HEADER MEMBRANE PROTEIN/IMMUNE SYSTEM 28-JUL-24 9IXJ TITLE HISTAMINE-BOUND H2R IN COMPLEX WITH GS 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 SYNONYM: GUANINE NUCLEOTIDE-BINDING PROTEIN G(S) SUBUNIT ALPHA (4A), COMPND 6 ADENYLATE CYCLASE-STIMULATING G ALPHA PROTEIN; COMPND 7 ENGINEERED: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 10 BETA-1; COMPND 11 CHAIN: B; COMPND 12 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 3; COMPND 15 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 16 GAMMA-2; COMPND 17 CHAIN: G; COMPND 18 SYNONYM: G GAMMA-I; COMPND 19 ENGINEERED: YES; COMPND 20 MOL_ID: 4; COMPND 21 MOLECULE: NB35; COMPND 22 CHAIN: N; COMPND 23 ENGINEERED: YES; COMPND 24 MOL_ID: 5; COMPND 25 MOLECULE: HISTAMINE H2 RECEPTOR; COMPND 26 CHAIN: R; COMPND 27 SYNONYM: H2R,HH2R,GASTRIC RECEPTOR I; COMPND 28 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: GNAS, GNAS1, GSP; 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: LAMA GLAMA; SOURCE 24 ORGANISM_TAXID: 9844; SOURCE 25 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 27 MOL_ID: 5; SOURCE 28 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 29 ORGANISM_COMMON: HUMAN; SOURCE 30 ORGANISM_TAXID: 9606; SOURCE 31 GENE: HRH2; SOURCE 32 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 33 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS GPCR-G-PROTEIN COMPLEX, MEMBRANE PROTEIN/IMMUNE SYSTEM, MEMBRANE KEYWDS 2 PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR Y.HE,K.CHEN REVDAT 1 30-JUL-25 9IXJ 0 JRNL AUTH Y.HE,K.CHEN JRNL TITL HISTAMINE-BOUND H2R IN COMPLEX WITH GS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.92 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) : 2.920 REMARK 3 NUMBER OF PARTICLES : 332748 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 9IXJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 30-JUL-24. REMARK 100 THE DEPOSITION ID IS D_1300049886. 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 : 7.00 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 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 1 REMARK 465 GLY A 2 REMARK 465 CYS A 3 REMARK 465 LEU A 4 REMARK 465 GLY A 5 REMARK 465 ASN A 6 REMARK 465 SER A 7 REMARK 465 LYS A 8 REMARK 465 GLY A 49 REMARK 465 GLU A 50 REMARK 465 SER A 51 REMARK 465 GLY A 52 REMARK 465 LYS A 53 REMARK 465 ARG A 61 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 THR A 204 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 VAL A 367 REMARK 465 ASP A 368 REMARK 465 THR A 369 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 MET N -21 REMARK 