HEADER MEMBRANE PROTEIN 17-OCT-24 9K25 TITLE CRYO-EM STRUCTURE OF APO-P2Y PURINOCEPTOR 2-MINIGQ-NB35 COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(S) SUBUNIT ALPHA COMPND 3 ISOFORMS SHORT; COMPND 4 CHAIN: A; COMPND 5 EC: 3.6.5.-; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 9 BETA-1; COMPND 10 CHAIN: B; 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: G; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 4; COMPND 18 MOLECULE: P2Y PURINOCEPTOR 2; COMPND 19 CHAIN: I; COMPND 20 SYNONYM: P2Y2,ATP RECEPTOR,P2U PURINOCEPTOR 1,P2U1,P2U RECEPTOR 1, COMPND 21 PURINERGIC RECEPTOR; COMPND 22 ENGINEERED: YES; COMPND 23 MUTATION: YES; COMPND 24 MOL_ID: 5; COMPND 25 MOLECULE: NANOBODY 35; COMPND 26 CHAIN: N; COMPND 27 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: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; 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: TRICHOPLUSIA NI; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 GENE: GNG2; SOURCE 20 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 24 ORGANISM_COMMON: HUMAN; SOURCE 25 ORGANISM_TAXID: 9606; SOURCE 26 GENE: P2RY2, P2RU1; SOURCE 27 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 29 MOL_ID: 5; SOURCE 30 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 31 ORGANISM_TAXID: 30538; SOURCE 32 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 33 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS G PROTEIN-COUPLED RECEPTORS, G-PROTEIN SIGNALING, NUCLEOTIDE KEYWDS 2 RECEPTORS, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR B.LAN,S.ZHANG,X.LIU,B.LIN REVDAT 1 11-JUN-25 9K25 0 JRNL AUTH B.LAN,S.ZHANG,K.CHEN,S.DAI,J.FEI,K.GAO,X.SUN,B.LIN,X.LIU JRNL TITL STRUCTURAL INSIGHT INTO THE SELF-ACTIVATION AND G-PROTEIN JRNL TITL 2 COUPLING OF P2Y2 RECEPTOR. JRNL REF CELL DISCOV V. 11 47 2025 JRNL REFN ESSN 2056-5968 JRNL PMID 40360475 JRNL DOI 10.1038/S41421-025-00797-X REMARK 2 REMARK 2 RESOLUTION. 3.31 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.310 REMARK 3 NUMBER OF PARTICLES : 211545 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 9K25 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 18-OCT-24. REMARK 100 THE DEPOSITION ID IS D_1300052709. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : CRYO-EM STRUCTURE OF APO-P2Y REMARK 245 PURINOCEPTOR 2-MINIGQ-NB35 REMARK 245 COMPLEX REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.50 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1600.00 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) : 5000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, G, I, N 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 THR A 11 REMARK 465 LEU A 194 REMARK 465 HIS A 195 REMARK 465 GLY A 196 REMARK 465 GLY A 197 REMARK 465 SER A 198 REMARK 465 GLY A 199 REMARK 465 GLY A 200 REMARK 465 SER A 201 REMARK 465 GLY A 202 REMARK 465 GLY A 203 REMARK 465 THR A 204 REMARK 465 SER A 205 REMARK 465 GLY A 206 REMARK 465 GLY A 304 REMARK 465 LYS A 305 REMARK 465 SER A 306 REMARK 465 LYS A 307 REMARK 465 ILE A 308 REMARK 465 GLU A 309 REMARK 465 ASP A 310 REMARK 465 GLU A 322 REMARK 465 ASP A 323 REMARK 465 ALA A 324 REMARK 465 THR A 325 REMARK 465 PRO A 326 REMARK 465 GLU A 327 REMARK 465 PRO A 328 REMARK 465 GLY A 329 REMARK 465 