HEADER MEMBRANE PROTEIN 19-JUN-25 9VJF TITLE CRYO-EM STRUCTURE OF 5-HT1AR-GI3 IN COMPLEX WITH BUSPIRONE COMPND MOL_ID: 1; COMPND 2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I) SUBUNIT ALPHA-3; COMPND 3 CHAIN: B; COMPND 4 SYNONYM: G(I) ALPHA-3; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 8 BETA-1; COMPND 9 CHAIN: C; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 13 GAMMA-2; COMPND 14 CHAIN: D; COMPND 15 SYNONYM: G GAMMA-I; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 4; COMPND 18 MOLECULE: SCFV16; COMPND 19 CHAIN: E; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 5; COMPND 22 MOLECULE: SOLUBLE CYTOCHROME B562,5-HYDROXYTRYPTAMINE RECEPTOR 1A; COMPND 23 CHAIN: R; COMPND 24 SYNONYM: CYTOCHROME B-562,5-HT-1A,5-HT1A,G-21,SEROTONIN RECEPTOR 1A; 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: GNAI3; 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: GNB1; SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 GENE: GNG2; SOURCE 20 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 24 ORGANISM_TAXID: 10090; SOURCE 25 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 27 MOL_ID: 5; SOURCE 28 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 29 ORGANISM_COMMON: HUMAN; SOURCE 30 ORGANISM_TAXID: 9606; SOURCE 31 GENE: CYBC, HTR1A, ADRB2RL1, ADRBRL1; SOURCE 32 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 33 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS SIGNAL TRANSDUCTION, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR C.WANG,C.CAO REVDAT 1 12-NOV-25 9VJF 0 JRNL AUTH C.WANG,C.CAO JRNL TITL PATHWAY-SELECTIVE 5-HT1AR AGONIST AS A RAPID ANTIDEPRESSANT JRNL TITL 2 STRATEGY JRNL REF CELL 2025 REMARK 2 REMARK 2 RESOLUTION. 2.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, CRYOSPARC, CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : 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) : 2.700 REMARK 3 NUMBER OF PARTICLES : 120290 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 9VJF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 24-JUN-25. REMARK 100 THE DEPOSITION ID IS D_1300060665. 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 5-HT1AR REMARK 245 -GI3 IN COMPLEX WITH BUSPIRONE REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 1.50 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.50 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 600.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 18000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, D, E, R 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 1 REMARK 465 GLY B 2 REMARK 465 CYS B 3 REMARK 465 THR B 4 REMARK 465 ILE B 55 REMARK 465 ILE B 56 REMARK 465 HIS B 57 REMARK 465 GLU B 58 REMARK 465 ASP B 59 REMARK 465 GLY B 60 REMARK 465 TYR B 61 REMARK 465 SER B 62 REMARK 465 GLU B 63 REMARK 465 ASP B 64 REMARK 465 GLU B 65 REMARK 465 CYS B 66 REMARK 465 LYS B 67 REMARK 465 GLN B 68 REMARK 465 TYR B 69 REMARK 465 LYS B 70 REMARK 465 VAL B 71 REMARK 465 VAL B 72 REMARK 465 VAL B 73 REMARK 465 TYR B 74 REMARK 465 SER B 75 REMARK 465 ASN B 76 REMARK 465 THR B 77 REMARK 465 ILE B 78 REMARK 465 GLN B 79 REMARK 465 SER B 80 REMARK 465 ILE B 81 REMARK 465 ILE B 82 REMARK 465 ALA B 83 REMARK 465 ILE B 84 REMARK 465 ILE B 85 REMARK 465 ARG B 86 REMARK 465 ALA B 87 REMARK 465 MET B 88 REMARK 465 GLY B 89 REMARK 465 ARG B 90 REMARK 465 LEU B 91 REMARK 465 LYS B 92 REMARK 465 ILE B 93 REMARK 465 ASP B 94 REMARK 465 PHE B 95 REMARK 465 GLY B 96 REMARK 465 GLU B 97 REMARK 465 ALA B 98 REMARK 465 ALA B 99 REMARK 465 ARG B 100 REMARK 465 ALA B 101 REMARK 465 ASP B 102 REMARK 465 ASP B 103 