465 LYS N -20 REMARK 465 TYR N -19 REMARK 465 LEU N -18 REMARK 465 LEU N -17 REMARK 465 PRO N -16 REMARK 465 THR N -15 REMARK 465 ALA N -14 REMARK 465 ALA N -13 REMARK 465 ALA N -12 REMARK 465 GLY N -11 REMARK 465 LEU N -10 REMARK 465 LEU N -9 REMARK 465 LEU N -8 REMARK 465 LEU N -7 REMARK 465 ALA N -6 REMARK 465 ALA N -5 REMARK 465 GLN N -4 REMARK 465 PRO N -3 REMARK 465 ALA N -2 REMARK 465 MET N -1 REMARK 465 ALA N 0 REMARK 465 ALA N 129 REMARK 465 ALA N 130 REMARK 465 ALA N 131 REMARK 465 LEU N 132 REMARK 465 GLU N 133 REMARK 465 HIS N 134 REMARK 465 HIS N 135 REMARK 465 HIS N 136 REMARK 465 HIS N 137 REMARK 465 HIS N 138 REMARK 465 HIS N 139 REMARK 465 MET R 1 REMARK 465 ALA R 2 REMARK 465 PRO R 3 REMARK 465 ASN R 4 REMARK 465 GLY R 5 REMARK 465 THR R 6 REMARK 465 ALA R 7 REMARK 465 SER R 8 REMARK 465 SER R 9 REMARK 465 PHE R 10 REMARK 465 CYS R 11 REMARK 465 LEU R 12 REMARK 465 ASP R 13 REMARK 465 ASN R 162 REMARK 465 GLU R 163 REMARK 465 THR R 164 REMARK 465 SER R 165 REMARK 465 LYS R 166 REMARK 465 GLY R 167 REMARK 465 ASN R 168 REMARK 465 HIS R 169 REMARK 465 THR R 170 REMARK 465 THR R 171 REMARK 465 TYR R 299 REMARK 465 GLN R 300 REMARK 465 GLN R 301 REMARK 465 LEU R 302 REMARK 465 PHE R 303 REMARK 465 CYS R 304 REMARK 465 CYS R 305 REMARK 465 ARG R 306 REMARK 465 LEU R 307 REMARK 465 ALA R 308 REMARK 465 ASN R 309 REMARK 465 ARG R 310 REMARK 465 ASN R 311 REMARK 465 SER R 312 REMARK 465 HIS R 313 REMARK 465 LYS R 314 REMARK 465 THR R 315 REMARK 465 SER R 316 REMARK 465 LEU R 317 REMARK 465 ARG R 318 REMARK 465 SER R 319 REMARK 465 ASN R 320 REMARK 465 ALA R 321 REMARK 465 SER R 322 REMARK 465 GLN R 323 REMARK 465 LEU R 324 REMARK 465 SER R 325 REMARK 465 ARG R 326 REMARK 465 THR R 327 REMARK 465 GLN R 328 REMARK 465 SER R 329 REMARK 465 ARG R 330 REMARK 465 GLU R 331 REMARK 465 PRO R 332 REMARK 465 ARG R 333 REMARK 465 GLN R 334 REMARK 465 GLN R 335 REMARK 465 GLU R 336 REMARK 465 GLU R 337 REMARK 465 LYS R 338 REMARK 465 PRO R 339 REMARK 465 LEU R 340 REMARK 465 LYS R 341 REMARK 465 LEU R 342 REMARK 465 GLN R 343 REMARK 465 VAL R 344 REMARK 465 TRP R 345 REMARK 465 SER R 346 REMARK 465 GLY R 347 REMARK 465 THR R 348 REMARK 465 GLU R 349 REMARK 465 VAL R 350 REMARK 465 THR R 351 REMARK 465 ALA R 352 REMARK 465 PRO R 353 REMARK 465 GLN R 354 REMARK 465 GLY R 355 REMARK 465 ALA R 356 REMARK 465 THR R 357 REMARK 465 ASP R 358 REMARK 465 ARG R 359 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 A 10 CG CD OE1 OE2 REMARK 470 ILE A 56 CG1 CG2 CD1 REMARK 470 LYS A 58 CG CD CE NZ REMARK 470 TYR A 253 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG A 265 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 293 CG CD CE NZ REMARK 470 LYS A 300 CG CD CE NZ REMARK 470 LYS A 305 CG CD CE NZ REMARK 470 GLU A 370 CG CD OE1 OE2 REMARK 470 ILE A 372 CG1 CG2 CD1 REMARK 470 ARG A 373 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 8 CG CD NE CZ NH1 NH2 REMARK 470 ARG R 47 CG CD NE CZ NH1 NH2 REMARK 470 ARG R 48 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 OG SER B 281 OD2 ASP G 48 2.18 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 THR A 350 34.75 -98.23 REMARK 500 THR B 87 -5.00 75.13 REMARK 500 ASP B 205 20.38 -140.55 REMARK 500 SER B 277 149.83 -171.09 REMARK 500 ALA N 92 -169.51 -167.62 REMARK 500 ARG R 228 -8.29 73.60 REMARK 500 LYS R 231 -60.30 -93.56 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-60971 RELATED DB: EMDB REMARK 900 HISTAMINE-BOUND H2R IN COMPLEX WITH GS DBREF 9IXJ A 1 398 UNP P63092 GNAS2_HUMAN 1 394 DBREF 9IXJ B 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 9IXJ G 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 9IXJ N -21 139 PDB 9IXJ 9IXJ -21 139 DBREF 9IXJ R 1 359 UNP P25021 HRH2_HUMAN 1 359 SEQADV 9IXJ ASP A 188 UNP P63092 ALA 188 VARIANT SEQADV 9IXJ ALA A 374 UNP P63092 INSERTION SEQADV 9IXJ ALA A 375 UNP P63092 INSERTION SEQADV 9IXJ ALA A 376 UNP P63092 INSERTION SEQADV 9IXJ ALA A 377 UNP P63092 INSERTION SEQADV 9IXJ ILE A 379 UNP P63092 VAL 375 CONFLICT SEQADV 9IXJ MET B -4 UNP P62873 INITIATING METHIONINE SEQADV 9IXJ GLY B -3 UNP P62873 EXPRESSION TAG SEQADV 9IXJ SER B -2 UNP P62873 EXPRESSION TAG SEQADV 9IXJ LEU B -1 UNP P62873 EXPRESSION TAG SEQADV 9IXJ LEU B 0 UNP P62873 EXPRESSION TAG SEQADV 9IXJ GLN B 1 UNP P62873 EXPRESSION TAG SEQADV 9IXJ GLY B 341 UNP P62873 EXPRESSION TAG SEQADV 9IXJ SER B 342 UNP P62873 EXPRESSION TAG SEQRES 1 A 398 MET GLY CYS LEU GLY ASN SER LYS THR GLU ASP GLN ARG SEQRES 2 A 398 ASN GLU GLU LYS ALA GLN ARG GLU ALA ASN LYS LYS ILE SEQRES 3 A 398 GLU LYS GLN LEU GLN LYS ASP LYS GLN VAL TYR ARG ALA SEQRES 4 A 398 THR HIS ARG LEU LEU LEU LEU GLY ALA GLY GLU SER GLY SEQRES 5 A 398 LYS SER THR ILE VAL LYS GLN MET ARG ILE LEU HIS VAL SEQRES 6 A 398 ASN GLY PHE ASN GLY GLU GLY GLY GLU GLU ASP PRO GLN SEQRES 7 A 398 ALA ALA ARG SER ASN SER ASP GLY GLU LYS ALA THR LYS SEQRES 8 A 398 VAL GLN ASP ILE LYS ASN ASN LEU LYS GLU ALA ILE GLU SEQRES 9 A 398 THR ILE VAL ALA ALA MET SER ASN LEU VAL PRO PRO VAL SEQRES 10 A 398 GLU LEU ALA ASN PRO GLU ASN GLN PHE ARG VAL ASP TYR SEQRES 11 A 398 ILE LEU SER VAL MET ASN VAL PRO ASP PHE ASP PHE PRO SEQRES 12 A 398 PRO GLU PHE TYR GLU HIS ALA LYS