HEADER MEMBRANE PROTEIN 03-SEP-24 9JEQ TITLE CRYO-EM STRUCTURE OF HISTAMINE-BOUND HISTAMINE RECEPTOR 3 H3R G TITLE 2 PROTEIN COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 3 BETA-1; COMPND 4 CHAIN: B; COMPND 5 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 9 GAMMA-2; COMPND 10 CHAIN: G; COMPND 11 SYNONYM: G GAMMA-I; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 3; COMPND 14 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I) SUBUNIT ALPHA-1; COMPND 15 CHAIN: A; COMPND 16 SYNONYM: ADENYLATE CYCLASE-INHIBITING G ALPHA PROTEIN; COMPND 17 ENGINEERED: YES; COMPND 18 MOL_ID: 4; COMPND 19 MOLECULE: HISTAMINE H3 RECEPTOR; COMPND 20 CHAIN: R; COMPND 21 SYNONYM: H3R,HH3R,G-PROTEIN COUPLED RECEPTOR 97; COMPND 22 ENGINEERED: YES; COMPND 23 MOL_ID: 5; COMPND 24 MOLECULE: SCFV16; COMPND 25 CHAIN: S; COMPND 26 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: TRICHOPLUSIA NI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 10 ORGANISM_COMMON: DOMESTIC CATTLE; SOURCE 11 ORGANISM_TAXID: 9913; SOURCE 12 GENE: GNG2; SOURCE 13 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 GENE: GNAI1; SOURCE 20 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 24 ORGANISM_COMMON: HUMAN; SOURCE 25 ORGANISM_TAXID: 9606; SOURCE 26 GENE: HRH3, GPCR97; SOURCE 27 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 29 MOL_ID: 5; SOURCE 30 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 31 ORGANISM_TAXID: 10090; SOURCE 32 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 33 EXPRESSION_SYSTEM_TAXID: 7111 KEYWDS COMPLEX, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR S.S.JIN,H.ZHANG,Y.JIANG REVDAT 1 24-SEP-25 9JEQ 0 JRNL AUTH S.S.JIN,H.ZHANG,J.H.YAN,C.R.WU,X.Q.CAI,K.WU,M.W.WANG,H.E.XU, JRNL AUTH 2 D.H.YANG,Y.JIANG JRNL TITL DECODING LIGAND RECOGNITION AND CONSTITUTIVE ACTIVATION OF JRNL TITL 2 HISTAMINE H3 AND H4 RECEPTORS. JRNL REF ACTA PHARMACOL.SIN. 2025 JRNL REFN ESSN 1745-7254 JRNL PMID 40877594 JRNL DOI 10.1038/S41401-025-01633-4 REMARK 2 REMARK 2 RESOLUTION. 3.05 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : 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) : 3.050 REMARK 3 NUMBER OF PARTICLES : 98993 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 9JEQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 06-SEP-24. REMARK 100 THE DEPOSITION ID IS D_1300051152. 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 HISTAMINE REMARK 245 -BOUND HISTAMINE RECEPTOR 3 H3R REMARK 245 G PROTEIN COMPLEX 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 : 7.20 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 TECNAI ARCTICA REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1800.