HEADER SIGNALING PROTEIN 07-FEB-24 8VY7 TITLE CRYOEM STRUCTURE OF GI-COUPLED TAS2R14 WITH CHOLESTEROL AND AN TITLE 2 INTRACELLULAR TASTANT COMPND MOL_ID: 1; COMPND 2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I) SUBUNIT ALPHA-1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: ADENYLATE CYCLASE-INHIBITING G ALPHA PROTEIN; 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 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 14 GAMMA-2; COMPND 15 CHAIN: C; COMPND 16 SYNONYM: G GAMMA-I; COMPND 17 ENGINEERED: YES; COMPND 18 MOL_ID: 4; COMPND 19 MOLECULE: SCFV16; COMPND 20 CHAIN: D; COMPND 21 ENGINEERED: YES; COMPND 22 MOL_ID: 5; COMPND 23 MOLECULE: TASTE RECEPTOR TYPE 2 MEMBER 14; COMPND 24 CHAIN: R; COMPND 25 SYNONYM: T2R14,TASTE RECEPTOR FAMILY B MEMBER 1,TRB1; 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: GNAI1; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 GENE: GNB1; SOURCE 14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 15 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 19 ORGANISM_COMMON: HUMAN; SOURCE 20 ORGANISM_TAXID: 9606; SOURCE 21 GENE: GNG2; SOURCE 22 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 23 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 25 MOL_ID: 4; SOURCE 26 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 27 ORGANISM_COMMON: MOUSE; SOURCE 28 ORGANISM_TAXID: 10090; SOURCE 29 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 30 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 31 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 32 MOL_ID: 5; SOURCE 33 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 34 ORGANISM_COMMON: HUMAN; SOURCE 35 ORGANISM_TAXID: 9606; SOURCE 36 GENE: TAS2R14; SOURCE 37 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 38 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 39 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS GPCR, COMPLEX, SIGNALING PROTEIN, TASTE RECEPTOR EXPDTA ELECTRON MICROSCOPY AUTHOR Y.KIM,R.H.GUMPPER,B.L.ROTH JRNL AUTH Y.KIM,B.L.ROTH,R.H.GUMPPER JRNL TITL BITTER TASTE RECEPTOR ACTIVATION BY CHOLESTEROL AND AN JRNL TITL 2 INTRACELLULAR TASTANT JRNL REF NATURE 2024 JRNL REFN ESSN 1476-4687 JRNL DOI 10.1038/S41586-024-07253-Y REMARK 2 REMARK 2 RESOLUTION. 2.68 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) : 2.680 REMARK 3 NUMBER OF PARTICLES : 787890 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 8VY7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000281447. 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 : TERNARY COMPLEX OF TAS2R14 WITH REMARK 245 GI HETEROTRIMER 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 TALOS ARCTICA REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : OTHER REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 50.00 REMARK 245 ILLUMINATION MODE : SPOT SCAN REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : OTHER REMARK 245 ACCELERATION VOLTAGE (KV) : 200 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, 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 THR A 4 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 HIS B -16 REMARK 465 HIS B -15 REMARK 465 HIS B -14 REMARK 465 HIS B -13 REMARK 465 HIS B -12 REMARK 465 HIS B -11 REMARK 465 LEU B -10 REMARK 465 GLU B -9 REMARK 465 VAL B -8 REMARK 465 LEU B -7 REMARK 465 PHE B -6 REMARK 465 GLN B -5 REMARK 465 GLY B -4 REMARK 465 PRO B -3 REMARK 465 GLY B -2 REMARK 465 SER B -1 REMARK 465 SER B 0 REMARK 465 GLY B 1 REMARK 465 GLY B 341 REMARK 465 GLY B 342 REMARK 465 SER B 343 REMARK 465 GLY B 344 REMARK 465 GLY B 345 REMARK 465 GLY B 346 REMARK 465 GLY B 347 REMARK 465 SER B 348 REMARK 465 GLY B 349 REMARK 465 GLY B 350 REMARK 465 SER B 351 REMARK 465 SER B 352 REMARK 465 SER B 353 REMARK 465 GLY B 354 REMARK 465 GLY B 355 REMARK 465 GLY B 356 REMARK 465 GLY B 357 REMARK 465 SER B 358 REMARK 465 GLY B 359 REMARK 465 GLY B 360 REMARK 465 GLY B 361 REMARK 465 GLY B 362 REMARK 465 SER B 363 REMARK 465 GLY B 364 REMARK 