HEADER SIGNALING PROTEIN 07-FEB-24 8VY9 TITLE CRYOEM STRUCTURE OF GGUST-COUPLED TAS2R14 WITH CHOLESTEROL AND AN TITLE 2 INTRACELLULAR TASTANT COMPND MOL_ID: 1; COMPND 2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(T) SUBUNIT ALPHA-3; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 7 BETA-1; COMPND 8 CHAIN: B; COMPND 9 SYNONYM: TRANSDUCIN BETA CHAIN 1; 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: C; COMPND 15 SYNONYM: G GAMMA-I; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 4; COMPND 18 MOLECULE: SCFV16; COMPND 19 CHAIN: D; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 5; COMPND 22 MOLECULE: TASTE RECEPTOR TYPE 2 MEMBER 14,GPCR; COMPND 23 CHAIN: R; COMPND 24 SYNONYM: T2R14,TASTE RECEPTOR FAMILY B MEMBER 1,TRB1; COMPND 25 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; 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_COMMON: FALL ARMYWORM; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 16 MOL_ID: 3; SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 18 ORGANISM_COMMON: HUMAN; SOURCE 19 ORGANISM_TAXID: 9606; SOURCE 20 GENE: GNG2; SOURCE 21 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 22 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 23 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 24 MOL_ID: 4; SOURCE 25 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 26 ORGANISM_COMMON: MOUSE; SOURCE 27 ORGANISM_TAXID: 10090; SOURCE 28 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 29 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 30 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 31 EXPRESSION_SYSTEM_STRAIN: F; 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. 2.88 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) : 2.880 REMARK 3 NUMBER OF PARTICLES : 458284 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 8VY9 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_1000281451. 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 GGUST 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 SER A 3 REMARK 465 THR A 4 REMARK 465 LYS A 54A REMARK 465 ILE A 54B REMARK 465 ILE A 54C REMARK 465 HIS A 54D REMARK 465 LYS A 54E REMARK 465 ASN A 54F REMARK 465 GLY A 54G REMARK 465 TYR A 54H REMARK 465 SER A 54I REMARK 465 GLU A 54J REMARK 465 GLN A 54K REMARK 465 GLU A 54L REMARK 465 CYS A 54M REMARK 465 MET A 54N REMARK 465 GLU A 54O REMARK 465 PHE A 54P REMARK 465 LYS A 54Q REMARK 465 ALA A 54R REMARK 465 VAL A 54S REMARK 465 ILE A 54T REMARK 465 TYR A 54U REMARK 465 SER A 54V REMARK 465 ASN A 54W REMARK 465 THR A 54X REMARK 465 LEU A 54Y REMARK 465 GLN A 54Z REMARK 465 SER A 55A REMARK 465 ILE A 55B REMARK 465 LEU A 55C REMARK 465 ALA A 55D REMARK 465 ILE A 55E REMARK 465 VAL A 55F REMARK 465 LYS A 55G REMARK 465 ALA A 55H REMARK 465 MET A 55I REMARK 465 THR A 55J REMARK 465 THR A 55K REMARK 465 LEU A 55L REMARK 465 GLY A 55M REMARK 465 ILE A 55N REMARK 465 ASP A 55O REMARK 465 TYR A 55P REMARK 465 VAL A 55Q REMARK 465 ASN A 55R REMARK 465 PRO A 55S REMARK 465 ARG A 55T REMARK 465 SER A 55U REMARK 465 ALA A 55V REMARK 465 GLU A 55W REMARK 465 ASP A 55X REMARK 465 GLN A 55Y REMARK 465 ARG A 55Z REMARK 465 GLN A 56A REMARK 465 LEU A 56B REMARK 465 TYR A 56C REMARK 465 ALA A 56D REMARK 465 MET A 56E REMARK 465 ALA A 56F REMARK 465 ASN A 56G REMARK 465 THR A 56H REMARK 465 LEU A 56I REMARK 465 GLU A 56J