HEADER MEMBRANE PROTEIN 16-OCT-24 9K20 TITLE CRYO-EM STRUCTURE OF ATP-BOUND P2Y PURINOCEPTOR 2-MINIGO-SCFV16 TITLE 2 COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: P2Y PURINOCEPTOR 2; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: P2Y2,ATP RECEPTOR,P2U PURINOCEPTOR 1,P2U1,P2U RECEPTOR 1, COMPND 5 PURINERGIC RECEPTOR; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(O) SUBUNIT ALPHA; COMPND 10 CHAIN: B; COMPND 11 EC: 3.6.5.-; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 3; COMPND 14 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 15 BETA-1; COMPND 16 CHAIN: C; COMPND 17 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 18 ENGINEERED: YES; COMPND 19 MOL_ID: 4; COMPND 20 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 21 GAMMA-2; COMPND 22 CHAIN: D; COMPND 23 SYNONYM: G GAMMA-I; COMPND 24 ENGINEERED: YES; COMPND 25 MOL_ID: 5; COMPND 26 MOLECULE: SINGLE FAB CHAIN (SVFV16); COMPND 27 CHAIN: E; COMPND 28 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: P2RY2, P2RU1; 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: GNAO1; SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 GENE: GNB1; 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: GNG2; SOURCE 27 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 29 MOL_ID: 5; SOURCE 30 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 31 ORGANISM_TAXID: 10090; SOURCE 32 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 33 EXPRESSION_SYSTEM_TAXID: 7111 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 9K20 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. 2.65 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 2.650 REMARK 3 NUMBER OF PARTICLES : 273351 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 9K20 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_1300052678. 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 ATP-BOUND REMARK 245 P2Y PURINOCEPTOR 2-MINIGO- REMARK 245 SCFV16 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, C, D, E 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 -23 REMARK 465 LYS A -22 REMARK 465 THR A -21 REMARK 465 ILE A -20 REMARK 465 ILE A -19 REMARK 465 ALA A -18 REMARK 465 LEU A -17 REMARK 465 SER A -16 REMARK 465 TYR A -15 REMARK 465 ILE A -14 REMARK 465 PHE A -13 REMARK 465 CYS A -12 REMARK 465 LEU A -11 REMARK 465 VAL A -10 REMARK 465 PHE A -9 REMARK 465 ALA A -8 REMARK 465 ASP A -7 REMARK 465 TYR A -6 REMARK 465 LYS A -5 REMARK 465 ASP A -4 REMARK 465 ASP A -3 REMARK 465 ASP A -2 REMARK 465 ASP A -1 REMARK 465 ALA A 0 REMARK 465 MET A 1 REMARK 465 ALA A 2 REMARK 465 ALA A 3 REMARK 465 ASP A 4 REMARK 465 LEU A 5 REMARK 465 GLY A 6 REMARK 465 PRO A 7 REMARK 465 TRP A 8 REMARK 465 ASN A 9 REMARK 465 ASP A 10 REMARK 465 THR A 11 REMARK 465 ILE A 12 REMARK 465 ASN A 13 REMARK 465 GLY A 14 REMARK 465 THR A 15 REMARK 465 TRP A 16 REMARK 465 ASP A 17 REMARK 465 GLY A 18 REMARK 465 ASP A 19 REMARK 465 GLU A 20 REMARK 465 ALA A 309 REMARK 465 GLY A 310 REMARK 465 GLN A 311 REMARK 465 SER A 312 REMARK 465 LEU A 313 REMARK 465 VAL A 314 REMARK 465 ARG A 315 REMARK 465 PHE A 316 REMARK 465 ALA A 317 REMARK 465 ARG A 318 REMARK 465 ASP A 319 REMARK 465 ALA A 320 REMARK 465 LYS A 321 REMARK 465 PRO A 322 REMARK 465 PRO A 323 REMARK 465 THR A 324 REMARK 465 GLY A 325 REMARK 465 PRO A 326 REMARK 465 SER A 327 REMARK 465 PRO A 328 REMARK 465 ALA A 329 REMARK 465 THR A 330 REMARK 465 PRO A 331 REMARK 465 ALA A 332 REMARK 465 ARG A 333 REMARK 465 ARG A 334 REMARK 465 ARG A 335 REMARK 465 LEU