HEADER MEMBRANE PROTEIN 24-OCT-23 8WW2 TITLE GPR3/GS COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(S) SUBUNIT ALPHA COMPND 3 ISOFORMS SHORT; COMPND 4 CHAIN: A; 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: B; 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: G; COMPND 15 SYNONYM: G GAMMA-I; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 4; COMPND 18 MOLECULE: NB35; COMPND 19 CHAIN: N; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 5; COMPND 22 MOLECULE: G-PROTEIN COUPLED RECEPTOR 3; COMPND 23 CHAIN: R; COMPND 24 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_COMMON: HUMAN; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 GENE: GNB1; SOURCE 11 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_COMMON: HUMAN; SOURCE 16 ORGANISM_TAXID: 9606; SOURCE 17 GENE: GNG2; SOURCE 18 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 20 MOL_ID: 4; SOURCE 21 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 22 ORGANISM_TAXID: 9844; SOURCE 23 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 25 MOL_ID: 5; SOURCE 26 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 27 ORGANISM_COMMON: HUMAN; SOURCE 28 ORGANISM_TAXID: 9606; SOURCE 29 GENE: GPR3; SOURCE 30 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 31 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS GPCR-G-PROTEIN COMPLEX, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR Y.HE,Y.XIONG REVDAT 1 14-FEB-24 8WW2 0 JRNL AUTH Y.XIONG,Z.XU,X.LI,Y.WANG,J.ZHAO,N.WANG,Y.DUAN,R.XIA,Z.HAN, JRNL AUTH 2 Y.QIAN,J.LIANG,A.ZHANG,C.GUO,A.INOUE,Y.XIA,Z.CHEN,Y.HE JRNL TITL IDENTIFICATION OF OLEIC ACID AS AN ENDOGENOUS LIGAND OF JRNL TITL 2 GPR3. JRNL REF CELL RES. 2024 JRNL REFN ISSN 1001-0602 JRNL PMID 38287117 JRNL DOI 10.1038/S41422-024-00932-5 REMARK 2 REMARK 2 RESOLUTION. 2.79 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 2.790 REMARK 3 NUMBER OF PARTICLES : 288793 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 8WW2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-OCT-23. REMARK 100 THE DEPOSITION ID IS D_1300042126. 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 : GPCR/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 : 7.50 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 : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2200.