REMARK 465 ASP A 56K REMARK 465 GLY A 56L REMARK 465 GLY A 56M REMARK 465 MET A 56N REMARK 465 THR A 56O REMARK 465 PRO A 56P REMARK 465 GLN A 56Q REMARK 465 LEU A 56R REMARK 465 ALA A 56S REMARK 465 GLU A 56T REMARK 465 VAL A 56U REMARK 465 ILE A 56V REMARK 465 LYS A 56W REMARK 465 ARG A 56X REMARK 465 LEU A 56Y REMARK 465 TRP A 56Z REMARK 465 ARG A 57A REMARK 465 ASP A 57B REMARK 465 PRO A 57C REMARK 465 GLY A 57D REMARK 465 ILE A 57E REMARK 465 GLN A 57F REMARK 465 ALA A 57G REMARK 465 CYS A 57H REMARK 465 PHE A 57I REMARK 465 GLU A 57J REMARK 465 ARG A 57K REMARK 465 ALA A 57L REMARK 465 SER A 57M REMARK 465 GLU A 57N REMARK 465 TYR A 57O REMARK 465 GLN A 57P REMARK 465 LEU A 57Q REMARK 465 ASN A 57R REMARK 465 ASP A 57S REMARK 465 SER A 57T REMARK 465 ALA A 57U REMARK 465 ALA A 57V REMARK 465 TYR A 57W REMARK 465 TYR A 57X REMARK 465 LEU A 57Y REMARK 465 ASN A 57Z REMARK 465 ASP A 58A REMARK 465 LEU A 58B REMARK 465 ASP A 58C REMARK 465 ARG A 58D REMARK 465 ILE A 58E REMARK 465 THR A 58F REMARK 465 ALA A 58G REMARK 465 SER A 58H REMARK 465 GLY A 58I REMARK 465 TYR A 58J REMARK 465 VAL A 58K REMARK 465 PRO A 58L REMARK 465 ASN A 58M REMARK 465 GLU A 58N REMARK 465 GLN A 58O REMARK 465 ASP A 58P REMARK 465 VAL A 58Q REMARK 465 LEU A 58R REMARK 465 HIS A 58S REMARK 465 SER A 58T REMARK 465 ARG A 58U REMARK 465 VAL A 58V REMARK 465 LYS A 58W REMARK 465 MET B -17 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 SER B 2 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 SER C 8 REMARK 465 ILE C 9 REMARK 465 ALA C 10 REMARK 465 GLN C 11 REMARK 465 ARG C 62 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 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 ASP R 304 REMARK 465 GLY R 305 REMARK 465 GLU R 306 REMARK 465 PRO R 307 REMARK 465 SER R 308 REMARK 465 GLY R 309 REMARK 465 HIS R 310 REMARK 465 LYS R 311 REMARK 465 GLU R 312 REMARK 465 PHE R 313 REMARK 465 ARG R 314 REMARK 465 GLU R 315 REMARK 465 SER R 316 REMARK 465 SER R 317 REMARK 465 GLY R 318 REMARK 465 SER R 319 REMARK 465 ALA R 320 REMARK 465 GLY R 321 REMARK 465 SER R 322 REMARK 465 ALA R 323 REMARK 465 GLY R 324 REMARK 465 SER R 325 REMARK 465 GLY R 326 REMARK 465 GLY R 327 REMARK 465 SER R 328 REMARK 465 GLY R 329 REMARK 465 GLY R 330 REMARK 465 GLY R 331 REMARK 465 SER R 332 REMARK 465 GLY R 333 REMARK 465 GLY R 334 REMARK 465 GLY R 335 REMARK 465 GLY R 336 REMARK 465 SER R 337 REMARK 465 GLY R 338 REMARK 465 GLY R 339 REMARK 465 SER R 340 REMARK 465 SER R 341 REMARK 465 SER R 342 REMARK 465 GLY R 343 REMARK 465 GLY R 344 REMARK 465 VAL R 345 REMARK 465 PHE R 346 REMARK 465 THR R 347 REMARK 465 LEU R 348 REMARK 465 GLU R 349 REMARK 465 ASP R 350 REMARK 465 PHE R 351 REMARK 465 VAL R 352 REMARK 465 GLY R 353 REMARK 465 ASP R 354 REMARK 465 TRP R 355 REMARK 465 GLU R 356 REMARK 465 GLN R 357 REMARK 465 THR R 358 REMARK 465 ALA R 359 REMARK 465 ALA R 360 REMARK 465 TYR R 361 REMARK 465 ASN R 362 REMARK 465 LEU R 363 REMARK 465 ASP R 364 REMARK 465 GLN R 365 REMARK 465 VAL R 366 REMARK 465 LEU R 367 REMARK 465 GLU R 368 REMARK 465 GLN R 369 REMARK 465 GLY R 370 REMARK 465 GLY R 371 REMARK 465 VAL R 372 REMARK 465 SER R 373 REMARK 465 SER R 374 REMARK 465 LEU R 375 REMARK 465 LEU R 376 REMARK 465 GLN R 377 REMARK 465 ASN R 378 REMARK 465 LEU R 379 REMARK 465 ALA R 380 REMARK 465 VAL R 381 REMARK 465 SER R 382 REMARK 