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : DIFFRACTION REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5000.00 REMARK 245 ILLUMINATION MODE : SPOT SCAN REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 50 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G, A, R, S REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ILE A 55 REMARK 465 ILE A 56 REMARK 465 HIS A 57 REMARK 465 GLU A 58 REMARK 465 ALA A 59 REMARK 465 GLY A 60 REMARK 465 TYR A 61 REMARK 465 SER A 62 REMARK 465 GLU A 63 REMARK 465 GLU A 64 REMARK 465 GLU A 65 REMARK 465 CYS A 66 REMARK 465 LYS A 67 REMARK 465 GLN A 68 REMARK 465 TYR A 69 REMARK 465 LYS A 70 REMARK 465 ALA A 71 REMARK 465 VAL A 72 REMARK 465 VAL A 73 REMARK 465 TYR A 74 REMARK 465 SER A 75 REMARK 465 ASN A 76 REMARK 465 THR A 77 REMARK 465 ILE A 78 REMARK 465 GLN A 79 REMARK 465 SER A 80 REMARK 465 ILE A 81 REMARK 465 ILE A 82 REMARK 465 ALA A 83 REMARK 465 ILE A 84 REMARK 465 ILE A 85 REMARK 465 ARG A 86 REMARK 465 ALA A 87 REMARK 465 MET A 88 REMARK 465 GLY A 89 REMARK 465 ARG A 90 REMARK 465 LEU A 91 REMARK 465 LYS A 92 REMARK 465 ILE A 93 REMARK 465 ASP A 94 REMARK 465 PHE A 95 REMARK 465 GLY A 96 REMARK 465 ASP A 97 REMARK 465 SER A 98 REMARK 465 ALA A 99 REMARK 465 ARG A 100 REMARK 465 ALA A 101 REMARK 465 ASP A 102 REMARK 465 ASP A 103 REMARK 465 ALA A 104 REMARK 465 ARG A 105 REMARK 465 GLN A 106 REMARK 465 LEU A 107 REMARK 465 PHE A 108 REMARK 465 VAL A 109 REMARK 465 LEU A 110 REMARK 465 ALA A 111 REMARK 465 GLY A 112 REMARK 465 ALA A 113 REMARK 465 ALA A 114 REMARK 465 GLU A 115 REMARK 465 GLU A 116 REMARK 465 GLY A 117 REMARK 465 PHE A 118 REMARK 465 MET A 119 REMARK 465 THR A 120 REMARK 465 ALA A 121 REMARK 465 GLU A 122 REMARK 465 LEU A 123 REMARK 465 ALA A 124 REMARK 465 GLY A 125 REMARK 465 VAL A 126 REMARK 465 ILE A 127 REMARK 465 LYS A 128 REMARK 465 ARG A 129 REMARK 465 LEU A 130 REMARK 465 TRP A 131 REMARK 465 LYS A 132 REMARK 465 ASP A 133 REMARK 465 SER A 134 REMARK 465 GLY A 135 REMARK 465 VAL A 136 REMARK 465 GLN A 137 REMARK 465 ALA A 138 REMARK 465 CYS A 139 REMARK 465 PHE A 140 REMARK 465 ASN A 141 REMARK 465 ARG A 142 REMARK 465 SER A 143 REMARK 465 ARG A 144 REMARK 465 GLU A 145 REMARK 465 TYR A 146 REMARK 465 GLN A 147 REMARK 465 LEU A 148 REMARK 465 ASN A 149 REMARK 465 ASP A 150 REMARK 465 SER A 151 REMARK 465 ALA A 152 REMARK 465 ALA A 153 REMARK 465 TYR A 154 REMARK 465 TYR A 155 REMARK 465 LEU A 156 REMARK 465 ASN A 157 REMARK 465 ASP A 158 REMARK 465 LEU A 159 REMARK 465 ASP A 160 REMARK 465 ARG A 161 REMARK 465 ILE A 162 REMARK 465 ALA A 163 REMARK 465 GLN A 164 REMARK 465 PRO A 165 REMARK 465 ASN A 166 REMARK 465 TYR A 167 REMARK 465 ILE A 168 REMARK 465 PRO A 169 REMARK 465 THR A 170 REMARK 465 GLN A 171 REMARK 465 GLN A 172 REMARK 465 ASP A 173 REMARK 465 VAL A 174 REMARK 465 LEU A 175 REMARK 465 ARG A 176 REMARK 465 THR A 177 REMARK 465 ARG A 178 REMARK 465 VAL A 179 REMARK 465 LYS