465 GLY B 365 REMARK 465 SER B 366 REMARK 465 SER B 367 REMARK 465 SER B 368 REMARK 465 GLY B 369 REMARK 465 GLY B 370 REMARK 465 VAL B 371 REMARK 465 SER B 372 REMARK 465 GLY B 373 REMARK 465 TRP B 374 REMARK 465 ARG B 375 REMARK 465 LEU B 376 REMARK 465 PHE B 377 REMARK 465 LYS B 378 REMARK 465 LYS B 379 REMARK 465 ILE B 380 REMARK 465 SER B 381 REMARK 465 GLY B 382 REMARK 465 GLY B 383 REMARK 465 SER B 384 REMARK 465 MET C 1 REMARK 465 ALA C 2 REMARK 465 SER C 3 REMARK 465 ASN C 4 REMARK 465 ASN C 5 REMARK 465 THR C 6 REMARK 465 ALA C 7 REMARK 465 GLU C 63 REMARK 465 LYS C 64 REMARK 465 LYS C 65 REMARK 465 PHE C 66 REMARK 465 PHE C 67 REMARK 465 CYS C 68 REMARK 465 ALA C 69 REMARK 465 ILE C 70 REMARK 465 LEU C 71 REMARK 465 ASP D 1 REMARK 465 GLY D 121A REMARK 465 GLY D 121B REMARK 465 GLY D 121C REMARK 465 GLY D 121D REMARK 465 SER D 121E REMARK 465 GLY D 121F REMARK 465 GLY D 121G REMARK 465 GLY D 121H REMARK 465 GLY D 121I REMARK 465 SER D 121J REMARK 465 GLY D 121K REMARK 465 GLY D 121L REMARK 465 GLY D 121M REMARK 465 GLY D 121N REMARK 465 LYS D 236 REMARK 465 ALA D 237 REMARK 465 ALA D 238 REMARK 465 ALA D 239 REMARK 465 LEU D 240 REMARK 465 GLU D 241 REMARK 465 VAL D 242 REMARK 465 LEU D 243 REMARK 465 PHE D 244 REMARK 465 GLN D 245 REMARK 465 GLY D 246 REMARK 465 PRO D 247 REMARK 465 HIS D 248 REMARK 465 HIS D 249 REMARK 465 HIS D 250 REMARK 465 HIS D 251 REMARK 465 HIS D 252 REMARK 465 HIS D 253 REMARK 465 HIS D 254 REMARK 465 HIS D 255 REMARK 465 ASP R -150 REMARK 465 TYR R -149 REMARK 465 LYS R -148 REMARK 465 ASP R -147 REMARK 465 ASP R -146 REMARK 465 ASP R -145 REMARK 465 ASP R -144 REMARK 465 ALA R -143 REMARK 465 LYS R -142 REMARK 465 LEU R -141 REMARK 465 GLN R -140 REMARK 465 THR R -139 REMARK 465 MET R -138 REMARK 465 HIS R -137 REMARK 465 HIS R -136 REMARK 465 HIS R -135 REMARK 465 HIS R -134 REMARK 465 HIS R -133 REMARK 465 HIS R -132 REMARK 465 HIS R -131 REMARK 465 HIS R -130 REMARK 465 HIS R -129 REMARK 465 HIS R -128 REMARK 465 GLU R -127 REMARK 465 ASN R -126 REMARK 465 LEU R -125 REMARK 465 TYR R -124 REMARK 465 PHE R -123 REMARK 465 GLN R -122 REMARK 465 GLY R -121 REMARK 465 GLY R -120 REMARK 465 THR R -119 REMARK 465 THR R -118 REMARK 465 MET R -117 REMARK 465 ALA R -116 REMARK 465 ASP R -115 REMARK 465 LEU R -114 REMARK 465 GLU R -113 REMARK 465 ASP R -112 REMARK 465 ASN R -111 REMARK 465 TRP R -110 REMARK 465 GLU R -109 REMARK 465 THR R -108 REMARK 465 LEU R -107 REMARK 465 ASN R -106 REMARK 465 ASP R -105 REMARK 465 ASN R -104 REMARK 465 LEU R -103 REMARK 465 LYS R -102 REMARK 465 VAL R -101 REMARK 465 ILE R -100 REMARK 465 GLU R -99 REMARK 465 LYS R -98 REMARK 465 ALA R -97 REMARK 465 ASP R -96 REMARK 465 ASN R -95 REMARK 465 ALA R -94 REMARK 465 ALA R -93 REMARK 465 GLN R -92 REMARK 465 VAL R -91 REMARK 465 LYS R -90 REMARK 465 ASP R -89 REMARK 465 ALA R -88 REMARK 465 LEU R -87 REMARK 465 THR R -86 REMARK 465 LYS R -85 REMARK 465 MET R -84 REMARK 465 ARG R -83 REMARK 465 ALA R -82 REMARK 465 ALA R -81 REMARK 465 ALA R -80 REMARK 465 LEU R -79 REMARK 465 ASP R -78 REMARK 465 ALA R -77 REMARK 465 GLN R -76 REMARK 465 LYS R -75 REMARK 465 ALA R -74 REMARK 465 THR R -73 REMARK 465 PRO R -72 REMARK 465 PRO R -71 REMARK 465 LYS R -70 REMARK 465 LEU R -69 REMARK 465 GLU R -68 REMARK 465 ASP R -67 REMARK 465 LYS R -66 REMARK 465 SER R -65 REMARK 465 PRO R -64 REMARK 465 ASP R -63 REMARK 465 SER R -62 REMARK 465 PRO R -61 REMARK 465 GLU R -60 REMARK 465 MET R -59 REMARK 465 LYS R -58 REMARK 465 ASP R -57 REMARK 465 PHE R -56 REMARK 465 ARG R -55 REMARK 465 HIS R -54 REMARK 465 GLY R -53 REMARK 465 PHE R -52 REMARK 465 ASP R -51 REMARK 465 ILE R -50 REMARK 465 LEU R -49 REMARK 465 VAL R -48 REMARK 465 GLY R -47 REMARK 465 GLN R -46 REMARK 465 ILE R -45 REMARK 465 ASP R -44 REMARK 465 ASP R -43 REMARK 465 ALA R -42 REMARK 465 LEU R -41 REMARK 465 LYS R -40 REMARK 465 LEU R -39 REMARK 465 ALA R -38 REMARK 465 ASN R -37 REMARK 465 GLU R -36 REMARK 465 GLY R -35 REMARK 465 