A 336 REMARK 465 GLY A 337 REMARK 465 LEU A 338 REMARK 465 ARG A 339 REMARK 465 ARG A 340 REMARK 465 SER A 341 REMARK 465 ASP A 342 REMARK 465 ARG A 343 REMARK 465 THR A 344 REMARK 465 ASP A 345 REMARK 465 MET A 346 REMARK 465 GLN A 347 REMARK 465 ARG A 348 REMARK 465 ILE A 349 REMARK 465 GLU A 350 REMARK 465 ASP A 351 REMARK 465 VAL A 352 REMARK 465 LEU A 353 REMARK 465 GLY A 354 REMARK 465 SER A 355 REMARK 465 SER A 356 REMARK 465 GLU A 357 REMARK 465 ASP A 358 REMARK 465 SER A 359 REMARK 465 ARG A 360 REMARK 465 ARG A 361 REMARK 465 THR A 362 REMARK 465 GLU A 363 REMARK 465 SER A 364 REMARK 465 THR A 365 REMARK 465 PRO A 366 REMARK 465 ALA A 367 REMARK 465 GLY A 368 REMARK 465 SER A 369 REMARK 465 GLU A 370 REMARK 465 ASN A 371 REMARK 465 THR A 372 REMARK 465 LYS A 373 REMARK 465 ASP A 374 REMARK 465 ILE A 375 REMARK 465 ARG A 376 REMARK 465 LEU A 377 REMARK 465 HIS A 378 REMARK 465 HIS A 379 REMARK 465 HIS A 380 REMARK 465 HIS A 381 REMARK 465 HIS A 382 REMARK 465 HIS A 383 REMARK 465 GLY A 384 REMARK 465 GLY A 385 REMARK 465 SER A 386 REMARK 465 GLY A 387 REMARK 465 GLY A 388 REMARK 465 LEU A 389 REMARK 465 GLU A 390 REMARK 465 VAL A 391 REMARK 465 LEU A 392 REMARK 465 PHE A 393 REMARK 465 GLN A 394 REMARK 465 GLY A 395 REMARK 465 PRO A 396 REMARK 465 ILE B 53 REMARK 465 ILE B 54 REMARK 465 HIS B 55 REMARK 465 GLY B 56 REMARK 465 GLY B 57 REMARK 465 SER B 58 REMARK 465 GLY B 59 REMARK 465 GLY B 60 REMARK 465 SER B 61 REMARK 465 GLY B 62 REMARK 465 GLY B 63 REMARK 465 THR B 64 REMARK 465 THR B 65 REMARK 465 MET C -17 REMARK 465 HIS C -16 REMARK 465 HIS C -15 REMARK 465 HIS C -14 REMARK 465 HIS C -13 REMARK 465 HIS C -12 REMARK 465 HIS C -11 REMARK 465 LEU C -10 REMARK 465 GLU C -9 REMARK 465 VAL C -8 REMARK 465 LEU C -7 REMARK 465 PHE C -6 REMARK 465 GLN C -5 REMARK 465 GLY C -4 REMARK 465 PRO C -3 REMARK 465 GLY C -2 REMARK 465 SER C -1 REMARK 465 SER C 0 REMARK 465 GLY C 1 REMARK 465 SER C 2 REMARK 465 GLU C 3 REMARK 465 LEU C 4 REMARK 465 ASP C 5 REMARK 465 GLN C 6 REMARK 465 LEU C 7 REMARK 465 ARG C 8 REMARK 465 GLN C 9 REMARK 465 MET D 1 REMARK 465 ALA D 2 REMARK 465 SER D 3 REMARK 465 ASN D 4 REMARK 465 ASN D 5 REMARK 465 THR D 6 REMARK 465 ALA D 7 REMARK 465 SER D 8 REMARK 465 ILE D 9 REMARK 465 ALA D 10 REMARK 465 GLN D 11 REMARK 465 ARG D 62 REMARK 465 GLU D 63 REMARK 465 LYS D 64 REMARK 465 LYS D 65 REMARK 465 PHE D 66 REMARK 465 PHE D 67 REMARK 465 CYS D 68 REMARK 465 ALA D 69 REMARK 465 ILE D 70 REMARK 465 LEU D 71 REMARK 465 MET E -19 REMARK 465 VAL E -18 REMARK 465 SER E -17 REMARK 465 ALA E -16 REMARK 465 ILE E -15 REMARK 465 VAL E -14 REMARK 465 LEU E -13 REMARK 465 TYR E -12 REMARK 465 VAL E -11 REMARK 465 LEU E -10 REMARK 465 LEU E -9 REMARK 465 ALA E -8 REMARK 465 ALA E -7 REMARK 465 ALA E -6 REMARK 465 ALA E -5 REMARK 465 HIS E -4 REMARK 465 SER E -3 REMARK 465 ALA E -2 REMARK 465 PHE E -1 REMARK 465 ALA E 0 REMARK 465 ASP E 1 REMARK 465 SER E 120A REMARK 465 GLY E 120B REMARK 465 GLY E 120C REMARK 465 GLY E 120D REMARK 465 GLY E 120E REMARK 465 SER E 120F REMARK 465 GLY E 120G REMARK 465 GLY E 120H REMARK 465 GLY E 120I REMARK 465 GLY E 120J REMARK 465 SER E 120K REMARK 465 GLY E 120L REMARK 465 GLY E 120M REMARK 465 GLY E 120N REMARK 465 GLY E 120O REMARK 465 SER E 120P REMARK 465 GLY E 197 REMARK 465 LYS E 236 REMARK 465 GLY E 237 REMARK 465 SER E 238 REMARK 465 LEU E 239 REMARK 465 GLU E 240 REMARK 465 VAL E 241 REMARK 465 LEU E 242 REMARK 465 PHE E 243 REMARK 465 GLN E 244 REMARK 465 GLY E 245 REMARK 465 PRO E 246 