A 180 REMARK 465 THR A 181 REMARK 465 MET R 1 REMARK 465 GLU R 2 REMARK 465 ARG R 3 REMARK 465 ALA R 4 REMARK 465 PRO R 5 REMARK 465 PRO R 6 REMARK 465 ASP R 7 REMARK 465 GLY R 8 REMARK 465 PRO R 9 REMARK 465 LEU R 10 REMARK 465 ASN R 11 REMARK 465 ALA R 12 REMARK 465 SER R 13 REMARK 465 GLY R 14 REMARK 465 ALA R 15 REMARK 465 LEU R 16 REMARK 465 ALA R 17 REMARK 465 GLY R 18 REMARK 465 GLU R 19 REMARK 465 ALA R 20 REMARK 465 ALA R 21 REMARK 465 ALA R 22 REMARK 465 ALA R 23 REMARK 465 GLY R 24 REMARK 465 GLY R 25 REMARK 465 ALA R 26 REMARK 465 ARG R 27 REMARK 465 GLY R 28 REMARK 465 PHE R 29 REMARK 465 SER R 30 REMARK 465 ALA R 236 REMARK 465 ARG R 237 REMARK 465 GLU R 238 REMARK 465 ALA R 239 REMARK 465 ALA R 240 REMARK 465 GLY R 241 REMARK 465 PRO R 242 REMARK 465 GLU R 243 REMARK 465 PRO R 244 REMARK 465 PRO R 245 REMARK 465 PRO R 246 REMARK 465 GLU R 247 REMARK 465 ALA R 248 REMARK 465 GLN R 249 REMARK 465 PRO R 250 REMARK 465 SER R 251 REMARK 465 PRO R 252 REMARK 465 PRO R 253 REMARK 465 PRO R 254 REMARK 465 PRO R 255 REMARK 465 PRO R 256 REMARK 465 GLY R 257 REMARK 465 CYS R 258 REMARK 465 TRP R 259 REMARK 465 GLY R 260 REMARK 465 CYS R 261 REMARK 465 TRP R 262 REMARK 465 GLN R 263 REMARK 465 LYS R 264 REMARK 465 GLY R 265 REMARK 465 HIS R 266 REMARK 465 GLY R 267 REMARK 465 GLU R 268 REMARK 465 ALA R 269 REMARK 465 MET R 270 REMARK 465 PRO R 271 REMARK 465 LEU R 272 REMARK 465 HIS R 273 REMARK 465 ARG R 274 REMARK 465 TYR R 275 REMARK 465 GLY R 276 REMARK 465 VAL R 277 REMARK 465 GLY R 278 REMARK 465 GLU R 279 REMARK 465 ALA R 280 REMARK 465 ALA R 281 REMARK 465 VAL R 282 REMARK 465 GLY R 283 REMARK 465 ALA R 284 REMARK 465 GLU R 285 REMARK 465 ALA R 286 REMARK 465 GLY R 287 REMARK 465 GLU R 288 REMARK 465 ALA R 289 REMARK 465 THR R 290 REMARK 465 LEU R 291 REMARK 465 GLY R 292 REMARK 465 GLY R 293 REMARK 465 GLY R 294 REMARK 465 GLY R 295 REMARK 465 GLY R 296 REMARK 465 GLY R 297 REMARK 465 GLY R 298 REMARK 465 SER R 299 REMARK 465 VAL R 300 REMARK 465 ALA R 301 REMARK 465 SER R 302 REMARK 465 PRO R 303 REMARK 465 THR R 304 REMARK 465 SER R 305 REMARK 465 SER R 306 REMARK 465 SER R 307 REMARK 465 GLY R 308 REMARK 465 SER R 309 REMARK 465 SER R 310 REMARK 465 SER R 311 REMARK 465 ARG R 312 REMARK 465 GLY R 313 REMARK 465 THR R 314 REMARK 465 GLU R 315 REMARK 465 ARG R 316 REMARK 465 PRO R 317 REMARK 465 ARG R 318 REMARK 465 SER R 319 REMARK 465 LEU R 320 REMARK 465 LYS R 321 REMARK 465 ARG R 322 REMARK 465 GLY R 323 REMARK 465 SER R 324 REMARK 465 LYS R 325 REMARK 465 PRO R 326 REMARK 465 SER R 327 REMARK 465 ALA R 328 REMARK 465 SER R 329 REMARK 465 SER R 330 REMARK 465 ALA R 331 REMARK 465 SER R 332 REMARK 465 LEU R 333 REMARK 465 GLU R 334 REMARK 465 LYS R 335 REMARK 465 ARG R 336 REMARK 465 MET R 337 REMARK 465 LYS R 338 REMARK 465 MET R 339 