HEADER MEMBRANE PROTEIN 24-FEB-24 9AS4 TITLE GLOBAL RECONSTRUCTION OF 5-HT2AR BOUND TO LSD IN COMPLEX WITH A MINI- TITLE 2 GQ PROTEIN AND SCFV16 OBTAINED BY CRYO-ELECTRON MICROSCOPY (CRYOEM) COMPND MOL_ID: 1; COMPND 2 MOLECULE: 5-HYDROXYTRYPTAMINE RECEPTOR 2A; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: 5-HT-2,5-HT-2A,SEROTONIN RECEPTOR 2A; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: G SUBUNIT Q (GI2-MINI-GQ CHIMERIC); COMPND 8 CHAIN: B; 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: C; COMPND 14 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 15 ENGINEERED: YES; COMPND 16 MOL_ID: 4; COMPND 17 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 18 GAMMA-2; COMPND 19 CHAIN: D; COMPND 20 SYNONYM: G GAMMA-I; COMPND 21 ENGINEERED: YES; COMPND 22 MOL_ID: 5; COMPND 23 MOLECULE: SINGLE CHAIN FAB (SVFV16); COMPND 24 CHAIN: E; COMPND 25 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: HTR2A, HTR2; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_COMMON: HUMAN; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 15 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS; SOURCE 18 MOL_ID: 3; SOURCE 19 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 20 ORGANISM_COMMON: HUMAN; SOURCE 21 ORGANISM_TAXID: 9606; SOURCE 22 GENE: GNB1; SOURCE 23 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 24 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 26 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS; SOURCE 27 MOL_ID: 4; SOURCE 28 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 29 ORGANISM_COMMON: HUMAN; SOURCE 30 ORGANISM_TAXID: 9606; SOURCE 31 GENE: GNG2; SOURCE 32 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 33 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 34 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 35 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS; SOURCE 36 MOL_ID: 5; SOURCE 37 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 38 ORGANISM_COMMON: HUMAN; SOURCE 39 ORGANISM_TAXID: 9606; SOURCE 40 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 41 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 42 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 43 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS KEYWDS GPCR, G-PROTEIN COUPLED RECEPTOR, 5-HT2AR, SEROTONIN, PSYCHEDELICS, KEYWDS 2 MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR R.H.GUMPPER,J.F.FAY,B.L.ROTH REVDAT 1 02-APR-25 9AS4 0 JRNL AUTH R.H.GUMPPER,M.K.JAIN,K.KIM,R.SUN,N.SUN,Z.XU,J.F.DIBERTO, JRNL AUTH 2 B.E.KRUMM,N.J.KAPOLKA,H.U.KANISKAN,D.E.NICHOLS,J.JIN, JRNL AUTH 3 J.F.FAY,B.L.ROTH JRNL TITL THE STRUCTURAL DIVERSITY OF PSYCHEDELIC DRUG ACTIONS JRNL TITL 2 REVEALED. JRNL REF NAT COMMUN V. 16 2734 2025 JRNL REFN ESSN 2041-1723 JRNL PMID 40108183 JRNL DOI 10.1038/S41467-025-57956-7 REMARK 2 REMARK 2 RESOLUTION. 3.06 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.060 REMARK 3 NUMBER OF PARTICLES : 168657 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 9AS4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-FEB-24. REMARK 100 THE DEPOSITION ID IS D_1000281843. 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 : 5-HT2AR IN COMPLEX WITH MINI-GQ 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 : FEI TALOS ARCTICA REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 160.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2600.