GLU A 330 REMARK 465 ASP A 331 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 GLU B 3 REMARK 465 LEU B 4 REMARK 465 ASP B 5 REMARK 465 GLN B 6 REMARK 465 LEU B 7 REMARK 465 ARG B 8 REMARK 465 GLN B 9 REMARK 465 GLU B 10 REMARK 465 ALA B 11 REMARK 465 GLU B 12 REMARK 465 GLN B 13 REMARK 465 ARG B 129 REMARK 465 GLU B 130 REMARK 465 GLY B 131 REMARK 465 ASN B 132 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 SER G 8 REMARK 465 ILE G 9 REMARK 465 ALA G 10 REMARK 465 GLN G 11 REMARK 465 ALA G 12 REMARK 465 ARG G 13 REMARK 465 LEU G 51 REMARK 465 THR G 52 REMARK 465 PRO G 53 REMARK 465 VAL G 54 REMARK 465 PRO G 55 REMARK 465 ALA G 56 REMARK 465 SER G 57 REMARK 465 GLU G 58 REMARK 465 ASN G 59 REMARK 465 PRO G 60 REMARK 465 PHE G 61 REMARK 465 ARG G 62 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 I -23 REMARK 465 LYS I -22 REMARK 465 THR I -21 REMARK 465 ILE I -20 REMARK 465 ILE I -19 REMARK 465 ALA I -18 REMARK 465 LEU I -17 REMARK 465 SER I -16 REMARK 465 TYR I -15 REMARK 465 ILE I -14 REMARK 465 PHE I -13 REMARK 465 CYS I -12 REMARK 465 LEU I -11 REMARK 465 VAL I -10 REMARK 465 PHE I -9 REMARK 465 ALA I -8 REMARK 465 ASP I -7 REMARK 465 TYR I -6 REMARK 465 LYS I -5 REMARK 465 ASP I -4 REMARK 465 ASP I -3 REMARK 465 ASP I -2 REMARK 465 ASP I -1 REMARK 465 ALA I 0 REMARK 465 MET I 1 REMARK 465 ALA I 2 REMARK 465 ALA I 3 REMARK 465 ASP I 4 REMARK 465 LEU I 5 REMARK 465 GLY I 6 REMARK 465 PRO I 7 REMARK 465 TRP I 8 REMARK 465 ASN I 9 REMARK 465 ASP I 10 REMARK 465 THR I 11 REMARK 465 ILE I 12 REMARK 465 ASN I 13 REMARK 465 GLY I 14 REMARK 465 ARG I 177 REMARK 465 GLY I 178 REMARK 465 GLY I 179 REMARK 465 ARG I 180 REMARK 465 VAL I 181 REMARK 465 PRO I 228 REMARK 465 ALA I 229 REMARK 465 TYR I 230 REMARK 465 GLY I 231 REMARK 465 THR I 232 REMARK 465 SER I 233 REMARK 465 GLY I 234 REMARK 465 GLY I 235 REMARK 465 LEU I 236 REMARK 465 PRO I 237 REMARK 465 ARG I 238 REMARK 465 ALA I 309 REMARK 465 GLY I 310 REMARK 465 GLN I 311 REMARK 465 SER I 312 REMARK 465 LEU I 313 REMARK 465 VAL I 314 REMARK 465 ARG I 315 REMARK 465 PHE I 316 REMARK 465 ALA I 317 REMARK 465 ARG I 318 REMARK 465 ASP I 319 REMARK 465 ALA I 320 REMARK 465 LYS I 321 REMARK 465 PRO I 322 REMARK 465 PRO I 323 REMARK 465 THR I 324 REMARK 465 GLY I 325 REMARK 465 PRO I 326 REMARK 465 SER I 327 REMARK 465 PRO I 328 REMARK 465 ALA I 329 REMARK 465 THR I 330 REMARK 465 PRO I 331 REMARK 465 ALA I 332 REMARK 465 ARG I 333 REMARK 465 ARG I 334 REMARK 465 ARG I 335 REMARK 465 LEU I 336 REMARK 465 GLY I 337 REMARK 465 LEU I 338 REMARK 465 ARG I 339 REMARK 465 ARG I 340 REMARK 465 SER I 341 REMARK 465 ASP I 342 REMARK 465 ARG I 343 REMARK 465 THR I 344 REMARK 465 ASP I 345 REMARK 465 MET I 346 REMARK 465 GLN I 347 REMARK 465 ARG I 348 REMARK 465 ILE I 349 REMARK 465 GLU I 350 REMARK 465 ASP I 351 REMARK 465 VAL I 352 REMARK 465 LEU I 353 REMARK 465 GLY I 354 REMARK 465 SER I 355 REMARK 465 SER I 356 REMARK 465 GLU I 357 REMARK 465 ASP I 358 REMARK 465 SER I 359 REMARK 465 ARG I 360 REMARK 465 ARG I 361 REMARK 465 THR I 362 REMARK 465 GLU I 363 REMARK 465 SER I 364 REMARK 465 THR I 365 REMARK 465 PRO I 366 REMARK 465 ALA I 367 REMARK 465 GLY I 368 REMARK 465 SER I 369 REMARK 465 GLU I 370 REMARK 465 ASN I 371 REMARK 465 THR I 372 