465 VAL R 383 REMARK 465 THR R 384 REMARK 465 PRO R 385 REMARK 465 ILE R 386 REMARK 465 GLN R 387 REMARK 465 ARG R 388 REMARK 465 ILE R 389 REMARK 465 VAL R 390 REMARK 465 ARG R 391 REMARK 465 SER R 392 REMARK 465 GLY R 393 REMARK 465 GLU R 394 REMARK 465 ASN R 395 REMARK 465 ALA R 396 REMARK 465 LEU R 397 REMARK 465 LYS R 398 REMARK 465 ILE R 399 REMARK 465 ASP R 400 REMARK 465 ILE R 401 REMARK 465 HIS R 402 REMARK 465 VAL R 403 REMARK 465 ILE R 404 REMARK 465 ILE R 405 REMARK 465 PRO R 406 REMARK 465 TYR R 407 REMARK 465 GLU R 408 REMARK 465 GLY R 409 REMARK 465 LEU R 410 REMARK 465 SER R 411 REMARK 465 ALA R 412 REMARK 465 ASP R 413 REMARK 465 GLN R 414 REMARK 465 MET R 415 REMARK 465 ALA R 416 REMARK 465 GLN R 417 REMARK 465 ILE R 418 REMARK 465 GLU R 419 REMARK 465 GLU R 420 REMARK 465 VAL R 421 REMARK 465 PHE R 422 REMARK 465 LYS R 423 REMARK 465 VAL R 424 REMARK 465 VAL R 425 REMARK 465 TYR R 426 REMARK 465 PRO R 427 REMARK 465 VAL R 428 REMARK 465 ASP R 429 REMARK 465 ASP R 430 REMARK 465 HIS R 431 REMARK 465 HIS R 432 REMARK 465 PHE R 433 REMARK 465 LYS R 434 REMARK 465 VAL R 435 REMARK 465 ILE R 436 REMARK 465 LEU R 437 REMARK 465 PRO R 438 REMARK 465 TYR R 439 REMARK 465 GLY R 440 REMARK 465 THR R 441 REMARK 465 LEU R 442 REMARK 465 VAL R 443 REMARK 465 ILE R 444 REMARK 465 ASP R 445 REMARK 465 GLY R 446 REMARK 465 VAL R 447 REMARK 465 THR R 448 REMARK 465 PRO R 449 REMARK 465 ASN R 450 REMARK 465 MET R 451 REMARK 465 LEU R 452 REMARK 465 ASN R 453 REMARK 465 TYR R 454 REMARK 465 PHE R 455 REMARK 465 GLY R 456 REMARK 465 ARG R 457 REMARK 465 PRO R 458 REMARK 465 TYR R 459 REMARK 465 GLU R 460 REMARK 465 GLY R 461 REMARK 465 ILE R 462 REMARK 465 ALA R 463 REMARK 465 VAL R 464 REMARK 465 PHE R 465 REMARK 465 ASP R 466 REMARK 465 GLY R 467 REMARK 465 LYS R 468 REMARK 465 LYS R 469 REMARK 465 ILE R 470 REMARK 465 THR R 471 REMARK 465 VAL R 472 REMARK 465 THR R 473 REMARK 465 GLY R 474 REMARK 465 THR R 475 REMARK 465 LEU R 476 REMARK 465 TRP R 477 REMARK 465 ASN R 478 REMARK 465 GLY R 479 REMARK 465 ASN R 480 REMARK 465 LYS R 481 REMARK 465 ILE R 482 REMARK 465 ILE R 483 REMARK 465 ASP R 484 REMARK 465 GLU R 485 REMARK 465 ARG R 486 REMARK 465 LEU R 487 REMARK 465 ILE R 488 REMARK 465 THR R 489 REMARK 465 PRO R 490 REMARK 465 ASP R 491 REMARK 465 GLY R 492 REMARK 465 SER R 493 REMARK 465 MET R 494 REMARK 465 LEU R 495 REMARK 465 PHE R 496 REMARK 465 ARG R 497 REMARK 465 VAL R 498 REMARK 465 THR R 499 REMARK 465 ILE R 500 REMARK 465 ASN R 501 REMARK 465 SER R 502 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 ARG A 29 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 30 CG OD1 OD2 REMARK 470 ASP A 193 CG OD1 OD2 REMARK 470 ALA A 203 CB REMARK 470 LYS A 209 CG CD CE NZ REMARK 470 ASP A 272 CG OD1 OD2 REMARK 470 ILE A 273 CG1 CG2 CD1 REMARK 470 GLN A 275 CG CD OE1 NE2 REMARK 470 GLU A 276 CG CD OE1 OE2 REMARK 470 VAL A 278 CG1 CG2 REMARK 470 THR A 279 OG1 CG2 REMARK 470 LYS A 280 CG CD CE NZ REMARK 470 HIS A 282 CG ND1 CD2 CE1 NE2 REMARK 470 LEU A 283 CG CD1 CD2 REMARK 470 THR A 291 OG1 CG2 REMARK 470 ASN A 294 CG OD1 ND2 REMARK 470 THR A 295 OG1 CG2 REMARK 470 ASP A 298 CG OD1 OD2 REMARK 470 GLU A 315 CG CD OE1 OE2 REMARK 470 ASP A 316 CG OD1 OD2 REMARK 470 ASP A 328 CG OD1 OD2 REMARK 470 LYS A 349 CG CD CE NZ REMARK 470 GLU B 3 CG CD OE1 OE2 REMARK 470 LEU B 4 CG CD1 CD2 REMARK 