HEADER MEMBRANE PROTEIN 13-MAY-24 9BSB TITLE GLOBAL RECONSTRUCTION OF DRD2 BOUND TO LSD IN COMPLEX WITH A MINI-GOA TITLE 2 AND SCFV16 OBTAINED BY CRYO-ELECTRON MICROSCOPY (CRYOEM) 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: C; COMPND 11 SYNONYM: G GAMMA-I; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 3; COMPND 14 MOLECULE: SOLUBLE CYTOCHROME B562,D(2) DOPAMINE RECEPTOR; COMPND 15 CHAIN: R; COMPND 16 SYNONYM: CYTOCHROME B-562,DOPAMINE D2 RECEPTOR; COMPND 17 ENGINEERED: YES; COMPND 18 MOL_ID: 4; COMPND 19 MOLECULE: SINGLE CHAIN FAB 16 (SCFV16); COMPND 20 CHAIN: E; COMPND 21 ENGINEERED: YES; COMPND 22 MOL_ID: 5; COMPND 23 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(O) SUBUNIT ALPHA; COMPND 24 CHAIN: A; 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: GNB1; 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 GENE: GNG2; SOURCE 15 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 16 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS; SOURCE 19 MOL_ID: 3; SOURCE 20 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI, HOMO SAPIENS; SOURCE 21 ORGANISM_COMMON: HUMAN; SOURCE 22 ORGANISM_TAXID: 562, 9606; SOURCE 23 GENE: CYBC, DRD2; SOURCE 24 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 25 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 27 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS; SOURCE 28 MOL_ID: 4; SOURCE 29 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 30 ORGANISM_TAXID: 10090; SOURCE 31 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 32 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 33 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 34 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS; SOURCE 35 MOL_ID: 5; SOURCE 36 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 37 ORGANISM_COMMON: HUMAN; SOURCE 38 ORGANISM_TAXID: 9606; SOURCE 39 GENE: GNAO1; 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, DRD2, SEROTONIN, PSYCHEDELICS, KEYWDS 2 MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR K.KIM,R.H.GUMPPER,J.F.FAY,B.L.ROTH REVDAT 1 17-SEP-25 9BSB 0 JRNL AUTH M.K.JAIN,R.H.GUMPPER,S.T.SLOCUM,G.P.SCHMITZ,J.S.MADSEN, JRNL AUTH 2 T.A.TUMMINO,C.M.SUOMIVUORI,X.P.HUANG,L.SHUB,J.F.DIBERTO, JRNL AUTH 3 K.KIM,C.DELEON,B.E.KRUMM,J.F.FAY,M.KEISER,A.S.HAUSER, JRNL AUTH 4 R.O.DROR,B.SHOICHET,D.E.GLORIAM,D.E.NICHOLS,B.L.ROTH JRNL TITL THE POLYPHARMACOLOGY OF PSYCHEDELICS REVEALS MULTIPLE JRNL TITL 2 TARGETS FOR POTENTIAL THERAPEUTICS. JRNL REF NEURON 2025 JRNL REFN ISSN 0896-6273 JRNL PMID 40683247 JRNL DOI 10.1016/J.NEURON.2025.06.012 REMARK 2 REMARK 2 RESOLUTION. 2.32 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) : 2.320 REMARK 3 NUMBER OF PARTICLES : 248552 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 9BSB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAY-24. REMARK 100 THE DEPOSITION ID IS D_1000281890. 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 : DRD2 IN COMPLEX MINI-GOA 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) : 170.00 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: B, C, R, E, A 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 -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 GLU B 3 REMARK 465 LEU B 4 REMARK 465 ASP B 5 REMARK 465 GLN B 6 REMARK 465 LEU B 7 REMARK 465 ARG B 8 REMARK 465 GLN B 9 REMARK 465 GLY B 341 REMARK 465 SER B 342 REMARK 465 SER B 343 REMARK 465 MET C 1 REMARK 465 ALA C 2 REMARK 465 SER C 3 REMARK 465 ASN C 4 REMARK 465 ASN C 5 REMARK 465 THR C 6 REMARK 465 ALA C 7 REMARK 465 SER C 8 REMARK 465 ILE C 9 REMARK 465 ALA C 10 REMARK 465 GLN C 11 REMARK 465 GLU C 63 REMARK 465 LYS C 64 REMARK 465 LYS C 65 REMARK 465 PHE C 66 REMARK 465 PHE C 67 REMARK 465 CYS C 68 REMARK 465 ALA C 69 REMARK 465 ILE C 70 REMARK 465 LEU C 71 REMARK 465 ASP R -144 REMARK 465 TYR R -143 REMARK 465 LYS R -142 REMARK 465 ASP R -141 REMARK 465 ASP R -140 REMARK 465 ASP R -139 REMARK 465 ASP R -138 REMARK 465 ALA R -137 REMARK 465 LYS R -136 REMARK 465 LEU R -135 REMARK 465 GLN R -134 REMARK 465 THR R -133 REMARK 465 MET R -132 REMARK 465 HIS R -131 REMARK 465 HIS R -130 REMARK 465 HIS R -129 REMARK 465 HIS R -128 REMARK 465 HIS R -127 REMARK 465 HIS R -126 REMARK 465 HIS R -125 REMARK 465 HIS R -124 REMARK 465 HIS R -123 REMARK 465 HIS R -122 REMARK 465 HIS R -121 REMARK 465 HIS R -120 REMARK 465 HIS R -119 REMARK 465 HIS R -118 REMARK 465 HIS R -117 REMARK 465 ALA R -116 REMARK 465 ASP R -115 REMARK 465 LEU R -114 REMARK 465 GLU R -113 REMARK 465 ASP R -112 REMARK 465 ASN R -111 REMARK 465 TRP R -110 REMARK 465 GLU R -109 REMARK 465 THR R -108 REMARK 465 LEU R -107 REMARK 465 ASN R -106 REMARK 465 ASP R -105 REMARK 465 ASN R -104 REMARK 465 LEU R -103 REMARK 465 LYS R -102 REMARK 465 VAL R -101 REMARK 465 ILE R -100 REMARK 465 GLU R -99 REMARK 465 LYS R -98 REMARK 465 ALA R -97 REMARK 465 ASP R -96 REMARK 465 ASN R -95 REMARK 465 ALA R -94 REMARK 465 ALA R -93 REMARK 465 GLN R -92 REMARK 465 VAL R -91 REMARK 465 LYS R -90 REMARK 465 ASP R -89 REMARK 465 ALA R -88 REMARK 465 LEU R -87 REMARK 465 THR R -86 REMARK 465 LYS R -85 REMARK 465 MET R -84 REMARK 465 ARG R -83 REMARK 465 ALA R -82 REMARK 465 ALA R -81 REMARK 465 ALA R -80 REMARK 465 LEU R -79 REMARK 465 ASP R -78 REMARK 465 ALA R -77 REMARK 465 GLN R -76 REMARK 465 LYS R -75 REMARK 465 ALA R -74 REMARK 465 THR R -73 REMARK 465 PRO R -72 REMARK 465 PRO R -71 REMARK 465 LYS R -70 REMARK 465 LEU R -69 REMARK 465 GLU R -68 REMARK 465 ASP R -67 REMARK 465 LYS R -66 REMARK 465 SER R -65 REMARK 465 PRO R -64 REMARK 465 ASP R -63 REMARK 465 SER R -62 REMARK 465 PRO R -61 REMARK 465 GLU R -60 REMARK 465 MET R -59 REMARK 465 LYS R -58 REMARK 465 ASP R -57 REMARK 465 PHE R -56 REMARK 465 ARG R -55 REMARK 465 HIS R -54 REMARK 465 GLY R -53 REMARK 465 PHE R -52 REMARK 465 ASP R -51 REMARK 465 ILE R -50 REMARK 465 LEU R -49 REMARK 465 VAL R -48 REMARK 465 GLY R -47 REMARK 465 GLN R -46 REMARK 465 ILE R -45 REMARK 465 ASP R -44 REMARK 465 ASP R -43 REMARK 465 ALA R -42 REMARK 465 LEU R -41 REMARK 465 LYS R -40 REMARK 465 LEU R -39 REMARK 465 ALA R -38 REMARK 465 ASN R -37 REMARK 465 GLU R -36 REMARK 465 GLY R -35 REMARK 465 LYS R -34 REMARK 465 VAL R -33 REMARK 465 LYS R -32 REMARK 465 GLU R -31 REMARK 465 ALA R -30 REMARK 465 GLN R -29 REMARK 465 ALA R -28 REMARK 465 ALA R -27 REMARK 465 ALA R -26 REMARK 465 GLU R -25 REMARK 465 GLN R -24 REMARK 465 LEU R -23 REMARK 465 LYS R -22 REMARK 465 THR R -21 REMARK 465 THR R -20 REMARK 465 ARG R -19 REMARK 465 ASN R -18 REMARK 465 ALA R -17 REMARK 465 TYR R -16 REMARK 465 ILE R -15 REMARK 465 GLN R -14 REMARK 465 LYS R -13 REMARK 465 TYR R -12 REMARK 465 LEU R -11 REMARK 465 ALA R -10 REMARK 465 SER R -9 REMARK 465 GLU R -8 REMARK 465 ASN R -7 REMARK 465 LEU R -6 REMARK 465 TYR R -5 REMARK 465 PHE R -4 REMARK 465 GLN R -3 REMARK 465 GLY R -2 REMARK 465 GLY R -1 REMARK 465 THR R 0 REMARK 465 MET R 1 REMARK 465 ASP R 2 REMARK 465 PRO R 3 REMARK 465 LEU R 4 REMARK 465 ASN R 5 REMARK 465 LEU R 6 REMARK 465 SER R 7 REMARK 465 TRP R 8 REMARK 465 TYR R 9 REMARK 465 ASP R 10 REMARK 465 ASP R 11 REMARK 465 ASP R 12 REMARK 465 LEU R 13 REMARK 465 GLU R 14 REMARK 465 ARG R 15 REMARK 465 GLN R 16 REMARK 465 ASN R 17 REMARK 465 TRP R 18 REMARK 465 SER R 19 REMARK 465 ARG R 20 REMARK 465 PRO R 21 REMARK 465 PHE R 22 REMARK 465 ASN R 23 REMARK 465 GLY R 24 REMARK 465 SER R 25 REMARK 465 ASP R 26 REMARK 465 GLY R 27 REMARK 465 LYS R 28 REMARK 465 ALA R 29 REMARK 465 ASP R 30 REMARK 465 ARG R 31 REMARK 465 PRO R 32 REMARK 465 HIS R 33 REMARK 465 ASN R 224 REMARK 465 THR R 225 REMARK 465 LYS R 226 REMARK 465 ARG R 227 REMARK 465 SER R 228 REMARK 465 SER R 229 REMARK 465 ARG R 230 REMARK 465 ALA R 231 REMARK 465 PHE R 232 REMARK 465 ARG R 233 REMARK 465 ALA R 234 REMARK 465 HIS R 235 REMARK 465 LEU R 236 REMARK 465 ARG R 237 REMARK 465 ALA R 238 REMARK 465 PRO R 239 REMARK 465 LEU R 240 REMARK 465 LYS R 241 REMARK 465 GLY R 242 REMARK 465 ASN R 243 REMARK 465 CYS R 244 REMARK 465 THR R 245 REMARK 465 HIS R 246 REMARK 465 PRO R 247 REMARK 465 GLU R 248 REMARK 465 ASP R 249 REMARK 465 MET R 250 REMARK 465 LYS R 251 REMARK 465 LEU R 252 REMARK 465 CYS R 253 REMARK 465 THR R 254 REMARK 465 VAL R 255 REMARK 465 ILE R 256 REMARK 465 MET R 257 REMARK 465 LYS R 258 REMARK 465 SER R 259 REMARK 465 ASN R 260 REMARK 465 GLY R 261 REMARK 465 SER R 262 REMARK 465 PHE R 263 REMARK 465 PRO R 264 REMARK 465 VAL R 265 REMARK 465 ASN R 266 REMARK 465 ARG R 267 REMARK 465 ARG R 268 REMARK 465 ARG R 269 REMARK 465 VAL R 270 REMARK 465 GLU R 271 REMARK 465 ALA R 272 REMARK 465 ALA R 