ALA LEU TRP GLU ASP SEQRES 13 A 398 GLU GLY VAL ARG ALA CYS TYR GLU ARG SER ASN GLU TYR SEQRES 14 A 398 GLN LEU ILE ASP CYS ALA GLN TYR PHE LEU ASP LYS ILE SEQRES 15 A 398 ASP VAL ILE LYS GLN ASP ASP TYR VAL PRO SER ASP GLN SEQRES 16 A 398 ASP LEU LEU ARG CYS ARG VAL LEU THR SER GLY ILE PHE SEQRES 17 A 398 GLU THR LYS PHE GLN VAL ASP LYS VAL ASN PHE HIS MET SEQRES 18 A 398 PHE ASP VAL GLY GLY GLN ARG ASP GLU ARG ARG LYS TRP SEQRES 19 A 398 ILE GLN CYS PHE ASN ASP VAL THR ALA ILE ILE PHE VAL SEQRES 20 A 398 VAL ALA SER SER SER TYR ASN MET VAL ILE ARG GLU ASP SEQRES 21 A 398 ASN GLN THR ASN ARG LEU GLN GLU ALA LEU ASN LEU PHE SEQRES 22 A 398 LYS SER ILE TRP ASN ASN ARG TRP LEU ARG THR ILE SER SEQRES 23 A 398 VAL ILE LEU PHE LEU ASN LYS GLN ASP LEU LEU ALA GLU SEQRES 24 A 398 LYS VAL LEU ALA GLY LYS SER LYS ILE GLU ASP TYR PHE SEQRES 25 A 398 PRO GLU PHE ALA ARG TYR THR THR PRO GLU ASP ALA THR SEQRES 26 A 398 PRO GLU PRO GLY GLU ASP PRO ARG VAL THR ARG ALA LYS SEQRES 27 A 398 TYR PHE ILE ARG ASP GLU PHE LEU ARG ILE SER THR ALA SEQRES 28 A 398 SER GLY ASP GLY ARG HIS TYR CYS TYR PRO HIS PHE THR SEQRES 29 A 398 CYS ALA VAL ASP THR GLU ASN ILE ARG ALA ALA ALA ALA SEQRES 30 A 398 ARG ILE PHE ASN ASP CYS ARG ASP ILE ILE GLN ARG MET SEQRES 31 A 398 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 161 MET LYS TYR LEU LEU PRO THR ALA ALA ALA GLY LEU LEU SEQRES 2 N 161 LEU LEU ALA ALA GLN PRO ALA MET ALA GLN VAL GLN LEU SEQRES 3 N 161 GLN GLU SER GLY GLY GLY LEU VAL GLN PRO GLY GLY SER SEQRES 4 N 161 LEU ARG LEU SER CYS ALA ALA SER GLY PHE THR PHE SER SEQRES 5 N 161 ASN TYR LYS MET ASN TRP VAL ARG GLN ALA PRO GLY LYS SEQRES 6 N 161 GLY LEU GLU TRP VAL SER ASP ILE SER GLN SER GLY ALA SEQRES 7 N 161 SER ILE SER TYR THR GLY SER VAL LYS GLY ARG PHE THR SEQRES 8 N 161 ILE SER ARG ASP ASN ALA LYS ASN THR LEU TYR LEU GLN SEQRES 9 N 161 MET ASN SER LEU LYS PRO GLU ASP THR ALA VAL TYR TYR SEQRES 10 N 161 CYS ALA ARG CYS PRO ALA PRO PHE THR ARG ASP CYS PHE SEQRES 11 N 161 ASP VAL THR SER THR THR TYR ALA TYR ARG GLY GLN GLY SEQRES 12 N 161 THR GLN VAL THR VAL SER SER ALA ALA ALA LEU GLU HIS SEQRES 13 N 161 HIS HIS HIS HIS HIS SEQRES 1 R 359 MET ALA PRO ASN GLY THR ALA SER SER PHE CYS LEU ASP SEQRES 2 R 359 SER THR ALA CYS LYS ILE THR ILE THR VAL VAL LEU ALA SEQRES 3 R 359 VAL LEU ILE LEU ILE THR VAL ALA GLY ASN VAL VAL VAL SEQRES 4 R 359 CYS LEU ALA VAL GLY LEU ASN ARG ARG LEU ARG ASN LEU SEQRES 5 R 359 THR ASN CYS PHE ILE VAL SER LEU ALA ILE THR ASP LEU SEQRES 6 R 359 LEU LEU GLY LEU LEU VAL LEU PRO PHE SER ALA ILE TYR SEQRES 7 R 359 GLN LEU SER CYS LYS TRP