470 ASP B 5 CG OD1 OD2 REMARK 470 GLN B 6 CG CD OE1 NE2 REMARK 470 LEU B 7 CG CD1 CD2 REMARK 470 ARG B 8 CG CD NE CZ NH1 NH2 REMARK 470 GLN B 9 CG CD OE1 NE2 REMARK 470 GLU B 10 CG CD OE1 OE2 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 ASN B 16 CG OD1 ND2 REMARK 470 ARG B 19 CG CD NE CZ NH1 NH2 REMARK 470 ASP B 20 CG OD1 OD2 REMARK 470 ARG B 22 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 23 CG CD CE NZ REMARK 470 ASP B 27 CG OD1 OD2 REMARK 470 SER B 31 OG REMARK 470 THR B 34 OG1 CG2 REMARK 470 ARG B 42 CG CD NE CZ NH1 NH2 REMARK 470 GLN B 44 CG CD OE1 NE2 REMARK 470 ARG B 46 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 129 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 134 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 197 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 214 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 226 CG CD OE1 OE2 REMARK 470 ASP B 254 CG OD1 OD2 REMARK 470 HIS B 266 CG ND1 CD2 CE1 NE2 REMARK 470 ASP B 267 CG OD1 OD2 REMARK 470 ASN B 268 CG OD1 ND2 REMARK 470 ILE B 270 CG1 CG2 CD1 REMARK 470 LYS B 301 CG CD CE NZ REMARK 470 ASP B 303 CG OD1 OD2 REMARK 470 ASP B 322 CG OD1 OD2 REMARK 470 ARG C 13 CG CD NE CZ NH1 NH2 REMARK 470 LYS C 14 CG CD CE NZ REMARK 470 LEU C 15 CG CD1 CD2 REMARK 470 GLU C 17 CG CD OE1 OE2 REMARK 470 GLN C 18 CG CD OE1 NE2 REMARK 470 LYS C 20 CG CD CE NZ REMARK 470 GLU C 22 CG CD OE1 OE2 REMARK 470 ASN C 24 CG OD1 ND2 REMARK 470 ILE C 25 CG1 CG2 CD1 REMARK 470 ASP C 26 CG OD1 OD2 REMARK 470 LYS C 32 CG CD CE NZ REMARK 470 ASP C 36 CG OD1 OD2 REMARK 470 GLU C 42 CG CD OE1 OE2 REMARK 470 LYS C 46 CG CD CE NZ REMARK 470 GLU C 47 CG CD OE1 OE2 REMARK 470 HIS R 227 CG ND1 CD2 CE1 NE2 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 GLU A 43 61.84 -101.31 REMARK 500 PHE A 215 35.52 -99.86 REMARK 500 ALA A 229 43.53 -104.63 REMARK 500 ASP A 231 -62.72 -108.73 REMARK 500 MET A 232 64.02 38.55 REMARK 500 ASP A 237 -0.06 69.28 REMARK 500 PRO A 288 44.26 -85.20 REMARK 500 GLU A 289 12.87 -142.04 REMARK 500 ASN A 294 31.93 -94.46 REMARK 500 LEU A 312 46.29 -95.01 REMARK 500 LYS A 313 45.47 -143.72 REMARK 500 ASP B 163 30.97 -98.05 REMARK 500 ASP B 291 30.89 -90.87 REMARK 500 ALA C 56 18.31 56.67 REMARK 500 TYR D 178 -62.14 -94.57 REMARK 500 SER D 196 114.72 -160.65 REMARK 500 PRO D 224 39.32 -95.50 REMARK 500 PHE R 72 73.62 42.70 REMARK 500 ALA R 222 -103.90 51.72 REMARK 500 ARG R 256 -62.54 -94.81 REMARK 500 LEU R 257 -164.54 -162.34 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-43650 RELATED DB: EMDB REMARK 900 STRUCTURE OF GPCR COMPLEX-2 REMARK 900 RELATED ID: EMD-43657 RELATED DB: EMDB REMARK 900 LOCALLY REFINED MAP FOR GGUST-COUPLED TAS2R14 REMARK 900 RELATED ID: 8VY7 RELATED DB: PDB REMARK 900 STRUCTURE OF GI-COUPLED TAS2R14 REMARK 900 RELATED ID: EMD-43647 RELATED DB: EMDB REMARK 900 GLOBALLY REFINED MAP FOR GI-COUPLED TAS2R14 REMARK 900 RELATED ID: EMD-43656 RELATED DB: EMDB REMARK 900 LOCALLY REFINED MAP FOR GI-COUPLED TAS2R14 DBREF 8VY9 A 1 354 PDB 8VY9 8VY9 1 354 DBREF 8VY9 B 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 8VY9 C 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 8VY9 D 1 255 PDB 8VY9 8VY9 1 255 DBREF 8VY9 R -150 0 PDB 8VY9 8VY9 -150 0 DBREF 8VY9 R 1 317 UNP Q9NYV8 T2R14_HUMAN 1 317 DBREF 8VY9 R 318 502 PDB 8VY9 8VY9 318 502 SEQADV 8VY9 MET B -17 UNP P62873 