REMARK 465 ALA B 104 REMARK 465 ARG B 105 REMARK 465 GLN B 106 REMARK 465 LEU B 107 REMARK 465 PHE B 108 REMARK 465 VAL B 109 REMARK 465 LEU B 110 REMARK 465 ALA B 111 REMARK 465 GLY B 112 REMARK 465 SER B 113 REMARK 465 ALA B 114 REMARK 465 GLU B 115 REMARK 465 GLU B 116 REMARK 465 GLY B 117 REMARK 465 VAL B 118 REMARK 465 MET B 119 REMARK 465 THR B 120 REMARK 465 PRO B 121 REMARK 465 GLU B 122 REMARK 465 LEU B 123 REMARK 465 ALA B 124 REMARK 465 GLY B 125 REMARK 465 VAL B 126 REMARK 465 ILE B 127 REMARK 465 LYS B 128 REMARK 465 ARG B 129 REMARK 465 LEU B 130 REMARK 465 TRP B 131 REMARK 465 ARG B 132 REMARK 465 ASP B 133 REMARK 465 GLY B 134 REMARK 465 GLY B 135 REMARK 465 VAL B 136 REMARK 465 GLN B 137 REMARK 465 ALA B 138 REMARK 465 CYS B 139 REMARK 465 PHE B 140 REMARK 465 SER B 141 REMARK 465 ARG B 142 REMARK 465 SER B 143 REMARK 465 ARG B 144 REMARK 465 GLU B 145 REMARK 465 TYR B 146 REMARK 465 GLN B 147 REMARK 465 LEU B 148 REMARK 465 ASN B 149 REMARK 465 ASP B 150 REMARK 465 SER B 151 REMARK 465 ALA B 152 REMARK 465 SER B 153 REMARK 465 TYR B 154 REMARK 465 TYR B 155 REMARK 465 LEU B 156 REMARK 465 ASN B 157 REMARK 465 ASP B 158 REMARK 465 LEU B 159 REMARK 465 ASP B 160 REMARK 465 ARG B 161 REMARK 465 ILE B 162 REMARK 465 SER B 163 REMARK 465 GLN B 164 REMARK 465 SER B 165 REMARK 465 ASN B 166 REMARK 465 TYR B 167 REMARK 465 ILE B 168 REMARK 465 PRO B 169 REMARK 465 THR B 170 REMARK 465 GLN B 171 REMARK 465 GLN B 172 REMARK 465 ASP B 173 REMARK 465 VAL B 174 REMARK 465 LEU B 175 REMARK 465 ARG B 176 REMARK 465 THR B 177 REMARK 465 ARG B 178 REMARK 465 VAL B 179 REMARK 465 LYS B 180 REMARK 465 THR B 181 REMARK 465 ALA B 235 REMARK 465 GLU B 236 REMARK 465 ASP B 237 REMARK 465 GLU B 238 REMARK 465 GLU B 239 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 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 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 GLY E 121A REMARK 465 GLY E 121B REMARK 465 GLY E 121C REMARK 465 GLY E 121D REMARK 465 SER E 121E REMARK 465 GLY E 121F REMARK 465 GLY E 121G REMARK 465 GLY E 121H REMARK 465 GLY E 121I REMARK 465 SER E 121J REMARK 465 GLY E 121K REMARK 465 GLY E 121L REMARK 465 GLY E 121M REMARK 465 GLY E 121N REMARK 465 LYS E 236 REMARK 465 ALA E 237 REMARK 465 ALA E 238 REMARK 465 ALA E 239 REMARK 465 ASP R -126 REMARK 465 TYR R -125 REMARK 465 LYS R -124 REMARK 465 ASP R -123 REMARK 465 ASP R -122 REMARK 465 ASP R -121 REMARK 465 ASP R -120 REMARK 465 ALA R -119 REMARK 465 LYS R -118 REMARK 465 LEU R -117 REMARK 465 GLN R -116 REMARK 465 THR R -115 REMARK 465 MET R -114 REMARK 465 HIS R -113 REMARK 465 HIS R -112 REMARK 465 HIS R -111 REMARK 465 HIS R -110 REMARK 465 HIS R -109 REMARK 465 HIS R -108 REMARK 465 HIS R -107 REMARK 465 HIS R -106 REMARK 465 HIS R -105 REMARK 465 HIS R -104 REMARK 465 GLU R -103 REMARK 465 ASN R -102 REMARK 465 LEU R -101 REMARK 465 TYR R -100 REMARK 465 PHE R -99 REMARK 465 GLN R -98 REMARK 465 GLY R -97 REMARK 465 GLY R -96 REMARK 465 THR R -95 REMARK 465 THR R -94 REMARK 465 MET R -93 REMARK 465 ALA R -92 REMARK 465 ASP R -91 REMARK 465 LEU R -90 REMARK 465 GLU R -89 REMARK 465 ASP R -88 REMARK 465 ASN R -87 REMARK 465 TRP R -86 REMARK 465 GLU R -85 REMARK 465 THR R -84 REMARK 465 LEU R -83 REMARK 465 ASN R -82 REMARK 465 ASP R -81 REMARK 465 ASN R -80 REMARK 465 LEU R -79 REMARK 465 LYS R -78 REMARK 465 VAL R -77 REMARK 465 ILE R -76 REMARK 465 GLU R -75 REMARK 465 LYS R -74 REMARK 465 ALA R -73 REMARK 465 ASP R -72 REMARK 465 ASN R -71 REMARK 465 ALA R -70 REMARK 465 ALA R -69 REMARK 465 GLN R -68 REMARK 465 VAL R -67 REMARK 465 LYS R -66 REMARK 465 ASP R -65 REMARK 465 ALA R -64 REMARK 465 LEU R -63 REMARK 465 THR R -62 REMARK 465 LYS R -61 REMARK 465 MET R -60 REMARK 465 ARG R -59 REMARK 465 ALA R -58 REMARK 465 ALA R -57 REMARK 465 ALA R -56 REMARK 465 LEU R -55 REMARK 465 ASP R -54 REMARK 465 ALA R -53 REMARK 465 GLN R -52 REMARK 465 LYS R -51 REMARK 465 ALA R -50 REMARK 465 THR R -49 REMARK 465 PRO R -48 REMARK 465 PRO R -47 REMARK 465 LYS R -46 REMARK 465 LEU R -45 REMARK 465 GLU R -44 REMARK 465 ASP R -43 REMARK 465 LYS R -42 REMARK 465 SER R -41 REMARK 465 PRO R -40 REMARK 465 ASP R -39 REMARK 465 SER R -38 REMARK 465 PRO R -37 REMARK 465 GLU R -36 REMARK 465 MET R -35 REMARK 465 LYS R -34 REMARK 465 ASP R -33 REMARK 465 PHE R -32 REMARK 465 ARG R -31 REMARK 465 HIS R -30 REMARK 465 GLY R -29 REMARK 465 PHE R -28 REMARK 465 ASP R -27 REMARK 465 ILE R -26 REMARK 465 LEU R -25 REMARK 465 VAL R -24 REMARK 465 GLY R -23 REMARK 465 GLN R -22 REMARK 465 ILE R -21 REMARK 465 ASP R -20 REMARK 465 ASP R -19 REMARK 465 ALA R -18 REMARK 465 LEU R -17 REMARK 465 LYS R -16 REMARK 465 LEU R -15 REMARK 465 ALA R -14 REMARK 465 ASN R -13 REMARK 465 GLU R -12 REMARK 465 GLY R -11 REMARK 465 LYS R -10 REMARK 465 VAL R -9 REMARK 465 LYS R -8 REMARK 465 GLU R -7 REMARK 465 ALA R -6 REMARK 465 GLN R -5 REMARK 465 ALA R -4 REMARK 465 ALA R -3 REMARK 465 ALA R -2 REMARK 465 GLU R -1 REMARK 465 GLN R 0 REMARK 465 LEU R 1 REMARK 465 LYS R 2 REMARK 465 THR R 3 REMARK 465 THR R 4 REMARK 465 ARG R 5 REMARK 465 ASN R 6 REMARK 465 ALA R 7 REMARK 465 TYR R 8 REMARK 465 ILE R 9 REMARK 465 GLN R 10 REMARK 465 LYS R 11 REMARK 465 TYR R 12 REMARK 465 LEU R 13 REMARK 465 GLY R 14 REMARK 465 SER R 15 REMARK 465 THR R 16 REMARK 465 LEU R 17 REMARK 465 GLU R 18 REMARK 465 VAL R 19 REMARK 465 LEU R 20 REMARK 465 PHE R 21 REMARK 465 GLN R 22 REMARK 465 GLY R 23 REMARK 465 PRO R 24 REMARK 465 THR R 25 REMARK 465 THR R 26 REMARK 465 GLY R 27 REMARK 465 ILE R 28 REMARK 465 SER R 29 REMARK 465 ASP R 30 REMARK 465 VAL R 31 REMARK 465 THR R 32 REMARK 465 VAL R 33 REMARK 465 THR R 177 REMARK 465 PRO R 178 REMARK 465 GLU R 179 REMARK 465 ASP R 180 REMARK 465 ARG R 181 REMARK 465 SER R 182 REMARK 465 ASP R 183 REMARK 465 THR R 229 REMARK 465 VAL R 230 REMARK 465 LYS R 231 REMARK 465 LYS R 232 REMARK 465 VAL R 233 REMARK 465 GLU R 234 REMARK 465 LYS R 235 REMARK 465 THR R 236 REMARK 465 GLY R 237 REMARK 465 ALA R 238 REMARK 465 ASP R 239 REMARK 465 THR R 240 REMARK 465 ARG R 241 REMARK 465 HIS R 242 REMARK 465 GLY R 243 REMARK 465 ALA R 244 REMARK 465 SER R 245 REMARK 465 PRO R 246 REMARK 465 ALA R 247 REMARK 465 PRO R 248 REMARK 465 GLN R 249 REMARK 465 PRO R 250 REMARK 465 LYS R 251 REMARK 465 LYS R 252 REMARK 465 SER R 253 REMARK 465 VAL R 254 REMARK 465 ASN R 255 REMARK 465 GLY R 256 REMARK 465 GLU R 257 REMARK 465 SER R 258 REMARK 465 GLY R 259 REMARK 465 SER R 260 REMARK 465 ARG R 261 REMARK 465 ASN R 262 REMARK 465 TRP R 263 REMARK 465 ARG R 264 REMARK 465 LEU R 265 REMARK 465 GLY R 266 REMARK 465 VAL R 267 REMARK 465 GLU R 268 REMARK 465 SER R 269 REMARK 465 LYS R 270 REMARK 465 ALA R 271 REMARK 465 GLY R 272 REMARK 465 GLY R 273 REMARK 465 ALA R 274 REMARK 465 LEU R 275 REMARK 465 CYS R 276 REMARK 465 ALA R 277 REMARK 465 ASN R 278 REMARK 465 GLY R 279 REMARK 465 ALA R 280 REMARK 465 VAL R 281 REMARK 465 ARG R 282 REMARK 465 GLN R 283 REMARK 465 GLY R 284 REMARK 465 ASP R 285 REMARK 465 ASP R 286 REMARK 465 GLY R 287 REMARK 465 ALA R 288 REMARK 465 ALA R 289 REMARK 465 LEU R 290 REMARK 465 GLU R 291 REMARK 465 VAL R 292 REMARK 465 ILE R 293 REMARK 465 GLU R 294 REMARK 465 VAL R 295 REMARK 465 HIS R 296 REMARK 465 ARG R 297 REMARK 