SER PHE GLY LYS VAL PHE CYS SEQRES 8 R 359 ASN ILE TYR THR SER LEU ASP VAL MET LEU CYS THR ALA SEQRES 9 R 359 SER ILE LEU ASN LEU PHE MET ILE SER LEU ASP ARG TYR SEQRES 10 R 359 CYS ALA VAL MET ASP PRO LEU ARG TYR PRO VAL LEU VAL SEQRES 11 R 359 THR PRO VAL ARG VAL ALA ILE SER LEU VAL LEU ILE TRP SEQRES 12 R 359 VAL ILE SER ILE THR LEU SER PHE LEU SER ILE HIS LEU SEQRES 13 R 359 GLY TRP ASN SER ARG ASN GLU THR SER LYS GLY ASN HIS SEQRES 14 R 359 THR THR SER LYS CYS LYS VAL GLN VAL ASN GLU VAL TYR SEQRES 15 R 359 GLY LEU VAL ASP GLY LEU VAL THR PHE TYR LEU PRO LEU SEQRES 16 R 359 LEU ILE MET CYS ILE THR TYR TYR ARG ILE PHE LYS VAL SEQRES 17 R 359 ALA ARG ASP GLN ALA LYS ARG ILE ASN HIS ILE SER SER SEQRES 18 R 359 TRP LYS ALA ALA THR ILE ARG GLU HIS LYS ALA THR VAL SEQRES 19 R 359 THR LEU ALA ALA VAL MET GLY ALA PHE ILE ILE CYS TRP SEQRES 20 R 359 PHE PRO TYR PHE THR ALA PHE VAL TYR ARG GLY LEU ARG SEQRES 21 R 359 GLY ASP ASP ALA ILE ASN GLU VAL LEU GLU ALA ILE VAL SEQRES 22 R 359 LEU TRP LEU GLY TYR ALA ASN SER ALA LEU ASN PRO ILE SEQRES 23 R 359 LEU TYR ALA ALA LEU ASN ARG ASP PHE ARG THR GLY TYR SEQRES 24 R 359 GLN GLN LEU PHE CYS CYS ARG LEU ALA ASN ARG ASN SER SEQRES 25 R 359 HIS LYS THR SER LEU ARG SER ASN ALA SER GLN LEU SER SEQRES 26 R 359 ARG THR GLN SER ARG GLU PRO ARG GLN GLN GLU GLU LYS SEQRES 27 R 359 PRO LEU LYS LEU GLN VAL TRP SER GLY THR GLU VAL THR SEQRES 28 R 359 ALA PRO GLN GLY ALA THR ASP ARG HET HSM R 401 8 HET CLR R 402 28 HETNAM HSM HISTAMINE HETNAM CLR CHOLESTEROL FORMUL 6 HSM C5 H9 N3 FORMUL 7 CLR C27 H46 O HELIX 1 AA1 THR A 9 ALA A 39 1 31 HELIX 2 AA2 THR A 55 MET A 60 1 6 HELIX 3 AA3 TRP A 234 PHE A 238 5 5 HELIX 4 AA4 ASN A 264 ASN A 278 1 15 HELIX 5 AA5 GLN A 294 LEU A 302 1 9 HELIX 6 AA6 SER A 306 PHE A 312 1 7 HELIX 7 AA7 PRO A 313 ALA A 316 5 4 HELIX 8 AA8 ASP A 331 THR A 350 1 20 HELIX 9 AA9 ALA A 374 TYR A 395 1 22 HELIX 10 AB1 LEU B 4 CYS B 25 1 22 HELIX 11 AB2 ILE G 9 ASN G 24 1 16 HELIX 12 AB3 LYS G 29 HIS G 44 1 16 HELIX 13 AB4 THR N 28 TYR N 32 5 5 HELIX 14 AB5 LYS N 87 THR N 91 5 5 HELIX 15 AB6 THR R 15 ASN R 46 1 32 HELIX 16 AB7 ASN R 51 THR R 53 5 3 HELIX 17 AB8 ASN R 54 VAL R 71 1 18 HELIX 18 AB9 VAL R 71 CYS R 82 1 12 HELIX 19 AC1 LYS R 88 ASP R 122 1 35 HELIX 20 AC2 ARG R 125 LEU R 129 5 5 HELIX 21 AC3 THR R 131 HIS R 155 1 25 HELIX 22 AC4 ASN R 179 PHE R 191 1 13 HELIX 23 AC5 PHE R 191 ASN R 217 1 27 HELIX 24 AC6 LYS R 231 GLY R 261 1 31 HELIX 25 AC7 ASP R 262 ILE R 265 5 4 HELIX 26 AC8 ASN R 266 ALA R 279 1 14 HELIX 27 AC9 ALA R 279 ALA R 290 1 12 HELIX 28 AD1 ASN R 292 GLY R 298 1 7 SHEET 1 AA1 