INITIATING METHIONINE SEQADV 8VY9 HIS B -16 UNP P62873 EXPRESSION TAG SEQADV 8VY9 HIS B -15 UNP P62873 EXPRESSION TAG SEQADV 8VY9 HIS B -14 UNP P62873 EXPRESSION TAG SEQADV 8VY9 HIS B -13 UNP P62873 EXPRESSION TAG SEQADV 8VY9 HIS B -12 UNP P62873 EXPRESSION TAG SEQADV 8VY9 HIS B -11 UNP P62873 EXPRESSION TAG SEQADV 8VY9 LEU B -10 UNP P62873 EXPRESSION TAG SEQADV 8VY9 GLU B -9 UNP P62873 EXPRESSION TAG SEQADV 8VY9 VAL B -8 UNP P62873 EXPRESSION TAG SEQADV 8VY9 LEU B -7 UNP P62873 EXPRESSION TAG SEQADV 8VY9 PHE B -6 UNP P62873 EXPRESSION TAG SEQADV 8VY9 GLN B -5 UNP P62873 EXPRESSION TAG SEQADV 8VY9 GLY B -4 UNP P62873 EXPRESSION TAG SEQADV 8VY9 PRO B -3 UNP P62873 EXPRESSION TAG SEQADV 8VY9 GLY B -2 UNP P62873 EXPRESSION TAG SEQADV 8VY9 SER B -1 UNP P62873 EXPRESSION TAG SEQADV 8VY9 SER B 0 UNP P62873 EXPRESSION TAG SEQADV 8VY9 GLY B 1 UNP P62873 EXPRESSION TAG SEQADV 8VY9 GLY B 341 UNP P62873 EXPRESSION TAG SEQADV 8VY9 GLY B 342 UNP P62873 EXPRESSION TAG SEQADV 8VY9 SER B 343 UNP P62873 EXPRESSION TAG SEQADV 8VY9 GLY B 344 UNP P62873 EXPRESSION TAG SEQADV 8VY9 GLY B 345 UNP P62873 EXPRESSION TAG SEQADV 8VY9 GLY B 346 UNP P62873 EXPRESSION TAG SEQADV 8VY9 GLY B 347 UNP P62873 EXPRESSION TAG SEQADV 8VY9 SER B 348 UNP P62873 EXPRESSION TAG SEQADV 8VY9 GLY B 349 UNP P62873 EXPRESSION TAG SEQADV 8VY9 GLY B 350 UNP P62873 EXPRESSION TAG SEQADV 8VY9 SER B 351 UNP P62873 EXPRESSION TAG SEQADV 8VY9 SER B 352 UNP P62873 EXPRESSION TAG SEQADV 8VY9 SER B 353 UNP P62873 EXPRESSION TAG SEQADV 8VY9 GLY B 354 UNP P62873 EXPRESSION TAG SEQADV 8VY9 GLY B 355 UNP P62873 EXPRESSION TAG SEQADV 8VY9 GLY B 356 UNP P62873 EXPRESSION TAG SEQADV 8VY9 GLY B 357 UNP P62873 EXPRESSION TAG SEQADV 8VY9 SER B 358 UNP P62873 EXPRESSION TAG SEQADV 8VY9 GLY B 359 UNP P62873 EXPRESSION TAG SEQADV 8VY9 GLY B 360 UNP P62873 EXPRESSION TAG SEQADV 8VY9 GLY B 361 UNP P62873 EXPRESSION TAG SEQADV 8VY9 GLY B 362 UNP P62873 EXPRESSION TAG SEQADV 8VY9 SER B 363 UNP P62873 EXPRESSION TAG SEQADV 8VY9 GLY B 364 UNP P62873 EXPRESSION TAG SEQADV 8VY9 GLY B 365 UNP P62873 EXPRESSION TAG SEQADV 8VY9 SER B 366 UNP P62873 EXPRESSION TAG SEQADV 8VY9 SER B 367 UNP P62873 EXPRESSION TAG SEQADV 8VY9 SER B 368 UNP P62873 EXPRESSION TAG SEQADV 8VY9 GLY B 369 UNP P62873 EXPRESSION TAG SEQADV 8VY9 GLY B 370 UNP P62873 EXPRESSION TAG SEQADV 8VY9 VAL B 371 UNP P62873 EXPRESSION TAG SEQADV 8VY9 SER B 372 UNP P62873 EXPRESSION TAG SEQADV 8VY9 GLY B 373 UNP P62873 EXPRESSION TAG SEQADV 8VY9 TRP B 374 UNP P62873 EXPRESSION TAG SEQADV 8VY9 ARG B 375 UNP P62873 EXPRESSION TAG SEQADV 8VY9 LEU B 376 UNP P62873 EXPRESSION TAG SEQADV 8VY9 PHE B 377 UNP P62873 EXPRESSION TAG SEQADV 8VY9 LYS B 378 UNP P62873 EXPRESSION TAG SEQADV 8VY9 LYS B 379 UNP P62873 EXPRESSION TAG SEQADV 8VY9 ILE B 380 UNP P62873 EXPRESSION TAG SEQADV 8VY9 SER B 381 UNP P62873 EXPRESSION TAG SEQADV 8VY9 GLY B 382 UNP P62873 EXPRESSION TAG SEQADV 8VY9 GLY B 383 UNP P62873 EXPRESSION TAG SEQADV 8VY9 SER B 384 UNP P62873 EXPRESSION TAG SEQRES 1 A 355 MET GLY SER THR VAL SER ALA GLU ASP LYS ALA ALA ALA SEQRES 2 A 355 GLU ARG SER LYS MET ILE ASP LYS ASN LEU ARG GLU ASP SEQRES 3 A 355 ALA GLU ARG ASP ALA ARG THR VAL LYS LEU LEU LEU LEU SEQRES 4 A 355 GLY ALA GLY GLU SER GLY LYS ALA THR ILE VAL LYS GLN SEQRES 5 A 355 GLN MET LYS ILE ILE HIS LYS ASN GLY TYR SER GLU GLN SEQRES 6 A 355 GLU CYS MET GLU PHE LYS