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : OTHER REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 4950.00 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) : 200 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 1 REMARK 465 ASP A 2 REMARK 465 ILE A 3 REMARK 465 LEU A 4 REMARK 465 CYS A 5 REMARK 465 GLU A 6 REMARK 465 GLU A 7 REMARK 465 ASN A 8 REMARK 465 THR A 9 REMARK 465 SER A 10 REMARK 465 LEU A 11 REMARK 465 SER A 12 REMARK 465 SER A 13 REMARK 465 THR A 14 REMARK 465 THR A 15 REMARK 465 ASN A 16 REMARK 465 SER A 17 REMARK 465 LEU A 18 REMARK 465 MET A 19 REMARK 465 GLN A 20 REMARK 465 LEU A 21 REMARK 465 ASN A 22 REMARK 465 ASP A 23 REMARK 465 ASP A 24 REMARK 465 THR A 25 REMARK 465 ARG A 26 REMARK 465 LEU A 27 REMARK 465 TYR A 28 REMARK 465 SER A 29 REMARK 465 ASN A 30 REMARK 465 ASP A 31 REMARK 465 PHE A 32 REMARK 465 ASN A 33 REMARK 465 SER A 34 REMARK 465 GLY A 35 REMARK 465 GLU A 36 REMARK 465 ALA A 37 REMARK 465 ASN A 38 REMARK 465 THR A 39 REMARK 465 SER A 40 REMARK 465 ASP A 41 REMARK 465 ALA A 42 REMARK 465 PHE A 43 REMARK 465 ASN A 44 REMARK 465 TRP A 45 REMARK 465 THR A 46 REMARK 465 VAL A 47 REMARK 465 ASP A 48 REMARK 465 SER A 49 REMARK 465 GLU A 50 REMARK 465 ASN A 51 REMARK 465 ARG A 52 REMARK 465 THR A 53 REMARK 465 ASN A 54 REMARK 465 LEU A 55 REMARK 465 SER A 56 REMARK 465 CYS A 57 REMARK 465 GLU A 58 REMARK 465 GLY A 59 REMARK 465 CYS A 60 REMARK 465 LEU A 61 REMARK 465 SER A 62 REMARK 465 PRO A 63 REMARK 465 SER A 64 REMARK 465 CYS A 65 REMARK 465 LEU A 66 REMARK 465 SER A 67 REMARK 465 LEU A 68 REMARK 465 LEU A 69 REMARK 465 HIS A 70 REMARK 465 LEU A 71 REMARK 465 GLN A 72 REMARK 465 GLU A 73 REMARK 465 LYS A 74 REMARK 465 ASN A 75 REMARK 465 TRP A 76 REMARK 465 SER A 77 REMARK 465 ALA A 78 REMARK 465 LEU A 79 REMARK 465 LEU A 80 REMARK 465 THR A 81 REMARK 465 ALA A 82 REMARK 465 VAL A 83 REMARK 465 SER A 100 REMARK 465 LEU A 101 REMARK 465 GLU A 102 REMARK 465 LYS A 103 REMARK 465 LYS A 104 REMARK 465 LEU A 143 REMARK 465 PRO A 144 REMARK 465 LYS A 263 REMARK 465 GLU A 264 REMARK 465 ALA A 265 REMARK 465 THR A 266 REMARK 465 LEU A 267 REMARK 465 CYS A 268 REMARK 465 VAL A 269 REMARK 465 SER A 270 REMARK 465 ASP A 271 REMARK 465 LEU A 272 REMARK 465 GLY A 273 REMARK 465 THR A 274 REMARK 465 ARG A 275 REMARK 465 ALA A 276 REMARK 465 LYS A 277 REMARK 465 LEU A 278 REMARK 465 ALA A 279 REMARK 465 SER A 280 REMARK 465 PHE A 281 REMARK 465 SER A 282 REMARK 465 PHE A 283 REMARK 465 LEU A 284 REMARK 465 PRO A 285 REMARK 465 GLN A 286 REMARK 465 SER A 287 REMARK 465 SER A 288 REMARK 465 LEU A 289 REMARK 465 SER A 290 REMARK 465 SER A 291 REMARK 465 GLU A 292 REMARK 465 LYS A 293 REMARK 465 LEU A 294 REMARK 465 PHE A 295 REMARK 465 GLN A 296 REMARK 465 ARG A 297 REMARK 465 SER A 298 REMARK 465 ILE A 299 REMARK 465 HIS A 300 REMARK 465 ARG A 301 REMARK 465 GLU A 302 REMARK 465 PRO A 303 REMARK 465 GLY A 304 REMARK 465 SER A 305 REMARK 465 TYR A 306 REMARK 465 THR A 307 REMARK 465 GLY A 308 REMARK 465 ARG A 309 REMARK 465 ARG A 310 REMARK 465 THR A 311 REMARK 465 MET A 312 REMARK 465 GLN A 313 REMARK 465 SER A 314 REMARK 465 ILE A 348 REMARK 465 CYS A 349 REMARK 465 LYS A 350 REMARK 465 GLU A 351 REMARK 465 SER A 352 REMARK 465 CYS A 353 REMARK 465 TYR A 394 REMARK 465 ILE A 395 REMARK 465 GLN A 396 REMARK 465 CYS A 397 REMARK 465 GLN A 398 