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 6000.00 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, G, N, 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 A 8 REMARK 465 GLY A 9 REMARK 465 CYS A 10 REMARK 465 THR A 11 REMARK 465 LEU A 12 REMARK 465 ILE A 62 REMARK 465 LEU A 63 REMARK 465 HIS A 64 REMARK 465 VAL A 65 REMARK 465 ASN A 66 REMARK 465 GLY A 67 REMARK 465 PHE A 68 REMARK 465 ASN A 69 REMARK 465 GLY A 70 REMARK 465 GLU A 71 REMARK 465 GLY A 72 REMARK 465 GLY A 73 REMARK 465 GLU A 74 REMARK 465 GLU A 75 REMARK 465 ASP A 76 REMARK 465 PRO A 77 REMARK 465 GLN A 78 REMARK 465 ALA A 79 REMARK 465 ALA A 80 REMARK 465 ARG A 81 REMARK 465 SER A 82 REMARK 465 ASN A 83 REMARK 465 SER A 84 REMARK 465 ASP A 85 REMARK 465 GLY A 86 REMARK 465 GLU A 87 REMARK 465 LYS A 88 REMARK 465 ALA A 89 REMARK 465 THR A 90 REMARK 465 LYS A 91 REMARK 465 VAL A 92 REMARK 465 GLN A 93 REMARK 465 ASP A 94 REMARK 465 ILE A 95 REMARK 465 LYS A 96 REMARK 465 ASN A 97 REMARK 465 ASN A 98 REMARK 465 LEU A 99 REMARK 465 LYS A 100 REMARK 465 GLU A 101 REMARK 465 ALA A 102 REMARK 465 ILE A 103 REMARK 465 GLU A 104 REMARK 465 THR A 105 REMARK 465 ILE A 106 REMARK 465 VAL A 107 REMARK 465 ALA A 108 REMARK 465 ALA A 109 REMARK 465 MET A 110 REMARK 465 SER A 111 REMARK 465 ASN A 112 REMARK 465 LEU A 113 REMARK 465 VAL A 114 REMARK 465 PRO A 115 REMARK 465 PRO A 116 REMARK 465 VAL A 117 REMARK 465 GLU A 118 REMARK 465 LEU A 119 REMARK 465 ALA A 120 REMARK 465 ASN A 121 REMARK 465 PRO A 122 REMARK 465 GLU A 123 REMARK 465 ASN A 124 REMARK 465 GLN A 125 REMARK 465 PHE A 126 REMARK 465 ARG A 127 REMARK 465 VAL A 128 REMARK 465 ASP A 129 REMARK 465 TYR A 130 REMARK 465 ILE A 131 REMARK 465 LEU A 132 REMARK 465 SER A 133 REMARK 465 VAL A 134 REMARK 465 MET A 135 REMARK 465 ASN A 136 REMARK 465 VAL A 137 REMARK 465 PRO A 138 REMARK 465 ASP A 139 REMARK 465 PHE A 140 REMARK 465 ASP A 141 REMARK 465 PHE A 142 REMARK 465 PRO A 143 REMARK 465 PRO A 144 REMARK 465 GLU A 145 REMARK 465 PHE A 146 REMARK 465 TYR A 147 REMARK 465 GLU A 148 REMARK 465 HIS A 149 REMARK 465 ALA A 150 REMARK 465 LYS A 151 REMARK 465 ALA A 152 REMARK 465 LEU A 153 REMARK 465 TRP A 154 REMARK 465 GLU A 155 REMARK 465 ASP A 156 REMARK 465 GLU A 157 REMARK 465 GLY A 158 REMARK 465 VAL A 159 REMARK 465 ARG A 160 REMARK 465 ALA A 161 REMARK 465 CYS A 162 REMARK 465 TYR A 163 REMARK 465 GLU A 164 REMARK 465 ARG A 165 REMARK 465 SER A 166 REMARK 465 ASN A 167 REMARK 465 GLU A 168 REMARK 465 TYR A 169 REMARK 465 GLN A 170 REMARK 465 LEU A 171 REMARK 465 ILE A 172 REMARK 465 ASP A 173 REMARK 465 CYS A 174 REMARK 465 ALA A 175 REMARK 465 GLN A 176 REMARK 465 TYR A 177 REMARK 465 PHE A 178 REMARK 465 LEU A 179 REMARK 465 ASP A 180 REMARK 465 LYS A 181 REMARK 465 ILE A 182 REMARK 465 ASP A 183 REMARK 465 VAL A 184 REMARK 465 ILE A 185 REMARK 465 LYS A 186 REMARK 465 GLN A 187 REMARK 465 ASP A 