REMARK 465 VAL R 340 REMARK 465 SER R 341 REMARK 465 GLN R 342 REMARK 465 SER R 343 REMARK 465 PHE R 344 REMARK 465 THR R 345 REMARK 465 GLN R 346 REMARK 465 LYS R 425 REMARK 465 LEU R 426 REMARK 465 LEU R 427 REMARK 465 CYS R 428 REMARK 465 PRO R 429 REMARK 465 GLN R 430 REMARK 465 LYS R 431 REMARK 465 LEU R 432 REMARK 465 LYS R 433 REMARK 465 ILE R 434 REMARK 465 GLN R 435 REMARK 465 PRO R 436 REMARK 465 HIS R 437 REMARK 465 SER R 438 REMARK 465 SER R 439 REMARK 465 LEU R 440 REMARK 465 GLU R 441 REMARK 465 HIS R 442 REMARK 465 CYS R 443 REMARK 465 TRP R 444 REMARK 465 LYS R 445 REMARK 465 ASP S 1 REMARK 465 SER S 121 REMARK 465 GLY S 122 REMARK 465 GLY S 123 REMARK 465 GLY S 124 REMARK 465 GLY S 125 REMARK 465 SER S 126 REMARK 465 GLY S 127 REMARK 465 GLY S 128 REMARK 465 GLY S 129 REMARK 465 GLY S 130 REMARK 465 SER S 131 REMARK 465 GLY S 132 REMARK 465 GLY S 133 REMARK 465 GLY S 134 REMARK 465 GLY S 135 REMARK 465 LYS S 248 REMARK 465 ALA S 249 REMARK 465 ALA S 250 REMARK 465 ALA S 251 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 B 46 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 197 CG CD NE CZ NH1 NH2 REMARK 470 ASP B 322 CG OD1 OD2 REMARK 470 GLU G 47 CG CD OE1 OE2 REMARK 470 GLU A 43 CG CD OE1 OE2 REMARK 470 LYS S 43 CG CD CE NZ REMARK 470 LYS S 65 CG CD CE NZ REMARK 470 ASP S 90 CG OD1 OD2 REMARK 470 THR S 91 OG1 CG2 REMARK 470 SER S 136 OG REMARK 470 ARG S 218 CG CD NE CZ NH1 NH2 REMARK 470 GLU S 220 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 THR B 34 30.51 -95.36 REMARK 500 ASP B 153 -164.36 -162.14 REMARK 500 SER G 57 -4.51 72.90 REMARK 500 ALA R 32 -66.41 -92.85 REMARK 500 VAL R 389 110.54 -27.13 REMARK 500 PRO R 413 46.63 -78.13 REMARK 500 MET S 192 -48.23 75.61 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-61421 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF HISTAMINE-BOUND HISTAMINE RECEPTOR 3 H3R G REMARK 900 PROTEIN COMPLEX DBREF 9JEQ B 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 9JEQ G 5 62 UNP P63212 GBG2_BOVIN 5 62 DBREF 9JEQ A 3 354 UNP P63096 GNAI1_HUMAN 3 354 DBREF 9JEQ R 1 445 UNP Q9Y5N1 HRH3_HUMAN 1 445 DBREF 9JEQ S 1 251 PDB 9JEQ 9JEQ 1 251 SEQADV 9JEQ ASN A 47 UNP P63096 SER 47 CONFLICT SEQADV 9JEQ ALA A 203 UNP P63096 GLY 203 CONFLICT SEQADV 9JEQ ALA A 245 UNP P63096 GLU 245 CONFLICT SEQADV 9JEQ SER A 326 UNP P63096 ALA 326 CONFLICT SEQADV 9JEQ ASN R 146 UNP Q9Y5N1 GLN 146 CONFLICT SEQRES 1 B 339 SER GLU LEU ASP GLN LEU ARG GLN GLU ALA GLU GLN LEU SEQRES 2 B 339 LYS ASN GLN ILE ARG ASP ALA ARG LYS ALA CYS ALA ASP SEQRES 3 B 339 ALA THR LEU SER GLN ILE THR ASN ASN ILE ASP PRO VAL SEQRES 4 B 339 GLY ARG ILE GLN MET ARG THR ARG ARG THR LEU ARG GLY SEQRES 5 B 339 HIS LEU ALA LYS ILE TYR ALA MET HIS TRP GLY THR ASP SEQRES 6 B 339 SER ARG LEU LEU VAL SER ALA SER GLN ASP GLY LYS