273 REMARK 465 ARG R 274 REMARK 465 ARG R 275 REMARK 465 ALA R 276 REMARK 465 GLN R 277 REMARK 465 GLU R 278 REMARK 465 LEU R 279 REMARK 465 GLU R 280 REMARK 465 MET R 281 REMARK 465 GLU R 282 REMARK 465 MET R 283 REMARK 465 LEU R 284 REMARK 465 SER R 285 REMARK 465 SER R 286 REMARK 465 THR R 287 REMARK 465 SER R 288 REMARK 465 PRO R 289 REMARK 465 PRO R 290 REMARK 465 GLU R 291 REMARK 465 ARG R 292 REMARK 465 THR R 293 REMARK 465 ARG R 294 REMARK 465 TYR R 295 REMARK 465 SER R 296 REMARK 465 PRO R 297 REMARK 465 ILE R 298 REMARK 465 PRO R 299 REMARK 465 PRO R 300 REMARK 465 SER R 301 REMARK 465 HIS R 302 REMARK 465 HIS R 303 REMARK 465 GLN R 304 REMARK 465 LEU R 305 REMARK 465 THR R 306 REMARK 465 LEU R 307 REMARK 465 PRO R 308 REMARK 465 ASP R 309 REMARK 465 PRO R 310 REMARK 465 SER R 311 REMARK 465 HIS R 312 REMARK 465 HIS R 313 REMARK 465 GLY R 314 REMARK 465 LEU R 315 REMARK 465 HIS R 316 REMARK 465 SER R 317 REMARK 465 THR R 318 REMARK 465 PRO R 319 REMARK 465 ASP R 320 REMARK 465 SER R 321 REMARK 465 PRO R 322 REMARK 465 ALA R 323 REMARK 465 LYS R 324 REMARK 465 PRO R 325 REMARK 465 GLU R 326 REMARK 465 LYS R 327 REMARK 465 ASN R 328 REMARK 465 GLY R 329 REMARK 465 HIS R 330 REMARK 465 ALA R 331 REMARK 465 LYS R 332 REMARK 465 ASP R 333 REMARK 465 HIS R 334 REMARK 465 PRO R 335 REMARK 465 LYS R 336 REMARK 465 ILE R 337 REMARK 465 ALA R 338 REMARK 465 LYS R 339 REMARK 465 ILE R 340 REMARK 465 PHE R 341 REMARK 465 GLU R 342 REMARK 465 ILE R 343 REMARK 465 GLN R 344 REMARK 465 THR R 345 REMARK 465 MET R 346 REMARK 465 PRO R 347 REMARK 465 ASN R 348 REMARK 465 GLY R 349 REMARK 465 LYS R 350 REMARK 465 THR R 351 REMARK 465 ARG R 352 REMARK 465 THR R 353 REMARK 465 SER R 354 REMARK 465 LEU R 355 REMARK 465 LYS R 356 REMARK 465 THR R 357 REMARK 465 MET R 358 REMARK 465 SER R 359 REMARK 465 ARG R 360 REMARK 465 ARG R 361 REMARK 465 LYS R 362 REMARK 465 LEU R 363 REMARK 465 CYS R 399 REMARK 465 ASP R 400 REMARK 465 CYS R 401 REMARK 465 ILE R 440 REMARK 465 LEU R 441 REMARK 465 HIS R 442 REMARK 465 CYS R 443 REMARK 465 GLY E 122 REMARK 465 GLY E 123 REMARK 465 GLY E 124 REMARK 465 GLY E 125 REMARK 465 SER E 126 REMARK 465 GLY E 127 REMARK 465 GLY E 128 REMARK 465 GLY E 129 REMARK 465 GLY E 130 REMARK 465 SER E 131 REMARK 465 GLY E 132 REMARK 465 GLY E 133 REMARK 465 GLY E 134 REMARK 465 GLY E 135 REMARK 465 LYS E 248 REMARK 465 GLY E 249 REMARK 465 SER E 250 REMARK 465 LEU E 251 REMARK 465 GLU E 252 REMARK 465 VAL E 253 REMARK 465 LEU E 254 REMARK 465 PHE E 255 REMARK 465 GLN E 256 REMARK 465 GLY E 257 REMARK 465 PRO E 258 REMARK 465 ALA E 259 REMARK 465 ALA E 260 REMARK 465 ALA E 261 REMARK 465 HIS E 262 REMARK 465 HIS E 263 REMARK 465 HIS E 264 REMARK 465 HIS E 265 REMARK 465 HIS E 266 REMARK 465 HIS E 267 REMARK 465 HIS E 268 REMARK 465 MET A 1 REMARK 465 GLY A 2 REMARK 465 CYS A 3 REMARK 465 THR A 4 REMARK 465 ILE A 56 REMARK 465 HIS A 57 REMARK 465 GLU A 58 REMARK 465 ASP A 59 REMARK 465 GLY A 60 REMARK 465 PHE A 61 REMARK 465 SER A 62 REMARK 465 GLY A 63 REMARK 465 GLU A 64 REMARK 465 ASP A 65 REMARK 465 VAL A 66 REMARK 465 LYS A 67 REMARK 465 GLN A 68 REMARK 465 TYR A 69 REMARK 465 LYS A 70 REMARK 465 PRO 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 LEU A 81 REMARK 465 ALA A 82 REMARK 465 ALA A 83 REMARK 465 ILE A 84 REMARK 465 VAL A 85 REMARK 465 ARG A 86 REMARK 465 ALA A 87 REMARK 465 MET A 88 REMARK 465 ASP A 89 REMARK 465 THR A 90 REMARK 465 LEU A 91 REMARK 465 GLY A 92 REMARK 465 ILE A 93 REMARK 465 GLU A 94 REMARK 465 TYR A 95 REMARK 465 GLY A 96 REMARK 465 ASP A 97 REMARK 465 LYS A 98 REMARK 465 GLU A 99 REMARK 465 ARG A 100 REMARK 465 LYS A 101 REMARK 465 ALA A 102 REMARK 465 ASP A 103 REMARK 465 ALA A 104 REMARK 465 LYS A 105 REMARK 465 MET A 106 REMARK 465 VAL A 107 REMARK 465 CYS A 108 REMARK 465 ASP A 109 REMARK 465 VAL A 110 REMARK 465 VAL A 111 REMARK 465 SER A 112 REMARK 465 ARG A 113 REMARK 465 MET A 114 REMARK 465 GLU A 115 REMARK 465 ASP A 116 REMARK 465 THR A 117 REMARK 465 GLU A 118 REMARK 465 PRO A 119 REMARK 465 PHE A 120 REMARK 465 SER A 121 REMARK 465 ALA A 122 REMARK 465 GLU A 123 REMARK 465 LEU A 124 REMARK 465 LEU A 125 REMARK 465 SER A 126 REMARK 465 ALA A 127 REMARK 465 MET A 128 REMARK 465 MET A 129 REMARK 465 ARG A 130 REMARK 465 LEU A 131 REMARK 465 TRP