188 REMARK 465 ASP A 189 REMARK 465 TYR A 190 REMARK 465 VAL A 191 REMARK 465 PRO A 192 REMARK 465 SER A 193 REMARK 465 ASP A 194 REMARK 465 GLN A 195 REMARK 465 ASP A 196 REMARK 465 LEU A 197 REMARK 465 LEU A 198 REMARK 465 ARG A 199 REMARK 465 CYS A 200 REMARK 465 ARG A 201 REMARK 465 VAL A 202 REMARK 465 LEU A 203 REMARK 465 SER A 252 REMARK 465 TYR A 253 REMARK 465 ASN A 254 REMARK 465 MET A 255 REMARK 465 VAL A 256 REMARK 465 ILE A 257 REMARK 465 ARG A 258 REMARK 465 GLU A 259 REMARK 465 ASP A 260 REMARK 465 ASN A 261 REMARK 465 GLN A 262 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 MET G 1 REMARK 465 ALA G 2 REMARK 465 SER G 3 REMARK 465 ASN G 4 REMARK 465 ASN G 5 REMARK 465 THR G 6 REMARK 465 ALA G 7 REMARK 465 GLU G 63 REMARK 465 LYS G 64 REMARK 465 LYS G 65 REMARK 465 PHE G 66 REMARK 465 PHE G 67 REMARK 465 CYS G 68 REMARK 465 ALA G 69 REMARK 465 ILE G 70 REMARK 465 LEU G 71 REMARK 465 HIS N 129 REMARK 465 HIS N 130 REMARK 465 HIS N 131 REMARK 465 HIS N 132 REMARK 465 HIS N 133 REMARK 465 HIS N 134 REMARK 465 GLU N 135 REMARK 465 PRO N 136 REMARK 465 GLU N 137 REMARK 465 ALA N 138 REMARK 465 MET R 1 REMARK 465 MET R 2 REMARK 465 TRP R 3 REMARK 465 GLY R 4 REMARK 465 ALA R 5 REMARK 465 GLY R 6 REMARK 465 SER R 7 REMARK 465 PRO R 8 REMARK 465 LEU R 9 REMARK 465 ALA R 10 REMARK 465 TRP R 11 REMARK 465 LEU R 12 REMARK 465 SER R 13 REMARK 465 ALA R 14 REMARK 465 GLY R 15 REMARK 465 SER R 16 REMARK 465 GLY R 17 REMARK 465 ASN R 18 REMARK 465 VAL R 19 REMARK 465 ASN R 20 REMARK 465 VAL R 21 REMARK 465 SER R 22 REMARK 465 SER R 23 REMARK 465 VAL R 24 REMARK 465 GLY R 25 REMARK 465 PRO R 26 REMARK 465 ALA R 27 REMARK 465 GLU R 28 REMARK 465 GLY R 29 REMARK 465 PRO R 30 REMARK 465 THR R 31 REMARK 465 GLY R 32 REMARK 465 PRO R 33 REMARK 465 ALA R 34 REMARK 465 ALA R 35 REMARK 465 PRO R 36 REMARK 465 LEU R 233 REMARK 465 LEU R 234 REMARK 465 PRO R 235 REMARK 465 ALA R 236 REMARK 465 SER R 237 REMARK 465 HIS R 238 REMARK 465 TYR R 239 REMARK 465 VAL R 240 REMARK 465 ALA R 241 REMARK 465 CYS R 314 REMARK 465 CYS R 315 REMARK 465 SER R 316 REMARK 465 SER R 317 REMARK 465 SER R 318 REMARK 465 LYS R 319 REMARK 465 ILE R 320 REMARK 465 PRO R 321 REMARK 465 PHE R 322 REMARK 465 ARG R 323 REMARK 465 SER R 324 REMARK 465 ARG R 325 REMARK 465 SER R 326 REMARK 465 PRO R 327 REMARK 465 SER R 328 REMARK 465 ASP R 329 REMARK 465 VAL R 330 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 LYS A 17 CG CD CE NZ REMARK 470 LYS A 24 CG CD CE NZ REMARK 470 ARG A 31 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 50 CG CD OE1 OE2 REMARK 470 LYS A 58 CG CD