REMARK 465 LYS I 373 REMARK 465 ASP I 374 REMARK 465 ILE I 375 REMARK 465 ARG I 376 REMARK 465 LEU I 377 REMARK 465 HIS I 378 REMARK 465 HIS I 379 REMARK 465 HIS I 380 REMARK 465 HIS I 381 REMARK 465 HIS I 382 REMARK 465 HIS I 383 REMARK 465 GLY I 384 REMARK 465 GLY I 385 REMARK 465 SER I 386 REMARK 465 GLY I 387 REMARK 465 GLY I 388 REMARK 465 LEU I 389 REMARK 465 GLU I 390 REMARK 465 VAL I 391 REMARK 465 LEU I 392 REMARK 465 PHE I 393 REMARK 465 GLN I 394 REMARK 465 GLY I 395 REMARK 465 PRO I 396 REMARK 465 SER N 127 REMARK 465 SER N 128 REMARK 465 HIS N 129 REMARK 465 HIS N 130 REMARK 465 HIS N 131 REMARK 465 HIS N 132 REMARK 465 HIS N 133 REMARK 465 HIS N 134 REMARK 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 GLU A 21 CG CD OE1 OE2 REMARK 470 MET A 25 CG SD CE REMARK 470 GLU A 27 CG CD OE1 OE2 REMARK 470 LYS A 28 CG CD CE NZ REMARK 470 GLN A 31 CG CD OE1 NE2 REMARK 470 LYS A 32 CG CD CE NZ REMARK 470 ASP A 33 CG OD1 OD2 REMARK 470 LYS A 34 CG CD CE NZ REMARK 470 GLN A 35 CG CD OE1 NE2 REMARK 470 ARG A 38 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 49 CG OD1 OD2 REMARK 470 LYS A 58 CG CD CE NZ REMARK 470 MET A 60 CG SD CE REMARK 470 ILE A 62 CG1 CG2 CD1 REMARK 470 GLU A 209 CG CD OE1 OE2 REMARK 470 LYS A 211 CG CD CE NZ REMARK 470 LYS A 216 CG CD CE NZ REMARK 470 ARG A 280 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 283 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 295 CG OD1 OD2 REMARK 470 GLU A 299 CG CD OE1 OE2 REMARK 470 GLU A 314 CG CD OE1 OE2 REMARK 470 ARG A 317 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 344 CG CD OE1 OE2 REMARK 470 ARG A 347 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 354 CG OD1 OD2 REMARK 470 ARG A 356 CG CD NE CZ NH1 NH2 REMARK 470 VAL A 367 CG1 CG2 REMARK 470 GLU A 370 CG CD OE1 OE2 REMARK 470 MET A 386 CG SD CE REMARK 470 ARG A 389 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 15 CG CD CE NZ REMARK 470 ASN B 16 CG OD1 ND2 REMARK 470 GLN B 17 CG CD OE1 NE2 REMARK 470 ARG B 19 CG CD NE CZ NH1 NH2 REMARK 470 ASP B 20 CG OD1 OD2 REMARK 470 LYS B 23 CG CD CE NZ REMARK 470 ASP B 27 CG OD1 OD2 REMARK 470 ILE B 33 CG1 CG2 CD1 REMARK 470 ASN B 35 CG OD1 ND2 REMARK 470 ASN B 36 CG OD1 ND2 REMARK 470 ASP B 38 CG OD1 OD2 REMARK 470 ARG B 42 CG CD NE CZ NH1 NH2 REMARK 470 GLN B 44 CG CD OE1 NE2 REMARK 470 MET B 45 CG SD CE REMARK 470 ARG B 46 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 48 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 52 CG CD NE CZ NH1 NH2 REMARK 470 SER B 84 OG REMARK 470 ASN B 88 CG OD1 ND2 REMARK 470 ARG B 96 CG CD NE CZ NH1 NH2 REMARK 470 TYR B 105 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 SER B 108 OG REMARK 470 LYS B 127 CG CD CE NZ REMARK 470 ARG B 134 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 138 CG CD OE1 OE2 REMARK 470 ASP B 153 CG OD1 OD2 REMARK 470 ASN B 155 CG OD1 ND2 REMARK 470 GLU B 172 CG CD OE1 OE2 REMARK 470 GLN B 175 CG CD OE1 NE2 REMARK 470 GLN B 176 CG CD OE1 NE2 REMARK 470 ASP B 186 CG OD1 OD2 REMARK 470 ASP B 195 CG OD1 OD2 REMARK 470 THR B 196 OG1 CG2 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 215 CG CD OE1 OE2 REMARK 470 MET B 217 CG SD CE REMARK 470 THR B 223 OG1 CG2 REMARK 470 GLU B 226 CG CD OE1 OE2 REMARK 470 ASP