REMARK 465 ALA E 247 REMARK 465 ALA E 248 REMARK 465 ALA E 249 REMARK 465 HIS E 250 REMARK 465 HIS E 251 REMARK 465 HIS E 252 REMARK 465 HIS E 253 REMARK 465 HIS E 254 REMARK 465 HIS E 255 REMARK 465 HIS E 256 REMARK 465 HIS E 257 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 ASN A 28 CG OD1 ND2 REMARK 470 CYS A 49 SG REMARK 470 ARG A 61 CG CD NE CZ NH1 NH2 REMARK 470 TYR A 91 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 PHE A 101 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG A 148 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 177 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 238 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 241 CG CD NE CZ NH1 NH2 REMARK 470 VAL A 250 CG2 REMARK 470 ASP A 275 CG OD1 OD2 REMARK 470 HIS A 279 CG ND1 CD2 CE1 NE2 REMARK 470 GLU B 23 CG CD OE1 OE2 REMARK 470 ASP B 40 CG OD1 OD2 REMARK 470 ASN B 41 CG OD1 ND2 REMARK 470 LYS B 49 CG CD CE NZ REMARK 470 LYS B 52 CG CD CE NZ REMARK 470 ARG B 88 CG CD NE CZ NH1 NH2 REMARK 470 SER B 89 OG REMARK 470 GLU B 90 CG CD OE1 OE2 REMARK 470 LYS B 92 CG CD CE NZ REMARK 470 ASP B 100 CG OD1 OD2 REMARK 470 ASN B 114 CG OD1 ND2 REMARK 470 ARG B 115 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 118 CG CD OE1 OE2 REMARK 470 MET B 121 CG SD CE REMARK 470 ASP B 122 CG OD1 OD2 REMARK 470 ASP B 134 CG OD1 OD2 REMARK 470 GLU B 149 CG CD OE1 OE2 REMARK 470 LYS B 153 CG CD CE NZ REMARK 470 GLU B 162 CG CD OE1 OE2 REMARK 470 ASN B 167 CG OD1 ND2 REMARK 470 GLU B 170 CG CD OE1 OE2 REMARK 470 ASP B 171 CG OD1 OD2 REMARK 470 THR B 199 OG1 CG2 REMARK 470 GLU C 10 CG CD OE1 OE2 REMARK 470 GLU C 12 CG CD OE1 OE2 REMARK 470 GLN C 13 CG CD OE1 NE2 REMARK 470 LYS C 15 CG CD CE NZ REMARK 470 ASN C 16 CG OD1 ND2 REMARK 470 GLN C 17 CG CD OE1 NE2 REMARK 470 ARG C 19 CG CD NE CZ NH1 NH2 REMARK 470 ASP C 20 CG OD1 OD2 REMARK 470 LYS C 23 CG CD CE NZ REMARK 470 CYS C 25 SG REMARK 470 LEU C 30 CG CD1 CD2 REMARK 470 GLN C 32 CG CD OE1 NE2 REMARK 470 THR C 34 OG1 CG2 REMARK 470 ASN C 36 CG OD1 ND2 REMARK 470 ASP C 38 CG OD1 OD2 REMARK 470 ARG C 42 CG CD NE CZ NH1 NH2 REMARK 470 GLN C 44 CG CD OE1 NE2 REMARK 470 ARG C 46 CG CD NE CZ NH1 NH2 REMARK 470 LYS C 57 CG CD CE NZ REMARK 470 ARG C 96 CG CD NE CZ NH1 NH2 REMARK 470 SER C 97 OG REMARK 470 ASP C 170 CG OD1 OD2 REMARK 470 GLU C 172 CG CD OE1 OE2 REMARK 470 THR C 173 OG1 CG2 REMARK 470 THR C 196 OG1 CG2 REMARK 470 ARG C 197 CG CD NE CZ NH1 NH2 REMARK 470 ARG C 214 CG CD NE CZ NH1 NH2 REMARK 470 MET C 217 CG SD CE REMARK 470 THR C 221 OG1 CG2 REMARK 470 GLU C 226 CG CD OE1 OE2 REMARK 470 SER C 245 OG REMARK 470 ARG C 256 CG CD NE CZ NH1 NH2 REMARK 470 SER C 265 OG REMARK 470 ASP C 267 CG OD1 OD2 REMARK 470 ASN C 268 CG OD1 ND2 REMARK 470 ASP C 303 CG OD1 OD2 REMARK 470 SER C 331 OG REMARK 470 ARG D 13 CG CD NE CZ NH1 NH2 REMARK 470 LYS D 14 CG CD CE NZ REMARK 470 VAL D 16 CG1 CG2 REMARK 470 GLU D 17 CG CD OE1 OE2 REMARK 470 GLN D 18 CG CD OE1 NE2 REMARK 470 LYS D 20 CG CD CE NZ REMARK 470 MET D 21 CG SD CE REMARK 470 GLU D 22 CG CD OE1 OE2 REMARK 470 ASN D 24 CG OD1 ND2 REMARK 470 ILE D 28 CG1 CG2 CD1 REMARK 470 LYS D 29 CG CD CE NZ REMARK 470 SER D 31 OG REMARK 470 LYS D 32 CG CD CE NZ REMARK 470 ASP D 36 CG OD1 OD2 REMARK 470 MET D 38 CG SD CE REMARK 470 GLU D 42 CG CD OE1 OE2 REMARK 470 LYS D 46 CG CD CE NZ REMARK 470 GLU D 47 CG CD OE1 OE2 REMARK 470 THR D 52 OG1 CG2 REMARK 470 VAL D 54 CG1 CG2 REMARK 470 SER D 57 OG REMARK 470 GLU D 58 CG CD OE1 OE2 REMARK 470 GLU E 42 CG CD OE1 OE2 REMARK 470 LYS E 