A 132 REMARK 465 GLY A 133 REMARK 465 ASP A 134 REMARK 465 SER A 135 REMARK 465 GLY A 136 REMARK 465 ILE A 137 REMARK 465 GLN A 138 REMARK 465 GLU A 139 REMARK 465 CYS A 140 REMARK 465 PHE A 141 REMARK 465 ASN A 142 REMARK 465 ARG A 143 REMARK 465 SER A 144 REMARK 465 ARG A 145 REMARK 465 GLU A 146 REMARK 465 TYR A 147 REMARK 465 GLN A 148 REMARK 465 LEU A 149 REMARK 465 ASN A 150 REMARK 465 ASP A 151 REMARK 465 SER A 152 REMARK 465 ALA A 153 REMARK 465 LYS A 154 REMARK 465 TYR A 155 REMARK 465 TYR A 156 REMARK 465 LEU A 157 REMARK 465 ASP A 158 REMARK 465 SER A 159 REMARK 465 LEU A 160 REMARK 465 ASP A 161 REMARK 465 ARG A 162 REMARK 465 ILE A 163 REMARK 465 GLY A 164 REMARK 465 ALA A 165 REMARK 465 ALA A 166 REMARK 465 ASP A 167 REMARK 465 TYR A 168 REMARK 465 GLN A 169 REMARK 465 PRO A 170 REMARK 465 THR A 171 REMARK 465 GLU A 172 REMARK 465 GLN A 173 REMARK 465 ASP A 174 REMARK 465 ILE A 175 REMARK 465 LEU A 176 REMARK 465 ARG A 177 REMARK 465 THR A 178 REMARK 465 ARG A 179 REMARK 465 VAL A 180 REMARK 465 LYS A 181 REMARK 465 THR A 182 REMARK 465 ASP A 232 REMARK 465 GLN A 233 REMARK 465 VAL A 234 REMARK 465 LEU A 235 REMARK 465 HIS A 236 REMARK 465 GLU A 237 REMARK 465 ASP A 238 REMARK 465 GLU A 239 REMARK 465 THR A 240 REMARK 465 THR A 241 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 GLU B 12 CG CD OE1 OE2 REMARK 470 GLN B 13 CG CD OE1 NE2 REMARK 470 LYS B 15 CG CD CE NZ REMARK 470 ASN B 16 CG OD1 ND2 REMARK 470 GLN B 17 CG CD OE1 NE2 REMARK 470 ARG B 19 CG CD NE CZ NH1 NH2 REMARK 470 ASP B 20 CG OD1 OD2 REMARK 470 LYS B 23 CG CD CE NZ REMARK 470 ASN B 36 CG OD1 ND2 REMARK 470 ARG B 46 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 134 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 172 CG CD OE1 OE2 REMARK 470 ARG B 197 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 214 CG CD NE CZ NH1 NH2 REMARK 470 ARG C 13 CG CD NE CZ NH1 NH2 REMARK 470 LYS C 14 CG CD CE NZ REMARK 470 GLU C 17 CG CD OE1 OE2 REMARK 470 LYS C 20 CG CD CE NZ REMARK 470 MET C 21 CG SD CE REMARK 470 GLU C 22 CG CD OE1 OE2 REMARK 470 ASN C 24 CG OD1 ND2 REMARK 470 ASP C 26 CG OD1 OD2 REMARK 470 LYS C 32 CG CD CE NZ REMARK 470 GLU C 42 CG CD OE1 OE2 REMARK 470 LYS C 46 CG CD CE NZ REMARK 470 GLU C 47 CG CD OE1 OE2 REMARK 470 GLU C 58 CG CD OE1 OE2 REMARK 470 ARG C 62 CG CD NE CZ NH1 NH2 REMARK 470 TYR R 34 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TYR R 36 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TYR R 37 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 MET R 57 CG SD CE REMARK 470 ARG R 61 CG CD NE CZ NH1 NH2 REMARK 470 GLU R 62 CG CD OE1 OE2 REMARK 470 LYS R 63 CG CD CE NZ REMARK 470 GLU R 99 CG CD OE1 OE2 REMARK 470 LYS R 101 CG CD CE NZ REMARK 470 ARG R 104 CG CD NE CZ NH1 NH2 REMARK 470 ARG R 145 CG CD NE CZ NH1 NH2 REMARK 470 TYR R 146 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG R 150 CG CD NE CZ NH1 NH2 REMARK 470 PHE R 164 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASP R 178 CG OD1 OD2 REMARK 470 TYR R 192 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG R 217 CG CD NE CZ NH1 NH2 REMARK 470 ARG R 220 CG CD NE CZ NH1 NH2 REMARK 470 LYS R 221 CG CD CE NZ REMARK 470 ARG R 222 CG CD NE CZ NH1 NH2 REMARK 470 GLN R 366 CG CD OE1 NE2 REMARK 470 LYS R 367 CG CD CE NZ REMARK 470 LYS R 369 CG CD CE NZ REMARK 470 ASN R 396 CG OD1 ND2 REMARK 470 ASN R 402 CG OD1 ND2 REMARK 470 LYS R 435 CG CD CE NZ REMARK 470 LYS R 439 CG CD CE NZ REMARK 470 GLU E 42 CG CD OE1 OE2 REMARK 470 LYS E 43 CG CD CE NZ REMARK 470 LYS E 76 CG CD CE NZ REMARK 470 GLU E 89 CG CD OE1 OE2 REMARK 470 GLU E 153 CG CD OE1 OE2 REMARK 470 ARG E 160 CG CD NE CZ NH1 NH2 REMARK 470 ARG E 218 CG CD NE CZ NH1 NH2 REMARK 470 GLU E 222 CG CD OE1 OE2 REMARK 470 GLU E 246 CG CD OE1 OE2 REMARK 470 GLU A 14 CG CD OE1 OE2 REMARK 470 GLU A 20 CG CD OE1 OE2 REMARK 470 ASP A 42 CG OD1 OD2 REMARK 470 ASN A 43 CG OD1 ND2 REMARK 470 THR A 48 OG1 CG2 REMARK 470 LYS A 51 CG CD CE NZ REMARK 470 MET A 53 CG SD CE REMARK 470 LYS A 54 CG CD CE NZ REMARK 470 ILE A 55 CG1 CG2 CD1 REMARK 470 GLU A 187 CG CD OE1 OE2 REMARK 470 ASN A 194 CG OD1 ND2 REMARK 470 ASP A 201 CG OD1 OD2 REMARK 470 ARG A 206 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 208 CG CD OE1 OE2 REMARK 470 LYS A 210 CG CD CE NZ REMARK 