LYS R -34 REMARK 465 VAL R -33 REMARK 465 LYS R -32 REMARK 465 GLU R -31 REMARK 465 ALA R -30 REMARK 465 GLN R -29 REMARK 465 ALA R -28 REMARK 465 ALA R -27 REMARK 465 ALA R -26 REMARK 465 GLU R -25 REMARK 465 GLN R -24 REMARK 465 LEU R -23 REMARK 465 LYS R -22 REMARK 465 THR R -21 REMARK 465 THR R -20 REMARK 465 ARG R -19 REMARK 465 ASN R -18 REMARK 465 ALA R -17 REMARK 465 TYR R -16 REMARK 465 ILE R -15 REMARK 465 GLN R -14 REMARK 465 LYS R -13 REMARK 465 TYR R -12 REMARK 465 LEU R -11 REMARK 465 GLY R -10 REMARK 465 SER R -9 REMARK 465 THR R -8 REMARK 465 LEU R -7 REMARK 465 GLU R -6 REMARK 465 VAL R -5 REMARK 465 LEU R -4 REMARK 465 PHE R -3 REMARK 465 GLN R -2 REMARK 465 GLY R -1 REMARK 465 PRO R 0 REMARK 465 TYR R 159 REMARK 465 ARG R 160 REMARK 465 ARG R 161 REMARK 465 ASN R 162 REMARK 465 LYS R 163 REMARK 465 THR R 164 REMARK 465 CYS R 165 REMARK 465 SER R 166 REMARK 465 SER R 167 REMARK 465 ASP R 168 REMARK 465 SER R 169 REMARK 465 SER R 170 REMARK 465 ASN R 171 REMARK 465 PHE R 172 REMARK 465 THR R 173 REMARK 465 GLY R 303 REMARK 465 SER R 304 REMARK 465 ALA R 305 REMARK 465 GLY R 306 REMARK 465 SER R 307 REMARK 465 ALA R 308 REMARK 465 GLY R 309 REMARK 465 SER R 310 REMARK 465 GLY R 311 REMARK 465 GLY R 312 REMARK 465 SER R 313 REMARK 465 GLY R 314 REMARK 465 GLY R 315 REMARK 465 GLY R 316 REMARK 465 SER R 317 REMARK 465 GLY R 318 REMARK 465 GLY R 319 REMARK 465 GLY R 320 REMARK 465 GLY R 321 REMARK 465 SER R 322 REMARK 465 GLY R 323 REMARK 465 GLY R 324 REMARK 465 SER R 325 REMARK 465 SER R 326 REMARK 465 SER R 327 REMARK 465 GLY R 328 REMARK 465 GLY R 329 REMARK 465 VAL R 330 REMARK 465 PHE R 331 REMARK 465 THR R 332 REMARK 465 LEU R 333 REMARK 465 GLU R 334 REMARK 465 ASP R 335 REMARK 465 PHE R 336 REMARK 465 VAL R 337 REMARK 465 GLY R 338 REMARK 465 ASP R 339 REMARK 465 TRP R 340 REMARK 465 GLU R 341 REMARK 465 GLN R 342 REMARK 465 THR R 343 REMARK 465 ALA R 344 REMARK 465 ALA R 345 REMARK 465 TYR R 346 REMARK 465 ASN R 347 REMARK 465 LEU R 348 REMARK 465 ASP R 349 REMARK 465 GLN R 350 REMARK 465 VAL R 351 REMARK 465 LEU R 352 REMARK 465 GLU R 353 REMARK 465 GLN R 354 REMARK 465 GLY R 355 REMARK 465 GLY R 356 REMARK 465 VAL R 357 REMARK 465 SER R 358 REMARK 465 SER R 359 REMARK 465 LEU R 360 REMARK 465 LEU R 361 REMARK 465 GLN R 362 REMARK 465 ASN R 363 REMARK 465 LEU R 364 REMARK 465 ALA R 365 REMARK 465 VAL R 366 REMARK 465 SER R 367 REMARK 465 VAL R 368 REMARK 465 THR R 369 REMARK 465 PRO R 370 REMARK 465 ILE R 371 REMARK 465 GLN R 372 REMARK 465 ARG R 373 REMARK 465 ILE R 374 REMARK 465 VAL R 375 REMARK 465 ARG R 376 REMARK 465 SER R 377 REMARK 465 GLY R 378 REMARK 465 GLU R 379 REMARK 465 ASN R 380 REMARK 465 ALA R 381 REMARK 465 LEU R 382 REMARK 465 LYS R 383 REMARK 465 ILE R 384 REMARK 465 ASP R 385 REMARK 465 ILE R 386 REMARK 465 HIS R 387 REMARK 465 VAL R 388 REMARK 465 ILE R 389 REMARK 465 ILE R 390 REMARK 465 PRO R 391 REMARK 465 TYR R 392 REMARK 465 GLU R 393 REMARK 465 GLY R 394 REMARK 465 LEU R 395 REMARK 465 SER R 396 REMARK 465 ALA R 397 REMARK 465 ASP R 398 REMARK 465 GLN R 399 REMARK 465 MET R 400 REMARK 465 ALA R 401 REMARK 465 GLN R 402 REMARK 465 ILE R 403 REMARK 465 GLU R 404 REMARK 465 GLU R 405 REMARK 465 VAL R 406 REMARK 465 PHE R 407 REMARK 465 LYS R 408 REMARK 465 VAL R 409 REMARK 465 VAL R 410 REMARK 465 TYR R 411 REMARK 465 PRO R 412 REMARK 465 VAL R 413 REMARK 465 ASP R 414 REMARK 465 ASP R 415 REMARK 465 HIS R 416 REMARK 465 HIS R 417 REMARK 465 PHE R 418 REMARK 465 LYS R 419 REMARK 465 VAL R 420 REMARK 465 ILE R 421 REMARK 465 LEU R 422 REMARK 465 PRO R 423 REMARK 465 TYR R 424 REMARK 465 GLY R 425 REMARK 465 THR R 426 REMARK 465 LEU R 427 REMARK 465 VAL R 428 REMARK 465 ILE R 429 REMARK 465 ASP R 430 REMARK 465 GLY R 431 REMARK 465 VAL R 432 REMARK 465 THR R 433 REMARK 465 PRO R 434 REMARK 465 ASN R 435 REMARK 465 MET R 436 REMARK 465 LEU R 437 REMARK 465 ASN R 438 REMARK 465 TYR R 439 REMARK 465 PHE R 440 REMARK 465 GLY R 441 REMARK 465 ARG R 442 