43 CG CD CE NZ REMARK 470 LYS E 65 CG CD CE NZ REMARK 470 SER E 71 OG REMARK 470 LYS E 76 CG CD CE NZ REMARK 470 GLU E 89 CG CD OE1 OE2 REMARK 470 THR E 91 OG1 CG2 REMARK 470 VAL E 119 CG1 CG2 REMARK 470 THR E 132 OG1 CG2 REMARK 470 SER E 134 OG REMARK 470 VAL E 137 CG1 CG2 REMARK 470 THR E 138 OG1 CG2 REMARK 470 GLU E 141 CG CD OE1 OE2 REMARK 470 THR E 160 OG1 CG2 REMARK 470 SER E 185 OG REMARK 470 SER E 196 OG REMARK 470 ARG E 206 CG CD NE CZ NH1 NH2 REMARK 470 GLU E 208 CG CD OE1 OE2 REMARK 470 GLU E 210 CG CD OE1 OE2 REMARK 470 GLU E 222 CG CD OE1 OE2 REMARK 470 TYR E 223 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU E 234 CG CD OE1 OE2 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 LEU A 191 58.66 -98.81 REMARK 500 PHE B 98 50.24 -91.60 REMARK 500 THR C 87 -7.25 72.69 REMARK 500 ASP C 246 45.22 -88.90 REMARK 500 ALA C 309 31.82 -98.23 REMARK 500 SER E 99 112.74 -160.45 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-61986 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF ATP-BOUND P2Y PURINOCEPTOR 2-MINIGO-SCFV16 REMARK 900 COMPLEX DBREF 9K20 A 1 377 UNP P41231 P2RY2_HUMAN 1 377 DBREF 9K20 B 1 55 UNP P09471 GNAO_HUMAN 4 57 DBREF 9K20 B 64 226 UNP P09471 GNAO_HUMAN 182 354 DBREF 9K20 C 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 9K20 D 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 9K20 E -19 257 PDB 9K20 9K20 -19 257 SEQADV 9K20 MET A -23 UNP P41231 INITIATING METHIONINE SEQADV 9K20 LYS A -22 UNP P41231 EXPRESSION TAG SEQADV 9K20 THR A -21 UNP P41231 EXPRESSION TAG SEQADV 9K20 ILE A -20 UNP P41231 EXPRESSION TAG SEQADV 9K20 ILE A -19 UNP P41231 EXPRESSION TAG SEQADV 9K20 ALA A -18 UNP P41231 EXPRESSION TAG SEQADV 9K20 LEU A -17 UNP P41231 EXPRESSION TAG SEQADV 9K20 SER A -16 UNP P41231 EXPRESSION TAG SEQADV 9K20 TYR A -15 UNP P41231 EXPRESSION TAG SEQADV 9K20 ILE A -14 UNP P41231 EXPRESSION TAG SEQADV 9K20 PHE A -13 UNP P41231 EXPRESSION TAG SEQADV 9K20 CYS A -12 UNP P41231 EXPRESSION TAG SEQADV 9K20 LEU A -11 UNP P41231 EXPRESSION TAG SEQADV 9K20 VAL A -10 UNP P41231 EXPRESSION TAG SEQADV 9K20 PHE A -9 UNP P41231 EXPRESSION TAG SEQADV 9K20 ALA A -8 UNP P41231 EXPRESSION TAG SEQADV 9K20 ASP A -7 UNP P41231 EXPRESSION TAG SEQADV 9K20 TYR A -6 UNP P41231 EXPRESSION TAG SEQADV 9K20 LYS A -5 UNP P41231 EXPRESSION TAG SEQADV 9K20 ASP A -4 UNP P41231 EXPRESSION TAG SEQADV 9K20 ASP A -3 UNP P41231 EXPRESSION TAG SEQADV 9K20 ASP A -2 UNP P41231 EXPRESSION TAG SEQADV 9K20 ASP A -1 UNP P41231 EXPRESSION TAG SEQADV 9K20 ALA A 0 UNP P41231 EXPRESSION TAG SEQADV 9K20 LEU A 46 UNP P41231 PRO 46 CONFLICT SEQADV 9K20 ASN A 302 UNP P41231 ASP 302 ENGINEERED MUTATION SEQADV 9K20 SER A 312 UNP P41231 ARG 312 CONFLICT SEQADV 9K20 HIS A 378 UNP P41231 EXPRESSION TAG SEQADV 9K20 HIS A 379 UNP P41231 EXPRESSION TAG SEQADV 9K20 HIS A 380 UNP P41231 EXPRESSION TAG SEQADV 9K20 HIS A 381 UNP P41231 EXPRESSION TAG SEQADV 9K20 HIS A 382 UNP P41231 EXPRESSION TAG SEQADV 9K20 HIS A 383 UNP P41231 EXPRESSION TAG SEQADV 9K20 GLY A 384 UNP P41231 EXPRESSION TAG SEQADV 9K20 GLY A 385 UNP P41231 EXPRESSION TAG SEQADV 9K20 SER A 386 UNP P41231 EXPRESSION TAG SEQADV 9K20 GLY A 387 UNP P41231 EXPRESSION TAG SEQADV 9K20 GLY A 388 UNP P41231 EXPRESSION TAG SEQADV 9K20 LEU A 389 UNP P41231 EXPRESSION TAG SEQADV 9K20 GLU A 390 UNP P41231 EXPRESSION TAG SEQADV 9K20 VAL A 391 UNP P41231 EXPRESSION TAG SEQADV 9K20 LEU A 392 UNP P41231 EXPRESSION TAG SEQADV 9K20 PHE A 393 UNP P41231 EXPRESSION TAG SEQADV 9K20 GLN A 394 UNP P41231 EXPRESSION TAG