LEU SEQRES 7 B 339 ILE ILE TRP ASP SER TYR THR THR ASN LYS VAL HIS ALA SEQRES 8 B 339 ILE PRO LEU ARG SER SER TRP VAL MET THR CYS ALA TYR SEQRES 9 B 339 ALA PRO SER GLY ASN TYR VAL ALA CYS GLY GLY LEU ASP SEQRES 10 B 339 ASN ILE CYS SER ILE TYR ASN LEU LYS THR ARG GLU GLY SEQRES 11 B 339 ASN VAL ARG VAL SER ARG GLU LEU ALA GLY HIS THR GLY SEQRES 12 B 339 TYR LEU SER CYS CYS ARG PHE LEU ASP ASP ASN GLN ILE SEQRES 13 B 339 VAL THR SER SER GLY ASP THR THR CYS ALA LEU TRP ASP SEQRES 14 B 339 ILE GLU THR GLY GLN GLN THR THR THR PHE THR GLY HIS SEQRES 15 B 339 THR GLY ASP VAL MET SER LEU SER LEU ALA PRO ASP THR SEQRES 16 B 339 ARG LEU PHE VAL SER GLY ALA CYS ASP ALA SER ALA LYS SEQRES 17 B 339 LEU TRP ASP VAL ARG GLU GLY MET CYS ARG GLN THR PHE SEQRES 18 B 339 THR GLY HIS GLU SER ASP ILE ASN ALA ILE CYS PHE PHE SEQRES 19 B 339 PRO ASN GLY ASN ALA PHE ALA THR GLY SER ASP ASP ALA SEQRES 20 B 339 THR CYS ARG LEU PHE ASP LEU ARG ALA ASP GLN GLU LEU SEQRES 21 B 339 MET THR TYR SER HIS ASP ASN ILE ILE CYS GLY ILE THR SEQRES 22 B 339 SER VAL SER PHE SER LYS SER GLY ARG LEU LEU LEU ALA SEQRES 23 B 339 GLY TYR ASP ASP PHE ASN CYS ASN VAL TRP ASP ALA LEU SEQRES 24 B 339 LYS ALA ASP ARG ALA GLY VAL LEU ALA GLY HIS ASP ASN SEQRES 25 B 339 ARG VAL SER CYS LEU GLY VAL THR ASP ASP GLY MET ALA SEQRES 26 B 339 VAL ALA THR GLY SER TRP ASP SER PHE LEU LYS ILE TRP SEQRES 27 B 339 ASN SEQRES 1 G 58 ASN THR ALA SER ILE ALA GLN ALA ARG LYS LEU VAL GLU SEQRES 2 G 58 GLN LEU LYS MET GLU ALA ASN ILE ASP ARG ILE LYS VAL SEQRES 3 G 58 SER LYS ALA ALA ALA ASP LEU MET ALA TYR CYS GLU ALA SEQRES 4 G 58 HIS ALA LYS GLU ASP PRO LEU LEU THR PRO VAL PRO ALA SEQRES 5 G 58 SER GLU ASN PRO PHE ARG SEQRES 1 A 352 CYS THR LEU SER ALA GLU ASP LYS ALA ALA VAL GLU ARG SEQRES 2 A 352 SER LYS MET ILE ASP ARG ASN LEU ARG GLU ASP GLY GLU SEQRES 3 A 352 LYS ALA ALA ARG GLU VAL LYS LEU LEU LEU LEU GLY ALA SEQRES 4 A 352 GLY GLU SER GLY LYS ASN THR ILE VAL LYS GLN MET LYS SEQRES 5 A 352 ILE ILE HIS GLU ALA GLY TYR SER GLU GLU GLU CYS LYS SEQRES 6 A 352 GLN TYR LYS ALA VAL VAL TYR SER ASN THR ILE GLN SER SEQRES 7 A 352 ILE ILE ALA ILE ILE ARG ALA MET GLY ARG LEU LYS ILE SEQRES 8 A 352 ASP PHE GLY ASP SER ALA ARG ALA ASP ASP ALA ARG GLN SEQRES 9 A 352 LEU PHE VAL LEU ALA GLY ALA ALA GLU GLU GLY PHE MET SEQRES 10 A 352 THR ALA GLU LEU ALA GLY VAL ILE LYS ARG LEU TRP LYS SEQRES 11 A 352 ASP SER GLY VAL GLN ALA CYS PHE ASN ARG SER ARG GLU SEQRES 12 A 352 TYR GLN LEU ASN ASP SER ALA ALA TYR TYR LEU ASN ASP SEQRES 13 A 352 LEU ASP ARG ILE ALA GLN PRO ASN TYR ILE PRO THR GLN SEQRES 14 A 352 GLN ASP VAL LEU ARG THR ARG VAL LYS THR THR GLY ILE SEQRES 15 A 352 VAL GLU THR HIS PHE THR PHE LYS ASP LEU HIS PHE LYS SEQRES 16 A 352 MET PHE ASP VAL GLY ALA GLN ARG SER GLU ARG LYS LYS SEQRES 17 A 352 TRP ILE HIS CYS PHE GLU