REMARK 465 TYR A 399 REMARK 465 LYS A 400 REMARK 465 GLU A 401 REMARK 465 ASN A 402 REMARK 465 LYS A 403 REMARK 465 LYS A 404 REMARK 465 PRO A 405 REMARK 465 LEU A 406 REMARK 465 GLN A 407 REMARK 465 LEU A 408 REMARK 465 ILE A 409 REMARK 465 LEU A 410 REMARK 465 VAL A 411 REMARK 465 ASN A 412 REMARK 465 THR A 413 REMARK 465 ILE A 414 REMARK 465 PRO A 415 REMARK 465 ALA A 416 REMARK 465 LEU A 417 REMARK 465 ALA A 418 REMARK 465 TYR A 419 REMARK 465 LYS A 420 REMARK 465 SER A 421 REMARK 465 SER A 422 REMARK 465 GLN A 423 REMARK 465 LEU A 424 REMARK 465 GLN A 425 REMARK 465 MET A 426 REMARK 465 GLY A 427 REMARK 465 GLN A 428 REMARK 465 LYS A 429 REMARK 465 LYS A 430 REMARK 465 ASN A 431 REMARK 465 SER A 432 REMARK 465 LYS A 433 REMARK 465 GLN A 434 REMARK 465 ASP A 435 REMARK 465 ALA A 436 REMARK 465 LYS A 437 REMARK 465 THR A 438 REMARK 465 THR A 439 REMARK 465 ASP A 440 REMARK 465 ASN A 441 REMARK 465 ASP A 442 REMARK 465 CYS A 443 REMARK 465 SER A 444 REMARK 465 MET A 445 REMARK 465 VAL A 446 REMARK 465 ALA A 447 REMARK 465 LEU A 448 REMARK 465 GLY A 449 REMARK 465 LYS A 450 REMARK 465 GLN A 451 REMARK 465 HIS A 452 REMARK 465 SER A 453 REMARK 465 GLU A 454 REMARK 465 GLU A 455 REMARK 465 ALA A 456 REMARK 465 SER A 457 REMARK 465 LYS A 458 REMARK 465 ASP A 459 REMARK 465 ASN A 460 REMARK 465 SER A 461 REMARK 465 ASP A 462 REMARK 465 GLY A 463 REMARK 465 VAL A 464 REMARK 465 ASN A 465 REMARK 465 GLU A 466 REMARK 465 LYS A 467 REMARK 465 VAL A 468 REMARK 465 SER A 469 REMARK 465 CYS A 470 REMARK 465 VAL A 471 REMARK 465 MET B 1 REMARK 465 GLY B 2 REMARK 465 SER B 3 REMARK 465 ILE B 55 REMARK 465 LEU B 56 REMARK 465 HIS B 57 REMARK 465 GLY B 58 REMARK 465 GLY B 59 REMARK 465 SER B 60 REMARK 465 GLY B 61 REMARK 465 GLY B 62 REMARK 465 SER B 63 REMARK 465 GLY B 64 REMARK 465 GLY B 65 REMARK 465 GLU B 174 REMARK 465 ASP B 175 REMARK 465 ALA B 176 REMARK 465 THR B 177 REMARK 465 PRO B 178 REMARK 465 GLU B 179 REMARK 465 PRO B 180 REMARK 465 GLY B 181 REMARK 465 MET C -17 REMARK 465 HIS C -16 REMARK 465 HIS C -15 REMARK 465 HIS C -14 REMARK 465 HIS C -13 REMARK 465 HIS C -12 REMARK 465 HIS C -11 REMARK 465 LEU C -10 REMARK 465 GLU C -9 REMARK 465 VAL C -8 REMARK 465 LEU C -7 REMARK 465 PHE C -6 REMARK 465 GLN C -5 REMARK 465 GLY C -4 REMARK 465 PRO C -3 REMARK 465 GLY C -2 REMARK 465 SER C -1 REMARK 465 SER C 0 REMARK 465 GLY C 1 REMARK 465 SER C 2 REMARK 465 GLU C 3 REMARK 465 LEU C 4 REMARK 465 ASP C 5 REMARK 465 GLN C 6 REMARK 465 LEU C 7 REMARK 465 ARG C 8 REMARK 465 GLN C 9 REMARK 465 MET D 1 REMARK 465 ALA D 2 REMARK 465 SER D 3 REMARK 465 ASN D 4 REMARK 465 ASN D 5 REMARK 465 THR D 6 REMARK 465 ALA D 7 REMARK 465 SER D 8 REMARK 465 ILE D 9 REMARK 465 ALA D 10 REMARK 465 GLN D 11 REMARK 465 ARG D 62 REMARK 465 GLU D 63 REMARK 465 LYS D 64 REMARK 465 LYS D 65 REMARK 465 PHE D 66 REMARK 465 PHE D 67 REMARK 465 CYS D 68 REMARK 465 ALA D 69 REMARK 465 ILE D 70 REMARK 465 LEU D 71 REMARK 465 ASP E 1 REMARK 465 TRP E 36 REMARK 465 SER E 119A REMARK 465 SER E 119B REMARK 465 GLY E 119C REMARK 465 GLY E 119D REMARK 465 GLY E 119E REMARK 465 GLY E 119F REMARK 465 SER E 119G REMARK 465 GLY E 119H REMARK 465 GLY E 119I REMARK 465 GLY E 119J REMARK 465 GLY E 119K REMARK 465 SER E 119L REMARK 465 GLY E 119M REMARK 465 GLY E 119N REMARK 465 GLY E 119O REMARK 465 GLY E 119P REMARK 465 SER E 119Q REMARK 465 LYS E 236 REMARK 