CE NZ REMARK 470 GLN A 59 CG CD OE1 NE2 REMARK 470 ARG A 61 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 265 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 299 CG CD OE1 OE2 REMARK 470 LYS A 300 CG CD CE NZ REMARK 470 LYS A 305 CG CD CE NZ REMARK 470 LYS A 307 CG CD CE NZ REMARK 470 GLU A 309 CG CD OE1 OE2 REMARK 470 GLU A 327 CG CD OE1 OE2 REMARK 470 SER A 352 OG REMARK 470 ASP A 354 CG OD1 OD2 REMARK 470 ASP B 5 CG OD1 OD2 REMARK 470 ARG B 8 CG CD NE CZ NH1 NH2 REMARK 470 GLN B 9 CG CD OE1 NE2 REMARK 470 LYS B 23 CG CD CE NZ REMARK 470 ARG B 42 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 46 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 127 CG CD CE NZ REMARK 470 THR B 128 OG1 CG2 REMARK 470 ARG B 129 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 130 CG CD OE1 OE2 REMARK 470 LYS G 14 CG CD CE NZ REMARK 470 GLU G 42 CG CD OE1 OE2 REMARK 470 LYS G 46 CG CD CE NZ REMARK 470 ARG G 62 CG CD NE CZ NH1 NH2 REMARK 470 ARG N 105 CG CD NE CZ NH1 NH2 REMARK 470 THR N 113 OG1 CG2 REMARK 470 LYS R 41 CG CD CE NZ REMARK 470 CYS R 56 SG REMARK 470 GLU R 107 CG CD OE1 OE2 REMARK 470 TRP R 175 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP R 175 CZ3 CH2 REMARK 470 LEU R 178 CG CD1 CD2 REMARK 470 LEU R 181 CG CD1 CD2 REMARK 470 THR R 182 OG1 CG2 REMARK 470 HIS R 232 CG ND1 CD2 CE1 NE2 REMARK 470 ARG R 243 CG CD NE CZ NH1 NH2 REMARK 470 ASP R 271 CG OD1 OD2 REMARK 470 LYS R 306 CG CD CE NZ REMARK 470 TRP R 309 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP R 309 CZ3 CH2 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 O LEU R 95 CD1 LEU R 112 1.81 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 LYS A 17 6.26 59.20 REMARK 500 PHE B 292 8.90 81.25 REMARK 500 ASP N 109 43.24 -141.89 REMARK 500 TRP R 175 16.15 -140.40 REMARK 500 CYS R 177 -168.25 -126.17 REMARK 500 PRO R 189 46.57 -88.12 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-37881 RELATED DB: EMDB REMARK 900 GPR3/GS COMPLEX DBREF 8WW2 A 8 394 PDB 8WW2 8WW2 8 394 DBREF 8WW2 B 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 8WW2 G 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 8WW2 N 1 138 PDB 8WW2 8WW2 1 138 DBREF 8WW2 R 1 330 UNP P46089 GPR3_HUMAN 1 330 SEQADV 8WW2 MET B -4 UNP P62873 INITIATING METHIONINE SEQADV 8WW2 GLY B -3 UNP P62873 EXPRESSION TAG SEQADV 8WW2 SER B -2 UNP P62873 EXPRESSION TAG SEQADV 8WW2 LEU B -1 UNP P62873 EXPRESSION TAG SEQADV 8WW2 LEU B 0 UNP P62873 EXPRESSION TAG SEQADV 8WW2 GLN B 1 UNP P62873 EXPRESSION TAG SEQADV 8WW2 GLY B 341 UNP P62873 EXPRESSION TAG SEQADV 8WW2 SER B 342 UNP P62873 EXPRESSION