B 228 CG OD1 OD2 REMARK 470 ASP B 247 CG OD1 OD2 REMARK 470 ASP B 254 CG OD1 OD2 REMARK 470 ASP B 258 CG OD1 OD2 REMARK 470 GLN B 259 CG CD OE1 NE2 REMARK 470 GLU B 260 CG CD OE1 OE2 REMARK 470 MET B 262 CG SD CE REMARK 470 SER B 265 OG 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 CYS B 271 SG REMARK 470 ASP B 290 CG OD1 OD2 REMARK 470 ASP B 291 CG OD1 OD2 REMARK 470 PHE B 292 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASN B 293 CG OD1 ND2 REMARK 470 ASP B 303 CG OD1 OD2 REMARK 470 ASP B 312 CG OD1 OD2 REMARK 470 ASP B 322 CG OD1 OD2 REMARK 470 SER B 331 OG REMARK 470 LYS G 14 CG CD CE NZ REMARK 470 LEU G 15 CG CD1 CD2 REMARK 470 GLU G 17 CG CD OE1 OE2 REMARK 470 LYS G 20 CG CD CE NZ REMARK 470 GLU G 22 CG CD OE1 OE2 REMARK 470 ASN G 24 CG OD1 ND2 REMARK 470 ASP G 26 CG OD1 OD2 REMARK 470 ARG G 27 CG CD NE CZ NH1 NH2 REMARK 470 ILE G 28 CG1 CG2 CD1 REMARK 470 LYS G 29 CG CD CE NZ REMARK 470 LYS G 32 CG CD CE NZ REMARK 470 ASP G 36 CG OD1 OD2 REMARK 470 GLU G 42 CG CD OE1 OE2 REMARK 470 LYS G 46 CG CD CE NZ REMARK 470 GLU G 47 CG CD OE1 OE2 REMARK 470 ASP G 48 CG OD1 OD2 REMARK 470 ARG I 24 CG CD NE CZ NH1 NH2 REMARK 470 PHE I 27 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASN I 28 CG OD1 ND2 REMARK 470 GLU I 29 CG CD OE1 OE2 REMARK 470 ASP I 30 CG OD1 OD2 REMARK 470 PHE I 31 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU I 35 CG CD1 CD2 REMARK 470 VAL I 42 CG1 CG2 REMARK 470 LEU I 46 CG CD1 CD2 REMARK 470 LEU I 48 CG CD1 CD2 REMARK 470 PHE I 58 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG I 61 CG CD NE CZ NH1 NH2 REMARK 470 LYS I 63 CG CD CE NZ REMARK 470 LEU I 86 CG CD1 CD2 REMARK 470 TYR I 93 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 HIS I 98 CG ND1 CD2 CE1 NE2 REMARK 470 PHE I 101 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU I 105 CG CD1 CD2 REMARK 470 ARG I 143 CG CD NE CZ NH1 NH2 REMARK 470 ARG I 148 CG CD NE CZ NH1 NH2 REMARK 470 ARG I 152 CG CD NE CZ NH1 NH2 REMARK 470 GLU I 190 CG CD OE1 OE2 REMARK 470 LYS I 240 CG CD CE NZ REMARK 470 LEU I 274 CG CD1 CD2 REMARK 470 SER I 277 OG REMARK 470 HIS I 279 CG ND1 CD2 CE1 NE2 REMARK 470 THR I 280 OG1 CG2 REMARK 470 ASN I 282 CG OD1 ND2 REMARK 470 SER I 299 OG REMARK 470 GLN N 1 CG CD OE1 NE2 REMARK 470 GLN N 3 CG CD OE1 NE2 REMARK 470 GLN N 5 CG CD OE1 NE2 REMARK 470 SER N 7 OG REMARK 470 LEU N 11 CG CD1 CD2 REMARK 470 VAL N 12 CG1 CG2 REMARK 470 GLN N 13 CG CD OE1 NE2 REMARK 470 SER N 17 OG REMARK 470 LYS N 43 CG CD CE NZ REMARK 470 GLU N 46 CG CD OE1 OE2 REMARK 470 SER N 54 OG REMARK 470 LYS N 65 CG CD CE NZ REMARK 470 THR N 69 OG1 CG2 REMARK 470 ASP N 73 CG OD1 OD2 REMARK 470 LYS N 76 CG CD CE NZ REMARK 470 SER N 85 OG REMARK 470 LYS N 87 CG CD CE NZ REMARK 470 GLU N 89 CG CD OE1 OE2 REMARK 470 THR N 91 OG1 CG2 REMARK 470 PHE N 106 CG CD1 CD2 CE1 CE2 CZ REMARK 470 CYS N 107 SG REMARK 470 GLN N 120 CG CD OE1 NE2 REMARK 470 THR N 125 OG1 CG2 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 SER A 13 -168.65 -161.22 REMARK 500 SER B 67 -5.66 77.21 REMARK 500 ASP B 118 -5.85 83.40 REMARK 500 LEU B 152 -61.23 -94.61 REMARK 500 ASP B 154 -2.36 74.61 REMARK 500 CYS B 166 -169.31 -76.97 REMARK 500 ALA B 167 149.24 -170.94 REMARK 500 SER B 201 116.01 -160.42 REMARK 500 ASP B 291 