465 VAL R 298 REMARK 465 GLY R 299 REMARK 465 ASN R 300 REMARK 465 SER R 301 REMARK 465 LYS R 302 REMARK 465 GLU R 303 REMARK 465 HIS R 304 REMARK 465 LEU R 305 REMARK 465 PRO R 306 REMARK 465 LEU R 307 REMARK 465 PRO R 308 REMARK 465 SER R 309 REMARK 465 GLU R 310 REMARK 465 ALA R 311 REMARK 465 GLY R 312 REMARK 465 PRO R 313 REMARK 465 THR R 314 REMARK 465 PRO R 315 REMARK 465 CYS R 316 REMARK 465 ALA R 317 REMARK 465 PRO R 318 REMARK 465 ALA R 319 REMARK 465 SER R 320 REMARK 465 PHE R 321 REMARK 465 GLU R 322 REMARK 465 ILE R 415 REMARK 465 LYS R 416 REMARK 465 CYS R 417 REMARK 465 LYS R 418 REMARK 465 PHE R 419 REMARK 465 CYS R 420 REMARK 465 ARG R 421 REMARK 465 GLN R 422 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 43 CG CD OE1 OE2 REMARK 470 LYS B 51 CG CD CE NZ REMARK 470 ARG B 205 CG CD NE CZ NH1 NH2 REMARK 470 MET B 240 CG SD CE REMARK 470 ARG B 280 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 298 CG CD OE1 OE2 REMARK 470 ASP C 5 CG OD1 OD2 REMARK 470 ARG C 8 CG CD NE CZ NH1 NH2 REMARK 470 LYS C 15 CG CD CE NZ REMARK 470 GLN D 11 CG CD OE1 NE2 REMARK 470 LYS D 14 CG CD CE NZ REMARK 470 LYS D 20 CG CD CE NZ REMARK 470 VAL D 54 CG1 CG2 REMARK 470 SER D 57 OG REMARK 470 GLU D 58 CG CD OE1 OE2 REMARK 470 ARG D 62 CG CD NE CZ NH1 NH2 REMARK 470 SER R 34 OG REMARK 470 TYR R 35 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG R 323 CG CD NE CZ NH1 NH2 REMARK 470 LYS R 324 CG CD CE NZ REMARK 470 GLU R 326 CG CD OE1 OE2 REMARK 470 ARG R 327 CG CD NE CZ NH1 NH2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OG1 THR C 274 O VAL C 315 2.03 REMARK 500 OG SER C 245 OD1 ASP C 247 2.09 REMARK 500 OG SER E 149 O LYS E 151 2.10 REMARK 500 O ILE C 58 OG SER C 316 2.10 REMARK 500 OE2 GLU C 215 NH1 ARG C 219 2.11 REMARK 500 OE2 GLU B 8 OH TYR E 163 2.12 REMARK 500 OG SER C 331 OD2 ASP C 333 2.13 REMARK 500 O ILE R 61 NE2 GLN R 68 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASP B 193 -2.70 72.00 REMARK 500 SER B 228 48.20 -83.37 REMARK 500 ARG B 280 -61.10 -95.42 REMARK 500 SER B 326 -1.93 -150.44 REMARK 500 THR B 329 9.72 59.57 REMARK 500 THR C 34 30.65 -97.95 REMARK 500 TRP C 99 58.34 -90.68 REMARK 500 THR C 196 14.20 57.77 REMARK 500 PHE C 292 -2.55 82.25 REMARK 500 LEU C 308 73.29 -101.24 REMARK 500 GLU E 42 17.92 -140.02 REMARK 500 VAL E 48 -60.28 -94.03 REMARK 500 MET E 180 127.26 -34.98 REMARK 500 ASP E 189 49.51 -80.46 REMARK 500 ASN R 100 10.07 59.14 REMARK 500 PHE R 204 -38.86 -130.74 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 TYR E 223 PRO E 224 125.26 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 T7M R 503 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-65111 RELATED DB: EMDB REMARK 900 STRUCTURE OF A GPCR-G PROTEIN COMPLEX WITH COMPOUND-2 DBREF 9VJF B 1 354 UNP P08754 GNAI3_HUMAN 1 354 DBREF 9VJF C 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 9VJF D 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 9VJF E 1 239 PDB 9VJF 9VJF 1 239 DBREF 9VJF R -85 12 UNP P0ABE7 C562_ECOLX 30 127 DBREF 9VJF R 25 422 UNP P08908 5HT1A_HUMAN 25 422 SEQADV 9VJF ASN B 47 UNP P08754 SER 47 VARIANT SEQADV 9VJF ALA B 203 UNP P08754 GLY 203 CONFLICT SEQADV 9VJF ALA B 245 UNP P08754 GLU 245 CONFLICT SEQADV 9VJF SER B 326 UNP P08754 ALA 326 CONFLICT SEQADV 9VJF MET C -17 UNP P62873 INITIATING METHIONINE SEQADV 9VJF HIS C -16 UNP P62873 EXPRESSION TAG SEQADV 9VJF HIS C -15 UNP P62873 EXPRESSION TAG SEQADV 9VJF HIS C -14 UNP P62873 EXPRESSION TAG SEQADV 9VJF HIS C -13 UNP P62873 EXPRESSION TAG SEQADV 9VJF HIS C -12 UNP P62873 EXPRESSION TAG SEQADV 9VJF HIS C -11 UNP P62873 EXPRESSION TAG SEQADV 