REMARK 465 PRO R 443 REMARK 465 TYR R 444 REMARK 465 GLU R 445 REMARK 465 GLY R 446 REMARK 465 ILE R 447 REMARK 465 ALA R 448 REMARK 465 VAL R 449 REMARK 465 PHE R 450 REMARK 465 ASP R 451 REMARK 465 GLY R 452 REMARK 465 LYS R 453 REMARK 465 LYS R 454 REMARK 465 ILE R 455 REMARK 465 THR R 456 REMARK 465 VAL R 457 REMARK 465 THR R 458 REMARK 465 GLY R 459 REMARK 465 THR R 460 REMARK 465 LEU R 461 REMARK 465 TRP R 462 REMARK 465 ASN R 463 REMARK 465 GLY R 464 REMARK 465 ASN R 465 REMARK 465 LYS R 466 REMARK 465 ILE R 467 REMARK 465 ILE R 468 REMARK 465 ASP R 469 REMARK 465 GLU R 470 REMARK 465 ARG R 471 REMARK 465 LEU R 472 REMARK 465 ILE R 473 REMARK 465 THR R 474 REMARK 465 PRO R 475 REMARK 465 ASP R 476 REMARK 465 GLY R 477 REMARK 465 SER R 478 REMARK 465 MET R 479 REMARK 465 LEU R 480 REMARK 465 PHE R 481 REMARK 465 ARG R 482 REMARK 465 VAL R 483 REMARK 465 THR R 484 REMARK 465 ILE R 485 REMARK 465 ASN R 486 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 25 CG CD OE1 OE2 REMARK 470 GLU A 43 CG CD OE1 OE2 REMARK 470 LYS A 51 CG CD CE NZ REMARK 470 ASP A 193 CG OD1 OD2 REMARK 470 ARG A 205 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 209 CG CD CE NZ REMARK 470 ASP A 261 CG OD1 OD2 REMARK 470 LYS A 280 CG CD CE NZ REMARK 470 GLU A 289 CG CD OE1 OE2 REMARK 470 GLU A 298 CG CD OE1 OE2 REMARK 470 ASP A 315 CG OD1 OD2 REMARK 470 THR A 327 OG1 CG2 REMARK 470 SER B 2 OG 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 GLU B 12 CG CD OE1 OE2 REMARK 470 GLN B 13 CG CD OE1 NE2 REMARK 470 LYS B 15 CG CD CE NZ REMARK 470 ARG B 42 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 46 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 172 CG CD OE1 OE2 REMARK 470 SER C 8 OG REMARK 470 GLN C 11 CG CD OE1 NE2 REMARK 470 LYS C 14 CG CD CE NZ REMARK 470 GLU C 17 CG CD OE1 OE2 REMARK 470 GLU C 58 CG CD OE1 OE2 REMARK 470 ARG C 62 CG CD NE CZ NH1 NH2 REMARK 470 GLU D 42 CG CD OE1 OE2 REMARK 470 ASP D 62 CG OD1 OD2 REMARK 470 LYS D 76 CG CD CE NZ REMARK 470 GLU D 89 CG CD OE1 OE2 REMARK 470 GLN D 113 CG CD OE1 NE2 REMARK 470 SER D 121 OG REMARK 470 SER D 124 OG REMARK 470 THR D 132 OG1 CG2 REMARK 470 SER D 134 OG REMARK 470 GLU D 141 CG CD OE1 OE2 REMARK 470 GLU D 208 CG CD OE1 OE2 REMARK 470 GLU D 210 CG CD OE1 OE2 REMARK 470 GLU D 234 CG CD OE1 OE2 REMARK 470 TRP R 252 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP R 252 CZ3 CH2 REMARK 470 ARG R 256 CG CD NE CZ NH1 NH2 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 ARG A 205 53.23 -93.18 REMARK 500 ASN A 294 50.34 -91.64 REMARK 500 CYS B 25 36.23 -98.68 REMARK 500 PHE B 292 -0.86 77.85 REMARK 500 GLU C 47 52.05 -92.30 REMARK 500 PRO D 224 37.96 -96.64 REMARK 500 LYS R 37 47.95 -94.33 REMARK 500 LYS R 225 -160.13 -160.90 REMARK 500 ARG R 256 -73.15 -66.76 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 LYS R 217 ILE R 218 -148.99 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-43647 RELATED DB: EMDB REMARK 900 STRUCTURE OF GPCR COMPLEX-1 REMARK 900 RELATED ID: EMD-43656 RELATED DB: EMDB REMARK 900 LOCALLY REFINED MAP FOR GI-COUPLED TAS2R14 REMARK 900 RELATED ID: 8VY9 RELATED DB: PDB REMARK 900 STRUCTURE OF GGUST-COUPLED TAS2R14 REMARK 900 RELATED ID: EMD-43650 RELATED DB: EMDB REMARK 900 GLOBALLY REFINED MAP FOR GGUST-COUPLED TAS2R14 REMARK 900 RELATED ID: EMD-43657 RELATED DB: EMDB REMARK 900 LOCALLY REFINED MAP FOR GGUST-COUPLED TAS2R14 DBREF 8VY7 A 1 354 UNP P63096 GNAI1_HUMAN 1 354 DBREF 8VY7 B 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 8VY7 C 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 8VY7 D 1 255 PDB 8VY7 8VY7 1 255 DBREF 8VY7 R -150 0 PDB 8VY7 8VY7 -150 0 DBREF 8VY7 R 1 302 UNP Q9NYV8 T2R14_HUMAN 1 302 DBREF 8VY7 R 303 486 PDB 8VY7 8VY7 303 486 SEQADV 8VY7 ASN A 47 UNP P63096 SER 47 ENGINEERED MUTATION SEQADV 8VY7 ALA A 203 UNP P63096 GLY 203 ENGINEERED MUTATION SEQADV 8VY7 ALA A 245 UNP P63096 GLU 245 ENGINEERED MUTATION SEQADV 8VY7 SER A 326 UNP P63096 ALA 326 ENGINEERED MUTATION SEQADV 