARK 465 GLY R 367 REMARK 465 VAL R 368 REMARK 465 SER R 369 REMARK 465 SER R 370 REMARK 465 LEU R 371 REMARK 465 LEU R 372 REMARK 465 GLN R 373 REMARK 465 ASN R 374 REMARK 465 LEU R 375 REMARK 465 ALA R 376 REMARK 465 VAL R 377 REMARK 465 SER R 378 REMARK 465 VAL R 379 REMARK 465 THR R 380 REMARK 465 PRO R 381 REMARK 465 ILE R 382 REMARK 465 GLN R 383 REMARK 465 ARG R 384 REMARK 465 ILE R 385 REMARK 465 VAL R 386 REMARK 465 ARG R 387 REMARK 465 SER R 388 REMARK 465 GLY R 389 REMARK 465 GLU R 390 REMARK 465 ASN R 391 REMARK 465 ALA R 392 REMARK 465 LEU R 393 REMARK 465 LYS R 394 REMARK 465 ILE R 395 REMARK 465 ASP R 396 REMARK 465 ILE R 397 REMARK 465 HIS R 398 REMARK 465 VAL R 399 REMARK 465 ILE R 400 REMARK 465 ILE R 401 REMARK 465 PRO R 402 REMARK 465 TYR R 403 REMARK 465 GLU R 404 REMARK 465 GLY R 405 REMARK 465 LEU R 406 REMARK 465 SER R 407 REMARK 465 ALA R 408 REMARK 465 ASP R 409 REMARK 465 GLN R 410 REMARK 465 MET R 411 REMARK 465 ALA R 412 REMARK 465 GLN R 413 REMARK 465 ILE R 414 REMARK 465 GLU R 415 REMARK 465 GLU R 416 REMARK 465 VAL R 417 REMARK 465 PHE R 418 REMARK 465 LYS R 419 REMARK 465 VAL R 420 REMARK 465 VAL R 421 REMARK 465 TYR R 422 REMARK 465 PRO R 423 REMARK 465 VAL R 424 REMARK 465 ASP R 425 REMARK 465 ASP R 426 REMARK 465 HIS R 427 REMARK 465 HIS R 428 REMARK 465 PHE R 429 REMARK 465 LYS R 430 REMARK 465 VAL R 431 REMARK 465 ILE R 432 REMARK 465 LEU R 433 REMARK 465 PRO R 434 REMARK 465 TYR R 435 REMARK 465 GLY R 436 REMARK 465 THR R 437 REMARK 465 LEU R 438 REMARK 465 VAL R 439 REMARK 465 ILE R 440 REMARK 465 ASP R 441 REMARK 465 GLY R 442 REMARK 465 VAL R 443 REMARK 465 THR R 444 REMARK 465 PRO R 445 REMARK 465 ASN R 446 REMARK 465 MET R 447 REMARK 465 LEU R 448 REMARK 465 ASN R 449 REMARK 465 TYR R 450 REMARK 465 PHE R 451 REMARK 465 GLY R 452 REMARK 465 ARG R 453 REMARK 465 PRO R 454 REMARK 465 TYR R 455 REMARK 465 GLU R 456 REMARK 465 GLY R 457 REMARK 465 ILE R 458 REMARK 465 ALA R 459 REMARK 465 VAL R 460 REMARK 465 PHE R 461 REMARK 465 ASP R 462 REMARK 465 GLY R 463 REMARK 465 LYS R 464 REMARK 465 LYS R 465 REMARK 465 ILE R 466 REMARK 465 THR R 467 REMARK 465 VAL R 468 REMARK 465 THR R 469 REMARK 465 GLY R 470 REMARK 465 THR R 471 REMARK 465 LEU R 472 REMARK 465 TRP R 473 REMARK 465 ASN R 474 REMARK 465 GLY R 475 REMARK 465 ASN R 476 REMARK 465 LYS R 477 REMARK 465 ILE R 478 REMARK 