465 ALA E 237 REMARK 465 ALA E 238 REMARK 465 ALA E 239 REMARK 465 LEU E 240 REMARK 465 GLU E 241 REMARK 465 VAL E 242 REMARK 465 LEU E 243 REMARK 465 PHE E 244 REMARK 465 GLN E 245 REMARK 465 GLY E 246 REMARK 465 PRO E 247 REMARK 465 HIS E 248 REMARK 465 HIS E 249 REMARK 465 HIS E 250 REMARK 465 HIS E 251 REMARK 465 HIS E 252 REMARK 465 HIS E 253 REMARK 465 HIS E 254 REMARK 465 HIS E 255 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ARG A 140 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 185 CG CD NE CZ NH1 NH2 REMARK 470 ASN A 187 CG OD1 ND2 REMARK 470 ARG A 189 CG CD NE CZ NH1 NH2 REMARK 470 PHE A 213 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASP A 218 CG OD1 OD2 REMARK 470 SER A 219 OG REMARK 470 LYS A 220 CG CD CE NZ REMARK 470 PHE A 222 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS A 223 CG CD CE NZ REMARK 470 ASP A 231 CG OD1 OD2 REMARK 470 ASP A 232 CG OD1 OD2 REMARK 470 ILE A 315 CG1 CG2 CD1 REMARK 470 GLN A 319 CG CD OE1 NE2 REMARK 470 ASN A 354 CG OD1 ND2 REMARK 470 GLU A 355 CG CD OE1 OE2 REMARK 470 ASP A 356 CG OD1 OD2 REMARK 470 SER A 392 OG REMARK 470 ARG A 393 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 28 CG CD OE1 OE2 REMARK 470 ARG B 32 CG CD NE CZ NH1 NH2 REMARK 470 GLN B 52 CG CD OE1 NE2 REMARK 470 PHE B 70 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS B 78 CG CD CE NZ REMARK 470 ARG B 90 CG CD NE CZ NH1 NH2 REMARK 470 ASP B 91 CG OD1 OD2 REMARK 470 ARG B 94 CG CD NE CZ NH1 NH2 REMARK 470 ASP B 111 CG OD1 OD2 REMARK 470 GLU B 120 CG CD OE1 OE2 REMARK 470 LEU B 148 CG CD1 CD2 REMARK 470 LYS B 157 CG CD CE NZ REMARK 470 LYS B 159 CG CD CE NZ REMARK 470 GLU B 161 CG CD OE1 OE2 REMARK 470 ASP B 162 CG OD1 OD2 REMARK 470 ARG B 169 CG CD NE CZ NH1 NH2 REMARK 470 THR B 171 OG1 CG2 REMARK 470 ARG B 185 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 195 CG CD CE NZ REMARK 470 ASP B 206 CG OD1 OD2 REMARK 470 ARG B 208 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 10 CG CD OE1 OE2 REMARK 470 GLU C 12 CG CD OE1 OE2 REMARK 470 GLN C 13 CG CD OE1 NE2 REMARK 470 LYS C 15 CG CD CE NZ REMARK 470 ASN C 16 CG OD1 ND2 REMARK 470 ARG C 19 CG CD NE CZ NH1 NH2 REMARK 470 ASP C 20 CG OD1 OD2 REMARK 470 LYS C 23 CG CD CE NZ REMARK 470 ASN C 35 CG OD1 ND2 REMARK 470 ASP C 38 CG OD1 OD2 REMARK 470 GLN C 44 CG CD OE1 NE2 REMARK 470 ARG C 46 CG CD NE CZ NH1 NH2 REMARK 470 ARG C 197 CG CD NE CZ NH1 NH2 REMARK 470 ASP C 291 CG OD1 OD2 REMARK 470 ARG D 13 CG CD NE CZ NH1 NH2 REMARK 470 LYS D 14 CG CD CE NZ REMARK 470 GLU D 17 CG CD OE1 OE2 REMARK 470 LYS D 20 CG CD CE NZ REMARK 470 MET D 21 CG SD CE REMARK 470 GLU D 22 CG CD OE1 OE2 REMARK 470 ASP D 26 CG OD1 OD2 REMARK 470 LYS D 29 CG CD CE NZ REMARK 470 LYS D 32 CG CD CE NZ REMARK 470 ASP D 36 CG OD1 OD2 REMARK 470 LYS D 46 CG CD CE NZ REMARK 470 GLU E 42 CG CD OE1 OE2 REMARK 470 GLU E 46 CG CD OE1 OE2 REMARK 470 LYS E 76 CG CD CE NZ REMARK 470 GLU E 89 CG CD OE1 OE2 REMARK 470 GLN E 130 CG CD OE1 NE2 REMARK 470 THR E 132 OG1 CG2 REMARK 470 THR E 138 OG1 CG2 REMARK 470 GLU E 141 CG CD OE1 OE2 REMARK 470 ARG E 206 CG CD NE CZ NH1 NH2 REMARK 470 GLU E 210 CG CD OE1 OE2 REMARK 470 GLU E 234 CG CD OE1 OE2 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 TYR A 139 -4.84 74.44 REMARK 500 SER A 219 -3.84 -140.79 REMARK 500 LYS A 220 -64.31 -90.05 REMARK 500 PHE A 222 -171.48 -171.71 REMARK 500 PHE