SEQADV 9K20 GLY A 395 UNP P41231 EXPRESSION TAG SEQADV 9K20 PRO A 396 UNP P41231 EXPRESSION TAG SEQADV 9K20 ASP B 6 UNP P09471 GLU 9 CONFLICT SEQADV 9K20 LYS B 7 UNP P09471 ARG 10 CONFLICT SEQADV 9K20 VAL B 10 UNP P09471 LEU 13 CONFLICT SEQADV 9K20 MET B 15 UNP P09471 INSERTION SEQADV 9K20 GLY B 16 UNP P09471 ALA 18 CONFLICT SEQADV 9K20 ASP B 40 UNP P09471 GLY 42 CONFLICT SEQADV 9K20 ASN B 41 UNP P09471 GLU 43 CONFLICT SEQADV 9K20 GLY B 56 UNP P09471 LINKER SEQADV 9K20 GLY B 57 UNP P09471 LINKER SEQADV 9K20 SER B 58 UNP P09471 LINKER SEQADV 9K20 GLY B 59 UNP P09471 LINKER SEQADV 9K20 GLY B 60 UNP P09471 LINKER SEQADV 9K20 SER B 61 UNP P09471 LINKER SEQADV 9K20 GLY B 62 UNP P09471 LINKER SEQADV 9K20 GLY B 63 UNP P09471 LINKER SEQADV 9K20 ASP B 109 UNP P09471 ALA 227 CONFLICT SEQADV 9K20 ASP B 112 UNP P09471 GLY 230 CONFLICT SEQADV 9K20 B UNP P09471 ASP 232 DELETION SEQADV 9K20 B UNP P09471 GLN 233 DELETION SEQADV 9K20 B UNP P09471 VAL 234 DELETION SEQADV 9K20 B UNP P09471 LEU 235 DELETION SEQADV 9K20 B UNP P09471 HIS 236 DELETION SEQADV 9K20 B UNP P09471 GLU 237 DELETION SEQADV 9K20 B UNP P09471 ASP 238 DELETION SEQADV 9K20 B UNP P09471 GLU 239 DELETION SEQADV 9K20 B UNP P09471 THR 240 DELETION SEQADV 9K20 B UNP P09471 THR 241 DELETION SEQADV 9K20 ASP B 122 UNP P09471 LEU 250 CONFLICT SEQADV 9K20 ALA B 204 UNP P09471 ILE 332 CONFLICT SEQADV 9K20 ILE B 207 UNP P09471 VAL 335 CONFLICT SEQADV 9K20 MET C -17 UNP P62873 INITIATING METHIONINE SEQADV 9K20 HIS C -16 UNP P62873 EXPRESSION TAG SEQADV 9K20 HIS C -15 UNP P62873 EXPRESSION TAG SEQADV 9K20 HIS C -14 UNP P62873 EXPRESSION TAG SEQADV 9K20 HIS C -13 UNP P62873 EXPRESSION TAG SEQADV 9K20 HIS C -12 UNP P62873 EXPRESSION TAG SEQADV 9K20 HIS C -11 UNP P62873 EXPRESSION TAG SEQADV 9K20 LEU C -10 UNP P62873 EXPRESSION TAG SEQADV 9K20 GLU C -9 UNP P62873 EXPRESSION TAG SEQADV 9K20 VAL C -8 UNP P62873 EXPRESSION TAG SEQADV 9K20 LEU C -7 UNP P62873 EXPRESSION TAG SEQADV 9K20 PHE C -6 UNP P62873 EXPRESSION TAG SEQADV 9K20 GLN C -5 UNP P62873 EXPRESSION TAG SEQADV 9K20 GLY C -4 UNP P62873 EXPRESSION TAG SEQADV 9K20 PRO C -3 UNP P62873 EXPRESSION TAG SEQADV 9K20 GLY C -2 UNP P62873 EXPRESSION TAG SEQADV 9K20 SER C -1 UNP P62873 EXPRESSION TAG SEQADV 9K20 SER C 0 UNP P62873 EXPRESSION TAG SEQADV 9K20 GLY C 1 UNP P62873 EXPRESSION TAG SEQRES 1 A 420 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU SEQRES 2 A 420 VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP ALA MET ALA SEQRES 3 A 420 ALA ASP LEU GLY PRO TRP ASN ASP THR ILE ASN GLY THR SEQRES 4 A 420 TRP ASP GLY ASP GLU LEU GLY TYR ARG CYS ARG PHE ASN SEQRES 5 A 420 GLU ASP PHE LYS TYR VAL LEU LEU PRO VAL SER TYR GLY SEQRES 6 A 420 VAL VAL CYS VAL LEU GLY LEU CYS LEU ASN ALA VAL ALA SEQRES 7 A 420 LEU TYR ILE PHE LEU CYS ARG LEU LYS THR TRP ASN ALA SEQRES 8 A 420 SER THR THR TYR MET PHE HIS LEU ALA VAL SER ASP ALA SEQRES 9 A 420 LEU TYR ALA ALA SER LEU PRO LEU LEU VAL TYR TYR TYR SEQRES 10 A 420 ALA ARG GLY ASP HIS TRP PRO PHE SER THR VAL LEU CYS SEQRES 11 A 420 LYS LEU VAL ARG PHE LEU PHE TYR THR ASN LEU TYR CYS SEQRES 12 A 420 SER ILE LEU PHE LEU THR CYS ILE SER VAL HIS ARG CYS SEQRES 13 A 420 LEU GLY VAL LEU ARG PRO LEU ARG SER LEU ARG TRP GLY SEQRES 14 A 420 ARG ALA ARG TYR ALA ARG ARG VAL ALA GLY ALA VAL TRP SEQRES 15 A 420 VAL LEU VAL LEU ALA CYS GLN ALA PRO VAL LEU TYR PHE SEQRES 16 A 420 VAL THR THR SER ALA ARG GLY GLY ARG VAL THR CYS HIS SEQRES 17 A 420 ASP THR SER ALA PRO GLU LEU PHE SER ARG PHE VAL ALA SEQRES 18 A 420 TYR SER SER VAL