GLY VAL THR ALA ILE ILE PHE SEQRES 18 A 352 CYS VAL ALA LEU SER ASP TYR ASP LEU VAL LEU ALA GLU SEQRES 19 A 352 ASP GLU GLU MET ASN ARG MET HIS ALA SER MET LYS LEU SEQRES 20 A 352 PHE ASP SER ILE CYS ASN ASN LYS TRP PHE THR ASP THR SEQRES 21 A 352 SER ILE ILE LEU PHE LEU ASN LYS LYS ASP LEU PHE GLU SEQRES 22 A 352 GLU LYS ILE LYS LYS SER PRO LEU THR ILE CYS TYR PRO SEQRES 23 A 352 GLU TYR ALA GLY SER ASN THR TYR GLU GLU ALA ALA ALA SEQRES 24 A 352 TYR ILE GLN CYS GLN PHE GLU ASP LEU ASN LYS ARG LYS SEQRES 25 A 352 ASP THR LYS GLU ILE TYR THR HIS PHE THR CYS SER THR SEQRES 26 A 352 ASP THR LYS ASN VAL GLN PHE VAL PHE ASP ALA VAL THR SEQRES 27 A 352 ASP VAL ILE ILE LYS ASN ASN LEU LYS ASP CYS GLY LEU SEQRES 28 A 352 PHE SEQRES 1 R 445 MET GLU ARG ALA PRO PRO ASP GLY PRO LEU ASN ALA SER SEQRES 2 R 445 GLY ALA LEU ALA GLY GLU ALA ALA ALA ALA GLY GLY ALA SEQRES 3 R 445 ARG GLY PHE SER ALA ALA TRP THR ALA VAL LEU ALA ALA SEQRES 4 R 445 LEU MET ALA LEU LEU ILE VAL ALA THR VAL LEU GLY ASN SEQRES 5 R 445 ALA LEU VAL MET LEU ALA PHE VAL ALA ASP SER SER LEU SEQRES 6 R 445 ARG THR GLN ASN ASN PHE PHE LEU LEU ASN LEU ALA ILE SEQRES 7 R 445 SER ASP PHE LEU VAL GLY ALA PHE CYS ILE PRO LEU TYR SEQRES 8 R 445 VAL PRO TYR VAL LEU THR GLY ARG TRP THR PHE GLY ARG SEQRES 9 R 445 GLY LEU CYS LYS LEU TRP LEU VAL VAL ASP TYR LEU LEU SEQRES 10 R 445 CYS THR SER SER ALA PHE ASN ILE VAL LEU ILE SER TYR SEQRES 11 R 445 ASP ARG PHE LEU SER VAL THR ARG ALA VAL SER TYR ARG SEQRES 12 R 445 ALA GLN ASN GLY ASP THR ARG ARG ALA VAL ARG LYS MET SEQRES 13 R 445 LEU LEU VAL TRP VAL LEU ALA PHE LEU LEU TYR GLY PRO SEQRES 14 R 445 ALA ILE LEU SER TRP GLU TYR LEU SER GLY GLY SER SER SEQRES 15 R 445 ILE PRO GLU GLY HIS CYS TYR ALA GLU PHE PHE TYR ASN SEQRES 16 R 445 TRP TYR PHE LEU ILE THR ALA SER THR LEU GLU PHE PHE SEQRES 17 R 445 THR PRO PHE LEU SER VAL THR PHE PHE ASN LEU SER ILE SEQRES 18 R 445 TYR LEU ASN ILE GLN ARG ARG THR ARG LEU ARG LEU ASP SEQRES 19 R 445 GLY ALA ARG GLU ALA ALA GLY PRO GLU PRO PRO PRO GLU SEQRES 20 R 445 ALA GLN PRO SER PRO PRO PRO PRO PRO GLY CYS TRP GLY SEQRES 21 R 445 CYS TRP GLN LYS GLY HIS GLY GLU ALA MET PRO LEU HIS SEQRES 22 R 445 ARG TYR GLY VAL GLY GLU ALA ALA VAL GLY ALA GLU ALA SEQRES 23 R 445 GLY GLU ALA THR LEU GLY GLY GLY GLY GLY GLY GLY SER SEQRES 24 R 445 VAL ALA SER PRO THR SER SER SER GLY SER SER SER ARG SEQRES 25 R 445 GLY THR GLU ARG PRO ARG SER LEU LYS ARG GLY SER LYS SEQRES 26 R 445 PRO SER ALA SER SER ALA SER LEU GLU LYS ARG MET LYS SEQRES 27 R 445 MET VAL SER GLN SER PHE THR GLN ARG PHE ARG LEU SER SEQRES 28 R 445 ARG ASP ARG LYS VAL ALA LYS SER LEU ALA VAL ILE VAL SEQRES 29 R 445 SER ILE PHE GLY LEU CYS TRP ALA PRO TYR THR LEU LEU SEQRES 30 R 445 MET ILE ILE ARG ALA ALA CYS HIS GLY HIS CYS VAL PRO SEQRES 31 R 445 ASP TYR TRP TYR GLU THR SER