8VY7 HIS B -16 UNP P62873 EXPRESSION TAG SEQADV 8VY7 HIS B -15 UNP P62873 EXPRESSION TAG SEQADV 8VY7 HIS B -14 UNP P62873 EXPRESSION TAG SEQADV 8VY7 HIS B -13 UNP P62873 EXPRESSION TAG SEQADV 8VY7 HIS B -12 UNP P62873 EXPRESSION TAG SEQADV 8VY7 HIS B -11 UNP P62873 EXPRESSION TAG SEQADV 8VY7 LEU B -10 UNP P62873 EXPRESSION TAG SEQADV 8VY7 GLU B -9 UNP P62873 EXPRESSION TAG SEQADV 8VY7 VAL B -8 UNP P62873 EXPRESSION TAG SEQADV 8VY7 LEU B -7 UNP P62873 EXPRESSION TAG SEQADV 8VY7 PHE B -6 UNP P62873 EXPRESSION TAG SEQADV 8VY7 GLN B -5 UNP P62873 EXPRESSION TAG SEQADV 8VY7 GLY B -4 UNP P62873 EXPRESSION TAG SEQADV 8VY7 PRO B -3 UNP P62873 EXPRESSION TAG SEQADV 8VY7 GLY B -2 UNP P62873 EXPRESSION TAG SEQADV 8VY7 SER B -1 UNP P62873 EXPRESSION TAG SEQADV 8VY7 SER B 0 UNP P62873 EXPRESSION TAG SEQADV 8VY7 GLY B 1 UNP P62873 EXPRESSION TAG SEQADV 8VY7 GLY B 341 UNP P62873 EXPRESSION TAG SEQADV 8VY7 GLY B 342 UNP P62873 EXPRESSION TAG SEQADV 8VY7 SER B 343 UNP P62873 EXPRESSION TAG SEQADV 8VY7 GLY B 344 UNP P62873 EXPRESSION TAG SEQADV 8VY7 GLY B 345 UNP P62873 EXPRESSION TAG SEQADV 8VY7 GLY B 346 UNP P62873 EXPRESSION TAG SEQADV 8VY7 GLY B 347 UNP P62873 EXPRESSION TAG SEQADV 8VY7 SER B 348 UNP P62873 EXPRESSION TAG SEQADV 8VY7 GLY B 349 UNP P62873 EXPRESSION TAG SEQADV 8VY7 GLY B 350 UNP P62873 EXPRESSION TAG SEQADV 8VY7 SER B 351 UNP P62873 EXPRESSION TAG SEQADV 8VY7 SER B 352 UNP P62873 EXPRESSION TAG SEQADV 8VY7 SER B 353 UNP P62873 EXPRESSION TAG SEQADV 8VY7 GLY B 354 UNP P62873 EXPRESSION TAG SEQADV 8VY7 GLY B 355 UNP P62873 EXPRESSION TAG SEQADV 8VY7 GLY B 356 UNP P62873 EXPRESSION TAG SEQADV 8VY7 GLY B 357 UNP P62873 EXPRESSION TAG SEQADV 8VY7 SER B 358 UNP P62873 EXPRESSION TAG SEQADV 8VY7 GLY B 359 UNP P62873 EXPRESSION TAG SEQADV 8VY7 GLY B 360 UNP P62873 EXPRESSION TAG SEQADV 8VY7 GLY B 361 UNP P62873 EXPRESSION TAG SEQADV 8VY7 GLY B 362 UNP P62873 EXPRESSION TAG SEQADV 8VY7 SER B 363 UNP P62873 EXPRESSION TAG SEQADV 8VY7 GLY B 364 UNP P62873 EXPRESSION TAG SEQADV 8VY7 GLY B 365 UNP P62873 EXPRESSION TAG SEQADV 8VY7 SER B 366 UNP P62873 EXPRESSION TAG SEQADV 8VY7 SER B 367 UNP P62873 EXPRESSION TAG SEQADV 8VY7 SER B 368 UNP P62873 EXPRESSION TAG SEQADV 8VY7 GLY B 369 UNP P62873 EXPRESSION TAG SEQADV 8VY7 GLY B 370 UNP P62873 EXPRESSION TAG SEQADV 8VY7 VAL B 371 UNP P62873 EXPRESSION TAG SEQADV 8VY7 SER B 372 UNP P62873 EXPRESSION TAG SEQADV 8VY7 GLY B 373 UNP P62873 EXPRESSION TAG SEQADV 8VY7 TRP B 374 UNP P62873 EXPRESSION TAG SEQADV 8VY7 ARG B 375 UNP P62873 EXPRESSION TAG SEQADV 8VY7 LEU B 376 UNP P62873 EXPRESSION TAG SEQADV 8VY7 PHE B 377 UNP P62873 EXPRESSION TAG SEQADV 8VY7 LYS B 378 UNP P62873 EXPRESSION TAG SEQADV 8VY7 LYS B 379 UNP P62873 EXPRESSION TAG SEQADV 8VY7 ILE B 380 UNP P62873 EXPRESSION TAG SEQADV 8VY7 SER B 381 UNP P62873 EXPRESSION TAG SEQADV 8VY7 GLY B 382 UNP P62873 EXPRESSION TAG SEQADV 8VY7 GLY B 383 UNP P62873 EXPRESSION TAG SEQADV 8VY7 SER B 384 UNP P62873 EXPRESSION TAG SEQRES 1 A 354 MET GLY CYS THR LEU SER ALA GLU ASP LYS ALA ALA VAL SEQRES 2 A 354 GLU ARG SER LYS MET ILE ASP ARG ASN LEU ARG GLU ASP SEQRES 3 A 354 GLY GLU LYS ALA ALA ARG GLU VAL LYS LEU LEU LEU LEU SEQRES 4 A 354 GLY ALA GLY GLU SER GLY LYS ASN THR ILE VAL LYS GLN SEQRES 5 A 354 MET LYS ILE ILE HIS GLU ALA GLY TYR SER GLU GLU GLU SEQRES 6 A 354 CYS LYS GLN TYR LYS ALA VAL VAL TYR SER ASN THR ILE SEQRES 7 A 354 GLN SER ILE ILE ALA ILE ILE ARG ALA MET GLY ARG LEU SEQRES 8 A 354 LYS ILE ASP PHE GLY ASP SER ALA ARG ALA ASP ASP ALA SEQRES 9 A 354 ARG GLN LEU PHE VAL LEU ALA GLY ALA ALA GLU GLU GLY SEQRES 10 A 354 PHE MET THR ALA GLU LEU ALA GLY VAL ILE LYS ARG LEU SEQRES 11 A 354 TRP LYS ASP SER GLY VAL GLN ALA CYS PHE ASN ARG SER SEQRES 12 A 354 ARG GLU TYR GLN LEU ASN ASP SER ALA ALA TYR TYR LEU SEQRES 13 A 354 ASN ASP LEU ASP ARG ILE ALA GLN PRO ASN TYR ILE PRO SEQRES 14 A 354 THR GLN GLN ASP VAL LEU ARG THR ARG VAL LYS THR THR SEQRES 15 A 354 GLY ILE VAL GLU THR HIS PHE THR PHE LYS ASP LEU HIS