3 THR A 40 HIS A 41 0 SHEET 2 AA1 3 VAL A 217 VAL A 224 1 O HIS A 220 N HIS A 41 SHEET 3 AA1 3 ILE A 207 VAL A 214 -1 N PHE A 212 O PHE A 219 SHEET 1 AA2 6 THR A 40 HIS A 41 0 SHEET 2 AA2 6 VAL A 217 VAL A 224 1 O HIS A 220 N HIS A 41 SHEET 3 AA2 6 LEU A 43 GLY A 47 1 N LEU A 45 O PHE A 222 SHEET 4 AA2 6 ALA A 243 ALA A 249 1 O ILE A 245 N LEU A 44 SHEET 5 AA2 6 SER A 286 ASN A 292 1 O ILE A 288 N PHE A 246 SHEET 6 AA2 6 CYS A 359 PHE A 363 1 O TYR A 360 N LEU A 289 SHEET 1 AA3 4 ARG B 46 LEU B 51 0 SHEET 2 AA3 4 LEU B 336 ASN B 340 -1 O ASN B 340 N ARG B 46 SHEET 3 AA3 4 VAL B 327 SER B 331 -1 N VAL B 327 O TRP B 339 SHEET 4 AA3 4 VAL B 315 VAL B 320 -1 N CYS B 317 O GLY B 330 SHEET 1 AA4 4 ILE B 58 TRP B 63 0 SHEET 2 AA4 4 LEU B 69 SER B 74 -1 O ALA B 73 N TYR B 59 SHEET 3 AA4 4 LYS B 78 ASP B 83 -1 O LYS B 78 N SER B 74 SHEET 4 AA4 4 LYS B 89 PRO B 94 -1 O VAL B 90 N ILE B 81 SHEET 1 AA5 4 VAL B 100 TYR B 105 0 SHEET 2 AA5 4 TYR B 111 GLY B 116 -1 O GLY B 115 N MET B 101 SHEET 3 AA5 4 ILE B 120 ASN B 125 -1 O TYR B 124 N VAL B 112 SHEET 4 AA5 4 VAL B 135 ALA B 140 -1 O LEU B 139 N CYS B 121 SHEET 1 AA6 4 LEU B 146 ASP B 153 0 SHEET 2 AA6 4 GLN B 156 SER B 161 -1 O SER B 160 N SER B 147 SHEET 3 AA6 4 THR B 165 ASP B 170 -1 O TRP B 169 N ILE B 157 SHEET 4 AA6 4 GLN B 175 THR B 181 -1 O PHE B 180 N CYS B 166 SHEET 1 AA7 4 VAL B 187 LEU B 192 0 SHEET 2 AA7 4 LEU B 198 ALA B 203 -1 O GLY B 202 N MET B 188 SHEET 3 AA7 4 ALA B 208 ASP B 212 -1 O TRP B 211 N PHE B 199 SHEET 4 AA7 4 CYS B 218 PHE B 222 -1 O PHE B 222 N ALA B 208 SHEET 1 AA8 4 ILE B 229 PHE B 234 0 SHEET 2 AA8 4 ALA B 240 SER B 245 -1 O GLY B 244 N ASN B 230 SHEET 3 AA8 4 CYS B 250 ASP B 254 -1 O PHE B 253 N PHE B 241 SHEET 4 AA8 4 GLN B 259 TYR B 264 -1 O LEU B 261 N LEU B 252 SHEET 1 AA9 4 ILE B 273 PHE B 278 0 SHEET 2 AA9 4 LEU B 284 TYR B 289 -1 O GLY B 288 N THR B 274 SHEET 3 AA9 4 CYS B 294 ASP B 298 -1 O TRP B 297 N LEU B 285 SHEET 4 AA9 4 ARG B 304 LEU B 308 -1 O LEU B 308 N CYS B 294 SHEET 1 AB1 4 GLN N 3 SER N 7 0 SHEET 2 AB1 4 SER N 17 SER N 25 -1 O SER N 21 N SER N 7 SHEET 3 AB1 4 THR N 78 ASN N 84 -1 O MET N 83 N LEU N 18 SHEET 4 AB1 4 PHE N 68 ASP N 73 -1 N ASP N 73 O THR N 78 SHEET 1 AB2 6 GLY N 10 VAL N 12 0 SHEET 2 AB2 6 THR N 122 VAL N 126 1 O THR N 125 N GLY N 10 SHEET 3 AB2 6 ALA N 92 ARG N 98 -1 N ALA N 92 O VAL N 124 SHEET 4 AB2 6 MET N 34 GLN N 39 -1 N VAL N 37 O TYR N 95 SHEET 5 AB2 6 LEU N 45 ILE N 51 -1 O ILE N 51 N MET N 34 SHEET 6 AB2 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 91 CYS R 174 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