465 ILE R 479 REMARK 465 ASP R 480 REMARK 465 GLU R 481 REMARK 465 ARG R 482 REMARK 465 LEU R 483 REMARK 465 ILE R 484 REMARK 465 THR R 485 REMARK 465 PRO R 486 REMARK 465 ASP R 487 REMARK 465 GLY R 488 REMARK 465 SER R 489 REMARK 465 MET R 490 REMARK 465 LEU R 491 REMARK 465 PHE R 492 REMARK 465 ARG R 493 REMARK 465 VAL R 494 REMARK 465 THR R 495 REMARK 465 ILE R 496 REMARK 465 ASN R 497 REMARK 465 SER R 498 REMARK 465 MET A 8 REMARK 465 GLY A 9 REMARK 465 CYS A 10 REMARK 465 THR A 11 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 MET 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 2 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 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 ALA G 7 REMARK 465 SER G 8 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 S -36 REMARK 465 LEU S -35 REMARK 465 LEU S -34 REMARK 465 VAL S -33 REMARK 465 ASN S -32 REMARK 465 GLN S -31 REMARK 465 SER S -30 REMARK 465 HIS S -29 REMARK 465 GLN S -28 REMARK 465 GLY S -27 REMARK 465 PHE S -26 REMARK 465 ASN S -25 REMARK 465 LYS S -24 REMARK 465 GLU S -23 REMARK 465 HIS S -22 REMARK 465 THR S -21 REMARK 465 SER S -20 REMARK 465 LYS S -19 REMARK 465 MET S -18 REMARK 465 VAL S -17 REMARK 465 SER S -16 REMARK 465 ALA S -15 REMARK 465 ILE S -14 REMARK 465 VAL S -13 REMARK 465 LEU S -12 REMARK 465 TYR S -11 REMARK 465 VAL S -10 REMARK 465 LEU S -9 REMARK 465 LEU S -8 REMARK 465 ALA S -7 REMARK 465 ALA S -6 REMARK 465 ALA S -5 REMARK 465 ALA S -4 REMARK 465 HIS S -3 REMARK 465 SER S -2 REMARK 465 ALA S -1 REMARK 465 PHE S 0 REMARK 465 ALA 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 ALA S 120Q 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 91 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP R 91 CZ3 CH2 REMARK 470 ILE R 106 CG1 CG2 CD1 REMARK 470 TYR R 269 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG R 272 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 3 CG CD OE1 OE2 REMARK 470 ASP B 5 CG OD1 OD2 REMARK 470 GLU B 12 CG CD OE1 OE2 REMARK 470 ASN B 35 CG OD1 ND2 REMARK 470 GLU B 130 CG CD OE1 OE2 REMARK 470 GLU B 215 CG CD OE1 OE2 REMARK 470 ASN B 268 CG OD1 ND2 REMARK 470 SER B 331 OG REMARK 470 TYR S 235 CG CD1 CD2 CE1 CE2 CZ OH 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 ND2 ASN R 54 OD2 ASP R 82 2.12 REMARK 500 O ILE B 58 OG SER B 316 2.14 REMARK 500 NE2 GLN B 220 OD1 