SEQRES 16 A 354 PHE LYS MET PHE ASP VAL GLY ALA GLN ARG SER GLU ARG SEQRES 17 A 354 LYS LYS TRP ILE HIS CYS PHE GLU GLY VAL THR ALA ILE SEQRES 18 A 354 ILE PHE CYS VAL ALA LEU SER ASP TYR ASP LEU VAL LEU SEQRES 19 A 354 ALA GLU ASP GLU GLU MET ASN ARG MET HIS ALA SER MET SEQRES 20 A 354 LYS LEU PHE ASP SER ILE CYS ASN ASN LYS TRP PHE THR SEQRES 21 A 354 ASP THR SER ILE ILE LEU PHE LEU ASN LYS LYS ASP LEU SEQRES 22 A 354 PHE GLU GLU LYS ILE LYS LYS SER PRO LEU THR ILE CYS SEQRES 23 A 354 TYR PRO GLU TYR ALA GLY SER ASN THR TYR GLU GLU ALA SEQRES 24 A 354 ALA ALA TYR ILE GLN CYS GLN PHE GLU ASP LEU ASN LYS SEQRES 25 A 354 ARG LYS ASP THR LYS GLU ILE TYR THR HIS PHE THR CYS SEQRES 26 A 354 SER THR ASP THR LYS ASN VAL GLN PHE VAL PHE ASP ALA SEQRES 27 A 354 VAL THR ASP VAL ILE ILE LYS ASN ASN LEU LYS ASP CYS SEQRES 28 A 354 GLY LEU PHE SEQRES 1 B 401 HIS HIS HIS HIS HIS HIS LEU GLU VAL LEU PHE GLN GLY SEQRES 2 B 401 PRO GLY SER SER GLY SER GLU LEU ASP GLN LEU ARG GLN SEQRES 3 B 401 GLU ALA GLU GLN LEU LYS ASN GLN ILE ARG ASP ALA ARG SEQRES 4 B 401 LYS ALA CYS ALA ASP ALA THR LEU SER GLN ILE THR ASN SEQRES 5 B 401 ASN ILE ASP PRO VAL GLY ARG ILE GLN MET ARG THR ARG SEQRES 6 B 401 ARG THR LEU ARG GLY HIS LEU ALA LYS ILE TYR ALA MET SEQRES 7 B 401 HIS TRP GLY THR ASP SER ARG LEU LEU VAL SER ALA SER SEQRES 8 B 401 GLN ASP GLY LYS LEU ILE ILE TRP ASP SER TYR THR THR SEQRES 9 B 401 ASN LYS VAL HIS ALA ILE PRO LEU ARG SER SER TRP VAL SEQRES 10 B 401 MET THR CYS ALA TYR ALA PRO SER GLY ASN TYR VAL ALA SEQRES 11 B 401 CYS GLY GLY LEU ASP ASN ILE CYS SER ILE TYR ASN LEU SEQRES 12 B 401 LYS THR ARG GLU GLY ASN VAL ARG VAL SER ARG GLU LEU SEQRES 13 B 401 ALA GLY HIS THR GLY TYR LEU SER CYS CYS ARG PHE LEU SEQRES 14 B 401 ASP ASP ASN GLN ILE VAL THR SER SER GLY ASP THR THR SEQRES 15 B 401 CYS ALA LEU TRP ASP ILE GLU THR GLY GLN GLN THR THR SEQRES 16 B 401 THR PHE THR GLY HIS THR GLY ASP VAL MET SER LEU SER SEQRES 17 B 401 LEU ALA PRO ASP THR ARG LEU PHE VAL SER GLY ALA CYS SEQRES 18 B 401 ASP ALA SER ALA LYS LEU TRP ASP VAL ARG GLU GLY MET SEQRES 19 B 401 CYS ARG GLN THR PHE THR GLY HIS GLU SER ASP ILE ASN SEQRES 20 B 401 ALA ILE CYS PHE PHE PRO ASN GLY ASN ALA PHE ALA THR SEQRES 21 B 401 GLY SER ASP ASP ALA THR CYS ARG LEU PHE ASP LEU ARG SEQRES 22 B 401 ALA ASP GLN GLU LEU MET THR TYR SER HIS ASP ASN ILE SEQRES 23 B 401 ILE CYS GLY ILE THR SER VAL SER PHE SER LYS SER GLY SEQRES 24 B 401 ARG LEU LEU LEU ALA GLY TYR ASP ASP PHE ASN CYS ASN SEQRES 25 B 401 VAL TRP ASP ALA LEU LYS ALA ASP ARG ALA GLY VAL LEU SEQRES 26 B 401 ALA GLY HIS ASP ASN ARG VAL SER CYS LEU GLY VAL THR SEQRES 27 B 401 ASP ASP GLY MET ALA VAL ALA THR GLY SER TRP ASP SER SEQRES 28 B 401 PHE LEU LYS ILE TRP ASN GLY GLY SER GLY GLY GLY GLY SEQRES 29 B 401 SER GLY GLY SER SER SER GLY GLY GLY GLY SER GLY GLY SEQRES 30 B 401 GLY GLY SER GLY GLY SER SER SER GLY GLY VAL SER GLY SEQRES 31 B 401 TRP ARG LEU PHE LYS LYS ILE SER GLY GLY SER SEQRES 1 C 71 MET ALA SER ASN ASN THR ALA SER ILE ALA GLN ALA ARG SEQRES 2 C 71 LYS LEU VAL GLU GLN LEU LYS MET GLU ALA ASN ILE ASP SEQRES 3 C 71 ARG ILE LYS VAL SER LYS ALA ALA ALA ASP LEU MET ALA SEQRES 4 C 71 TYR CYS GLU ALA HIS ALA LYS GLU ASP PRO LEU LEU THR SEQRES 5 C 71 PRO VAL PRO ALA SER GLU ASN PRO PHE ARG GLU LYS LYS SEQRES 6 C 71 PHE PHE CYS ALA ILE LEU SEQRES 1 D 267 ASP VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 D 267 PRO GLY GLY SER ARG LYS LEU SER CYS SER ALA SER GLY SEQRES 3 D 267 PHE ALA PHE SER SER PHE GLY MET HIS TRP VAL ARG GLN SEQRES 4 D 267 ALA PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SEQRES 5 D 267 SER GLY SER GLY THR ILE TYR TYR ALA ASP THR VAL LYS SEQRES 6 D 267 GLY ARG PHE THR ILE SER ARG ASP ASP PRO LYS ASN THR SEQRES 7 D 267 LEU PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR SEQRES 8 D 267 ALA MET TYR TYR CYS VAL ARG SER ILE TYR TYR TYR GLY SEQRES 9 D 267 SER SER PRO PHE ASP PHE TRP GLY GLN GLY THR THR LEU SEQRES 10 D 267 THR VAL SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SEQRES 11 D 267 SER GLY GLY GLY GLY SER ASP ILE VAL MET THR GLN ALA SEQRES 12 D 267 THR SER SER VAL PRO VAL THR PRO GLY GLU SER VAL SER SEQRES 13 D 267 ILE SER CYS ARG SER SER LYS SER LEU LEU HIS SER ASN SEQRES 14 D 267 GLY ASN THR TYR LEU TYR TRP PHE LEU GLN ARG PRO GLY SEQRES 15 D 267 GLN SER PRO GLN LEU LEU ILE TYR ARG MET SER ASN LEU SEQRES 16 D 267 ALA SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SER SEQRES 17 D 267 GLY THR ALA PHE THR LEU THR ILE SER ARG LEU GLU ALA SEQRES 18 D 267 GLU ASP VAL GLY VAL TYR TYR CYS MET GLN HIS LEU GLU SEQRES 19 D 267 TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU LEU SEQRES 20 D 267 LYS ALA ALA ALA LEU GLU VAL LEU PHE GLN GLY PRO HIS SEQRES 21 D 267 HIS HIS HIS HIS HIS HIS HIS SEQRES 1 R 637 ASP TYR LYS ASP ASP ASP ASP ALA LYS LEU GLN THR MET SEQRES 2 R 637 HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS GLU ASN LEU SEQRES 3 R 637 TYR PHE GLN GLY GLY THR THR MET ALA ASP LEU GLU ASP SEQRES 4 R 637 ASN TRP GLU THR LEU ASN ASP ASN LEU LYS VAL ILE GLU SEQRES 5 R 637 LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP ALA LEU THR SEQRES 6 R 637 LYS MET ARG ALA ALA ALA LEU ASP ALA GLN LYS ALA THR SEQRES 7 R 637 PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SER PRO GLU SEQRES 8 R 637 MET LYS ASP PHE ARG HIS GLY PHE ASP ILE LEU VAL GLY SEQRES 9 R 637 GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN GLU GLY LYS SEQRES 10 R 637 VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN LEU LYS THR SEQRES 11 R 637 THR ARG ASN ALA TYR ILE GLN LYS TYR LEU GLY SER THR SEQRES 12 R 637 LEU GLU VAL LEU PHE GLN GLY PRO MET GLY GLY VAL ILE SEQRES 13 R 637 LYS SER ILE PHE THR PHE VAL LEU ILE VAL GLU PHE ILE SEQRES 14 R 637 ILE GLY ASN LEU GLY ASN SER PHE ILE ALA LEU VAL ASN SEQRES 15 R 637 CYS ILE ASP TRP VAL LYS GLY ARG LYS ILE SER SER VAL SEQRES 16 R 637 ASP ARG ILE LEU THR ALA LEU ALA ILE SER ARG ILE SER SEQRES 17 R 637 LEU VAL TRP LEU ILE PHE GLY SER TRP CYS VAL SER VAL SEQRES 18 R 637 PHE PHE PRO ALA LEU PHE ALA THR GLU LYS MET PHE ARG SEQRES 19 R 637 MET LEU THR ASN ILE TRP THR VAL ILE ASN HIS PHE SER SEQRES 20 R 637 VAL TRP LEU ALA THR GLY LEU GLY THR PHE TYR PHE LEU SEQRES 21 R 637 LYS ILE ALA ASN PHE SER ASN SER ILE PHE LEU TYR LEU SEQRES 22 R 637 LYS TRP ARG VAL LYS LYS VAL VAL LEU VAL LEU LEU LEU SEQRES 23 R 637 VAL THR SER VAL PHE LEU PHE LEU ASN ILE ALA LEU ILE SEQRES 24 R 637 ASN ILE HIS ILE ASN ALA SER ILE ASN GLY TYR ARG ARG SEQRES 25 R 637 ASN LYS THR CYS SER SER ASP SER SER ASN PHE THR ARG SEQRES 26 R 637 PHE SER SER LEU ILE VAL LEU THR SER THR VAL PHE ILE SEQRES 27 R 637 PHE ILE PRO PHE THR LEU SER LEU ALA MET PHE LEU LEU SEQRES 28 R 637 LEU ILE PHE SER MET TRP LYS HIS ARG LYS LYS MET GLN SEQRES 29 R 637 HIS THR VAL LYS ILE SER GLY ASP ALA SER THR LYS ALA SEQRES 30 R 637 HIS ARG GLY VAL LYS SER VAL ILE THR PHE PHE LEU LEU SEQRES 31 R 637 TYR ALA ILE PHE SER LEU SER PHE PHE ILE SER VAL TRP SEQRES 32 R 637 THR SER GLU ARG LEU GLU GLU ASN LEU ILE ILE LEU SER SEQRES 33 R 637 GLN VAL MET GLY MET ALA TYR PRO SER CYS HIS SER CYS SEQRES 34 R 637 VAL LEU ILE LEU GLY ASN LYS LYS LEU ARG GLN ALA SER SEQRES 35 R 637 LEU SER VAL LEU LEU TRP LEU ARG TYR MET PHE GLY SER SEQRES 36 R 637 ALA GLY SER ALA GLY SER GLY GLY SER GLY GLY GLY SER SEQRES 37 R 637 GLY GLY GLY GLY SER GLY GLY SER SER SER GLY GLY VAL SEQRES 38 R 637 PHE THR LEU GLU ASP PHE VAL GLY ASP TRP GLU GLN THR SEQRES 39 R 637 ALA ALA TYR ASN LEU ASP GLN VAL LEU GLU GLN GLY GLY SEQRES 40 R 637 VAL SER SER LEU LEU GLN ASN LEU ALA VAL SER VAL THR SEQRES 41 R 637 PRO ILE GLN ARG ILE VAL ARG SER GLY GLU ASN ALA LEU SEQRES 42 R 637 LYS ILE ASP ILE HIS VAL ILE ILE PRO TYR GLU GLY LEU SEQRES 43 R 637 SER ALA ASP GLN MET ALA GLN ILE GLU GLU VAL PHE LYS SEQRES 44 R 637 VAL VAL TYR PRO VAL ASP ASP HIS HIS PHE LYS VAL ILE SEQRES 45 R 637 LEU PRO TYR GLY THR LEU VAL ILE ASP GLY VAL THR PRO SEQRES 46 R 637 ASN MET LEU ASN TYR PHE GLY ARG PRO TYR GLU GLY ILE SEQRES 