36.08 -96.05 REMARK 500 PHE B 292 -6.87 75.56 REMARK 500 LEU B 318 142.26 -170.76 REMARK 500 ALA I 94 -61.78 -95.47 REMARK 500 HIS I 98 62.60 64.49 REMARK 500 ARG I 148 -2.36 73.36 REMARK 500 ALA I 188 162.23 179.21 REMARK 500 SER I 273 -89.17 -121.05 REMARK 500 PHE N 29 33.82 -99.91 REMARK 500 VAL N 48 -63.62 -120.23 REMARK 500 SER N 57 98.61 -160.79 REMARK 500 ALA N 75 -3.64 71.34 REMARK 500 ASN N 77 94.97 -69.51 REMARK 500 ALA N 92 -64.33 -97.00 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-61990 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF APO-P2Y PURINOCEPTOR 2-MINIGQ-NB35 COMPLEX DBREF 9K25 A 11 203 PDB 9K25 9K25 11 203 DBREF 9K25 A 204 394 PDB 9K25 9K25 204 394 DBREF 9K25 B 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 9K25 G 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 9K25 I 1 377 UNP P41231 P2RY2_HUMAN 1 377 DBREF 9K25 N 1 134 PDB 9K25 9K25 1 134 SEQADV 9K25 MET B -17 UNP P62873 INITIATING METHIONINE SEQADV 9K25 HIS B -16 UNP P62873 EXPRESSION TAG SEQADV 9K25 HIS B -15 UNP P62873 EXPRESSION TAG SEQADV 9K25 HIS B -14 UNP P62873 EXPRESSION TAG SEQADV 9K25 HIS B -13 UNP P62873 EXPRESSION TAG SEQADV 9K25 HIS B -12 UNP P62873 EXPRESSION TAG SEQADV 9K25 HIS B -11 UNP P62873 EXPRESSION TAG SEQADV 9K25 LEU B -10 UNP P62873 EXPRESSION TAG SEQADV 9K25 GLU B -9 UNP P62873 EXPRESSION TAG SEQADV 9K25 VAL B -8 UNP P62873 EXPRESSION TAG SEQADV 9K25 LEU B -7 UNP P62873 EXPRESSION TAG SEQADV 9K25 PHE B -6 UNP P62873 EXPRESSION TAG SEQADV 9K25 GLN B -5 UNP P62873 EXPRESSION TAG SEQADV 9K25 GLY B -4 UNP P62873 EXPRESSION TAG SEQADV 9K25 PRO B -3 UNP P62873 EXPRESSION TAG SEQADV 9K25 GLY B -2 UNP P62873 EXPRESSION TAG SEQADV 9K25 SER B -1 UNP P62873 EXPRESSION TAG SEQADV 9K25 SER B 0 UNP P62873 EXPRESSION TAG SEQADV 9K25 GLY B 1 UNP P62873 EXPRESSION TAG SEQADV 9K25 MET I -23 UNP P41231 INITIATING METHIONINE SEQADV 9K25 LYS I -22 UNP P41231 EXPRESSION TAG SEQADV 9K25 THR I -21 UNP P41231 EXPRESSION TAG SEQADV 9K25 ILE I -20 UNP P41231 EXPRESSION TAG SEQADV 9K25 ILE I -19 UNP P41231 EXPRESSION TAG SEQADV 9K25 ALA I -18 UNP P41231 EXPRESSION TAG SEQADV 9K25 LEU I -17 UNP P41231 EXPRESSION TAG SEQADV 9K25 SER I -16 UNP P41231 EXPRESSION TAG SEQADV 9K25 TYR I -15 UNP P41231 EXPRESSION TAG SEQADV 9K25 ILE I -14 UNP P41231 EXPRESSION TAG SEQADV 9K25 PHE I -13 UNP P41231 EXPRESSION TAG SEQADV 9K25 CYS I -12 UNP P41231 EXPRESSION TAG SEQADV 9K25 LEU I -11 UNP P41231 EXPRESSION TAG SEQADV 9K25 VAL I -10 UNP P41231 EXPRESSION TAG SEQADV 9K25 PHE I -9 UNP P41231 EXPRESSION TAG SEQADV 9K25 ALA I -8 UNP P41231 EXPRESSION TAG SEQADV 9K25 ASP I -7 UNP P41231 EXPRESSION TAG SEQADV 9K25 TYR I -6 UNP P41231 EXPRESSION TAG SEQADV 9K25 LYS I -5 UNP P41231 EXPRESSION TAG SEQADV 9K25 ASP I -4 UNP P41231 EXPRESSION TAG SEQADV 9K25 ASP I -3 UNP P41231 EXPRESSION TAG SEQADV 9K25 ASP I -2 UNP P41231 EXPRESSION TAG SEQADV 9K25 ASP I -1 UNP P41231 EXPRESSION TAG SEQADV 9K25 ALA I 0 UNP P41231 EXPRESSION TAG SEQADV 9K25 LEU I 46 UNP P41231 PRO 46 VARIANT SEQADV 9K25 ASN I 302 UNP P41231 ASP 302 ENGINEERED MUTATION SEQADV 9K25 SER I 312 UNP P41231 ARG 312 VARIANT SEQADV 9K25 HIS I 378 UNP P41231 EXPRESSION TAG SEQADV 9K25 HIS I 379 UNP P41231 EXPRESSION TAG SEQADV 9K25 HIS I 380 UNP P41231 EXPRESSION