ASP B 258 2.15 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 TRP R 91 47.33 -79.62 REMARK 500 TYR R 295 -61.59 -93.35 REMARK 500 CYS R 311 52.61 -93.17 REMARK 500 VAL A 20 -67.98 -122.85 REMARK 500 ARG A 38 46.14 -85.62 REMARK 500 ASN A 50 52.77 -91.23 REMARK 500 ARG A 265 53.42 -92.49 REMARK 500 ARG A 333 43.58 -85.84 REMARK 500 ASP A 354 51.87 -96.18 REMARK 500 SER A 366 -43.09 -137.53 REMARK 500 GLU A 370 48.75 -89.97 REMARK 500 GLU A 392 90.92 -65.87 REMARK 500 CYS B 25 57.48 -96.57 REMARK 500 THR B 87 18.47 56.42 REMARK 500 TRP B 99 58.05 -91.26 REMARK 500 LYS B 127 36.27 -98.55 REMARK 500 PRO B 194 42.40 -78.26 REMARK 500 CYS B 204 15.98 56.00 REMARK 500 LEU B 261 -64.05 -100.98 REMARK 500 ASN B 295 128.87 -36.16 REMARK 500 LEU B 318 118.16 -160.74 REMARK 500 SER S 99 117.13 -161.94 REMARK 500 SER S 161 -168.25 -126.15 REMARK 500 MET S 192 -14.26 71.80 REMARK 500 SER S 193 -15.41 -140.16 REMARK 500 ALA S 196 -167.48 -77.85 REMARK 500 GLU S 234 -141.61 -111.02 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-62015 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF THE LIGAND-FREE HUMAN MELANOCORTIN RECEPTOR 5 REMARK 900 (MC5R)-GS COMPLEX DBREF 9K3H R 1 325 UNP P33032 MC5R_HUMAN 1 325 DBREF 9K3H R 341 498 PDB 9K3H 9K3H 341 498 DBREF 9K3H A 8 26 UNP P63096 GNAI1_HUMAN 1 19 DBREF 9K3H A 27 83 UNP P63092 GNAS2_HUMAN 27 67 DBREF 9K3H A 84 204 UNP P63096 GNAI1_HUMAN 61 181 DBREF 9K3H A 205 253 UNP P63092 GNAS2_HUMAN 205 253 DBREF 9K3H A 264 394 UNP P63092 GNAS2_HUMAN 264 394 DBREF 9K3H B 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 9K3H B 356 366 PDB 9K3H 9K3H 356 366 DBREF 9K3H G 1 71 UNP P63212 GBG2_BOVIN 1 71 DBREF 9K3H S -36 247 PDB 9K3H 9K3H -36 247 SEQADV 9K3H GLY R 326 UNP P33032 LINKER SEQADV 9K3H SER R 327 UNP P33032 LINKER SEQADV 9K3H SER R 328 UNP P33032 LINKER SEQADV 9K3H GLY R 329 UNP P33032 LINKER SEQADV 9K3H GLY R 330 UNP P33032 LINKER SEQADV 9K3H GLY R 331 UNP P33032 LINKER SEQADV 9K3H GLY R 332 UNP P33032 LINKER SEQADV 9K3H SER R 333 UNP P33032 LINKER SEQADV 9K3H GLY R 334 UNP P33032 LINKER SEQADV 9K3H GLY R 335 UNP P33032 LINKER SEQADV 9K3H GLY R 336 UNP P33032 LINKER SEQADV 9K3H GLY R 337 UNP P33032 LINKER SEQADV 9K3H SER R 338 UNP P33032 LINKER SEQADV 9K3H SER R 339 UNP P33032 LINKER SEQADV 9K3H GLY R 340 UNP P33032 LINKER SEQADV 9K3H ASP A 49 UNP P63092 GLY 49 ENGINEERED