TAG SEQRES 1 A 387 MET GLY CYS THR LEU SER ALA GLU ASP LYS ALA ALA VAL SEQRES 2 A 387 GLU ARG SER LYS MET ILE ASP ARG ASN LEU ARG GLU ASP SEQRES 3 A 387 GLY GLU LYS ALA ALA ALA THR HIS ARG LEU LEU LEU LEU SEQRES 4 A 387 GLY ALA GLY GLU SER GLY LYS SER THR ILE VAL LYS GLN SEQRES 5 A 387 MET ARG ILE LEU HIS VAL ASN GLY PHE ASN GLY GLU GLY SEQRES 6 A 387 GLY GLU GLU ASP PRO GLN ALA ALA ARG SER ASN SER ASP SEQRES 7 A 387 GLY GLU LYS ALA THR LYS VAL GLN ASP ILE LYS ASN ASN SEQRES 8 A 387 LEU LYS GLU ALA ILE GLU THR ILE VAL ALA ALA MET SER SEQRES 9 A 387 ASN LEU VAL PRO PRO VAL GLU LEU ALA ASN PRO GLU ASN SEQRES 10 A 387 GLN PHE ARG VAL ASP TYR ILE LEU SER VAL MET ASN VAL SEQRES 11 A 387 PRO ASP PHE ASP PHE PRO PRO GLU PHE TYR GLU HIS ALA SEQRES 12 A 387 LYS ALA LEU TRP GLU ASP GLU GLY VAL ARG ALA CYS TYR SEQRES 13 A 387 GLU ARG SER ASN GLU TYR GLN LEU ILE ASP CYS ALA GLN SEQRES 14 A 387 TYR PHE LEU ASP LYS ILE ASP VAL ILE LYS GLN ASP ASP SEQRES 15 A 387 TYR VAL PRO SER ASP GLN ASP LEU LEU ARG CYS ARG VAL SEQRES 16 A 387 LEU THR SER GLY ILE PHE GLU THR LYS PHE GLN VAL ASP SEQRES 17 A 387 LYS VAL ASN PHE HIS MET PHE ASP VAL GLY ALA GLN ARG SEQRES 18 A 387 ASP GLU ARG ARG LYS TRP ILE GLN CYS PHE ASN ASP VAL SEQRES 19 A 387 THR ALA ILE ILE PHE VAL VAL ALA SER SER SER TYR ASN SEQRES 20 A 387 MET VAL ILE ARG GLU ASP ASN GLN THR ASN ARG LEU GLN SEQRES 21 A 387 GLU ALA LEU ASN LEU PHE LYS SER ILE TRP ASN ASN ARG SEQRES 22 A 387 TRP LEU ARG THR ILE SER VAL ILE LEU PHE LEU ASN LYS SEQRES 23 A 387 GLN ASP LEU LEU ALA GLU LYS VAL LEU ALA GLY LYS SER SEQRES 24 A 387 LYS ILE GLU ASP TYR PHE PRO GLU PHE ALA ARG TYR THR SEQRES 25 A 387 THR PRO GLU ASP ALA THR PRO GLU PRO GLY GLU ASP PRO SEQRES 26 A 387 ARG VAL THR ARG ALA LYS TYR PHE ILE ARG ASP GLU PHE SEQRES 27 A 387 LEU ARG ILE SER THR ALA SER GLY ASP GLY ARG HIS TYR SEQRES 28 A 387 CYS TYR PRO HIS PHE THR CYS SER VAL ASP THR GLU ASN SEQRES 29 A 387 ILE ARG ARG VAL PHE ASN ASP CYS ARG ASP ILE ILE GLN SEQRES 30 A 387 ARG MET HIS LEU ARG GLN TYR GLU LEU LEU SEQRES 1 B 347 MET GLY SER LEU LEU GLN SER GLU LEU ASP GLN LEU ARG SEQRES 2 B 347 GLN GLU ALA GLU GLN LEU LYS ASN GLN ILE ARG ASP ALA SEQRES 3 B 347 ARG LYS ALA CYS ALA ASP ALA THR LEU SER GLN ILE THR SEQRES 4 B 347 ASN ASN ILE ASP PRO VAL GLY ARG ILE GLN MET ARG THR SEQRES 5 B 347 ARG ARG THR LEU ARG GLY HIS LEU ALA LYS ILE TYR ALA SEQRES 6 B 347 MET HIS TRP GLY THR ASP SER ARG LEU LEU VAL SER ALA SEQRES 7 B 347 SER GLN ASP GLY LYS LEU ILE ILE TRP ASP SER TYR THR SEQRES 8 B 347 THR ASN LYS VAL HIS ALA ILE PRO LEU ARG SER SER TRP SEQRES 9 B 347 VAL MET THR CYS ALA TYR