TAG SEQADV 9K25 HIS I 381 UNP P41231 EXPRESSION TAG SEQADV 9K25 HIS I 382 UNP P41231 EXPRESSION TAG SEQADV 9K25 HIS I 383 UNP P41231 EXPRESSION TAG SEQADV 9K25 GLY I 384 UNP P41231 EXPRESSION TAG SEQADV 9K25 GLY I 385 UNP P41231 EXPRESSION TAG SEQADV 9K25 SER I 386 UNP P41231 EXPRESSION TAG SEQADV 9K25 GLY I 387 UNP P41231 EXPRESSION TAG SEQADV 9K25 GLY I 388 UNP P41231 EXPRESSION TAG SEQADV 9K25 LEU I 389 UNP P41231 EXPRESSION TAG SEQADV 9K25 GLU I 390 UNP P41231 EXPRESSION TAG SEQADV 9K25 VAL I 391 UNP P41231 EXPRESSION TAG SEQADV 9K25 LEU I 392 UNP P41231 EXPRESSION TAG SEQADV 9K25 PHE I 393 UNP P41231 EXPRESSION TAG SEQADV 9K25 GLN I 394 UNP P41231 EXPRESSION TAG SEQADV 9K25 GLY I 395 UNP P41231 EXPRESSION TAG SEQADV 9K25 PRO I 396 UNP P41231 EXPRESSION TAG SEQRES 1 A 243 THR LEU SER ALA GLU ASP LYS ALA ALA VAL GLU ARG SER SEQRES 2 A 243 LYS MET ILE GLU LYS GLN LEU GLN LYS ASP LYS GLN VAL SEQRES 3 A 243 TYR ARG ALA THR HIS ARG LEU LEU LEU LEU GLY ALA ASP SEQRES 4 A 243 ASN SER GLY LYS SER THR ILE VAL LYS GLN MET ARG ILE SEQRES 5 A 243 LEU HIS GLY GLY SER GLY GLY SER GLY GLY THR SER GLY SEQRES 6 A 243 ILE PHE GLU THR LYS PHE GLN VAL ASP LYS VAL ASN PHE SEQRES 7 A 243 HIS MET PHE ASP VAL GLY GLY GLN ARG ASP GLU ARG ARG SEQRES 8 A 243 LYS TRP ILE GLN CYS PHE ASN ASP VAL THR ALA ILE ILE SEQRES 9 A 243 PHE VAL VAL ASP SER SER ASP TYR ASN ARG LEU GLN GLU SEQRES 10 A 243 ALA LEU ASN ASP PHE LYS SER ILE TRP ASN ASN ARG TRP SEQRES 11 A 243 LEU ARG THR ILE SER VAL ILE LEU PHE LEU ASN LYS GLN SEQRES 12 A 243 ASP LEU LEU ALA GLU LYS VAL LEU ALA GLY LYS SER LYS SEQRES 13 A 243 ILE GLU ASP TYR PHE PRO GLU PHE ALA ARG TYR THR THR SEQRES 14 A 243 PRO GLU ASP ALA THR PRO GLU PRO GLY GLU ASP PRO ARG SEQRES 15 A 243 VAL THR ARG ALA LYS TYR PHE ILE ARG ASP GLU PHE LEU SEQRES 16 A 243 ARG ILE SER THR ALA SER GLY ASP GLY ARG HIS TYR CYS SEQRES 17 A 243 TYR PRO HIS PHE THR CYS ALA VAL ASP THR GLU ASN ALA SEQRES 18 A 243 ARG ARG ILE PHE ASN ASP CYS LYS ASP ILE ILE LEU GLN SEQRES 19 A 243 MET ASN LEU ARG GLU TYR ASN LEU VAL SEQRES 1 B 358 MET HIS HIS HIS HIS HIS HIS LEU GLU VAL LEU PHE GLN SEQRES 2 B 358 GLY PRO GLY SER SER GLY SER GLU LEU ASP GLN LEU ARG SEQRES 3 B 358 GLN GLU ALA GLU GLN LEU LYS ASN GLN ILE ARG ASP ALA SEQRES 4 B 358 ARG LYS ALA CYS ALA ASP ALA THR LEU SER GLN ILE THR SEQRES 5 B 358 ASN ASN ILE ASP PRO VAL GLY ARG ILE GLN MET ARG THR SEQRES 6 B 358 ARG ARG THR LEU ARG GLY HIS LEU ALA LYS ILE TYR ALA SEQRES 7 B 358 MET HIS TRP GLY THR ASP SER ARG LEU LEU VAL SER ALA SEQRES 8 B 358 SER GLN ASP GLY LYS LEU ILE ILE TRP ASP SER TYR THR SEQRES 9 B 358 THR ASN LYS VAL HIS ALA ILE PRO LEU ARG SER SER TRP SEQRES 10 B 358 VAL MET THR CYS ALA TYR ALA PRO SER GLY ASN TYR VAL SEQRES 11 B 358 ALA CYS GLY GLY LEU ASP ASN ILE CYS SER ILE TYR ASN SEQRES 12 B 358 LEU LYS THR ARG GLU GLY ASN VAL ARG VAL SER ARG GLU SEQRES 13 B 358 LEU ALA GLY HIS THR GLY TYR LEU SER CYS CYS ARG PHE SEQRES 14 B 358 LEU ASP ASP ASN GLN ILE VAL THR SER SER GLY ASP THR SEQRES 15 B 358 THR CYS ALA LEU TRP ASP ILE GLU THR GLY GLN GLN THR SEQRES 16 B 358 THR THR PHE THR GLY HIS THR GLY ASP VAL MET SER LEU SEQRES 17 B 358 SER LEU ALA PRO ASP THR ARG LEU PHE VAL SER GLY ALA SEQRES 18 B 358 CYS ASP ALA SER ALA LYS LEU TRP ASP VAL ARG GLU GLY