ALA VAL ILE TYR SER ASN THR SEQRES 7 A 355 LEU GLN SER ILE LEU ALA ILE VAL LYS ALA MET THR THR SEQRES 8 A 355 LEU GLY ILE ASP TYR VAL ASN PRO ARG SER ALA GLU ASP SEQRES 9 A 355 GLN ARG GLN LEU TYR ALA MET ALA ASN THR LEU GLU ASP SEQRES 10 A 355 GLY GLY MET THR PRO GLN LEU ALA GLU VAL ILE LYS ARG SEQRES 11 A 355 LEU TRP ARG ASP PRO GLY ILE GLN ALA CYS PHE GLU ARG SEQRES 12 A 355 ALA SER GLU TYR GLN LEU ASN ASP SER ALA ALA TYR TYR SEQRES 13 A 355 LEU ASN ASP LEU ASP ARG ILE THR ALA SER GLY TYR VAL SEQRES 14 A 355 PRO ASN GLU GLN ASP VAL LEU HIS SER ARG VAL LYS THR SEQRES 15 A 355 THR GLY ILE ILE GLU THR GLN PHE SER PHE LYS ASP LEU SEQRES 16 A 355 HIS PHE ARG MET PHE ASP VAL GLY ALA GLN ARG SER GLU SEQRES 17 A 355 ARG LYS LYS TRP ILE HIS CYS PHE GLU GLY VAL THR CYS SEQRES 18 A 355 ILE ILE PHE CYS ALA ALA LEU SER ALA TYR ASP MET VAL SEQRES 19 A 355 LEU VAL GLU ASP GLU GLU VAL ASN ARG MET HIS ALA SER SEQRES 20 A 355 LEU LYS LEU PHE ASP SER ILE CYS ASN HIS LYS TYR PHE SEQRES 21 A 355 SER ASP THR SER ILE VAL LEU PHE LEU ASN LYS LYS ASP SEQRES 22 A 355 ILE PHE GLN GLU LYS VAL THR LYS VAL HIS LEU SER ILE SEQRES 23 A 355 CYS PHE PRO GLU TYR THR GLY PRO ASN THR PHE GLU ASP SEQRES 24 A 355 ALA GLY ASN TYR ILE LYS ASN GLN PHE LEU ASP LEU ASN SEQRES 25 A 355 LEU LYS LYS GLU ASP LYS GLU ILE TYR SER HIS MET THR SEQRES 26 A 355 CYS SER THR ASP THR GLN ASN VAL LYS PHE VAL PHE ASP SEQRES 27 A 355 ALA VAL THR ASP ILE ILE ILE LYS GLU ASN LEU LYS ASP SEQRES 28 A 355 CYS GLY LEU PHE SEQRES 1 B 402 MET HIS HIS HIS HIS HIS HIS LEU GLU VAL LEU PHE GLN SEQRES 2 B 402 GLY PRO GLY SER SER GLY SER GLU LEU ASP GLN LEU ARG SEQRES 3 B 402 GLN GLU ALA GLU GLN LEU LYS ASN GLN ILE ARG ASP ALA SEQRES 4 B 402 ARG LYS ALA CYS ALA ASP ALA THR LEU SER GLN ILE THR SEQRES 5 B 402 ASN ASN ILE ASP PRO VAL GLY ARG ILE GLN MET ARG THR SEQRES 6 B 402 ARG ARG THR LEU ARG GLY HIS LEU ALA LYS ILE TYR ALA SEQRES 7 B 402 MET HIS TRP GLY THR ASP SER ARG LEU LEU VAL SER ALA SEQRES 8 B 402 SER GLN ASP GLY LYS LEU ILE ILE TRP ASP SER TYR THR SEQRES 9 B 402 THR ASN LYS VAL HIS ALA ILE PRO LEU ARG SER SER TRP SEQRES 10 B 402 VAL MET THR CYS ALA TYR ALA PRO SER GLY ASN TYR VAL SEQRES 11 B 402 ALA CYS GLY GLY LEU ASP ASN ILE CYS SER ILE TYR ASN SEQRES 12 B 402 LEU LYS THR ARG GLU GLY ASN VAL ARG VAL SER ARG GLU SEQRES 13 B 402 LEU ALA GLY HIS THR GLY TYR LEU SER CYS CYS ARG PHE SEQRES 14 B 402 LEU ASP ASP ASN GLN ILE VAL THR SER SER GLY ASP THR SEQRES 15 B 402 THR CYS ALA LEU TRP ASP ILE GLU THR GLY GLN GLN THR SEQRES 16 B 402 THR THR PHE THR GLY HIS THR GLY ASP VAL MET SER LEU SEQRES 17 B 402 SER LEU ALA PRO ASP THR ARG LEU PHE VAL SER GLY ALA SEQRES 18 B 402 CYS ASP ALA SER ALA LYS LEU TRP ASP VAL ARG GLU GLY SEQRES 19 B 402 MET CYS ARG GLN THR PHE THR GLY HIS GLU SER ASP ILE SEQRES 20 B 402 ASN ALA ILE CYS PHE PHE PRO ASN GLY ASN ALA PHE ALA SEQRES 21 B 402 THR GLY SER ASP ASP ALA THR CYS ARG LEU PHE ASP LEU SEQRES 22 B 402 ARG ALA ASP GLN GLU LEU MET THR TYR SER HIS ASP ASN SEQRES 23 B 402 ILE ILE CYS GLY ILE THR SER VAL SER PHE SER LYS SER SEQRES 24 B 402 GLY ARG LEU LEU LEU ALA GLY TYR ASP ASP PHE ASN CYS SEQRES 25 B 402 ASN VAL TRP ASP ALA LEU LYS ALA ASP ARG ALA GLY VAL SEQRES 26 B 402 LEU ALA GLY HIS ASP ASN ARG VAL SER CYS LEU GLY VAL SEQRES 27 B 402 THR ASP ASP GLY MET ALA VAL ALA THR GLY SER TRP ASP SEQRES 28 B 402 SER PHE LEU LYS ILE TRP ASN