9VJF LEU C -10 UNP P62873 EXPRESSION TAG SEQADV 9VJF GLU C -9 UNP P62873 EXPRESSION TAG SEQADV 9VJF VAL C -8 UNP P62873 EXPRESSION TAG SEQADV 9VJF LEU C -7 UNP P62873 EXPRESSION TAG SEQADV 9VJF PHE C -6 UNP P62873 EXPRESSION TAG SEQADV 9VJF GLN C -5 UNP P62873 EXPRESSION TAG SEQADV 9VJF GLY C -4 UNP P62873 EXPRESSION TAG SEQADV 9VJF PRO C -3 UNP P62873 EXPRESSION TAG SEQADV 9VJF GLY C -2 UNP P62873 EXPRESSION TAG SEQADV 9VJF SER C -1 UNP P62873 EXPRESSION TAG SEQADV 9VJF SER C 0 UNP P62873 EXPRESSION TAG SEQADV 9VJF GLY C 1 UNP P62873 EXPRESSION TAG SEQADV 9VJF ASP R -126 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF TYR R -125 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF LYS R -124 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF ASP R -123 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF ASP R -122 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF ASP R -121 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF ASP R -120 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF ALA R -119 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF LYS R -118 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF LEU R -117 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF GLN R -116 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF THR R -115 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF MET R -114 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF HIS R -113 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF HIS R -112 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF HIS R -111 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF HIS R -110 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF HIS R -109 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF HIS R -108 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF HIS R -107 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF HIS R -106 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF HIS R -105 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF HIS R -104 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF GLU R -103 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF ASN R -102 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF LEU R -101 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF TYR R -100 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF PHE R -99 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF GLN R -98 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF GLY R -97 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF GLY R -96 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF THR R -95 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF THR R -94 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF MET R -93 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF ALA R -92 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF ASP R -91 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF LEU R -90 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF GLU R -89 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF ASP R -88 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF ASN R -87 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF TRP R -86 UNP P0ABE7 EXPRESSION TAG SEQADV 9VJF ILE R 9 UNP P0ABE7 HIS 124 CONFLICT SEQADV 9VJF LEU R 13 UNP P0ABE7 LINKER SEQADV 9VJF GLY R 14 UNP P0ABE7 LINKER SEQADV 9VJF SER R 15 UNP P0ABE7 LINKER SEQADV 9VJF THR R 16 UNP P0ABE7 LINKER SEQADV 9VJF LEU R 17 UNP P0ABE7 LINKER SEQADV 9VJF GLU R 18 UNP P0ABE7 LINKER SEQADV 9VJF VAL R 19 UNP P0ABE7 LINKER SEQADV 9VJF LEU R 20 UNP P0ABE7 LINKER SEQADV 9VJF PHE R 