MUTATION SEQADV 9K3H ASN A 50 UNP P63092 GLU 50 ENGINEERED MUTATION SEQADV 9K3H TYR A 63 UNP P63092 LEU 63 ENGINEERED MUTATION SEQADV 9K3H ALA A 226 UNP P63092 GLY 226 ENGINEERED MUTATION SEQADV 9K3H ASP A 249 UNP P63092 ALA 249 ENGINEERED MUTATION SEQADV 9K3H ASP A 252 UNP P63092 SER 252 ENGINEERED MUTATION SEQADV 9K3H ASP A 272 UNP P63092 LEU 272 ENGINEERED MUTATION SEQADV 9K3H SER A 366 UNP P63092 ALA 366 ENGINEERED MUTATION SEQADV 9K3H ALA A 372 UNP P63092 ILE 372 ENGINEERED MUTATION SEQADV 9K3H ILE A 375 UNP P63092 VAL 375 ENGINEERED MUTATION SEQADV 9K3H MET B -4 UNP P62873 INITIATING METHIONINE SEQADV 9K3H GLY B -3 UNP P62873 EXPRESSION TAG SEQADV 9K3H SER B -2 UNP P62873 EXPRESSION TAG SEQADV 9K3H LEU B -1 UNP P62873 EXPRESSION TAG SEQADV 9K3H LEU B 0 UNP P62873 EXPRESSION TAG SEQADV 9K3H GLN B 1 UNP P62873 EXPRESSION TAG SEQADV 9K3H GLY B 341 UNP P62873 LINKER SEQADV 9K3H SER B 342 UNP P62873 LINKER SEQADV 9K3H SER B 343 UNP P62873 LINKER SEQADV 9K3H GLY B 344 UNP P62873 LINKER SEQADV 9K3H GLY B 345 UNP P62873 LINKER SEQADV 9K3H GLY B 346 UNP P62873 LINKER SEQADV 9K3H GLY B 347 UNP P62873 LINKER SEQADV 9K3H SER B 348 UNP P62873 LINKER SEQADV 9K3H GLY B 349 UNP P62873 LINKER SEQADV 9K3H GLY B 350 UNP P62873 LINKER SEQADV 9K3H GLY B 351 UNP P62873 LINKER SEQADV 9K3H GLY B 352 UNP P62873 LINKER SEQADV 9K3H SER B 353 UNP P62873 LINKER SEQADV 9K3H SER B 354 UNP P62873 LINKER SEQADV 9K3H GLY B 355 UNP P62873 LINKER SEQRES 1 R 498 MET ASN SER SER PHE HIS LEU HIS PHE LEU ASP LEU ASN SEQRES 2 R 498 LEU ASN ALA THR GLU GLY ASN LEU SER GLY PRO ASN VAL SEQRES 3 R 498 LYS ASN LYS SER SER PRO CYS GLU ASP MET GLY ILE ALA SEQRES 4 R 498 VAL GLU VAL PHE LEU THR LEU GLY VAL ILE SER LEU LEU SEQRES 5 R 498 GLU ASN ILE LEU VAL ILE GLY ALA ILE VAL LYS ASN LYS SEQRES 6 R 498 ASN LEU HIS SER PRO MET TYR PHE PHE VAL CYS SER LEU SEQRES 7 R 498 ALA VAL ALA ASP MET LEU VAL SER MET SER SER ALA TRP SEQRES 8 R 498 GLU THR ILE THR ILE TYR LEU LEU ASN ASN LYS HIS LEU SEQRES 9 R 498 VAL ILE ALA ASP ALA PHE VAL ARG HIS ILE ASP ASN VAL SEQRES 10 R 498 PHE ASP SER MET ILE CYS ILE SER VAL VAL ALA SER MET SEQRES 11 R 498 CYS SER LEU LEU ALA ILE ALA VAL ASP ARG TYR VAL THR SEQRES 12 R 498 ILE PHE TYR ALA LEU ARG TYR HIS HIS ILE MET THR ALA SEQRES 13 R 498 ARG ARG SER GLY ALA ILE ILE ALA GLY ILE TRP ALA PHE SEQRES 14 R 498 CYS THR GLY CYS GLY