SEQRES 19 B 358 MET CYS ARG GLN THR PHE THR GLY HIS GLU SER ASP ILE SEQRES 20 B 358 ASN ALA ILE CYS PHE PHE PRO ASN GLY ASN ALA PHE ALA SEQRES 21 B 358 THR GLY SER ASP ASP ALA THR CYS ARG LEU PHE ASP LEU SEQRES 22 B 358 ARG ALA ASP GLN GLU LEU MET THR TYR SER HIS ASP ASN SEQRES 23 B 358 ILE ILE CYS GLY ILE THR SER VAL SER PHE SER LYS SER SEQRES 24 B 358 GLY ARG LEU LEU LEU ALA GLY TYR ASP ASP PHE ASN CYS SEQRES 25 B 358 ASN VAL TRP ASP ALA LEU LYS ALA ASP ARG ALA GLY VAL SEQRES 26 B 358 LEU ALA GLY HIS ASP ASN ARG VAL SER CYS LEU GLY VAL SEQRES 27 B 358 THR ASP ASP GLY MET ALA VAL ALA THR GLY SER TRP ASP SEQRES 28 B 358 SER PHE LEU LYS ILE TRP ASN 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 I 420 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU SEQRES 2 I 420 VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP ALA MET ALA SEQRES 3 I 420 ALA ASP LEU GLY PRO TRP ASN ASP THR ILE ASN GLY THR SEQRES 4 I 420 TRP ASP GLY ASP GLU LEU GLY TYR ARG CYS ARG PHE ASN SEQRES 5 I 420 GLU ASP PHE LYS TYR VAL LEU LEU PRO VAL SER TYR GLY SEQRES 6 I 420 VAL VAL CYS VAL LEU GLY LEU CYS LEU ASN ALA VAL ALA SEQRES 7 I 420 LEU TYR ILE PHE LEU CYS ARG LEU LYS THR TRP ASN ALA SEQRES 8 I 420 SER THR THR TYR MET PHE HIS LEU ALA VAL SER ASP ALA SEQRES 9 I 420 LEU TYR ALA ALA SER LEU PRO LEU LEU VAL TYR TYR TYR SEQRES 10 I 420 ALA ARG GLY ASP HIS TRP PRO PHE SER THR VAL LEU CYS SEQRES 11 I 420 LYS LEU VAL ARG PHE LEU PHE TYR THR ASN LEU TYR CYS SEQRES 12 I 420 SER ILE LEU PHE LEU THR CYS ILE SER VAL HIS ARG CYS SEQRES 13 I 420 LEU GLY VAL LEU ARG PRO LEU ARG SER LEU ARG TRP GLY SEQRES 14 I 420 ARG ALA ARG TYR ALA ARG ARG VAL ALA GLY ALA VAL TRP SEQRES 15 I 420 VAL LEU VAL LEU ALA CYS GLN ALA PRO VAL LEU TYR PHE SEQRES 16 I 420 VAL THR THR SER ALA ARG GLY GLY ARG VAL THR CYS HIS SEQRES 17 I 420 ASP THR SER ALA PRO GLU LEU PHE SER ARG PHE VAL ALA SEQRES 18 I 420 TYR SER SER VAL MET LEU GLY LEU LEU PHE ALA VAL PRO SEQRES 19 I 420 PHE ALA VAL ILE LEU VAL CYS TYR VAL LEU MET ALA ARG SEQRES 20 I 420 ARG LEU LEU LYS PRO ALA TYR GLY THR SER GLY GLY LEU SEQRES 21 I 420 PRO ARG ALA LYS ARG LYS SER VAL ARG THR ILE ALA VAL SEQRES 22 I 420 VAL LEU ALA VAL PHE ALA LEU CYS PHE LEU PRO PHE HIS SEQRES 23 I 420 VAL THR ARG THR LEU TYR TYR SER PHE ARG SER LEU ASP SEQRES 24 I 420 LEU SER CYS HIS THR LEU ASN ALA ILE ASN MET ALA TYR SEQRES 25 I 420 LYS VAL THR ARG PRO LEU ALA SER ALA ASN SER CYS LEU SEQRES 26 I 420 ASN PRO VAL LEU TYR PHE LEU ALA GLY GLN SER LEU VAL SEQRES 27 I 420 ARG PHE ALA ARG ASP ALA LYS PRO PRO THR GLY PRO SER SEQRES 28 I 420 PRO ALA THR PRO ALA ARG ARG ARG LEU GLY LEU ARG ARG SEQRES 29 I 420 SER ASP ARG THR ASP MET GLN ARG ILE GLU ASP VAL LEU SEQRES 30 I 420 GLY SER SER GLU ASP SER ARG ARG THR GLU SER THR PRO SEQRES 31 I 420 ALA GLY SER GLU ASN THR LYS ASP ILE ARG LEU HIS HIS SEQRES 32 I 420 HIS HIS HIS HIS GLY GLY SER GLY GLY LEU GLU VAL LEU SEQRES 33 I 420 PHE GLN GLY PRO SEQRES 1 N 134 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 N 134 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 N 134 PHE THR PHE SER ASN TYR LYS MET ASN TRP VAL ARG GLN SEQRES 4 N 134 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ASP ILE SER SEQRES 5 N 134 GLN SER GLY ALA SER ILE SER TYR THR GLY SER VAL LYS