21 UNP P0ABE7 LINKER SEQADV 9VJF GLN R 22 UNP P0ABE7 LINKER SEQADV 9VJF GLY R 23 UNP P0ABE7 LINKER SEQADV 9VJF PRO R 24 UNP P0ABE7 LINKER SEQADV 9VJF TRP R 125 UNP P08908 LEU 125 CONFLICT SEQRES 1 B 354 MET GLY CYS THR LEU SER ALA GLU ASP LYS ALA ALA VAL SEQRES 2 B 354 GLU ARG SER LYS MET ILE ASP ARG ASN LEU ARG GLU ASP SEQRES 3 B 354 GLY GLU LYS ALA ALA LYS GLU VAL LYS LEU LEU LEU LEU SEQRES 4 B 354 GLY ALA GLY GLU SER GLY LYS ASN THR ILE VAL LYS GLN SEQRES 5 B 354 MET LYS ILE ILE HIS GLU ASP GLY TYR SER GLU ASP GLU SEQRES 6 B 354 CYS LYS GLN TYR LYS VAL VAL VAL TYR SER ASN THR ILE SEQRES 7 B 354 GLN SER ILE ILE ALA ILE ILE ARG ALA MET GLY ARG LEU SEQRES 8 B 354 LYS ILE ASP PHE GLY GLU ALA ALA ARG ALA ASP ASP ALA SEQRES 9 B 354 ARG GLN LEU PHE VAL LEU ALA GLY SER ALA GLU GLU GLY SEQRES 10 B 354 VAL MET THR PRO GLU LEU ALA GLY VAL ILE LYS ARG LEU SEQRES 11 B 354 TRP ARG ASP GLY GLY VAL GLN ALA CYS PHE SER ARG SER SEQRES 12 B 354 ARG GLU TYR GLN LEU ASN ASP SER ALA SER TYR TYR LEU SEQRES 13 B 354 ASN ASP LEU ASP ARG ILE SER GLN SER ASN TYR ILE PRO SEQRES 14 B 354 THR GLN GLN ASP VAL LEU ARG THR ARG VAL LYS THR THR SEQRES 15 B 354 GLY ILE VAL GLU THR HIS PHE THR PHE LYS ASP LEU TYR SEQRES 16 B 354 PHE LYS MET PHE ASP VAL GLY ALA GLN ARG SER GLU ARG SEQRES 17 B 354 LYS LYS TRP ILE HIS CYS PHE GLU GLY VAL THR ALA ILE SEQRES 18 B 354 ILE PHE CYS VAL ALA LEU SER ASP TYR ASP LEU VAL LEU SEQRES 19 B 354 ALA GLU ASP GLU GLU MET ASN ARG MET HIS ALA SER MET SEQRES 20 B 354 LYS LEU PHE ASP SER ILE CYS ASN ASN LYS TRP PHE THR SEQRES 21 B 354 GLU THR SER ILE ILE LEU PHE LEU ASN LYS LYS ASP LEU SEQRES 22 B 354 PHE GLU GLU LYS ILE LYS ARG SER PRO LEU THR ILE CYS SEQRES 23 B 354 TYR PRO GLU TYR THR GLY SER ASN THR TYR GLU GLU ALA SEQRES 24 B 354 ALA ALA TYR ILE GLN CYS GLN PHE GLU ASP LEU ASN ARG SEQRES 25 B 354 ARG LYS ASP THR LYS GLU ILE TYR THR HIS PHE THR CYS SEQRES 26 B 354 SER THR ASP THR LYS ASN VAL GLN PHE VAL PHE ASP ALA SEQRES 27 B 354 VAL THR ASP VAL ILE ILE LYS ASN ASN LEU LYS GLU CYS SEQRES 28 B 354 GLY LEU TYR 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 251 ASP VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 E 251 PRO GLY GLY SER ARG LYS LEU SER CYS SER ALA SER GLY SEQRES 3 E 251 PHE ALA PHE SER SER PHE GLY MET HIS TRP VAL ARG GLN SEQRES 4 E 251 ALA PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SEQRES 5 E 251 SER GLY SER GLY THR ILE TYR TYR ALA ASP THR VAL LYS SEQRES 6 E 251 GLY ARG PHE THR ILE SER ARG ASP ASP PRO LYS ASN THR SEQRES 7 E 251 LEU PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR SEQRES 8 E 251 ALA MET TYR TYR CYS VAL ARG SER ILE TYR TYR TYR GLY SEQRES 9 E 251 SER SER PRO PHE ASP PHE TRP GLY GLN GLY THR THR LEU SEQRES 10 E 251 THR VAL SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SEQRES 11 E 251 SER GLY GLY GLY GLY SER ASP ILE VAL MET THR GLN ALA SEQRES 12 E 251 THR SER SER VAL PRO VAL THR PRO GLY GLU SER VAL SER SEQRES 13 E 251 ILE SER CYS ARG SER SER LYS SER LEU LEU HIS SER ASN SEQRES 14 E 251 GLY ASN THR TYR LEU TYR TRP PHE LEU GLN ARG PRO GLY SEQRES 15 E 251 GLN SER PRO GLN LEU LEU ILE TYR ARG MET SER ASN LEU SEQRES 16 E 251 ALA SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SER SEQRES 17 E 251 GLY THR ALA PHE THR LEU THR ILE SER ARG LEU GLU ALA SEQRES 18 E 251 GLU ASP VAL GLY VAL TYR TYR CYS MET GLN HIS LEU GLU SEQRES 19 E 251 TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU LEU SEQRES 20 E 251 LYS ALA ALA ALA SEQRES 1 R 549 ASP TYR LYS ASP ASP ASP ASP ALA LYS LEU GLN THR MET SEQRES 2 R 549 HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS GLU ASN LEU SEQRES 3 R 549 TYR