MET LEU GLY LEU LEU PHE ALA VAL PRO SEQRES 19 A 420 PHE ALA VAL ILE LEU VAL CYS TYR VAL LEU MET ALA ARG SEQRES 20 A 420 ARG LEU LEU LYS PRO ALA TYR GLY THR SER GLY GLY LEU SEQRES 21 A 420 PRO ARG ALA LYS ARG LYS SER VAL ARG THR ILE ALA VAL SEQRES 22 A 420 VAL LEU ALA VAL PHE ALA LEU CYS PHE LEU PRO PHE HIS SEQRES 23 A 420 VAL THR ARG THR LEU TYR TYR SER PHE ARG SER LEU ASP SEQRES 24 A 420 LEU SER CYS HIS THR LEU ASN ALA ILE ASN MET ALA TYR SEQRES 25 A 420 LYS VAL THR ARG PRO LEU ALA SER ALA ASN SER CYS LEU SEQRES 26 A 420 ASN PRO VAL LEU TYR PHE LEU ALA GLY GLN SER LEU VAL SEQRES 27 A 420 ARG PHE ALA ARG ASP ALA LYS PRO PRO THR GLY PRO SER SEQRES 28 A 420 PRO ALA THR PRO ALA ARG ARG ARG LEU GLY LEU ARG ARG SEQRES 29 A 420 SER ASP ARG THR ASP MET GLN ARG ILE GLU ASP VAL LEU SEQRES 30 A 420 GLY SER SER GLU ASP SER ARG ARG THR GLU SER THR PRO SEQRES 31 A 420 ALA GLY SER GLU ASN THR LYS ASP ILE ARG LEU HIS HIS SEQRES 32 A 420 HIS HIS HIS HIS GLY GLY SER GLY GLY LEU GLU VAL LEU SEQRES 33 A 420 PHE GLN GLY PRO SEQRES 1 B 226 THR LEU SER ALA GLU ASP LYS ALA ALA VAL GLU ARG SER SEQRES 2 B 226 LYS MET GLY ILE GLU LYS ASN LEU LYS GLU ASP GLY ILE SEQRES 3 B 226 SER ALA ALA LYS ASP VAL LYS LEU LEU LEU LEU GLY ALA SEQRES 4 B 226 ASP ASN SER GLY LYS SER THR ILE VAL LYS GLN MET LYS SEQRES 5 B 226 ILE ILE HIS GLY GLY SER GLY GLY SER GLY GLY THR THR SEQRES 6 B 226 GLY ILE VAL GLU THR HIS PHE THR PHE LYS ASN LEU HIS SEQRES 7 B 226 PHE ARG LEU PHE ASP VAL GLY GLY GLN ARG SER GLU ARG SEQRES 8 B 226 LYS LYS TRP ILE HIS CYS PHE GLU ASP VAL THR ALA ILE SEQRES 9 B 226 ILE PHE CYS VAL ASP LEU SER ASP TYR ASN ARG MET HIS SEQRES 10 B 226 GLU SER LEU MET ASP PHE ASP SER ILE CYS ASN ASN LYS SEQRES 11 B 226 PHE PHE ILE ASP THR SER ILE ILE LEU PHE LEU ASN LYS SEQRES 12 B 226 LYS ASP LEU PHE GLY GLU LYS ILE LYS LYS SER PRO LEU SEQRES 13 B 226 THR ILE CYS PHE PRO GLU TYR THR GLY PRO ASN THR TYR SEQRES 14 B 226 GLU ASP ALA ALA ALA TYR ILE GLN ALA GLN PHE GLU SER SEQRES 15 B 226 LYS ASN ARG SER PRO ASN LYS GLU ILE TYR CYS HIS MET SEQRES 16 B 226 THR CYS ALA THR ASP THR ASN ASN ALA GLN VAL ILE PHE SEQRES 17 B 226 ASP ALA VAL THR ASP ILE ILE ILE ALA ASN ASN LEU ARG SEQRES 18 B 226 GLY CYS GLY LEU TYR SEQRES 1 C 358 MET HIS HIS HIS HIS HIS HIS LEU GLU VAL LEU PHE GLN SEQRES 2 C 358 GLY PRO GLY SER SER GLY SER GLU LEU ASP GLN LEU ARG SEQRES 3 C 358 GLN GLU ALA GLU GLN LEU LYS ASN GLN ILE ARG ASP ALA SEQRES 4 C 358 ARG LYS ALA CYS ALA ASP ALA THR LEU SER GLN ILE THR SEQRES 5 C 358 ASN ASN ILE ASP PRO VAL GLY ARG ILE GLN MET ARG THR SEQRES 6 C 358 ARG ARG THR LEU ARG GLY HIS LEU ALA LYS ILE TYR ALA SEQRES 7 C 358 MET HIS TRP GLY THR ASP SER ARG LEU LEU VAL SER ALA SEQRES 8 C 358 SER GLN ASP GLY LYS LEU ILE ILE TRP ASP SER TYR THR SEQRES 9 C 358 THR ASN LYS VAL HIS ALA ILE PRO LEU ARG SER SER TRP SEQRES 10 C 358 VAL MET THR CYS ALA TYR ALA PRO SER GLY ASN TYR VAL SEQRES 11 C 358 ALA CYS GLY GLY LEU ASP ASN ILE CYS SER ILE TYR ASN SEQRES 12 C 358 LEU LYS THR ARG GLU GLY ASN VAL ARG VAL SER ARG GLU SEQRES 13 C 358 LEU ALA GLY HIS THR GLY TYR LEU SER CYS CYS ARG PHE SEQRES 14 C 358 LEU ASP ASP ASN GLN ILE VAL THR SER SER GLY ASP THR SEQRES 15 C 358 THR CYS ALA LEU TRP ASP ILE GLU THR GLY GLN GLN THR SEQRES 16 C 358 THR THR PHE THR GLY HIS THR GLY ASP VAL MET SER LEU SEQRES 17 C 358 SER LEU ALA PRO ASP THR ARG LEU PHE VAL SER GLY ALA SEQRES 18 C 358 CYS ASP ALA SER ALA LYS LEU TRP ASP VAL ARG GLU GLY SEQRES 19 C 358 MET CYS ARG GLN THR PHE THR GLY HIS GLU SER ASP ILE SEQRES 20 C 358 ASN