ILE VAL PHE ILE LEU TYR SER GLU SEQRES 15 R 498 SER THR TYR VAL ILE LEU CYS LEU ILE SER MET PHE PHE SEQRES 16 R 498 ALA MET LEU PHE LEU LEU VAL SER LEU TYR ILE HIS MET SEQRES 17 R 498 PHE LEU LEU ALA ARG THR HIS VAL LYS ARG ILE ALA ALA SEQRES 18 R 498 LEU PRO GLY ALA SER SER ALA ARG GLN ARG THR SER MET SEQRES 19 R 498 GLN GLY ALA VAL THR VAL THR MET LEU LEU GLY VAL PHE SEQRES 20 R 498 THR VAL CYS TRP ALA PRO PHE PHE LEU HIS LEU THR LEU SEQRES 21 R 498 MET LEU SER CYS PRO GLN ASN LEU TYR CYS SER ARG PHE SEQRES 22 R 498 MET SER HIS PHE ASN MET TYR LEU ILE LEU ILE MET CYS SEQRES 23 R 498 ASN SER VAL MET ASP PRO LEU ILE TYR ALA PHE ARG SER SEQRES 24 R 498 GLN GLU MET ARG LYS THR PHE LYS GLU ILE ILE CYS CYS SEQRES 25 R 498 ARG GLY PHE ARG ILE ALA CYS SER PHE PRO ARG ARG ASP SEQRES 26 R 498 GLY SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER SEQRES 27 R 498 SER GLY VAL PHE THR LEU GLU ASP PHE VAL GLY ASP TRP SEQRES 28 R 498 GLU GLN THR ALA ALA TYR ASN LEU ASP GLN VAL LEU GLU SEQRES 29 R 498 GLN GLY GLY VAL SER SER LEU LEU GLN ASN LEU ALA VAL SEQRES 30 R 498 SER VAL THR PRO ILE GLN ARG ILE VAL ARG SER GLY GLU SEQRES 31 R 498 ASN ALA LEU LYS ILE ASP ILE HIS VAL ILE ILE PRO TYR SEQRES 32 R 498 GLU GLY LEU SER ALA ASP GLN MET ALA GLN ILE GLU GLU SEQRES 33 R 498 VAL PHE LYS VAL VAL TYR PRO VAL ASP ASP HIS HIS PHE SEQRES 34 R 498 LYS VAL ILE LEU PRO TYR GLY THR LEU VAL ILE ASP GLY SEQRES 35 R 498 VAL THR PRO ASN MET LEU ASN TYR PHE GLY ARG PRO TYR SEQRES 36 R 498 GLU GLY ILE ALA VAL PHE ASP GLY LYS LYS ILE THR VAL SEQRES 37 R 498 THR GLY THR LEU TRP ASN GLY ASN LYS ILE ILE ASP GLU SEQRES 38 R 498 ARG LEU ILE THR PRO ASP GLY SER MET LEU PHE ARG VAL SEQRES 39 R 498 THR 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 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 371 MET GLY SER LEU LEU GLN SER GLU LEU ASP GLN LEU ARG SEQRES 2 B 371 GLN GLU ALA GLU GLN LEU LYS ASN GLN ILE ARG ASP ALA SEQRES 3 B 371 ARG LYS ALA CYS ALA ASP ALA THR LEU SER GLN ILE THR SEQRES 4 B 371 ASN ASN ILE ASP PRO VAL GLY ARG ILE GLN MET ARG THR SEQRES 5 B 371 ARG ARG THR LEU ARG GLY HIS LEU ALA LYS ILE TYR ALA SEQRES 6 B 371 MET HIS TRP GLY THR ASP SER ARG LEU LEU VAL SER ALA SEQRES 7 B 371 SER GLN ASP GLY LYS LEU ILE ILE TRP ASP SER TYR THR SEQRES 8 B 371 THR ASN LYS VAL HIS ALA ILE PRO LEU ARG SER SER TRP SEQRES 9 B 371 VAL MET THR CYS