470 ASP A 218 CG OD1 OD2 REMARK 470 ASP A 227 CG OD1 OD2 REMARK 470 ASP A 230 CG OD1 OD2 REMARK 470 ASN A 242 CG OD1 ND2 REMARK 470 ARG A 243 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 246 CG CD OE1 OE2 REMARK 470 MET A 249 CG SD CE REMARK 470 ASP A 262 CG OD1 OD2 REMARK 470 ASP A 273 CG OD1 OD2 REMARK 470 LEU A 274 CG CD1 CD2 REMARK 470 GLU A 277 CG CD OE1 OE2 REMARK 470 LYS A 280 CG CD CE NZ REMARK 470 LYS A 281 CG CD CE NZ REMARK 470 THR A 285 OG1 CG2 REMARK 470 PHE A 288 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU A 290 CG CD OE1 OE2 REMARK 470 THR A 296 OG1 CG2 REMARK 470 TYR A 297 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU A 298 CG CD OE1 OE2 REMARK 470 ASP A 299 CG OD1 OD2 REMARK 470 SER A 314 OG REMARK 470 ASN A 316 CG OD1 ND2 REMARK 470 GLU A 318 CG CD OE1 OE2 REMARK 470 CYS A 325 SG REMARK 470 THR A 327 OG1 CG2 REMARK 470 ASP A 328 CG OD1 OD2 REMARK 470 ASP A 337 CG OD1 OD2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 CYS B 149 CA - CB - SG ANGL. DEV. = 8.1 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 TRP B 99 36.85 -97.95 REMARK 500 PHE B 292 10.57 81.19 REMARK 500 SER B 334 30.60 70.80 REMARK 500 THR R 427 -37.18 -131.16 REMARK 500 MET E 192 -12.34 75.46 REMARK 500 SER E 193 -22.60 -140.04 REMARK 500 ALA A 7 -8.92 75.68 REMARK 500 ILE A 286 -64.56 -122.92 REMARK 500 ASN A 295 30.02 -94.76 REMARK 500 ARG A 313 53.14 -94.48 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-44866 RELATED DB: EMDB REMARK 900 GLOBAL RECONSTRUCTION OF DRD2 BOUND TO LSD IN COMPLEX WITH A MINI- REMARK 900 GOA AND SCFV16 OBTAINED BY CRYO-ELECTRON MICROSCOPY (CRYOEM) DBREF 9BSB B 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 9BSB C 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 9BSB R -116 -12 UNP P0ABE7 C562_ECOLX 23 127 DBREF 9BSB R 1 443 UNP P14416 DRD2_HUMAN 1 443 DBREF 9BSB E 1 268 PDB 9BSB 9BSB 1 268 DBREF 9BSB A 1 354 UNP P09471 GNAO_HUMAN 1 354 SEQADV 9BSB MET B -4 UNP P62873 INITIATING METHIONINE SEQADV 9BSB GLY B -3 UNP P62873 EXPRESSION TAG SEQADV 9BSB SER B -2 UNP P62873 EXPRESSION TAG SEQADV 9BSB LEU B -1 UNP P62873 EXPRESSION TAG SEQADV 9BSB LEU B 0 UNP P62873 EXPRESSION TAG SEQADV 9BSB GLN B 1 UNP P62873 EXPRESSION TAG SEQADV 9BSB GLY B 341 UNP P62873 EXPRESSION TAG SEQADV 9BSB SER B 342 UNP P62873 EXPRESSION TAG SEQADV 9BSB SER B 343 UNP P62873 EXPRESSION TAG SEQADV 9BSB ASP R -144 UNP P0ABE7 EXPRESSION TAG SEQADV 9BSB TYR R -143 UNP P0ABE7 EXPRESSION TAG SEQADV 9BSB LYS R -142 UNP P0ABE7 EXPRESSION TAG SEQADV 9BSB ASP R -141 UNP P0ABE7 EXPRESSION TAG SEQADV 9BSB ASP R -140 UNP P0ABE7 EXPRESSION TAG SEQADV 9BSB ASP R -139 UNP P0ABE7 EXPRESSION TAG SEQADV 9BSB ASP R -138 UNP P0ABE7 EXPRESSION TAG SEQADV 9BSB ALA R -137 UNP P0ABE7 EXPRESSION TAG SEQADV 9BSB LYS R -136 UNP P0ABE7 EXPRESSION TAG SEQADV 9BSB LEU R -135 UNP P0ABE7 EXPRESSION TAG SEQADV 9BSB GLN R -134 UNP P0ABE7 EXPRESSION TAG SEQADV 9BSB THR R -133 UNP P0ABE7 EXPRESSION TAG SEQADV 9BSB MET R -132 UNP P0ABE7 EXPRESSION TAG SEQADV 9BSB HIS R -131 UNP P0ABE7 EXPRESSION TAG SEQADV 9BSB HIS R -130 UNP P0ABE7 EXPRESSION TAG SEQADV 9BSB HIS R -129 UNP P0ABE7 EXPRESSION TAG SEQADV 9BSB HIS R -128 UNP P0ABE7 EXPRESSION TAG SEQADV 9BSB HIS R -127 UNP P0ABE7 EXPRESSION TAG SEQADV 9BSB HIS R -126 UNP P0ABE7 EXPRESSION TAG SEQADV 9BSB HIS R -125 UNP P0ABE7 EXPRESSION TAG SEQADV 9BSB HIS R -124 UNP P0ABE7 EXPRESSION TAG SEQADV 9BSB HIS R -123 UNP P0ABE7 EXPRESSION TAG SEQADV 9BSB HIS R -122 UNP P0ABE7 EXPRESSION TAG SEQADV 9BSB HIS R -121 UNP P0ABE7 EXPRESSION TAG SEQADV 9BSB HIS R -120 UNP P0ABE7 EXPRESSION TAG SEQADV 9BSB HIS R -119 UNP P0ABE7 EXPRESSION TAG SEQADV 9BSB HIS R -118 UNP P0ABE7 EXPRESSION TAG SEQADV 9BSB HIS R -117 UNP P0ABE7 EXPRESSION TAG SEQADV 9BSB TRP R -110 UNP P0ABE7 MET 29 CONFLICT SEQADV 9BSB ILE R -15 UNP P0ABE7 HIS 124 CONFLICT SEQADV 9BSB LEU R -11 UNP P0ABE7 LINKER SEQADV 9BSB ALA R -10 UNP P0ABE7 LINKER SEQADV 9BSB SER R -9 UNP P0ABE7 LINKER SEQADV 9BSB GLU R -8 UNP P0ABE7 LINKER SEQADV 9BSB ASN R -7 UNP P0ABE7 LINKER SEQADV 9BSB LEU R -6 UNP P0ABE7 LINKER SEQADV 9BSB TYR R -5 UNP P0ABE7 LINKER SEQADV 9BSB PHE R -4 UNP P0ABE7 LINKER SEQADV 9BSB GLN R -3 UNP P0ABE7 LINKER SEQADV 9BSB GLY R -2 UNP P0ABE7 LINKER SEQADV 9BSB GLY R -1 UNP P0ABE7 LINKER