ALA ILE CYS PHE PHE PRO ASN GLY ASN ALA PHE ALA SEQRES 21 C 358 THR GLY SER ASP ASP ALA THR CYS ARG LEU PHE ASP LEU SEQRES 22 C 358 ARG ALA ASP GLN GLU LEU MET THR TYR SER HIS ASP ASN SEQRES 23 C 358 ILE ILE CYS GLY ILE THR SER VAL SER PHE SER LYS SER SEQRES 24 C 358 GLY ARG LEU LEU LEU ALA GLY TYR ASP ASP PHE ASN CYS SEQRES 25 C 358 ASN VAL TRP ASP ALA LEU LYS ALA ASP ARG ALA GLY VAL SEQRES 26 C 358 LEU ALA GLY HIS ASP ASN ARG VAL SER CYS LEU GLY VAL SEQRES 27 C 358 THR ASP ASP GLY MET ALA VAL ALA THR GLY SER TRP ASP SEQRES 28 C 358 SER PHE LEU LYS ILE TRP ASN SEQRES 1 D 71 MET ALA SER ASN ASN THR ALA SER ILE ALA GLN ALA ARG SEQRES 2 D 71 LYS LEU VAL GLU GLN LEU LYS MET GLU ALA ASN ILE ASP SEQRES 3 D 71 ARG ILE LYS VAL SER LYS ALA ALA ALA ASP LEU MET ALA SEQRES 4 D 71 TYR CYS GLU ALA HIS ALA LYS GLU ASP PRO LEU LEU THR SEQRES 5 D 71 PRO VAL PRO ALA SER GLU ASN PRO PHE ARG GLU LYS LYS SEQRES 6 D 71 PHE PHE CYS ALA ILE LEU SEQRES 1 E 289 MET VAL SER ALA ILE VAL LEU TYR VAL LEU LEU ALA ALA SEQRES 2 E 289 ALA ALA HIS SER ALA PHE ALA ASP VAL GLN LEU VAL GLU SEQRES 3 E 289 SER GLY GLY GLY LEU VAL GLN PRO GLY GLY SER ARG LYS SEQRES 4 E 289 LEU SER CYS SER ALA SER GLY PHE ALA PHE SER SER PHE SEQRES 5 E 289 GLY MET HIS TRP VAL ARG GLN ALA PRO GLU LYS GLY LEU SEQRES 6 E 289 GLU TRP VAL ALA TYR ILE SER SER GLY SER GLY THR ILE SEQRES 7 E 289 TYR TYR ALA ASP THR VAL LYS GLY ARG PHE THR ILE SER SEQRES 8 E 289 ARG ASP ASP PRO LYS ASN THR LEU PHE LEU GLN MET THR SEQRES 9 E 289 SER LEU ARG SER GLU ASP THR ALA MET TYR TYR CYS VAL SEQRES 10 E 289 ARG SER ILE TYR TYR TYR GLY SER SER PRO PHE ASP PHE SEQRES 11 E 289 TRP GLY GLN GLY THR THR LEU THR VAL SER SER GLY GLY SEQRES 12 E 289 GLY GLY SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER SEQRES 13 E 289 ASP ILE VAL MET THR GLN ALA THR SER SER VAL PRO VAL SEQRES 14 E 289 THR PRO GLY GLU SER VAL SER ILE SER CYS ARG SER SER SEQRES 15 E 289 LYS SER LEU LEU HIS SER ASN GLY ASN THR TYR LEU TYR SEQRES 16 E 289 TRP PHE LEU GLN ARG PRO GLY GLN SER PRO GLN LEU LEU SEQRES 17 E 289 ILE TYR ARG MET SER ASN LEU ALA SER GLY VAL PRO ASP SEQRES 18 E 289 ARG PHE SER GLY SER GLY SER GLY THR ALA PHE THR LEU SEQRES 19 E 289 THR ILE SER ARG LEU GLU ALA GLU ASP VAL GLY VAL TYR SEQRES 20 E 289 TYR CYS MET GLN HIS LEU GLU TYR PRO LEU THR PHE GLY SEQRES 21 E 289 ALA GLY THR LYS LEU GLU LEU LYS GLY SER LEU GLU VAL SEQRES 22 E 289 LEU PHE GLN GLY PRO ALA ALA ALA HIS HIS HIS HIS HIS SEQRES 23 E 289 HIS HIS HIS HET ATP A 401 31 HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE FORMUL 6 ATP C10 H16 N5 O13 P3 HELIX 1 AA1 PHE A 31 ARG A 61 1 31 HELIX 2 AA2 SER A 68 SER A 85 1 18 HELIX 3 AA3 SER A 85 ARG A 95 1 11 HELIX 4 AA4 SER A 102 ARG A 137 1 36 HELIX 5 AA5 ARG A 137 ARG A 143 1 7 HELIX 6 AA6 ALA A 147 ALA A 166 1 20 HELIX 7 AA7 ALA A 166 VAL A 172 1 7 HELIX 8 AA8 LEU A 191 LEU A 226 1 36 HELIX 9 AA9 PRO A 237 LEU A 274 1 38 HELIX 10 AB1 SER A 277 LEU A 308 1 32 HELIX 11 AB2 SER B 3 GLY B 16 1 14 HELIX 12 AB3 GLY B 16 ALA B 29 1 14 HELIX 13 AB4 GLY B 43 LYS B 52 1 10 HELIX 14 AB5 GLU B 90 TRP B 94 5 5 HELIX 15 AB6 TYR B 113 ASN B 128 1 16 HELIX 16 AB7 ASN B 129 ILE B 133 5 5 HELIX 17 AB8 LYS B 143 LYS B 152 1 10 HELIX 18 AB9 PRO B 155 CYS B 159 5 5 HELIX 19 AC1 THR B 168 SER B 182 1 15 HELIX 20 AC2 ASN B 202 CYS B 223 1 22 HELIX 21 AC3 ALA C 11 ALA C 26 1 16 HELIX 22 AC4 THR C 29 THR C 34 1 6 HELIX 23 AC5 ASN C 35 ILE C 37 5 3 HELIX 24 AC6 ARG D 13 GLU D 22 1 10 HELIX 25 AC7 LYS D 29 HIS D 44 1 16 HELIX 26 AC8 ALA E 28 PHE E 32 5 