GLY GLY SER GLY GLY GLY SEQRES 29 B 402 GLY SER GLY GLY SER SER SER GLY GLY GLY GLY SER GLY SEQRES 30 B 402 GLY GLY GLY SER GLY GLY SER SER SER GLY GLY VAL SER SEQRES 31 B 402 GLY 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 653 ASP TYR LYS ASP ASP ASP ASP ALA LYS LEU GLN THR MET SEQRES 2 R 653 HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS GLU ASN LEU SEQRES 3 R 653 TYR PHE GLN GLY GLY THR THR MET ALA ASP LEU GLU ASP SEQRES 4 R 653 ASN TRP GLU THR LEU ASN ASP ASN LEU LYS VAL ILE GLU SEQRES 5 R 653 LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP ALA LEU THR SEQRES 6 R 653 LYS MET ARG ALA ALA ALA LEU ASP ALA GLN LYS ALA THR SEQRES 7 R 653 PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SER PRO GLU SEQRES 8 R 653 MET LYS ASP PHE ARG HIS GLY PHE ASP ILE LEU VAL GLY SEQRES 9 R 653 GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN GLU GLY LYS SEQRES 10 R 653 VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN LEU LYS THR SEQRES 11 R 653 THR ARG ASN ALA TYR ILE GLN LYS TYR LEU GLY SER THR SEQRES 12 R 653 LEU GLU VAL LEU PHE GLN GLY PRO MET GLY GLY VAL ILE SEQRES 13 R 653 LYS SER ILE PHE THR PHE VAL LEU ILE VAL GLU PHE ILE SEQRES 14 R 653 ILE GLY ASN LEU GLY ASN SER PHE ILE ALA LEU VAL ASN SEQRES 15 R 653 CYS ILE ASP TRP VAL LYS GLY ARG LYS ILE SER SER VAL SEQRES 16 R 653 ASP ARG ILE LEU THR ALA LEU ALA ILE SER ARG ILE SER SEQRES 17 R 653 LEU VAL TRP LEU ILE PHE GLY SER TRP CYS VAL SER VAL SEQRES 18 R 653 PHE PHE PRO ALA LEU PHE ALA THR GLU LYS MET PHE ARG SEQRES 19 R 653 MET LEU THR ASN ILE TRP THR VAL ILE ASN HIS PHE SER SEQRES 20 R 653 VAL TRP LEU ALA THR GLY LEU GLY THR PHE TYR PHE LEU SEQRES 21 R 653 LYS ILE ALA ASN PHE SER ASN SER ILE PHE LEU TYR LEU SEQRES 22 R 653 LYS TRP ARG VAL LYS LYS VAL VAL LEU VAL LEU LEU LEU SEQRES 23 R 653 VAL THR SER VAL PHE LEU PHE LEU ASN ILE ALA LEU ILE SEQRES 24 R 653 ASN ILE HIS ILE ASN ALA SER ILE ASN GLY TYR ARG ARG SEQRES 25 R 653 ASN LYS THR CYS SER SER ASP SER SER ASN PHE THR ARG SEQRES 26 R 653 PHE SER SER LEU ILE VAL LEU THR SER THR VAL PHE ILE SEQRES 27 R 653 PHE ILE PRO PHE THR LEU SER LEU ALA MET PHE LEU LEU SEQRES 28 R 653 LEU ILE PHE SER MET TRP LYS HIS ARG LYS LYS MET GLN SEQRES 29 R 653 HIS THR VAL LYS ILE SER GLY ASP ALA SER THR LYS ALA SEQRES 30 R 653 HIS ARG GLY VAL LYS SER VAL ILE THR PHE PHE LEU LEU SEQRES 31 R 653 TYR ALA ILE PHE SER LEU SER PHE PHE ILE SER VAL TRP SEQRES 32 R 653 THR SER GLU ARG LEU GLU GLU ASN LEU ILE ILE LEU SER SEQRES 33 R 653 GLN VAL MET GLY MET ALA TYR PRO SER CYS HIS SER CYS SEQRES 34 R 653 VAL LEU ILE LEU GLY ASN LYS LYS LEU ARG GLN ALA SER SEQRES 35 R 653 LEU SER VAL LEU LEU TRP LEU ARG TYR MET PHE LYS ASP SEQRES 36 R 653 GLY GLU PRO SER GLY HIS LYS GLU PHE ARG GLU SER SER SEQRES 37 R 653 GLY SER ALA GLY SER ALA GLY SER GLY GLY SER GLY GLY SEQRES 38 R 653 GLY SER GLY GLY GLY GLY SER GLY GLY SER SER SER GLY SEQRES 39 R 653 GLY VAL PHE THR LEU GLU ASP PHE VAL GLY ASP TRP GLU SEQRES 40 R 653 GLN THR ALA ALA TYR ASN LEU ASP GLN VAL LEU GLU GLN SEQRES 41 R 653 GLY GLY VAL SER SER LEU LEU GLN ASN LEU ALA VAL SER SEQRES 42 R 653 VAL THR PRO ILE GLN ARG ILE VAL ARG SER GLY GLU ASN SEQRES 43 R 653 ALA LEU LYS ILE ASP ILE HIS VAL ILE ILE PRO TYR GLU SEQRES 44 R 653 GLY LEU SER ALA ASP GLN MET ALA GLN ILE GLU GLU VAL SEQRES 45 R 653 PHE LYS VAL VAL TYR PRO VAL ASP ASP HIS HIS PHE LYS