A 243 -50.48 -121.19 REMARK 500 ASN C 36 68.16 -102.05 REMARK 500 THR C 47 93.58 -68.21 REMARK 500 SER C 67 -3.82 80.57 REMARK 500 GLU C 130 -3.18 82.71 REMARK 500 THR C 196 -9.80 78.22 REMARK 500 MET E 180 -15.78 76.39 REMARK 500 THR E 198 -9.69 77.21 REMARK 500 GLU E 210 -0.24 78.47 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-43804 RELATED DB: EMDB REMARK 900 GLOBAL RECONSTRUCTION OF 5-HT2AR BOUND TO LSD IN COMPLEX WITH A REMARK 900 MINI-GQ PROTEIN AND SCFV16 OBTAINED BY CRYO-ELECTRON MICROSCOPY REMARK 900 (CRYOEM) DBREF 9AS4 A 1 471 UNP P28223 5HT2A_HUMAN 1 471 DBREF 9AS4 B 1 246 PDB 9AS4 9AS4 1 246 DBREF 9AS4 C 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 9AS4 D 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 9AS4 E 1 255 PDB 9AS4 9AS4 1 255 SEQADV 9AS4 MET C -17 UNP P62873 EXPRESSION TAG SEQADV 9AS4 HIS C -16 UNP P62873 EXPRESSION TAG SEQADV 9AS4 HIS C -15 UNP P62873 EXPRESSION TAG SEQADV 9AS4 HIS C -14 UNP P62873 EXPRESSION TAG SEQADV 9AS4 HIS C -13 UNP P62873 EXPRESSION TAG SEQADV 9AS4 HIS C -12 UNP P62873 EXPRESSION TAG SEQADV 9AS4 HIS C -11 UNP P62873 EXPRESSION TAG SEQADV 9AS4 LEU C -10 UNP P62873 EXPRESSION TAG SEQADV 9AS4 GLU C -9 UNP P62873 EXPRESSION TAG SEQADV 9AS4 VAL C -8 UNP P62873 EXPRESSION TAG SEQADV 9AS4 LEU C -7 UNP P62873 EXPRESSION TAG SEQADV 9AS4 PHE C -6 UNP P62873 EXPRESSION TAG SEQADV 9AS4 GLN C -5 UNP P62873 EXPRESSION TAG SEQADV 9AS4 GLY C -4 UNP P62873 EXPRESSION TAG SEQADV 9AS4 PRO C -3 UNP P62873 EXPRESSION TAG SEQADV 9AS4 GLY C -2 UNP P62873 EXPRESSION TAG SEQADV 9AS4 SER C -1 UNP P62873 EXPRESSION TAG SEQADV 9AS4 SER C 0 UNP P62873 EXPRESSION TAG SEQADV 9AS4 GLY C 1 UNP P62873 EXPRESSION TAG SEQRES 1 A 471 MET ASP ILE LEU CYS GLU GLU ASN THR SER LEU SER SER SEQRES 2 A 471 THR THR ASN SER LEU MET GLN LEU ASN ASP ASP THR ARG SEQRES 3 A 471 LEU TYR SER ASN ASP PHE ASN SER GLY GLU ALA ASN THR SEQRES 4 A 471 SER ASP ALA PHE ASN TRP THR VAL ASP SER GLU ASN ARG SEQRES 5 A 471 THR ASN LEU SER CYS GLU GLY CYS LEU SER PRO SER CYS SEQRES 6 A 471 LEU SER LEU LEU HIS LEU GLN GLU LYS ASN TRP SER ALA SEQRES 7 A 471 LEU LEU THR ALA VAL VAL ILE ILE LEU THR ILE ALA GLY SEQRES 8 A 471 ASN ILE LEU VAL ILE MET ALA VAL SER LEU GLU LYS LYS SEQRES 9 A 471 LEU GLN ASN ALA THR ASN TYR PHE LEU MET SER LEU ALA SEQRES 10 A 471 ILE ALA ASP MET LEU LEU GLY PHE LEU VAL MET PRO VAL SEQRES 11 A 471 SER MET LEU THR ILE LEU TYR GLY TYR ARG TRP PRO LEU SEQRES 12 A 471 PRO SER LYS LEU CYS ALA VAL TRP ILE TYR LEU ASP VAL SEQRES 13 A 471 LEU PHE SER THR ALA SER ILE MET HIS LEU CYS ALA ILE SEQRES 14 A 471 SER LEU ASP ARG TYR VAL ALA ILE GLN ASN PRO ILE HIS SEQRES 15 A 471 HIS SER ARG PHE ASN SER ARG THR LYS ALA PHE LEU LYS SEQRES 16 A 471 ILE ILE ALA VAL TRP THR ILE SER VAL GLY ILE SER MET SEQRES 17 A 471 PRO ILE PRO VAL PHE GLY LEU GLN ASP ASP SER LYS VAL SEQRES 18 A 471 PHE LYS GLU GLY SER CYS LEU LEU ALA ASP ASP ASN PHE SEQRES 19 A 471 VAL LEU ILE GLY SER PHE VAL SER PHE PHE ILE PRO LEU SEQRES 20 A 471 THR ILE MET VAL ILE THR TYR PHE LEU THR ILE LYS SER SEQRES 21 A 471 LEU GLN LYS GLU ALA THR LEU CYS VAL SER ASP LEU GLY SEQRES 22 A 471 THR ARG ALA LYS LEU ALA SER PHE SER PHE LEU PRO GLN SEQRES 23 A 471 SER SER LEU SER SER GLU LYS LEU PHE GLN ARG SER ILE SEQRES 24 A 471 HIS ARG GLU PRO GLY SER TYR THR GLY ARG ARG THR MET SEQRES 25 A 471 GLN SER ILE SER ASN GLU GLN LYS ALA CYS LYS VAL