PHE GLN GLY GLY THR THR MET ALA ASP LEU GLU ASP SEQRES 4 R 549 ASN TRP GLU THR LEU ASN ASP ASN LEU LYS VAL ILE GLU SEQRES 5 R 549 LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP ALA LEU THR SEQRES 6 R 549 LYS MET ARG ALA ALA ALA LEU ASP ALA GLN LYS ALA THR SEQRES 7 R 549 PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SER PRO GLU SEQRES 8 R 549 MET LYS ASP PHE ARG HIS GLY PHE ASP ILE LEU VAL GLY SEQRES 9 R 549 GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN GLU GLY LYS SEQRES 10 R 549 VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN LEU LYS THR SEQRES 11 R 549 THR ARG ASN ALA TYR ILE GLN LYS TYR LEU GLY SER THR SEQRES 12 R 549 LEU GLU VAL LEU PHE GLN GLY PRO THR THR GLY ILE SER SEQRES 13 R 549 ASP VAL THR VAL SER TYR GLN VAL ILE THR SER LEU LEU SEQRES 14 R 549 LEU GLY THR LEU ILE PHE CYS ALA VAL LEU GLY ASN ALA SEQRES 15 R 549 CYS VAL VAL ALA ALA ILE ALA LEU GLU ARG SER LEU GLN SEQRES 16 R 549 ASN VAL ALA ASN TYR LEU ILE GLY SER LEU ALA VAL THR SEQRES 17 R 549 ASP LEU MET VAL SER VAL LEU VAL LEU PRO MET ALA ALA SEQRES 18 R 549 LEU TYR GLN VAL LEU ASN LYS TRP THR LEU GLY GLN VAL SEQRES 19 R 549 THR CYS ASP LEU PHE ILE ALA LEU ASP VAL LEU CYS CYS SEQRES 20 R 549 THR SER SER ILE TRP HIS LEU CYS ALA ILE ALA LEU ASP SEQRES 21 R 549 ARG TYR TRP ALA ILE THR ASP PRO ILE ASP TYR VAL ASN SEQRES 22 R 549 LYS ARG THR PRO ARG ARG ALA ALA ALA LEU ILE SER LEU SEQRES 23 R 549 THR TRP LEU ILE GLY PHE LEU ILE SER ILE PRO PRO MET SEQRES 24 R 549 LEU GLY TRP ARG THR PRO GLU ASP ARG SER ASP PRO ASP SEQRES 25 R 549 ALA CYS THR ILE SER LYS ASP HIS GLY TYR THR ILE TYR SEQRES 26 R 549 SER THR PHE GLY ALA PHE TYR ILE PRO LEU LEU LEU MET SEQRES 27 R 549 LEU VAL LEU TYR GLY ARG ILE PHE ARG ALA ALA ARG PHE SEQRES 28 R 549 ARG ILE ARG LYS THR VAL LYS LYS VAL GLU LYS THR GLY SEQRES 29 R 549 ALA ASP THR ARG HIS GLY ALA SER PRO ALA PRO GLN PRO SEQRES 30 R 549 LYS LYS SER VAL ASN GLY GLU SER GLY SER ARG ASN TRP SEQRES 31 R 549 ARG LEU GLY VAL GLU SER LYS ALA GLY GLY ALA LEU CYS SEQRES 32 R 549 ALA ASN GLY ALA VAL ARG GLN GLY ASP ASP GLY ALA ALA SEQRES 33 R 549 LEU GLU VAL ILE GLU VAL HIS ARG VAL GLY ASN SER LYS SEQRES 34 R 549 GLU HIS LEU PRO LEU PRO SER GLU ALA GLY PRO THR PRO SEQRES 35 R 549 CYS ALA PRO ALA SER PHE GLU ARG LYS ASN GLU ARG ASN SEQRES 36 R 549 ALA GLU ALA LYS ARG LYS MET ALA LEU ALA ARG GLU ARG SEQRES 37 R 549 LYS THR VAL LYS THR LEU GLY ILE ILE MET GLY THR PHE SEQRES 38 R 549 ILE LEU CYS TRP LEU PRO PHE PHE ILE VAL ALA LEU VAL SEQRES 39 R 549 LEU PRO PHE CYS GLU SER SER CYS HIS MET PRO THR LEU SEQRES 40 R 549 LEU GLY ALA ILE ILE ASN TRP LEU GLY TYR SER ASN SER SEQRES 41 R 549 LEU LEU ASN PRO VAL ILE TYR ALA TYR PHE ASN LYS ASP SEQRES 42 R 549 PHE GLN ASN ALA PHE LYS LYS ILE ILE LYS CYS LYS PHE SEQRES 43 R 549 CYS ARG GLN HET CLR R 501 28 HET CLR R 502 28 HET T7M R 503 31 HET YLX R 504 28 HETNAM CLR CHOLESTEROL HETNAM T7M (2R)-1-(HEPTADECANOYLOXY)-3-{[(R)-HYDROXY{[(1R,2R,3R, HETNAM 2 T7M 4R,5S,6R)-2,3,5,6-TETRAHYDROXY-4-(PHOSPHONOOXY) HETNAM 3 T7M CYCLOHEXYL]OXY}PHOSPHORYL]OXY}PROPAN-2-YL (5Z,8Z,11Z, HETNAM 4 T7M 14Z)-ICOSA-5,8,11,14-TETRAENOATE HETNAM YLX BUSPIRONE HETSYN T7M PHOSPHATIDYLINOSITOL-4-PHOSPHATE HETSYN YLX BUSPIRONE FORMUL 6 CLR 2(C27 H46 O) FORMUL 8 T7M C46 H82 O16 P2 FORMUL 9 YLX C21 H31 N5 O2 HELIX 1 AA1 SER B 6 LYS B 32 1 27 HELIX 2 AA2 GLY B 45 LYS B 54 1 10 HELIX 3 AA3 GLU B 207 GLU B 216 5 10 HELIX 4 AA4 SER B 228 TYR B 230 5 3 HELIX 5 AA5 ASN B 241 ASN B 255 1 15 HELIX 6 AA6 LYS B 270 SER B 281 1 12 HELIX 7 AA7 PRO B 282 CYS B 286 5 5 HELIX 8 AA8 THR B 295 ASP B 309 1 15 HELIX 9 AA9 LYS B 330 GLY B 352 1 23 HELIX 