SEQRES 46 R 653 VAL ILE LEU PRO TYR GLY THR LEU VAL ILE ASP GLY VAL SEQRES 47 R 653 THR PRO ASN MET LEU ASN TYR PHE GLY ARG PRO TYR GLU SEQRES 48 R 653 GLY ILE ALA VAL PHE ASP GLY LYS LYS ILE THR VAL THR SEQRES 49 R 653 GLY THR LEU TRP ASN GLY ASN LYS ILE ILE ASP GLU ARG SEQRES 50 R 653 LEU ILE THR PRO ASP GLY SER MET LEU PHE ARG VAL THR SEQRES 51 R 653 ILE ASN SER HET AEI R 601 23 HET CLR R 602 28 HETNAM CLR CHOLESTEROL FORMUL 6 AEI FORMUL 7 CLR C27 H46 O HELIX 1 AA1 SER A 6 ALA A 31 1 26 HELIX 2 AA2 GLY A 45 MET A 54 1 10 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 THR A 279 1 10 HELIX 6 AA6 HIS A 282 CYS A 286 5 5 HELIX 7 AA7 THR A 295 ASP A 309 1 15 HELIX 8 AA8 GLN A 330 CYS A 351 1 22 HELIX 9 AA9 LEU B 4 ALA B 26 1 23 HELIX 10 AB1 THR B 29 THR B 34 1 6 HELIX 11 AB2 ARG C 13 ASN C 24 1 12 HELIX 12 AB3 LYS C 29 HIS C 44 1 16 HELIX 13 AB4 ALA D 28 PHE D 32 5 5 HELIX 14 AB5 GLU D 208 VAL D 212 5 5 HELIX 15 AB6 GLY R 2 LYS R 37 1 36 HELIX 16 AB7 SER R 42 PHE R 71 1 30 HELIX 17 AB8 ALA R 74 ALA R 77 5 4 HELIX 18 AB9 THR R 78 ALA R 112 1 35 HELIX 19 AC1 ASN R 116 ARG R 125 1 10 HELIX 20 AC2 ARG R 125 THR R 137 1 13 HELIX 21 AC3 THR R 137 ARG R 160 1 24 HELIX 22 AC4 PHE R 175 GLN R 213 1 39 HELIX 23 AC5 SER R 223 THR R 253 1 31 HELIX 24 AC6 LEU R 261 LEU R 282 1 22 HELIX 25 AC7 ASN R 284 PHE R 302 1 19 SHEET 1 AA1 6 ILE A 185 SER A 190 0 SHEET 2 AA1 6 HIS A 195 ASP A 200 -1 O PHE A 196 N PHE A 189 SHEET 3 AA1 6 THR A 33 GLY A 40 1 N VAL A 34 O HIS A 195 SHEET 4 AA1 6 CYS 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 VAL A 265 N PHE A 223 SHEET 6 AA1 6 ILE A 319 MET 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 VAL B 71 N HIS B 62 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 ASN B 88 N ASP B 83 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 ILE B 120 ASN B 125 -1 O TYR B 124 N VAL B 112 SHEET 4 AA4 4 ARG B 134 ALA B 140 -1 O ARG B 134 N ASN B 125 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 CYS B 148 SHEET 3 AA5 4 THR B 165 ASP B 170 -1 O ALA B 167 N THR B 159 SHEET 4 AA5 4 GLN B 175 THR B 181 -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 GLY B 288 N SER B 275 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 GLY B 306 N VAL B 296 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 21 N SER D 7 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 THR D 69 O GLN D 82 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 VAL D 12 SHEET 3 AB1 6 MET D 93 SER D 99 -1 N TYR D 94 O THR D 115 SHEET 4 AB1 6 GLY D 33 GLN D 39 -1 N GLY D 33 O SER D 99 SHEET 5 AB1 6 LEU D 45 ILE D 51 -1 O GLU D 46 N ARG D 38 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 VAL D 12 SHEET 3 AB2 4 MET D 93 SER D 99 -1 N TYR D 94 O THR D 115 SHEET 4 AB2 4 PHE D 110 TRP D 111 -1 O PHE D 110 N ARG D 98 SHEET 1 AB3 5 VAL D 135 PRO D 136 0 SHEET 2 AB3 5 THR D 231 GLU D 234 1 O LYS D 232 N VAL D 135 SHEET 3 AB3 5 VAL D 214 GLN D 219 -1 N TYR D 215 O THR D 231 SHEET 4 AB3 5 LEU D 162 GLN D 167 -1 N TYR D 163 O MET D 218 SHEET 5 AB3 5 PRO D 173 ILE D 177 -1 O ILE D 177 N TRP D 164 SHEET 1 AB4 3 VAL D 143 CYS D 147 0 SHEET 2 AB4 3 ALA D 199 ILE D 204 -1 O LEU D 202 N ILE D 145 SHEET 3 AB4 3 PHE D 191 SER D 196 -1 N SER D 194 O THR D 201 SSBOND 1 CYS D 147 CYS D 217 1555 1555 2.03 CISPEP 1 TYR D 223 PRO D 224 0 12.76 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