LEU SEQRES 26 A 471 GLY ILE VAL PHE PHE LEU PHE VAL VAL MET TRP CYS PRO SEQRES 27 A 471 PHE PHE ILE THR ASN ILE MET ALA VAL ILE CYS LYS GLU SEQRES 28 A 471 SER CYS ASN GLU ASP VAL ILE GLY ALA LEU LEU ASN VAL SEQRES 29 A 471 PHE VAL TRP ILE GLY TYR LEU SER SER ALA VAL ASN PRO SEQRES 30 A 471 LEU VAL TYR THR LEU PHE ASN LYS THR TYR ARG SER ALA SEQRES 31 A 471 PHE SER ARG TYR ILE GLN CYS GLN TYR LYS GLU ASN LYS SEQRES 32 A 471 LYS PRO LEU GLN LEU ILE LEU VAL ASN THR ILE PRO ALA SEQRES 33 A 471 LEU ALA TYR LYS SER SER GLN LEU GLN MET GLY GLN LYS SEQRES 34 A 471 LYS ASN SER LYS GLN ASP ALA LYS THR THR ASP ASN ASP SEQRES 35 A 471 CYS SER MET VAL ALA LEU GLY LYS GLN HIS SER GLU GLU SEQRES 36 A 471 ALA SER LYS ASP ASN SER ASP GLY VAL ASN GLU LYS VAL SEQRES 37 A 471 SER CYS VAL SEQRES 1 B 246 MET GLY SER THR VAL SER ALA GLU ASP LYS ALA ALA ALA SEQRES 2 B 246 GLU ARG SER LYS MET ILE ASP LYS ASN LEU ARG GLU ASP SEQRES 3 B 246 GLY GLU LYS ALA ARG ARG THR LEU ARG LEU LEU LEU LEU SEQRES 4 B 246 GLY ALA ASP ASN SER GLY LYS SER THR ILE VAL LYS GLN SEQRES 5 B 246 MET ARG ILE LEU HIS GLY GLY SER GLY GLY SER GLY GLY SEQRES 6 B 246 THR SER GLY ILE PHE GLU THR LYS PHE GLN VAL ASP LYS SEQRES 7 B 246 VAL ASN PHE HIS MET PHE ASP VAL GLY GLY GLN ARG ASP SEQRES 8 B 246 GLU ARG ARG LYS TRP ILE GLN CYS PHE ASN ASP VAL THR SEQRES 9 B 246 ALA ILE ILE PHE VAL VAL ASP SER SER ASP TYR ASN ARG SEQRES 10 B 246 LEU GLN GLU ALA LEU ASN ASP PHE LYS SER ILE TRP ASN SEQRES 11 B 246 ASN ARG TRP LEU ARG THR ILE SER VAL ILE LEU PHE LEU SEQRES 12 B 246 ASN LYS GLN ASP LEU LEU ALA GLU LYS VAL LEU ALA GLY SEQRES 13 B 246 LYS SER LYS ILE GLU ASP TYR PHE PRO GLU PHE ALA ARG SEQRES 14 B 246 TYR THR THR PRO GLU ASP ALA THR PRO GLU PRO GLY GLU SEQRES 15 B 246 ASP PRO ARG VAL THR ARG ALA LYS TYR PHE ILE ARG LYS SEQRES 16 B 246 GLU PHE VAL ASP ILE SER THR ALA SER GLY ASP GLY ARG SEQRES 17 B 246 HIS ILE CYS TYR PRO HIS PHE THR CYS ALA VAL ASP THR SEQRES 18 B 246 GLU ASN ALA ARG ARG ILE PHE ASN ASP CYS LYS ASP ILE SEQRES 19 B 246 ILE LEU GLN MET ASN LEU ARG GLU TYR ASN LEU VAL SEQRES 1 C 358 MET HIS HIS HIS HIS HIS HIS LEU GLU VAL LEU PHE GLN SEQRES 2 C 358 GLY PRO GLY SER SER GLY SER GLU LEU ASP GLN LEU ARG SEQRES 3 C 358 GLN GLU ALA GLU GLN LEU LYS ASN GLN ILE ARG ASP ALA SEQRES 4 C 358 ARG LYS ALA CYS ALA ASP ALA THR LEU SER GLN ILE THR SEQRES 5 C 358 ASN ASN ILE ASP PRO VAL GLY ARG ILE GLN MET ARG THR SEQRES 6 C 358 ARG ARG THR LEU ARG GLY HIS LEU ALA LYS ILE TYR ALA SEQRES 7 C 358 MET HIS TRP GLY THR ASP SER ARG LEU LEU VAL SER ALA SEQRES 8 C 358 SER GLN ASP GLY LYS LEU ILE ILE TRP ASP SER TYR THR SEQRES 9 C 358 THR ASN LYS VAL HIS ALA ILE PRO LEU ARG SER SER TRP SEQRES 10 C 358 VAL MET THR CYS ALA TYR ALA PRO SER GLY ASN TYR VAL SEQRES 11 C 358 ALA CYS GLY GLY LEU ASP ASN ILE CYS SER ILE TYR ASN SEQRES 12 C 358 LEU LYS THR ARG GLU GLY ASN VAL ARG VAL SER ARG GLU SEQRES 13 C 358 LEU ALA GLY HIS THR GLY TYR LEU SER CYS CYS ARG PHE SEQRES 14 C 358 LEU ASP ASP ASN GLN ILE VAL THR SER SER GLY ASP THR SEQRES 15 C 358 THR CYS ALA LEU TRP ASP ILE GLU THR GLY GLN GLN THR SEQRES 16 C 358 THR THR PHE THR GLY HIS THR GLY ASP VAL MET SER LEU SEQRES 17 C 358 SER LEU ALA PRO ASP THR ARG LEU PHE VAL SER GLY ALA SEQRES 18 C 358 CYS ASP ALA SER ALA LYS LEU TRP ASP VAL ARG GLU GLY SEQRES 19 C 358 MET CYS ARG GLN THR PHE THR GLY HIS GLU SER ASP ILE SEQRES 20 C 358 ASN ALA