ALA TYR ALA PRO SER GLY ASN TYR VAL SEQRES 10 B 371 ALA CYS GLY GLY LEU ASP ASN ILE CYS SER ILE TYR ASN SEQRES 11 B 371 LEU LYS THR ARG GLU GLY ASN VAL ARG VAL SER ARG GLU SEQRES 12 B 371 LEU ALA GLY HIS THR GLY TYR LEU SER CYS CYS ARG PHE SEQRES 13 B 371 LEU ASP ASP ASN GLN ILE VAL THR SER SER GLY ASP THR SEQRES 14 B 371 THR CYS ALA LEU TRP ASP ILE GLU THR GLY GLN GLN THR SEQRES 15 B 371 THR THR PHE THR GLY HIS THR GLY ASP VAL MET SER LEU SEQRES 16 B 371 SER LEU ALA PRO ASP THR ARG LEU PHE VAL SER GLY ALA SEQRES 17 B 371 CYS ASP ALA SER ALA LYS LEU TRP ASP VAL ARG GLU GLY SEQRES 18 B 371 MET CYS ARG GLN THR PHE THR GLY HIS GLU SER ASP ILE SEQRES 19 B 371 ASN ALA ILE CYS PHE PHE PRO ASN GLY ASN ALA PHE ALA SEQRES 20 B 371 THR GLY SER ASP ASP ALA THR CYS ARG LEU PHE ASP LEU SEQRES 21 B 371 ARG ALA ASP GLN GLU LEU MET THR TYR SER HIS ASP ASN SEQRES 22 B 371 ILE ILE CYS GLY ILE THR SER VAL SER PHE SER LYS SER SEQRES 23 B 371 GLY ARG LEU LEU LEU ALA GLY TYR ASP ASP PHE ASN CYS SEQRES 24 B 371 ASN VAL TRP ASP ALA LEU LYS ALA ASP ARG ALA GLY VAL SEQRES 25 B 371 LEU ALA GLY HIS ASP ASN ARG VAL SER CYS LEU GLY VAL SEQRES 26 B 371 THR ASP ASP GLY MET ALA VAL ALA THR GLY SER TRP ASP SEQRES 27 B 371 SER PHE LEU LYS ILE TRP ASN GLY SER SER GLY GLY GLY SEQRES 28 B 371 GLY SER GLY GLY GLY GLY SER SER GLY VAL SER GLY TRP SEQRES 29 B 371 ARG LEU PHE LYS LYS ILE SER 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 S 285 MET LEU LEU VAL ASN GLN SER HIS GLN GLY PHE ASN LYS SEQRES 2 S 285 GLU HIS THR SER LYS MET VAL SER ALA ILE VAL LEU TYR SEQRES 3 S 285 VAL LEU LEU ALA ALA ALA ALA HIS SER ALA PHE ALA VAL SEQRES 4 S 285 GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN PRO GLY SEQRES 5 S 285 GLY SER ARG LYS LEU SER CYS SER ALA SER GLY PHE ALA SEQRES 6 S 285 PHE SER SER PHE GLY MET HIS TRP VAL ARG GLN ALA PRO SEQRES 7 S 285 GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SER GLY SEQRES 8 S 285 SER GLY THR ILE TYR TYR ALA ASP THR VAL LYS GLY ARG SEQRES 9 S 285 PHE THR ILE SER ARG ASP ASP PRO LYS ASN THR LEU PHE SEQRES 10 S 285 LEU GLN MET THR SER LEU ARG SER GLU ASP THR ALA MET SEQRES 11 S 285 TYR TYR CYS VAL ARG SER ILE TYR TYR TYR GLY SER SER SEQRES 12 S 285 PRO PHE ASP PHE TRP GLY GLN GLY THR THR LEU THR VAL SEQRES 13 S 285 SER ALA GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLY SEQRES 14 S 285 GLY GLY GLY