ALA PRO SER GLY ASN TYR VAL SEQRES 10 B 347 ALA CYS GLY GLY LEU ASP ASN ILE CYS SER ILE TYR ASN SEQRES 11 B 347 LEU LYS THR ARG GLU GLY ASN VAL ARG VAL SER ARG GLU SEQRES 12 B 347 LEU ALA GLY HIS THR GLY TYR LEU SER CYS CYS ARG PHE SEQRES 13 B 347 LEU ASP ASP ASN GLN ILE VAL THR SER SER GLY ASP THR SEQRES 14 B 347 THR CYS ALA LEU TRP ASP ILE GLU THR GLY GLN GLN THR SEQRES 15 B 347 THR THR PHE THR GLY HIS THR GLY ASP VAL MET SER LEU SEQRES 16 B 347 SER LEU ALA PRO ASP THR ARG LEU PHE VAL SER GLY ALA SEQRES 17 B 347 CYS ASP ALA SER ALA LYS LEU TRP ASP VAL ARG GLU GLY SEQRES 18 B 347 MET CYS ARG GLN THR PHE THR GLY HIS GLU SER ASP ILE SEQRES 19 B 347 ASN ALA ILE CYS PHE PHE PRO ASN GLY ASN ALA PHE ALA SEQRES 20 B 347 THR GLY SER ASP ASP ALA THR CYS ARG LEU PHE ASP LEU SEQRES 21 B 347 ARG ALA ASP GLN GLU LEU MET THR TYR SER HIS ASP ASN SEQRES 22 B 347 ILE ILE CYS GLY ILE THR SER VAL SER PHE SER LYS SER SEQRES 23 B 347 GLY ARG LEU LEU LEU ALA GLY TYR ASP ASP PHE ASN CYS SEQRES 24 B 347 ASN VAL TRP ASP ALA LEU LYS ALA ASP ARG ALA GLY VAL SEQRES 25 B 347 LEU ALA GLY HIS ASP ASN ARG VAL SER CYS LEU GLY VAL SEQRES 26 B 347 THR ASP ASP GLY MET ALA VAL ALA THR GLY SER TRP ASP SEQRES 27 B 347 SER PHE LEU LYS ILE TRP ASN GLY SER SEQRES 1 G 71 MET ALA SER ASN ASN THR ALA SER ILE ALA GLN ALA ARG SEQRES 2 G 71 LYS LEU VAL GLU GLN LEU LYS MET GLU ALA ASN ILE ASP SEQRES 3 G 71 ARG ILE LYS VAL SER LYS ALA ALA ALA ASP LEU MET ALA SEQRES 4 G 71 TYR CYS GLU ALA HIS ALA LYS GLU ASP PRO LEU LEU THR SEQRES 5 G 71 PRO VAL PRO ALA SER GLU ASN PRO PHE ARG GLU LYS LYS SEQRES 6 G 71 PHE PHE CYS ALA ILE LEU SEQRES 1 N 138 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 N 138 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 N 138 PHE THR PHE SER ASN TYR LYS MET ASN TRP VAL ARG GLN SEQRES 4 N 138 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ASP ILE SER SEQRES 5 N 138 GLN SER GLY ALA SER ILE SER TYR THR GLY SER VAL LYS SEQRES 6 N 138 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 N 138 LEU TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 N 138 ALA VAL TYR TYR CYS ALA ARG CYS PRO ALA PRO PHE THR SEQRES 9 N 138 ARG ASP CYS PHE ASP VAL THR SER THR THR TYR ALA TYR SEQRES 10 N 138 ARG GLY GLN GLY THR GLN VAL THR VAL SER SER HIS HIS SEQRES 11 N 138 HIS HIS HIS HIS GLU PRO GLU ALA SEQRES 1 R 330 MET MET TRP GLY ALA GLY SER PRO LEU ALA TRP LEU SER SEQRES 2 R 330 ALA GLY SER GLY ASN VAL ASN VAL SER SER VAL GLY PRO SEQRES 3 R 330 ALA GLU GLY PRO THR GLY PRO ALA ALA PRO LEU PRO SER SEQRES 4 R 330 PRO LYS ALA TRP ASP VAL VAL LEU CYS ILE SER GLY THR SEQRES 5 R 330 