PHE TRP LEU LEU TRP ALA SEQRES 32 R 445 ASN SER ALA VAL ASN PRO VAL LEU TYR PRO LEU CYS HIS SEQRES 33 R 445 HIS SER PHE ARG ARG ALA PHE THR LYS LEU LEU CYS PRO SEQRES 34 R 445 GLN LYS LEU LYS ILE GLN PRO HIS SER SER LEU GLU HIS SEQRES 35 R 445 CYS TRP LYS SEQRES 1 S 251 ASP VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 S 251 PRO GLY GLY SER ARG LYS LEU SER CYS SER ALA SER GLY SEQRES 3 S 251 PHE ALA PHE SER SER PHE GLY MET HIS TRP VAL ARG GLN SEQRES 4 S 251 ALA PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SEQRES 5 S 251 SER GLY SER GLY THR ILE TYR TYR ALA ASP THR VAL LYS SEQRES 6 S 251 GLY ARG PHE THR ILE SER ARG ASP ASP PRO LYS ASN THR SEQRES 7 S 251 LEU PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR SEQRES 8 S 251 ALA MET TYR TYR CYS VAL ARG SER ILE TYR TYR TYR GLY SEQRES 9 S 251 SER SER PRO PHE ASP PHE TRP GLY GLN GLY THR THR LEU SEQRES 10 S 251 THR VAL SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SEQRES 11 S 251 SER GLY GLY GLY GLY SER ASP ILE VAL MET THR GLN ALA SEQRES 12 S 251 THR SER SER VAL PRO VAL THR PRO GLY GLU SER VAL SER SEQRES 13 S 251 ILE SER CYS ARG SER SER LYS SER LEU LEU HIS SER ASN SEQRES 14 S 251 GLY ASN THR TYR LEU TYR TRP PHE LEU GLN ARG PRO GLY SEQRES 15 S 251 GLN SER PRO GLN LEU LEU ILE TYR ARG MET SER ASN LEU SEQRES 16 S 251 ALA SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SER SEQRES 17 S 251 GLY THR ALA PHE THR LEU THR ILE SER ARG LEU GLU ALA SEQRES 18 S 251 GLU ASP VAL GLY VAL TYR TYR CYS MET GLN HIS LEU GLU SEQRES 19 S 251 TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU LEU SEQRES 20 S 251 LYS ALA ALA ALA HET HSM R 501 8 HETNAM HSM HISTAMINE FORMUL 6 HSM C5 H9 N3 HELIX 1 AA1 SER B 2 CYS B 25 1 24 HELIX 2 AA2 THR B 29 THR B 34 1 6 HELIX 3 AA3 THR G 6 ASN G 24 1 19 HELIX 4 AA4 LYS G 29 HIS G 44 1 16 HELIX 5 AA5 SER A 6 ALA A 31 1 26 HELIX 6 AA6 LYS A 46 LYS A 54 1 9 HELIX 7 AA7 GLU A 207 ILE A 212 1 6 HELIX 8 AA8 HIS A 213 GLU A 216 5 4 HELIX 9 AA9 SER A 228 TYR A 230 5 3 HELIX 10 AB1 ASN A 241 ASN A 256 1 16 HELIX 11 AB2 LYS A 270 SER A 281 1 12 HELIX 12 AB3 PRO A 282 CYS A 286 5 5 HELIX 13 AB4 THR A 295 ASP A 309 1 15 HELIX 14 AB5 THR A 329 LEU A 348 1 20 HELIX 15 AB6 LYS A 349 CYS A 351 5 3 HELIX 16 AB7 TRP R 33 ASP R 62 1 30 HELIX 17 AB8 THR R 67 THR R 97 1 31 HELIX 18 AB9 GLY R 105 ARG R 138 1 34 HELIX 19 AC1 ARG R 138 ASN R 146 1 9 HELIX 20 AC2 ASP R 148 GLY R 179 1 32 HELIX 21 AC3 TRP R 196 PHE R 207 1 12 HELIX 22 AC4 PHE R 207 GLY R 235 1 29 HELIX 23 AC5 PHE R 348 CYS R 384 1 37 HELIX 24 AC6 TYR R 392 TYR R 412 1 21 HELIX 25 AC7 HIS R 417 THR R 424 1 8 SHEET 1 AA1 4 THR B 47 LEU B 51 0 SHEET 2 AA1 4 LEU B 336 TRP B 339 -1 O LEU B 336 N LEU B 51 SHEET 3 AA1 4 VAL B 327 GLY B 330 -1 N VAL B 327 O TRP B 339 SHEET 4 AA1 4 CYS B 317 VAL B 320 -1 N CYS B 317 O GLY B 330 SHEET 