47 R 637 ALA VAL PHE ASP GLY LYS LYS ILE THR VAL THR GLY THR SEQRES 48 R 637 LEU TRP ASN GLY ASN LYS ILE ILE ASP GLU ARG LEU ILE SEQRES 49 R 637 THR PRO ASP GLY SER MET LEU PHE ARG VAL THR ILE ASN HET AEI R 501 23 HET CLR R 502 28 HETNAM CLR CHOLESTEROL FORMUL 6 AEI FORMUL 7 CLR C27 H46 O HELIX 1 AA1 SER A 6 ARG A 32 1 27 HELIX 2 AA2 LYS A 46 MET A 53 1 8 HELIX 3 AA3 GLU A 207 GLU A 216 5 10 HELIX 4 AA4 ASN A 241 ASN A 255 1 15 HELIX 5 AA5 LYS A 270 ILE A 278 1 9 HELIX 6 AA6 PRO A 282 CYS A 286 5 5 HELIX 7 AA7 THR A 295 ASP A 309 1 15 HELIX 8 AA8 LYS A 330 CYS A 351 1 22 HELIX 9 AA9 GLU B 3 CYS B 25 1 23 HELIX 10 AB1 THR B 29 THR B 34 1 6 HELIX 11 AB2 ASN B 35 ILE B 37 5 3 HELIX 12 AB3 ILE C 9 ASN C 24 1 16 HELIX 13 AB4 LYS C 29 HIS C 44 1 16 HELIX 14 AB5 SER D 53 GLY D 56 5 4 HELIX 15 AB6 ARG D 87 THR D 91 5 5 HELIX 16 AB7 GLY R 2 LYS R 37 1 36 HELIX 17 AB8 SER R 42 PHE R 72 1 31 HELIX 18 AB9 PHE R 72 ALA R 77 1 6 HELIX 19 AC1 THR R 78 ALA R 112 1 35 HELIX 20 AC2 ASN R 116 TRP R 124 1 9 HELIX 21 AC3 ARG R 125 THR R 137 1 13 HELIX 22 AC4 THR R 137 GLY R 158 1 22 HELIX 23 AC5 PHE R 175 GLN R 213 1 39 HELIX 24 AC6 ARG R 228 LEU R 257 1 30 HELIX 25 AC7 ASN R 260 MET R 270 1 11 HELIX 26 AC8 MET R 270 LEU R 282 1 13 HELIX 27 AC9 ASN R 284 PHE R 302 1 19 SHEET 1 AA1 6 VAL A 185 THR A 190 0 SHEET 2 AA1 6 HIS A 195 ASP A 200 -1 O MET A 198 N THR A 187 SHEET 3 AA1 6 VAL A 34 GLY A 40 1 N LEU A 38 O PHE A 199 SHEET 4 AA1 6 ALA A 220 ALA A 226 1 O ILE A 222 N LEU A 39 SHEET 5 AA1 6 SER A 263 ASN A 269 1 O ILE A 265 N ILE A 221 SHEET 6 AA1 6 ILE A 319 PHE A 323 1 O TYR A 320 N LEU A 266 SHEET 1 AA2 4 THR B 47 LEU B 51 0 SHEET 2 AA2 4 LEU B 336 TRP B 339 -1 O LEU B 336 N LEU B 51 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 CYS B 317 O GLY B 330 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 ALA B 60 SHEET 3 AA3 4 LYS B 78 ASP B 83 -1 O TRP B 82 N LEU B 70 SHEET 4 AA3 4 ASN B 88 PRO B 94 -1 O VAL B 90 N ILE B 81 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 TYR B 124 N VAL B 112 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 PHE B 151 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 176 PHE B 180 -1 O PHE B 180 N CYS B 166 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 ALA B 208 ASP B 212 -1 O TRP B 211 N PHE B 199 SHEET 4 AA6 4 CYS B 218 PHE B 222 -1 O ARG B 219 N LEU B 210 SHEET 1 AA7 4 ILE B 229 PHE B 234 0 SHEET 2 AA7 4 ALA B 240 SER B 245 -1 O ALA B 242 N CYS B 233 SHEET 3 AA7 4 CYS B 250 ASP B 254 -1 O PHE B 253 N PHE B 241 SHEET 4 AA7 4 GLN B 259 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 LEU B 308 N CYS B 294 SHEET 1 AA9 4 GLN D 3 SER D 7 0 SHEET 2 AA9 4 SER D 17 SER D 25 -1 O SER D 23 N VAL D 5 SHEET 3 AA9 4 THR D 78 THR D 84 -1 O LEU D 79 N CYS D 22 SHEET 4 AA9 4 PHE D 68 ASP D 73 -1 N SER D 71 O PHE D 80 SHEET 1 AB1 6 GLY D 10 VAL D 12 0 SHEET 2 AB1 6 THR D 115 VAL D 119 1 O THR D 118 N GLY D 10 SHEET 3 AB1 6 ALA D 92 SER D 99 -1 N ALA D 92 O LEU D 117 SHEET 4 AB1 6 GLY D 33 GLN D 39 -1 N VAL D 37 O TYR D 95 SHEET 5 AB1 6 LEU D 45 ILE D 51 -1 O VAL D 48 N TRP D 36 SHEET 6 AB1 6 ILE D 58 TYR D 60 -1 O TYR D 59 N TYR D 50 SHEET 1 AB2 4 GLY D 10 VAL D 12 0 SHEET 2 AB2 4 THR D 115 VAL D 119 1 O THR D 118 N GLY D 10 SHEET 3 AB2 4 ALA D 92 SER D 99 -1 N ALA D 92 O LEU D 117 SHEET 4 AB2 4 PHE D 110 TRP D 111 -1 O PHE D 110 N ARG D 98 SHEET 1 AB3 4 MET D 128 THR D 129 0 SHEET 2 AB3 4 VAL D 143 SER D 149 -1 O ARG D 148 N THR D 129 SHEET 3 AB3 4 ALA D 199 ILE D 204 -1 O PHE D 200 N CYS D 147 SHEET 4 AB3 4 PHE D 191 SER D 196 -1 N SER D 192 O THR D 203 SHEET 1 AB4 5 VAL D 135 PRO D 136 0 SHEET 2 AB4 5 THR D 231 GLU D 234 1 O LYS D 232 N VAL D 135 SHEET 3 AB4 5 VAL D 214 GLN D 219 -1 N TYR D 215 O THR D 231 SHEET 4 AB4 5 LEU D 162 GLN D 167 -1 N TYR D 163 O MET D 218 SHEET 5 AB4 5 GLN D 174 ILE D 177 -1 O GLN D 174 N LEU D 166 SSBOND 1 CYS D 147 CYS D 217 1555 1555 2.03 CISPEP 1 TYR D 223 PRO D 224 0 12.51 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