SEQADV 9BSB THR R 0 UNP P0ABE7 LINKER SEQADV 9BSB ASP A 9 UNP P09471 GLU 9 CONFLICT SEQADV 9BSB LYS A 10 UNP P09471 ARG 10 CONFLICT SEQADV 9BSB VAL A 13 UNP P09471 LEU 13 CONFLICT SEQADV 9BSB MET A 18 UNP P09471 ALA 18 CONFLICT SEQADV 9BSB ASP A 42 UNP P09471 GLY 42 CONFLICT SEQADV 9BSB ASN A 43 UNP P09471 GLU 43 CONFLICT SEQADV 9BSB ASP A 227 UNP P09471 ALA 227 CONFLICT SEQADV 9BSB ASP A 230 UNP P09471 GLY 230 CONFLICT SEQADV 9BSB ALA A 332 UNP P09471 ILE 332 CONFLICT SEQADV 9BSB ILE A 335 UNP P09471 VAL 335 CONFLICT SEQRES 1 B 348 MET GLY SER LEU LEU GLN SER GLU LEU ASP GLN LEU ARG SEQRES 2 B 348 GLN GLU ALA GLU GLN LEU LYS ASN GLN ILE ARG ASP ALA SEQRES 3 B 348 ARG LYS ALA CYS ALA ASP ALA THR LEU SER GLN ILE THR SEQRES 4 B 348 ASN ASN ILE ASP PRO VAL GLY ARG ILE GLN MET ARG THR SEQRES 5 B 348 ARG ARG THR LEU ARG GLY HIS LEU ALA LYS ILE TYR ALA SEQRES 6 B 348 MET HIS TRP GLY THR ASP SER ARG LEU LEU VAL SER ALA SEQRES 7 B 348 SER GLN ASP GLY LYS LEU ILE ILE TRP ASP SER TYR THR SEQRES 8 B 348 THR ASN LYS VAL HIS ALA ILE PRO LEU ARG SER SER TRP SEQRES 9 B 348 VAL MET THR CYS ALA TYR ALA PRO SER GLY ASN TYR VAL SEQRES 10 B 348 ALA CYS GLY GLY LEU ASP ASN ILE CYS SER ILE TYR ASN SEQRES 11 B 348 LEU LYS THR ARG GLU GLY ASN VAL ARG VAL SER ARG GLU SEQRES 12 B 348 LEU ALA GLY HIS THR GLY TYR LEU SER CYS CYS ARG PHE SEQRES 13 B 348 LEU ASP ASP ASN GLN ILE VAL THR SER SER GLY ASP THR SEQRES 14 B 348 THR CYS ALA LEU TRP ASP ILE GLU THR GLY GLN GLN THR SEQRES 15 B 348 THR THR PHE THR GLY HIS THR GLY ASP VAL MET SER LEU SEQRES 16 B 348 SER LEU ALA PRO ASP THR ARG LEU PHE VAL SER GLY ALA SEQRES 17 B 348 CYS ASP ALA SER ALA LYS LEU TRP ASP VAL ARG GLU GLY SEQRES 18 B 348 MET CYS ARG GLN THR PHE THR GLY HIS GLU SER ASP ILE SEQRES 19 B 348 ASN ALA ILE CYS PHE PHE PRO ASN GLY ASN ALA PHE ALA SEQRES 20 B 348 THR GLY SER ASP ASP ALA THR CYS ARG LEU PHE ASP LEU SEQRES 21 B 348 ARG ALA ASP GLN GLU LEU MET THR TYR SER HIS ASP ASN SEQRES 22 B 348 ILE ILE CYS GLY ILE THR SER VAL SER PHE SER LYS SER SEQRES 23 B 348 GLY ARG LEU LEU LEU ALA GLY TYR ASP ASP PHE ASN CYS SEQRES 24 B 348 ASN VAL TRP ASP ALA LEU LYS ALA ASP ARG ALA GLY VAL SEQRES 25 B 348 LEU ALA GLY HIS ASP ASN ARG VAL SER CYS LEU GLY VAL SEQRES 26 B 348 THR ASP ASP GLY MET ALA VAL ALA THR GLY SER TRP ASP SEQRES 27 B 348 SER PHE LEU LYS ILE TRP ASN GLY SER SER SEQRES 1 C 71 MET ALA SER ASN ASN THR ALA SER ILE ALA GLN ALA ARG SEQRES 2 C 71 LYS LEU VAL GLU GLN LEU LYS MET GLU ALA ASN ILE ASP SEQRES 3 C 71 ARG ILE LYS VAL SER LYS ALA ALA ALA ASP LEU MET ALA SEQRES 4 C 71 TYR CYS GLU ALA HIS ALA LYS GLU ASP PRO LEU LEU THR SEQRES 5 C 71 PRO VAL PRO ALA SER GLU ASN PRO PHE ARG GLU LYS LYS SEQRES 6 C 71 PHE PHE CYS ALA ILE LEU SEQRES 1 R 588 ASP TYR LYS ASP ASP ASP ASP ALA LYS LEU GLN THR MET SEQRES 2 R 588 HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SEQRES 3 R 588 HIS HIS ALA ASP LEU GLU ASP ASN TRP GLU THR LEU ASN SEQRES 4 R 588 ASP ASN LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA SEQRES 5 R 588 GLN VAL LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA SEQRES 6 R 588 LEU ASP ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP SEQRES 7 R 588 LYS SER PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS SEQRES 8 R 588 GLY PHE ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU SEQRES 9 R 588 LYS LEU ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA SEQRES 10 R 588 ALA ALA GLU GLN LEU LYS THR THR ARG ASN ALA TYR ILE SEQRES 11 R 588 GLN LYS TYR LEU ALA SER GLU ASN LEU TYR PHE GLN GLY SEQRES 12 R 588 GLY THR MET ASP PRO LEU ASN LEU SER TRP TYR ASP ASP SEQRES 13 R 588 ASP LEU GLU ARG GLN ASN TRP SER ARG PRO PHE ASN GLY SEQRES 14 R 588 SER ASP GLY LYS ALA ASP ARG PRO HIS TYR ASN TYR TYR SEQRES 15 R 588 ALA THR LEU LEU THR LEU LEU ILE ALA VAL ILE VAL PHE SEQRES 16 R 588 GLY ASN VAL LEU VAL CYS MET ALA VAL SER ARG GLU LYS SEQRES 17 R 588 ALA LEU GLN THR THR THR ASN TYR LEU ILE VAL SER LEU SEQRES 18 R 588 ALA VAL ALA ASP LEU LEU VAL ALA THR LEU VAL MET PRO SEQRES 19 R 588 TRP VAL VAL TYR LEU GLU VAL VAL GLY GLU TRP LYS PHE SEQRES 20 R 588 SER ARG ILE HIS CYS ASP ILE PHE VAL THR LEU ASP VAL SEQRES 21 R 588 MET MET CYS THR ALA SER ILE LEU ASN LEU CYS ALA ILE SEQRES 22 R 588 SER ILE ASP ARG TYR THR ALA VAL ALA MET PRO MET LEU SEQRES 23 