10 AB1 GLU C 3 ALA C 26 1 24 HELIX 11 AB2 THR C 29 THR C 34 1 6 HELIX 12 AB3 ILE D 9 ASN D 24 1 16 HELIX 13 AB4 LYS D 29 HIS D 44 1 16 HELIX 14 AB5 ALA D 45 ASP D 48 5 4 HELIX 15 AB6 ALA E 28 PHE E 32 5 5 HELIX 16 AB7 SER E 53 GLY E 56 5 4 HELIX 17 AB8 ARG E 87 THR E 91 5 5 HELIX 18 AB9 TYR R 35 GLU R 64 1 30 HELIX 19 AC1 ARG R 65 GLN R 68 5 4 HELIX 20 AC2 ASN R 69 VAL R 89 1 21 HELIX 21 AC3 VAL R 89 LEU R 99 1 11 HELIX 22 AC4 GLN R 106 ASP R 140 1 35 HELIX 23 AC5 ASP R 140 LYS R 147 1 8 HELIX 24 AC6 THR R 149 ILE R 169 1 21 HELIX 25 AC7 ILE R 169 GLY R 174 1 6 HELIX 26 AC8 ASP R 192 GLY R 202 1 11 HELIX 27 AC9 PHE R 204 LYS R 228 1 25 HELIX 28 AD1 LYS R 324 LEU R 368 1 45 HELIX 29 AD2 PRO R 378 ALA R 401 1 24 HELIX 30 AD3 ASN R 404 ILE R 414 1 11 SHEET 1 AA1 6 VAL B 185 PHE B 191 0 SHEET 2 AA1 6 LEU B 194 ASP B 200 -1 O MET B 198 N THR B 187 SHEET 3 AA1 6 GLU B 33 LEU B 39 1 N LEU B 36 O LYS B 197 SHEET 4 AA1 6 ALA B 220 ALA B 226 1 O ILE B 222 N LEU B 39 SHEET 5 AA1 6 SER B 263 ASN B 269 1 O PHE B 267 N PHE B 223 SHEET 6 AA1 6 HIS B 322 PHE B 323 1 O HIS B 322 N LEU B 268 SHEET 1 AA2 4 ARG C 46 LEU C 51 0 SHEET 2 AA2 4 LEU C 336 ASN C 340 -1 O LEU C 336 N LEU C 51 SHEET 3 AA2 4 VAL C 327 GLY C 330 -1 N VAL C 327 O TRP C 339 SHEET 4 AA2 4 CYS C 317 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 LYS C 89 PRO C 94 -1 O ILE C 93 N LEU C 79 SHEET 1 AA4 4 VAL C 100 TYR C 105 0 SHEET 2 AA4 4 TYR C 111 GLY C 116 -1 O ALA C 113 N ALA C 104 SHEET 3 AA4 4 ILE C 120 ASN C 125 -1 O TYR C 124 N VAL C 112 SHEET 4 AA4 4 ARG C 134 ALA C 140 -1 O ARG C 137 N ILE C 123 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 ALA C 167 N THR C 159 SHEET 4 AA5 4 GLN C 175 PHE C 180 -1 O THR C 178 N LEU C 168 SHEET 1 AA6 4 VAL C 187 LEU C 192 0 SHEET 2 AA6 4 LEU C 198 ALA C 203 -1 O GLY C 202 N MET C 188 SHEET 3 AA6 4 ALA C 208 ASP C 212 -1 O TRP C 211 N PHE C 199 SHEET 4 AA6 4 CYS C 218 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 ALA C 242 N CYS C 233 SHEET 3 AA7 4 THR C 249 ASP C 254 -1 O PHE C 253 N PHE C 241 SHEET 4 AA7 4 GLN C 259 SER C 265 -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 LEU C 286 N SER C 277 SHEET 3 AA8 4 CYS C 294 ASP C 298 -1 O TRP C 297 N LEU C 285 SHEET 4 AA8 4 ARG C 304 LEU C 308 -1 O LEU C 308 N CYS C 294 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 MET E 83 N ARG E 18 SHEET 4 AA9 4 PHE E 68 ASP E 73 -1 N ASP E 73 O THR E 78 SHEET 1 AB1 6 GLY E 10 VAL E 12 0 SHEET 2 AB1 6 THR E 115 VAL E 119 1 O THR E 118 N VAL E 12 SHEET 3 AB1 6 ALA E 92 ARG E 98 -1 N TYR E 94 O THR E 115 SHEET 4 AB1 6 MET E 34 GLN E 39 -1 N GLN E 39 O MET E 93 SHEET 5 AB1 6 LEU E 45 ILE E 51 -1 O VAL E 48 N TRP E 36 SHEET 6 AB1 6 ILE E 58 TYR E 60 -1 O TYR E 59 N TYR E 50 SHEET 1 AB2 4 GLY E 10 VAL E 12 0 SHEET 2 AB2 4 THR E 115 VAL E 119 1 O THR E 118 N VAL E 12 SHEET 3 AB2 4 ALA E 92 ARG E 98 -1 N TYR E 94 O THR E 115 SHEET 4 AB2 4 PHE E 110 TRP E 111 -1 O PHE E 110 N ARG E 98 SHEET 1 AB3 4 MET E 128 THR E 129 0 SHEET 2 AB3 4 VAL E 143 SER E 149 -1 O ARG E 148 N THR E 129 SHEET 3 AB3 4 ALA E 199 ILE E 204 -1 O PHE E 200 N CYS E 147 SHEET 4 AB3 4 PHE E 191 SER E 196 -1 N SER E 194 O THR E 201 SHEET 1 AB4 5 VAL E 135 PRO E 136 0 SHEET 2 AB4 5 THR E 231 GLU E 234 1 O LYS E 232 N VAL E 135 SHEET 3 AB4 5 GLY E 213 TYR E 216 -1 N GLY E 213 O LEU E 233 SHEET 4 AB4 5 TRP E 164 GLN E 167 -1 N GLN E 167 O VAL E 214 SHEET 5 AB4 5 LEU E 175 ILE E 177 -1 O LEU E 176 N TRP E 164 SSBOND 1 CYS E 147 CYS E 217 1555 1555 2.03 SSBOND 2 CYS R 109 CYS R 187 1555 1555 2.03 SSBOND 3 CYS R 371 CYS R 375 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