ILE CYS PHE PHE PRO ASN GLY ASN ALA PHE ALA SEQRES 21 C 358 THR GLY SER ASP ASP ALA THR CYS ARG LEU PHE ASP LEU SEQRES 22 C 358 ARG ALA ASP GLN GLU LEU MET THR TYR SER HIS ASP ASN SEQRES 23 C 358 ILE ILE CYS GLY ILE THR SER VAL SER PHE SER LYS SER SEQRES 24 C 358 GLY ARG LEU LEU LEU ALA GLY TYR ASP ASP PHE ASN CYS SEQRES 25 C 358 ASN VAL TRP ASP ALA LEU LYS ALA ASP ARG ALA GLY VAL SEQRES 26 C 358 LEU ALA GLY HIS ASP ASN ARG VAL SER CYS LEU GLY VAL SEQRES 27 C 358 THR ASP ASP GLY MET ALA VAL ALA THR GLY SER TRP ASP SEQRES 28 C 358 SER PHE LEU LYS ILE TRP ASN SEQRES 1 D 71 MET ALA SER ASN ASN THR ALA SER ILE ALA GLN ALA ARG SEQRES 2 D 71 LYS LEU VAL GLU GLN LEU LYS MET GLU ALA ASN ILE ASP SEQRES 3 D 71 ARG ILE LYS VAL SER LYS ALA ALA ALA ASP LEU MET ALA SEQRES 4 D 71 TYR CYS GLU ALA HIS ALA LYS GLU ASP PRO LEU LEU THR SEQRES 5 D 71 PRO VAL PRO ALA SER GLU ASN PRO PHE ARG GLU LYS LYS SEQRES 6 D 71 PHE PHE CYS ALA ILE LEU SEQRES 1 E 267 ASP VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 E 267 PRO GLY GLY SER ARG LYS LEU SER CYS SER ALA SER GLY SEQRES 3 E 267 PHE ALA PHE SER SER PHE GLY MET HIS TRP VAL ARG GLN SEQRES 4 E 267 ALA PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SEQRES 5 E 267 SER GLY SER GLY THR ILE TYR TYR ALA ASP THR VAL LYS SEQRES 6 E 267 GLY ARG PHE THR ILE SER ARG ASP ASP PRO LYS ASN THR SEQRES 7 E 267 LEU PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR SEQRES 8 E 267 ALA MET TYR TYR CYS VAL ARG SER ILE TYR TYR TYR GLY SEQRES 9 E 267 SER SER PRO PHE ASP PHE TRP GLY GLN GLY THR THR LEU SEQRES 10 E 267 THR VAL SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SEQRES 11 E 267 SER GLY GLY GLY GLY SER ASP ILE VAL MET THR GLN ALA SEQRES 12 E 267 THR SER SER VAL PRO VAL THR PRO GLY GLU SER VAL SER SEQRES 13 E 267 ILE SER CYS ARG SER SER LYS SER LEU LEU HIS SER ASN SEQRES 14 E 267 GLY ASN THR TYR LEU TYR TRP PHE LEU GLN ARG PRO GLY SEQRES 15 E 267 GLN SER PRO GLN LEU LEU ILE TYR ARG MET SER ASN LEU SEQRES 16 E 267 ALA SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SER SEQRES 17 E 267 GLY THR ALA PHE THR LEU THR ILE SER ARG LEU GLU ALA SEQRES 18 E 267 GLU ASP VAL GLY VAL TYR TYR CYS MET GLN HIS LEU GLU SEQRES 19 E 267 TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU LEU SEQRES 20 E 267 LYS ALA ALA ALA LEU GLU VAL LEU PHE GLN GLY PRO HIS SEQRES 21 E 267 HIS HIS HIS HIS HIS HIS HIS HET 7LD A 501 24 HETNAM 7LD (8ALPHA)-N,N-DIETHYL-6-METHYL-9,10-DIDEHYDROERGOLINE-8- HETNAM 2 7LD CARBOXAMIDE HETSYN 7LD LYSERGIC ACID DIETHYLAMIDE FORMUL 6 7LD C20 H25 N3 O HELIX 1 AA1 VAL A 84 VAL A 99 1 16 HELIX 2 AA2 THR A 109 LEU A 122 1 14 HELIX 3 AA3 VAL A 127 TYR A 137 1 11 HELIX 4 AA4 LEU A 147 ASN A 179 1 33 HELIX 5 AA5 ASN A 179 PHE A 186 1 8 HELIX 6 AA6 THR A 190 SER A 207 1 18 HELIX 7 AA7 MET A 208 PHE A 213 1 6 HELIX 8 AA8 ASN A 233 SER A 239 1 7 HELIX 9 AA9 PHE A 243 LEU A 261 1 19 HELIX 10 AB1 SER A 316 VAL A 347 1 32 HELIX 11 AB2 GLU A 355 LEU A 382 1 28 HELIX 12 AB3 ASN A 384 ARG A 393 1 10 HELIX 13 AB4 SER B 6 THR B 33 1 28 HELIX 14 AB5 GLY B 45 ILE B 49 5 5 HELIX 15 AB6 TYR B 115 ASN B 130 1 16 HELIX 16 AB7 LYS B 145 GLY B 156 1 12 HELIX 17 AB8 LYS B 159 PHE B 164 1 6 HELIX 18 AB9 PHE B 164 ARG B 169 1 6 HELIX 19 AC1 ASP B 183 ALA B 203 1 21 HELIX 20 AC2 ASN B 223 TYR B 243 1 21 HELIX 21 AC3 ALA C 11 ALA C 26 1 16 HELIX 22 AC4 THR C 29 ASN C 35 1 7 HELIX 23 AC5 ARG D 