R 588 TYR ASN THR ARG TYR SER SER LYS ARG ARG VAL THR VAL SEQRES 24 R 588 MET ILE SER ILE VAL TRP VAL LEU SER PHE THR ILE SER SEQRES 25 R 588 CYS PRO LEU LEU PHE GLY LEU ASN ASN ALA ASP GLN ASN SEQRES 26 R 588 GLU CYS ILE ILE ALA ASN PRO ALA PHE VAL VAL TYR SER SEQRES 27 R 588 SER ILE VAL SER PHE TYR VAL PRO PHE ILE VAL THR LEU SEQRES 28 R 588 LEU VAL TYR ILE LYS ILE TYR ILE VAL LEU ARG ARG ARG SEQRES 29 R 588 ARG LYS ARG VAL ASN THR LYS ARG SER SER ARG ALA PHE SEQRES 30 R 588 ARG ALA HIS LEU ARG ALA PRO LEU LYS GLY ASN CYS THR SEQRES 31 R 588 HIS PRO GLU ASP MET LYS LEU CYS THR VAL ILE MET LYS SEQRES 32 R 588 SER ASN GLY SER PHE PRO VAL ASN ARG ARG ARG VAL GLU SEQRES 33 R 588 ALA ALA ARG ARG ALA GLN GLU LEU GLU MET GLU MET LEU SEQRES 34 R 588 SER SER THR SER PRO PRO GLU ARG THR ARG TYR SER PRO SEQRES 35 R 588 ILE PRO PRO SER HIS HIS GLN LEU THR LEU PRO ASP PRO SEQRES 36 R 588 SER HIS HIS GLY LEU HIS SER THR PRO ASP SER PRO ALA SEQRES 37 R 588 LYS PRO GLU LYS ASN GLY HIS ALA LYS ASP HIS PRO LYS SEQRES 38 R 588 ILE ALA LYS ILE PHE GLU ILE GLN THR MET PRO ASN GLY SEQRES 39 R 588 LYS THR ARG THR SER LEU LYS THR MET SER ARG ARG LYS SEQRES 40 R 588 LEU SER GLN GLN LYS GLU LYS LYS ALA THR GLN MET LEU SEQRES 41 R 588 ALA ILE VAL LEU GLY VAL PHE ILE ILE CYS TRP LEU PRO SEQRES 42 R 588 PHE PHE ILE THR HIS ILE LEU ASN ILE HIS CYS ASP CYS SEQRES 43 R 588 ASN ILE PRO PRO VAL LEU TYR SER ALA PHE THR TRP LEU SEQRES 44 R 588 GLY TYR VAL ASN SER ALA VAL ASN PRO ILE ILE TYR THR SEQRES 45 R 588 THR PHE ASN ILE GLU PHE ARG LYS ALA PHE LEU LYS ILE SEQRES 46 R 588 LEU HIS CYS SEQRES 1 E 268 ASP VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 E 268 PRO GLY GLY SER ARG LYS LEU SER CYS SER ALA SER GLY SEQRES 3 E 268 PHE ALA PHE SER SER PHE GLY MET HIS TRP VAL ARG GLN SEQRES 4 E 268 ALA PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SEQRES 5 E 268 SER GLY SER GLY THR ILE TYR TYR ALA ASP THR VAL LYS SEQRES 6 E 268 GLY ARG PHE THR ILE SER ARG ASP ASP PRO LYS ASN THR SEQRES 7 E 268 LEU PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR SEQRES 8 E 268 ALA MET TYR TYR CYS VAL ARG SER ILE TYR TYR TYR GLY SEQRES 9 E 268 SER SER PRO PHE ASP PHE TRP GLY GLN GLY THR THR LEU SEQRES 10 E 268 THR VAL SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SEQRES 11 E 268 SER GLY GLY GLY GLY SER ASP ILE VAL MET THR GLN ALA SEQRES 12 E 268 THR SER SER VAL PRO VAL THR PRO GLY GLU SER VAL SER SEQRES 13 E 268 ILE SER CYS ARG SER SER LYS SER LEU LEU HIS SER ASN SEQRES 14 E 268 GLY ASN THR TYR LEU TYR TRP PHE LEU GLN ARG PRO GLY SEQRES 15 E 268 GLN SER PRO GLN LEU LEU ILE TYR ARG MET SER ASN LEU SEQRES 16 E 268 ALA SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SER SEQRES 17 E 268 GLY THR ALA PHE THR LEU THR ILE SER ARG LEU GLU ALA SEQRES 18 E 268 GLU ASP VAL GLY VAL TYR TYR CYS MET GLN HIS LEU GLU SEQRES 19 E 268 TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU LEU SEQRES 20 E 268 LYS GLY SER LEU GLU VAL LEU PHE GLN GLY PRO ALA ALA SEQRES 21 E 268 ALA HIS HIS HIS HIS HIS HIS HIS 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 GLU LYS ASN LEU LYS GLU ASP SEQRES 3 A 354 GLY ILE SER ALA ALA LYS ASP VAL LYS LEU LEU LEU LEU SEQRES 4 A 354 GLY ALA ASP ASN SER GLY LYS SER THR ILE VAL LYS GLN SEQRES 5 A 354 MET LYS ILE ILE HIS GLU ASP GLY PHE SER GLY GLU ASP SEQRES 6 A 354 VAL LYS GLN TYR LYS PRO VAL VAL TYR SER ASN THR ILE SEQRES 7 A 354 GLN SER LEU ALA ALA ILE VAL ARG ALA MET ASP THR LEU SEQRES 8 A 354 GLY ILE GLU TYR GLY ASP LYS GLU ARG LYS ALA ASP ALA SEQRES 9 A 354 LYS MET VAL CYS ASP VAL VAL SER ARG MET GLU ASP THR SEQRES 10 A 354 GLU PRO PHE SER ALA GLU LEU LEU SER ALA MET MET ARG SEQRES 11 A 354 LEU TRP GLY ASP SER GLY ILE GLN GLU CYS PHE ASN ARG SEQRES 12 A 354 SER ARG GLU TYR GLN LEU ASN ASP SER ALA LYS TYR TYR SEQRES 13 A 354 LEU ASP SER LEU ASP ARG ILE GLY ALA ALA ASP TYR GLN SEQRES 14 A 354 PRO THR GLU GLN ASP ILE LEU ARG THR ARG VAL LYS THR SEQRES 15 A 354 THR GLY ILE VAL GLU THR HIS PHE THR PHE LYS ASN LEU SEQRES 16 A 354 HIS PHE ARG LEU PHE ASP VAL GLY GLY GLN ARG SER GLU SEQRES 17 A 354 ARG LYS LYS TRP ILE HIS CYS PHE GLU ASP VAL THR ALA SEQRES 18 A 354 ILE ILE PHE CYS VAL ASP LEU SER ASP TYR ASP GLN VAL SEQRES 19 A 354 LEU HIS GLU ASP GLU THR THR ASN ARG MET HIS GLU SER SEQRES 20 A 354 LEU MET