SER ALA ASP ILE VAL MET THR GLN ALA THR SEQRES 15 S 285 SER SER VAL PRO VAL THR PRO GLY GLU SER VAL SER ILE SEQRES 16 S 285 SER CYS ARG SER SER LYS SER LEU LEU HIS SER ASN GLY SEQRES 17 S 285 ASN THR TYR LEU TYR TRP PHE LEU GLN ARG PRO GLY GLN SEQRES 18 S 285 SER PRO GLN LEU LEU ILE TYR ARG MET SER ASN LEU ALA SEQRES 19 S 285 SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SER GLY SEQRES 20 S 285 THR ALA PHE THR LEU THR ILE SER ARG LEU GLU ALA GLU SEQRES 21 S 285 ASP VAL GLY VAL TYR TYR CYS MET GLN HIS LEU GLU TYR SEQRES 22 S 285 PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU LEU HELIX 1 AA1 VAL R 40 ASN R 64 1 25 HELIX 2 AA2 SER R 69 LEU R 99 1 31 HELIX 3 AA3 ALA R 107 ALA R 109 5 3 HELIX 4 AA4 PHE R 110 TYR R 146 1 37 HELIX 5 AA5 ALA R 147 ILE R 153 5 7 HELIX 6 AA6 THR R 155 TYR R 180 1 26 HELIX 7 AA7 ILE R 187 ALA R 221 1 35 HELIX 8 AA8 THR R 232 CYS R 264 1 33 HELIX 9 AA9 ASN R 267 SER R 275 1 9 HELIX 10 AB1 HIS R 276 TYR R 295 1 20 HELIX 11 AB2 SER R 299 CYS R 311 1 13 HELIX 12 AB3 ARG A 22 ARG A 38 1 17 HELIX 13 AB4 GLY A 52 HIS A 64 1 13 HELIX 14 AB5 ILE A 235 ASN A 239 5 5 HELIX 15 AB6 LEU A 266 ASN A 278 1 13 HELIX 16 AB7 ASN A 279 ARG A 283 5 5 HELIX 17 AB8 LYS A 293 ALA A 303 1 11 HELIX 18 AB9 LYS A 307 PHE A 312 1 6 HELIX 19 AC1 PRO A 313 ALA A 316 5 4 HELIX 20 AC2 ASP A 331 ALA A 351 1 21 HELIX 21 AC3 GLU A 370 TYR A 391 1 22 HELIX 22 AC4 LEU B 4 CYS B 25 1 22 HELIX 23 AC5 THR B 29 ASN B 36 1 8 HELIX 24 AC6 ILE G 9 GLN G 11 5 3 HELIX 25 AC7 ALA G 12 ILE G 25 1 14 HELIX 26 AC8 LYS G 29 ALA G 43 1 15 HELIX 27 AC9 ALA S 28 PHE S 32 5 5 HELIX 28 AD1 ASP S 74 LYS S 76 5 3 HELIX 29 AD2 ARG S 191 SER S 193 5 3 SHEET 1 AA1 6 ILE A 207 GLN A 213 0 SHEET 2 AA1 6 ASN A 218 VAL A 224 -1 O ASP A 223 N PHE A 208 SHEET 3 AA1 6 THR A 40 GLY A 47 1 N LEU A 43 O HIS A 220 SHEET 4 AA1 6 ALA A 243 ASP A 249 1 O ILE A 245 N LEU A 44 SHEET 5 AA1 6 SER A 286 ASN A 292 1 O ILE A 288 N ILE A 244 SHEET 6 AA1 6 CYS A 359 TYR A 360 1 O TYR A 360 N VAL A 287 SHEET 1 AA2 4 ARG B 46 LEU B 51 0 SHEET 2 AA2 4 LEU B 336 ASN B 340 -1 O ILE B 338 N ARG B 48 SHEET 3 AA2 4 VAL B 327 SER B 331 -1 N VAL B 327 O TRP B 339 SHEET 4 AA2 4 VAL B 315 VAL B 320 -1 N SER B 316 O GLY B 330 SHEET 1 AA3 4 ILE B 58 TRP B 63 0 SHEET 2 AA3 4 LEU B 69 SER B 74 -1 O ALA B 73 N ALA B 60 SHEET 3 AA3 4 LYS B 78 ASP B 83 -1 O ILE B 80 N SER B 72 