13 ASN D 24 1 12 HELIX 24 AC6 LYS D 29 HIS D 44 1 16 HELIX 25 AC7 SER E 53 GLY E 56 5 4 HELIX 26 AC8 ARG E 87 THR E 91 5 5 SHEET 1 AA1 6 PHE B 70 VAL B 76 0 SHEET 2 AA1 6 VAL B 79 ASP B 85 -1 O ASP B 85 N PHE B 70 SHEET 3 AA1 6 LEU B 34 LEU B 39 1 N LEU B 36 O HIS B 82 SHEET 4 AA1 6 ALA B 105 ASP B 111 1 O ILE B 107 N LEU B 37 SHEET 5 AA1 6 SER B 138 ASN B 144 1 O ILE B 140 N ILE B 106 SHEET 6 AA1 6 CYS B 211 THR B 216 1 O HIS B 214 N LEU B 143 SHEET 1 AA2 4 THR C 47 LEU C 51 0 SHEET 2 AA2 4 LEU C 336 TRP C 339 -1 O ILE C 338 N ARG C 49 SHEET 3 AA2 4 VAL C 327 SER C 331 -1 N VAL C 327 O TRP C 339 SHEET 4 AA2 4 VAL C 315 VAL C 320 -1 N GLY C 319 O ALA C 328 SHEET 1 AA3 4 ILE C 58 TRP C 63 0 SHEET 2 AA3 4 LEU C 69 SER C 74 -1 O ALA C 73 N ALA C 60 SHEET 3 AA3 4 LYS C 78 ASP C 83 -1 O TRP C 82 N LEU C 70 SHEET 4 AA3 4 ASN C 88 PRO C 94 -1 O ASN C 88 N ASP C 83 SHEET 1 AA4 4 THR C 102 TYR C 105 0 SHEET 2 AA4 4 TYR C 111 GLY C 115 -1 O ALA C 113 N ALA C 104 SHEET 3 AA4 4 CYS C 121 ASN C 125 -1 O TYR C 124 N VAL C 112 SHEET 4 AA4 4 ARG C 134 LEU C 139 -1 O LEU C 139 N CYS C 121 SHEET 1 AA5 4 LEU C 146 PHE C 151 0 SHEET 2 AA5 4 GLN C 156 SER C 161 -1 O VAL C 158 N ARG C 150 SHEET 3 AA5 4 CYS C 166 ASP C 170 -1 O TRP C 169 N ILE C 157 SHEET 4 AA5 4 GLN C 175 PHE C 180 -1 O PHE C 180 N CYS C 166 SHEET 1 AA6 4 VAL C 187 LEU C 192 0 SHEET 2 AA6 4 LEU C 198 ALA C 203 -1 O VAL C 200 N SER C 191 SHEET 3 AA6 4 ALA C 208 ASP C 212 -1 O TRP C 211 N PHE C 199 SHEET 4 AA6 4 MET C 217 PHE C 222 -1 O PHE C 222 N ALA C 208 SHEET 1 AA7 4 ILE C 229 PHE C 234 0 SHEET 2 AA7 4 ALA C 240 SER C 245 -1 O GLY C 244 N ALA C 231 SHEET 3 AA7 4 CYS C 250 ASP C 254 -1 O PHE C 253 N PHE C 241 SHEET 4 AA7 4 GLU C 260 TYR C 264 -1 O TYR C 264 N CYS C 250 SHEET 1 AA8 4 ILE C 273 PHE C 278 0 SHEET 2 AA8 4 LEU C 284 TYR C 289 -1 O GLY C 288 N SER C 275 SHEET 3 AA8 4 CYS C 294 ASP C 298 -1 O TRP C 297 N LEU C 285 SHEET 4 AA8 4 ASP C 303 LEU C 308 -1 O ASP C 303 N ASP C 298 SHEET 1 AA9 4 GLN E 3 SER E 7 0 SHEET 2 AA9 4 ARG E 18 SER E 25 -1 O SER E 21 N SER E 7 SHEET 3 AA9 4 THR E 78 MET E 83 -1 O LEU E 81 N LEU E 20 SHEET 4 AA9 4 PHE E 68 ASP E 73 -1 N THR E 69 O GLN E 82 SHEET 1 AB1 5 GLY E 10 LEU E 11 0 SHEET 2 AB1 5 THR E 115 THR E 118 1 O THR E 116 N GLY E 10 SHEET 3 AB1 5 ALA E 92 TYR E 94 -1 N ALA E 92 O LEU E 117 SHEET 4 AB1 5 ARG E 38 GLN E 39 -1 N GLN E 39 O MET E 93 SHEET 5 AB1 5 LEU E 45 GLU E 46 -1 O GLU E 46 N ARG E 38 SHEET 1 AB2 3 GLY E 33 MET E 34 0 SHEET 2 AB2 3 VAL E 97 SER E 99 -1 O SER E 99 N GLY E 33 SHEET 3 AB2 3 PHE E 110 TRP E 111 -1 O PHE E 110 N ARG E 98 SHEET 1 AB3 2 ALA E 49 ILE E 51 0 SHEET 2 AB3 2 ILE E 58 TYR E 60 -1 O TYR E 59 N TYR E 50 SHEET 1 AB4 2 SER E 134 PRO E 136 0 SHEET 2 AB4 2 LYS E 232 GLU E 234 1 O GLU E 234 N VAL E 135 SHEET 1 AB5 3 VAL E 143 ARG E 148 0 SHEET 2 AB5 3 ALA E 199 ILE E 204 -1 O ILE E 204 N VAL E 143 SHEET 3 AB5 3 PHE E 191 SER E 196 -1 N SER E 192 O THR E 203 SHEET 1 AB6 4 ASN E 182 LEU E 183 0 SHEET 2 AB6 4 GLN E 174 TYR E 178 -1 N TYR E 178 O ASN E 182 SHEET 3 AB6 4 LEU E 162 GLN E 167 -1 N TRP E 164 O LEU E 176 SHEET 4 AB6 4 VAL E 214 GLN E 219 -1 O MET E 218 N TYR E 163 SSBOND 1 CYS A 148 CYS A 227 1555 1555 2.03 SSBOND 2 CYS E 22 CYS E 96 1555 1555 2.05 SSBOND 3 CYS E 147 CYS E 217 1555 1555 2.03 CISPEP 1 TYR E 223 PRO E 224 0 -1.50 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