LEU PHE ASP SER ILE CYS ASN ASN LYS PHE PHE SEQRES 21 A 354 ILE ASP THR SER ILE ILE LEU PHE LEU ASN LYS LYS ASP SEQRES 22 A 354 LEU PHE GLY GLU LYS ILE LYS LYS SER PRO LEU THR ILE SEQRES 23 A 354 CYS PHE PRO GLU TYR THR GLY PRO ASN THR TYR GLU ASP SEQRES 24 A 354 ALA ALA ALA TYR ILE GLN ALA GLN PHE GLU SER LYS ASN SEQRES 25 A 354 ARG SER PRO ASN LYS GLU ILE TYR CYS HIS MET THR CYS SEQRES 26 A 354 ALA THR ASP THR ASN ASN ALA GLN VAL ILE PHE ASP ALA SEQRES 27 A 354 VAL THR ASP ILE ILE ILE ALA ASN ASN LEU ARG GLY CYS SEQRES 28 A 354 GLY LEU TYR HET 7LD R 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 GLU B 10 CYS B 25 1 16 HELIX 2 AA2 THR B 29 THR B 34 1 6 HELIX 3 AA3 ARG C 13 ASN C 24 1 12 HELIX 4 AA4 LYS C 29 HIS C 44 1 16 HELIX 5 AA5 PRO C 55 ASN C 59 5 5 HELIX 6 AA6 ASN R 35 GLU R 62 1 28 HELIX 7 AA7 THR R 67 LEU R 86 1 20 HELIX 8 AA8 LEU R 86 GLY R 98 1 13 HELIX 9 AA9 SER R 103 MET R 138 1 36 HELIX 10 AB1 MET R 138 THR R 144 1 7 HELIX 11 AB2 THR R 144 CYS R 168 1 25 HELIX 12 AB3 PRO R 169 GLY R 173 5 5 HELIX 13 AB4 ASN R 186 PHE R 198 1 13 HELIX 14 AB5 PHE R 198 VAL R 223 1 26 HELIX 15 AB6 GLN R 365 HIS R 398 1 34 HELIX 16 AB7 PRO R 404 THR R 428 1 25 HELIX 17 AB8 ASN R 430 LYS R 439 1 10 HELIX 18 AB9 ALA E 28 PHE E 32 5 5 HELIX 19 AC1 ASP E 62 LYS E 65 5 4 HELIX 20 AC2 ARG E 87 THR E 91 5 5 HELIX 21 AC3 GLU E 220 VAL E 224 5 5 HELIX 22 AC4 GLU A 8 ALA A 31 1 24 HELIX 23 AC5 LYS A 46 VAL A 50 5 5 HELIX 24 AC6 GLU A 208 GLU A 217 5 10 HELIX 25 AC7 ARG A 243 ASN A 256 1 14 HELIX 26 AC8 LYS A 271 LYS A 280 1 10 HELIX 27 AC9 THR A 296 SER A 310 1 15 HELIX 28 AD1 ASN A 330 GLY A 352 1 23 SHEET 1 AA1 4 ARG B 46 LEU B 51 0 SHEET 2 AA1 4 LEU B 336 ASN B 340 -1 O LEU B 336 N LEU B 51 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 ILE B 58 TRP B 63 0 SHEET 2 AA2 4 LEU B 69 SER B 74 -1 O ALA B 73 N ALA B 60 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 ASN B 88 N ASP B 83 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 CYS B 121 ASN B 125 -1 O SER B 122 N CYS B 114 SHEET 4 AA3 4 ARG B 134 LEU B 139 -1 O ARG B 134 N ASN B 125 SHEET 1 AA4 4 LEU B 146 PHE B 151 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 PHE B 222 N ALA B 208 SHEET 1 AA6 4 ILE B 229 PHE B 234 0 SHEET 2 AA6 4 ALA B 240 SER B 245 -1 O ALA B 242 N CYS B 233 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 ASP B 303 LEU B 308 -1 O ASP B 303 N ASP B 298 SHEET 1 AA8 4 GLN E 3 SER E 7 0 SHEET 2 AA8 4 ARG E 18 SER E 25 -1 O SER E 23 N VAL E 5 SHEET 3 AA8 4 THR E 78 MET E 83 -1 O LEU E 81 N LEU E 20 SHEET 4 AA8 4 PHE E 68 ASP E 73 -1 N THR E 69 O GLN E 82 SHEET 1 AA9 5 ILE E 58 TYR E 60 0 SHEET 2 AA9 5 LEU E 45 ILE E 51 -1 N TYR E 50 O TYR E 59 SHEET 3 AA9 5 GLY E 33 GLN E 39 -1 N TRP E 36 O VAL E 48 SHEET 4 AA9 5 ALA E 92 SER E 99 -1 O SER E 99 N GLY E 33 SHEET 5 AA9 5 PHE E 110 TRP E 111 -1 O PHE E 110 N ARG E 98 SHEET 1 AB1 5 ILE E 58 TYR E 60 0 SHEET 2 AB1 5 LEU E 45 ILE E 51 -1 N TYR E 50 O TYR E 59 SHEET 3 AB1 5 GLY E 33 GLN E 39 -1 N TRP E 36 O VAL E 48 SHEET 4 AB1 5 ALA E 92 SER E 99 -1 O SER E 99 N GLY E 33 SHEET 5 AB1 5 THR E 115 LEU E 117 -1 O THR E 115 N TYR E 94 SHEET 1 AB2 4 MET E 140 THR E 141 0 SHEET 2 AB2 4 VAL E 155 SER E 161 -1 O ARG E 160 N THR E 141 SHEET 3 AB2 4 ALA E 211 ILE E 216 -1 O LEU E 214 N ILE E 157 SHEET 4 AB2 4 PHE E 203 SER E 208 -1 N SER E 206 O THR E 213 SHEET 1 AB3 6 SER E 146 PRO E 148 0 SHEET 2 AB3 6 THR E 243 GLU E 246 1 O LYS E 244 N VAL E 147 SHEET 3 AB3 6 VAL E 226 GLN E 231 -1 N TYR E 227 O THR E 243 SHEET 4 AB3 6 LEU E 174 GLN E 179 -1 N TYR E 175 O MET E 230 SHEET 5 AB3 6 GLN E 186 TYR E 190 -1 O LEU E 188 N TRP E 176 SHEET 6 AB3 6 ASN E 194 LEU E 195 -1 O ASN E 194 N TYR E 190 SHEET 1 AB4 6 VAL A 186 PHE A 192 0 SHEET 2 AB4 6 LEU A 195 ASP A 201 -1 O PHE A 197 N PHE A 190 SHEET 3 AB4 6 ASP A 33 GLY A 40 1 N VAL A 34 O HIS A 196 SHEET 4 AB4 6 ALA A 221 ASP A 227 1 O ILE A 223 N LEU A 37 SHEET 5 AB4 6 ILE A 265 ASN A 270 1 O ILE A 266 N ILE A 222 SHEET 6 AB4 6 ILE A 319 MET A 323 1 O HIS A 322 N LEU A 269 SSBOND 1 CYS B 121 CYS B 149 1555 1555 2.06 SSBOND 2 CYS R 107 CYS R 182 1555 1555 2.03 SSBOND 3 CYS E 22 CYS E 96 1555 1555 2.04 SSBOND 4 CYS E 159 CYS E 229 1555 1555 2.04 CISPEP 1 TYR E 235 PRO E 236 0 1.40 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