SEQRES 6 N 134 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 N 134 LEU TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 N 134 ALA VAL TYR TYR CYS ALA ARG CYS PRO ALA PRO PHE THR SEQRES 9 N 134 PRO PHE CYS PHE ASP VAL THR SER THR THR TYR ALA TYR SEQRES 10 N 134 ARG GLY GLN GLY THR GLN VAL THR VAL SER SER HIS HIS SEQRES 11 N 134 HIS HIS HIS HIS HELIX 1 AA1 ALA A 14 ARG A 38 1 25 HELIX 2 AA2 ASP A 252 ASN A 278 1 17 HELIX 3 AA3 LYS A 293 ALA A 303 1 11 HELIX 4 AA4 PHE A 312 ALA A 316 5 5 HELIX 5 AA5 ARG A 333 SER A 352 1 20 HELIX 6 AA6 GLU A 370 TYR A 391 1 22 HELIX 7 AA7 LYS B 15 CYS B 25 1 11 HELIX 8 AA8 THR B 29 THR B 34 1 6 HELIX 9 AA9 LEU G 15 ASN G 24 1 10 HELIX 10 AB1 LYS G 29 HIS G 44 1 16 HELIX 11 AB2 TRP I 16 CYS I 25 1 10 HELIX 12 AB3 GLU I 29 ARG I 61 1 33 HELIX 13 AB4 ASN I 66 ARG I 95 1 30 HELIX 14 AB5 SER I 102 ARG I 137 1 36 HELIX 15 AB6 ARG I 137 TRP I 144 1 8 HELIX 16 AB7 TYR I 149 GLN I 165 1 17 HELIX 17 AB8 GLN I 165 VAL I 172 1 8 HELIX 18 AB9 LEU I 191 PHE I 207 1 17 HELIX 19 AC1 PHE I 207 LYS I 227 1 21 HELIX 20 AC2 LYS I 240 SER I 270 1 31 HELIX 21 AC3 SER I 277 LEU I 308 1 32 HELIX 22 AC4 LYS N 87 THR N 91 5 5 SHEET 1 AA1 6 THR A 210 VAL A 214 0 SHEET 2 AA1 6 VAL A 217 PHE A 222 -1 O PHE A 219 N PHE A 212 SHEET 3 AA1 6 HIS A 41 GLY A 47 1 N LEU A 43 O HIS A 220 SHEET 4 AA1 6 ALA A 243 ASP A 249 1 O ILE A 245 N LEU A 44 SHEET 5 AA1 6 SER A 286 ASN A 292 1 O PHE A 290 N VAL A 248 SHEET 6 AA1 6 CYS A 359 HIS A 362 1 O HIS A 362 N LEU A 291 SHEET 1 AA2 4 ARG B 49 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 ALA B 328 -1 N VAL B 327 O TRP B 339 SHEET 4 AA2 4 GLY B 319 VAL B 320 -1 N GLY B 319 O ALA B 328 SHEET 1 AA3 4 ILE B 58 TRP B 63 0 SHEET 2 AA3 4 LEU B 70 SER B 74 -1 O ALA B 73 N TYR B 59 SHEET 3 AA3 4 LYS B 78 ILE B 81 -1 O ILE B 80 N SER B 72 SHEET 4 AA3 4 HIS B 91 PRO B 94 -1 O ILE B 93 N LEU B 79 SHEET 1 AA4 3 ALA B 104 TYR B 105 0 SHEET 2 AA4 3 TYR B 111 ALA B 113 -1 O ALA B 113 N ALA B 104 SHEET 3 AA4 3 ILE B 123 ASN B 125 -1 O TYR B 124 N VAL B 112 SHEET 1 AA5 4 CYS B 149 PHE B 151 0 SHEET 2 AA5 4 ILE B 157 THR B 159 -1 O VAL B 158 N ARG B 150 SHEET 3 AA5 4 CYS B 166 LEU B 168 -1 O ALA B 167 N THR B 159 SHEET 4 AA5 4 THR B 178 PHE B 180 -1 N THR B 178 O LEU B 168 SHEET 1 AA6 4 VAL B 187 LEU B 192 0 SHEET 2 AA6 4 LEU B 198 ALA B 203 -1 O GLY B 202 N SER B 189 SHEET 3 AA6 4 ALA B 208 ASP B 212 -1 O TRP B 211 N PHE B 199 SHEET 4 AA6 4 GLN B 220 THR B 221 -1 O GLN B 220 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 GLY B 244 N ALA B 231 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 3 SER B 275 SER B 277 0 SHEET 2 AA8 3 LEU B 284 GLY B 288 -1 O LEU B 286 N SER B 277 SHEET 3 AA8 3 ASN B 295 ASP B 298 -1 O TRP B 297 N LEU B 285 SHEET 1 AA9 4 GLN N 5 SER N 7 0 SHEET 2 AA9 4 LEU N 18 ALA N 23 -1 O ALA N 23 N GLN N 5 SHEET 3 AA9 4 THR N 78 MET N 83 -1 O MET N 83 N LEU N 18 SHEET 4 AA9 4 PHE N 68 ASP N 73 -1 N THR N 69 O GLN N 82 SHEET 1 AB1 3 MET N 34 GLN N 39 0 SHEET 2 AB1 3 VAL N 93 ARG N 98 -1 O ALA N 97 N ASN N 35 SHEET 3 AB1 3 THR N 122 GLN N 123 -1 O THR N 122 N TYR N 94 SSBOND 1 CYS I 25 CYS I 278 1555 1555 1.88 SSBOND 2 CYS I 106 CYS I 183 1555 1555 2.03 SSBOND 3 CYS N 22 CYS N 96 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