LEU VAL SER CYS GLU ASN ALA LEU VAL VAL ALA ILE ILE SEQRES 6 R 330 VAL GLY THR PRO ALA PHE ARG ALA PRO MET PHE LEU LEU SEQRES 7 R 330 VAL GLY SER LEU ALA VAL ALA ASP LEU LEU ALA GLY LEU SEQRES 8 R 330 GLY LEU VAL LEU HIS PHE ALA ALA VAL PHE CYS ILE GLY SEQRES 9 R 330 SER ALA GLU MET SER LEU VAL LEU VAL GLY VAL LEU ALA SEQRES 10 R 330 MET ALA PHE THR ALA SER ILE GLY SER LEU LEU ALA ILE SEQRES 11 R 330 THR VAL ASP ARG TYR LEU SER LEU TYR ASN ALA LEU THR SEQRES 12 R 330 TYR TYR SER GLU THR THR VAL THR ARG THR TYR VAL MET SEQRES 13 R 330 LEU ALA LEU VAL TRP GLY GLY ALA LEU GLY LEU GLY LEU SEQRES 14 R 330 LEU PRO VAL LEU ALA TRP ASN CYS LEU ASP GLY LEU THR SEQRES 15 R 330 THR CYS GLY VAL VAL TYR PRO LEU SER LYS ASN HIS LEU SEQRES 16 R 330 VAL VAL LEU ALA ILE ALA PHE PHE MET VAL PHE GLY ILE SEQRES 17 R 330 MET LEU GLN LEU TYR ALA GLN ILE CYS ARG ILE VAL CYS SEQRES 18 R 330 ARG HIS ALA GLN GLN ILE ALA LEU GLN ARG HIS LEU LEU SEQRES 19 R 330 PRO ALA SER HIS TYR VAL ALA THR ARG LYS GLY ILE ALA SEQRES 20 R 330 THR LEU ALA VAL VAL LEU GLY ALA PHE ALA ALA CYS TRP SEQRES 21 R 330 LEU PRO PHE THR VAL TYR CYS LEU LEU GLY ASP ALA HIS SEQRES 22 R 330 SER PRO PRO LEU TYR THR TYR LEU THR LEU LEU PRO ALA SEQRES 23 R 330 THR TYR ASN SER MET ILE ASN PRO ILE ILE TYR ALA PHE SEQRES 24 R 330 ARG ASN GLN ASP VAL GLN LYS VAL LEU TRP ALA VAL CYS SEQRES 25 R 330 CYS CYS CYS SER SER SER LYS ILE PRO PHE ARG SER ARG SEQRES 26 R 330 SER PRO SER ASP VAL HET OLA R 601 20 HET Y01 R 602 35 HET PLM R 603 18 HETNAM OLA OLEIC ACID HETNAM Y01 CHOLESTEROL HEMISUCCINATE HETNAM PLM PALMITIC ACID FORMUL 6 OLA C18 H34 O2 FORMUL 7 Y01 C31 H50 O4 FORMUL 8 PLM C16 H32 O2 FORMUL 9 HOH *2(H2 O) HELIX 1 AA1 ALA A 18 ALA A 37 1 20 HELIX 2 AA2 GLY A 52 ARG A 61 1 10 HELIX 3 AA3 LYS A 233 ASN A 239 5 7 HELIX 4 AA4 ASN A 264 ASN A 279 1 16 HELIX 5 AA5 LYS A 293 VAL A 301 1 9 HELIX 6 AA6 SER A 306 PHE A 312 1 7 HELIX 7 AA7 PRO A 313 TYR A 318 5 6 HELIX 8 AA8 ASP A 331 THR A 350 1 20 HELIX 9 AA9 GLU A 370 TYR A 391 1 22 HELIX 10 AB1 LEU B 4 ALA B 24 1 21 HELIX 11 AB2 THR B 29 THR B 34 1 6 HELIX 12 AB3 ILE G 9 ASN G 24 1 16 HELIX 13 AB4 LYS G 29 HIS G 44 1 16 HELIX 14 AB5 ALA G 45 ASP G 48 5 4 HELIX 15 AB6 PRO G 55 ASN G 59 5 5 HELIX 16 AB7 THR N 28 TYR N 32 5 5 HELIX 17 AB8 LYS N 87 THR N 91 5 5 HELIX 18 AB9 LYS R 41 GLY R 67 1 27 HELIX 19 AC1 ALA R 73 GLY R 92 1 20 HELIX 20 AC2 ALA R 106 ASN R 140 1 35 HELIX 21 AC3 ALA R 141 TYR R 144 5 4 HELIX 22 AC4 SER R 146 LEU R 167 1 22 HELIX 23 AC5 LYS R 192 GLN R 230 1 39 HELIX 24 AC6 ARG R 243 GLY R 270 1 28 HELIX 25 AC7 PRO R 275 LEU R 283 1 9 HELIX 26 AC8 LEU R 