1 AA2 4 ILE B 58 TRP B 63 0 SHEET 2 AA2 4 LEU B 69 SER B 74 -1 O VAL B 71 N HIS B 62 SHEET 3 AA2 4 LYS B 78 ASP B 83 -1 O TRP B 82 N LEU B 70 SHEET 4 AA2 4 ASN B 88 PRO B 94 -1 O ILE B 93 N LEU B 79 SHEET 1 AA3 4 CYS B 103 TYR B 105 0 SHEET 2 AA3 4 TYR B 111 CYS B 114 -1 O ALA B 113 N ALA B 104 SHEET 3 AA3 4 CYS B 121 ASN B 125 -1 O TYR B 124 N VAL B 112 SHEET 4 AA3 4 ARG B 134 LEU B 139 -1 O SER B 136 N ILE B 123 SHEET 1 AA4 4 LEU B 146 PHE B 151 0 SHEET 2 AA4 4 GLN B 156 SER B 161 -1 O VAL B 158 N ARG B 150 SHEET 3 AA4 4 CYS B 166 ASP B 170 -1 O TRP B 169 N ILE B 157 SHEET 4 AA4 4 GLN B 175 PHE B 180 -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 SER B 189 SHEET 3 AA5 4 ALA B 208 ASP B 212 -1 O LYS B 209 N SER B 201 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 THR B 249 ASP B 254 -1 O PHE B 253 N PHE B 241 SHEET 4 AA6 4 GLU B 260 SER B 265 -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 GLY B 288 N SER B 275 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 LEU B 308 N CYS B 294 SHEET 1 AA8 6 VAL A 185 THR A 190 0 SHEET 2 AA8 6 HIS A 195 ASP A 200 -1 O MET A 198 N THR A 187 SHEET 3 AA8 6 GLU A 33 GLY A 40 1 N LEU A 36 O LYS A 197 SHEET 4 AA8 6 ALA A 220 ALA A 226 1 O ILE A 222 N LEU A 37 SHEET 5 AA8 6 SER A 263 ASN A 269 1 O ILE A 265 N ILE A 221 SHEET 6 AA8 6 ILE A 319 PHE A 323 1 O TYR A 320 N ILE A 264 SHEET 1 AA9 4 GLN S 3 SER S 7 0 SHEET 2 AA9 4 SER S 17 SER S 25 -1 O SER S 23 N VAL S 5 SHEET 3 AA9 4 THR S 78 THR S 84 -1 O LEU S 81 N LEU S 20 SHEET 4 AA9 4 PHE S 68 ASP S 73 -1 N SER S 71 O PHE S 80 SHEET 1 AB1 2 LEU S 11 VAL S 12 0 SHEET 2 AB1 2 THR S 118 VAL S 119 1 O THR S 118 N VAL S 12 SHEET 1 AB2 5 GLY S 56 TYR S 60 0 SHEET 2 AB2 5 LEU S 45 SER S 52 -1 N TYR S 50 O TYR S 59 SHEET 3 AB2 5 GLY S 33 GLN S 39 -1 N TRP S 36 O VAL S 48 SHEET 4 AB2 5 MET S 93 SER S 99 -1 O TYR S 95 N VAL S 37 SHEET 5 AB2 5 PHE S 110 TRP S 111 -1 O PHE S 110 N ARG S 98 SHEET 1 AB3 6 SER S 146 VAL S 147 0 SHEET 2 AB3 6 THR S 243 LEU S 245 1 O LYS S 244 N VAL S 147 SHEET 3 AB3 6 GLY S 225 GLN S 231 -1 N TYR S 227 O THR S 243 SHEET 4 AB3 6 LEU S 174 GLN S 179 -1 N PHE S 177 O TYR S 228 SHEET 5 AB3 6 PRO S 185 TYR S 190 -1 O GLN S 186 N LEU S 178 SHEET 6 AB3 6 ASN S 194 LEU S 195 -1 O ASN S 194 N TYR S 190 SHEET 1 AB4 4 SER S 146 VAL S 147 0 SHEET 2 AB4 4 THR S 243 LEU S 245 1 O LYS S 244 N VAL S 147 SHEET 3 AB4 4 GLY S 225 GLN S 231 -1 N TYR S 227 O THR S 243 SHEET 4 AB4 4 THR S 238 PHE S 239 -1 O THR S 238 N GLN S 231 SHEET 1 AB5 2 VAL S 155 ARG S 160 0 SHEET 2 AB5 2 ALA S 211 ILE S 216 -1 O ILE S 216 N VAL S 155 SSBOND 1 CYS R 107 CYS R 188 1555 1555 2.02 SSBOND 2 CYS R 384 CYS R 388 1555 1555 2.03 CISPEP 1 TYR S 235 PRO S 236 0 28.47 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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