5 HELIX 27 AC9 ARG E 87 THR E 91 5 5 SHEET 1 AA1 2 THR A 174 ALA A 176 0 SHEET 2 AA1 2 VAL A 181 CYS A 183 -1 O THR A 182 N SER A 175 SHEET 1 AA2 6 VAL B 68 THR B 73 0 SHEET 2 AA2 6 HIS B 78 ASP B 83 -1 O LEU B 81 N THR B 70 SHEET 3 AA2 6 ASP B 31 LEU B 37 1 N VAL B 32 O HIS B 78 SHEET 4 AA2 6 ALA B 103 ASP B 109 1 O ILE B 105 N LEU B 35 SHEET 5 AA2 6 ILE B 137 ASN B 142 1 O PHE B 140 N PHE B 106 SHEET 6 AA2 6 HIS B 194 MET B 195 1 O HIS B 194 N LEU B 141 SHEET 1 AA3 4 ARG C 46 LEU C 51 0 SHEET 2 AA3 4 LEU C 336 ASN C 340 -1 O ILE C 338 N ARG C 48 SHEET 3 AA3 4 VAL C 327 GLY C 330 -1 N VAL C 327 O TRP C 339 SHEET 4 AA3 4 CYS C 317 VAL C 320 -1 N GLY C 319 O ALA C 328 SHEET 1 AA4 4 ILE C 58 TRP C 63 0 SHEET 2 AA4 4 LEU C 69 SER C 74 -1 O VAL C 71 N HIS C 62 SHEET 3 AA4 4 LYS C 78 ASP C 83 -1 O TRP C 82 N LEU C 70 SHEET 4 AA4 4 LYS C 89 PRO C 94 -1 O ILE C 93 N LEU C 79 SHEET 1 AA5 4 VAL C 100 TYR C 105 0 SHEET 2 AA5 4 TYR C 111 GLY C 116 -1 O GLY C 115 N MET C 101 SHEET 3 AA5 4 ILE C 120 ASN C 125 -1 O TYR C 124 N VAL C 112 SHEET 4 AA5 4 ARG C 134 ALA C 140 -1 O SER C 136 N ILE C 123 SHEET 1 AA6 4 LEU C 146 PHE C 151 0 SHEET 2 AA6 4 GLN C 156 SER C 161 -1 O VAL C 158 N ARG C 150 SHEET 3 AA6 4 THR C 165 ASP C 170 -1 O TRP C 169 N ILE C 157 SHEET 4 AA6 4 GLN C 175 THR C 181 -1 O PHE C 180 N CYS C 166 SHEET 1 AA7 4 VAL C 187 LEU C 192 0 SHEET 2 AA7 4 LEU C 198 ALA C 203 -1 O GLY C 202 N MET C 188 SHEET 3 AA7 4 ALA C 208 ASP C 212 -1 O TRP C 211 N PHE C 199 SHEET 4 AA7 4 CYS C 218 PHE C 222 -1 O PHE C 222 N ALA C 208 SHEET 1 AA8 4 ILE C 229 PHE C 234 0 SHEET 2 AA8 4 ALA C 240 SER C 245 -1 O GLY C 244 N ASN C 230 SHEET 3 AA8 4 CYS C 250 ASP C 254 -1 O PHE C 253 N PHE C 241 SHEET 4 AA8 4 GLN C 259 TYR C 264 -1 O TYR C 264 N CYS C 250 SHEET 1 AA9 4 ILE C 273 PHE C 278 0 SHEET 2 AA9 4 LEU C 284 TYR C 289 -1 O LEU C 286 N SER C 277 SHEET 3 AA9 4 CYS C 294 ASP C 298 -1 O TRP C 297 N LEU C 285 SHEET 4 AA9 4 ARG C 304 VAL C 307 -1 O ALA C 305 N VAL C 296 SHEET 1 AB1 4 GLN E 3 SER E 7 0 SHEET 2 AB1 4 SER E 17 SER E 25 -1 O SER E 23 N VAL E 5 SHEET 3 AB1 4 THR E 78 THR E 84 -1 O LEU E 81 N LEU E 20 SHEET 4 AB1 4 PHE E 68 ASP E 73 -1 N SER E 71 O PHE E 80 SHEET 1 AB2 2 LEU E 11 VAL E 12 0 SHEET 2 AB2 2 THR E 118 VAL E 119 1 O THR E 118 N VAL E 12 SHEET 1 AB3 5 ILE E 58 TYR E 60 0 SHEET 2 AB3 5 GLY E 44 ILE E 51 -1 N TYR E 50 O TYR E 59 SHEET 3 AB3 5 GLY E 33 ALA E 40 -1 N ARG E 38 O GLU E 46 SHEET 4 AB3 5 MET E 93 SER E 99 -1 O TYR E 95 N VAL E 37 SHEET 5 AB3 5 PHE E 110 TRP E 111 -1 O PHE E 110 N ARG E 98 SHEET 1 AB4 5 ILE E 58 TYR E 60 0 SHEET 2 AB4 5 GLY E 44 ILE E 51 -1 N TYR E 50 O TYR E 59 SHEET 3 AB4 5 GLY E 33 ALA E 40 -1 N ARG E 38 O GLU E 46 SHEET 4 AB4 5 MET E 93 SER E 99 -1 O TYR E 95 N VAL E 37 SHEET 5 AB4 5 THR E 115 THR E 116 -1 O THR E 115 N TYR E 94 SHEET 1 AB5 4 MET E 128 THR E 129 0 SHEET 2 AB5 4 VAL E 143 SER E 149 -1 O ARG E 148 N THR E 129 SHEET 3 AB5 4 ALA E 199 ILE E 204 -1 O LEU E 202 N ILE E 145 SHEET 4 AB5 4 PHE E 191 SER E 194 -1 N SER E 194 O THR E 201 SHEET 1 AB6 5 SER E 134 PRO E 136 0 SHEET 2 AB6 5 THR E 231 GLU E 234 1 O GLU E 234 N VAL E 135 SHEET 3 AB6 5 GLY E 213 GLN E 219 -1 N TYR E 215 O THR E 231 SHEET 4 AB6 5 LEU E 162 GLN E 167 -1 N GLN E 167 O VAL E 214 SHEET 5 AB6 5 PRO E 173 ILE E 177 -1 O ILE E 177 N TRP E 164 SSBOND 1 CYS A 25 CYS A 278 1555 1555 2.03 SSBOND 2 CYS A 106 CYS A 183 1555 1555 2.02 SSBOND 3 CYS E 22 CYS E 96 1555 1555 2.03 SSBOND 4 CYS E 147 CYS E 217 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