284 ALA R 298 1 15 HELIX 27 AC9 ASN R 301 CYS R 313 1 13 SHEET 1 AA1 6 ILE A 207 VAL A 214 0 SHEET 2 AA1 6 VAL A 217 VAL A 224 -1 O PHE A 219 N PHE A 212 SHEET 3 AA1 6 THR A 40 LEU A 46 1 N HIS A 41 O HIS A 220 SHEET 4 AA1 6 ALA A 243 ALA A 249 1 O ILE A 245 N LEU A 44 SHEET 5 AA1 6 SER A 286 ASN A 292 1 O PHE A 290 N PHE A 246 SHEET 6 AA1 6 CYS A 359 PHE A 363 1 O TYR A 360 N VAL A 287 SHEET 1 AA2 4 ARG B 46 LEU B 51 0 SHEET 2 AA2 4 LEU B 336 ASN B 340 -1 O ASN B 340 N ARG B 46 SHEET 3 AA2 4 VAL B 327 SER B 331 -1 N VAL B 327 O TRP B 339 SHEET 4 AA2 4 VAL B 315 VAL B 320 -1 N GLY B 319 O ALA B 328 SHEET 1 AA3 4 ILE B 58 TRP B 63 0 SHEET 2 AA3 4 LEU B 69 SER B 74 -1 O ALA B 73 N TYR B 59 SHEET 3 AA3 4 LYS B 78 ASP B 83 -1 O TRP B 82 N LEU B 70 SHEET 4 AA3 4 LYS B 89 PRO B 94 -1 O ILE B 93 N LEU B 79 SHEET 1 AA4 4 VAL B 100 TYR B 105 0 SHEET 2 AA4 4 TYR B 111 GLY B 116 -1 O GLY B 115 N MET B 101 SHEET 3 AA4 4 CYS B 121 ASN B 125 -1 O SER B 122 N CYS B 114 SHEET 4 AA4 4 ARG B 134 LEU B 139 -1 O SER B 136 N ILE B 123 SHEET 1 AA5 4 LEU B 146 ASP B 153 0 SHEET 2 AA5 4 GLN B 156 SER B 161 -1 O SER B 160 N SER B 147 SHEET 3 AA5 4 THR B 165 ASP B 170 -1 O TRP B 169 N ILE B 157 SHEET 4 AA5 4 GLN B 175 THR B 181 -1 O THR B 177 N LEU B 168 SHEET 1 AA6 4 VAL B 187 LEU B 192 0 SHEET 2 AA6 4 LEU B 198 ALA B 203 -1 O GLY B 202 N MET B 188 SHEET 3 AA6 4 SER B 207 ASP B 212 -1 O TRP B 211 N PHE B 199 SHEET 4 AA6 4 CYS B 218 THR B 223 -1 O PHE B 222 N ALA B 208 SHEET 1 AA7 4 ILE B 229 PHE B 234 0 SHEET 2 AA7 4 ALA B 240 SER B 245 -1 O GLY B 244 N ASN B 230 SHEET 3 AA7 4 CYS B 250 ASP B 254 -1 O PHE B 253 N PHE B 241 SHEET 4 AA7 4 GLU B 260 TYR B 264 -1 O TYR B 264 N CYS B 250 SHEET 1 AA8 4 ILE B 273 PHE B 278 0 SHEET 2 AA8 4 LEU B 284 TYR B 289 -1 O LEU B 286 N SER B 277 SHEET 3 AA8 4 CYS B 294 ASP B 298 -1 O TRP B 297 N LEU B 285 SHEET 4 AA8 4 ARG B 304 LEU B 308 -1 O ALA B 305 N VAL B 296 SHEET 1 AA9 4 GLN N 3 SER N 7 0 SHEET 2 AA9 4 SER N 17 SER N 25 -1 O ALA N 23 N GLN N 5 SHEET 3 AA9 4 THR N 78 ASN N 84 -1 O MET N 83 N LEU N 18 SHEET 4 AA9 4 PHE N 68 ASP N 73 -1 N SER N 71 O TYR N 80 SHEET 1 AB1 6 GLY N 10 VAL N 12 0 SHEET 2 AB1 6 THR N 122 VAL N 126 1 O THR N 125 N GLY N 10 SHEET 3 AB1 6 ALA N 92 ARG N 98 -1 N ALA N 92 O VAL N 124 SHEET 4 AB1 6 MET N 34 GLN N 39 -1 N GLN N 39 O VAL N 93 SHEET 5 AB1 6 LEU N 45 ILE N 51 -1 O GLU N 46 N ARG N 38 SHEET 6 AB1 6 ILE N 58 TYR N 60 -1 O SER N 59 N ASP N 50 SSBOND 1 CYS N 22 CYS N 96 1555 1555 2.04 SSBOND 2 CYS N 99 CYS N 107 1555 1555 2.03 SSBOND 3 CYS R 177 CYS R 184 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