SHEET 4 AA3 4 LYS B 89 PRO B 94 -1 O VAL B 90 N ILE B 81 SHEET 1 AA4 4 VAL B 100 TYR B 105 0 SHEET 2 AA4 4 TYR B 111 GLY B 116 -1 O GLY B 115 N MET B 101 SHEET 3 AA4 4 CYS B 121 ASN B 125 -1 O TYR B 124 N VAL B 112 SHEET 4 AA4 4 ARG B 134 LEU B 139 -1 O SER B 136 N ILE B 123 SHEET 1 AA5 4 LEU B 146 ASP B 153 0 SHEET 2 AA5 4 GLN B 156 SER B 161 -1 O GLN B 156 N LEU B 152 SHEET 3 AA5 4 THR B 165 ASP B 170 -1 O TRP B 169 N ILE B 157 SHEET 4 AA5 4 THR B 178 THR B 181 -1 O PHE B 180 N CYS B 166 SHEET 1 AA6 4 SER B 191 LEU B 192 0 SHEET 2 AA6 4 LEU B 198 GLY B 202 -1 O VAL B 200 N SER B 191 SHEET 3 AA6 4 SER B 207 ASP B 212 -1 O TRP B 211 N PHE B 199 SHEET 4 AA6 4 CYS B 218 THR B 223 -1 O GLN B 220 N LEU B 210 SHEET 1 AA7 4 ILE B 229 PHE B 234 0 SHEET 2 AA7 4 PHE B 241 SER B 245 -1 O GLY B 244 N ASN B 230 SHEET 3 AA7 4 CYS B 250 PHE B 253 -1 O ARG B 251 N THR B 243 SHEET 4 AA7 4 THR B 263 TYR B 264 -1 O TYR B 264 N CYS B 250 SHEET 1 AA8 4 SER B 275 SER B 277 0 SHEET 2 AA8 4 LEU B 284 GLY B 288 -1 O GLY B 288 N SER B 275 SHEET 3 AA8 4 VAL B 296 ASP B 298 -1 O TRP B 297 N LEU B 285 SHEET 4 AA8 4 ARG B 304 GLY B 306 -1 O GLY B 306 N VAL B 296 SHEET 1 AA9 4 GLN S 3 SER S 7 0 SHEET 2 AA9 4 SER S 17 SER S 25 -1 O SER S 23 N VAL S 5 SHEET 3 AA9 4 THR S 78 THR S 84 -1 O LEU S 79 N CYS S 22 SHEET 4 AA9 4 THR S 69 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 VAL S 12 SHEET 3 AB1 6 ALA S 92 SER S 99 -1 N TYR S 94 O THR S 115 SHEET 4 AB1 6 GLY S 33 GLN S 39 -1 N VAL S 37 O TYR S 95 SHEET 5 AB1 6 LEU S 45 ILE S 51 -1 O GLU S 46 N ARG S 38 SHEET 6 AB1 6 ILE S 58 TYR S 60 -1 O TYR S 59 N TYR S 50 SHEET 1 AB2 4 MET S 140 THR S 141 0 SHEET 2 AB2 4 VAL S 155 SER S 161 -1 O ARG S 160 N THR S 141 SHEET 3 AB2 4 ALA S 211 ILE S 216 -1 O PHE S 212 N CYS S 159 SHEET 4 AB2 4 PHE S 203 GLY S 207 -1 N SER S 204 O THR S 215 SHEET 1 AB3 6 SER S 146 PRO S 148 0 SHEET 2 AB3 6 THR S 243 GLU S 246 1 O LYS S 244 N VAL S 147 SHEET 3 AB3 6 GLY S 225 GLN S 231 -1 N TYR S 227 O THR S 243 SHEET 4 AB3 6 LEU S 174 GLN S 179 -1 N TYR S 175 O MET S 230 SHEET 5 AB3 6 PRO S 185 TYR S 190 -1 O LEU S 188 N TRP S 176 SHEET 6 AB3 6 ASN S 194 LEU S 195 -1 O ASN S 194 N TYR S 190 SSBOND 1 CYS R 264 CYS R 270 1555 1555 2.03 SSBOND 2 CYS S 22 CYS S 96 1555 1555 2.03 SSBOND 3 CYS S 159 CYS S 229 1555 1555 2.03 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000