HEADER SIGNALING PROTEIN 10-DEC-24 9KZK TITLE STRUCTURE OF MOUSE C3A BOUND MOUSE C3AR IN COMPLEX WITH GO COMPND MOL_ID: 1; COMPND 2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(O) SUBUNIT ALPHA; COMPND 3 CHAIN: A; COMPND 4 EC: 3.6.5.-; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: 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 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 3; COMPND 14 MOLECULE: C3A ANAPHYLATOXIN; COMPND 15 CHAIN: D; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 4; COMPND 18 MOLECULE: MUSCARINIC ACETYLCHOLINE RECEPTOR M4,C3A ANAPHYLATOXIN COMPND 19 CHEMOTACTIC RECEPTOR; COMPND 20 CHAIN: E; COMPND 21 SYNONYM: C3AR,C3A-R,COMPLEMENT COMPONENT 3A RECEPTOR 1; COMPND 22 ENGINEERED: YES; COMPND 23 MOL_ID: 5; COMPND 24 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 25 GAMMA-2; COMPND 26 CHAIN: G; COMPND 27 SYNONYM: G GAMMA-I; COMPND 28 ENGINEERED: YES; COMPND 29 MOL_ID: 6; COMPND 30 MOLECULE: ANTIBODY FRAGMENT - SCFV16; COMPND 31 CHAIN: H; COMPND 32 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: GNAO1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 GENE: GNB1; SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 17 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 18 ORGANISM_TAXID: 10090; SOURCE 19 GENE: C3; SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS, MUS MUSCULUS; SOURCE 24 ORGANISM_COMMON: HUMAN, HOUSE MOUSE; SOURCE 25 ORGANISM_TAXID: 9606, 10090; SOURCE 26 GENE: CHRM4, C3AR1, C3R1; SOURCE 27 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 29 MOL_ID: 5; SOURCE 30 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 31 ORGANISM_COMMON: HUMAN; SOURCE 32 ORGANISM_TAXID: 9606; SOURCE 33 GENE: GNG2; SOURCE 34 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 35 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 36 MOL_ID: 6; SOURCE 37 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 38 ORGANISM_TAXID: 10090; SOURCE 39 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 40 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS GPCR, G PROTEIN, SIGNALING PROTEIN, BETA-ARRESTIN EXPDTA ELECTRON MICROSCOPY AUTHOR R.BANERJEE,R.YADAV,M.K.YADAV,M.GANGULY,S.MISHRA,A.DALAL,C.GATI, AUTHOR 2 A.K.SHUKLA REVDAT 1 26-NOV-25 9KZK 0 JRNL AUTH S.MISHRA,M.K.YADAV,A.DALAL,M.GANGULY,R.YADAV,K.SAWADA, JRNL AUTH 2 D.TIWARI,N.ROY,N.BANERJEE,J.N.FUNG,J.MARALLAG,C.S.CUI, JRNL AUTH 3 X.X.LI,J.D.LEE,C.A.DSOUZA,S.SAHA,P.SARMA,G.RAWAT,H.ZHU, JRNL AUTH 4 H.A.KHANT,R.J.CLARK,F.K.SANO,R.BANERJEE,T.M.WOODRUFF, JRNL AUTH 5 O.NUREKI,C.GATI,A.K.SHUKLA JRNL TITL MOLECULAR FINGERPRINTS OF A CONVERGENT MECHANISM JRNL TITL 2 ORCHESTRATING DIVERSE LIGAND RECOGNITION AND JRNL TITL 3 SPECIES-SPECIFIC PHARMACOLOGY AT THE COMPLEMENT JRNL TITL 4 ANAPHYLATOXIN RECEPTORS. JRNL REF BIORXIV 2025 JRNL REFN ISSN 2692-8205 JRNL PMID 40501890 JRNL DOI 10.1101/2025.05.26.656101 REMARK 2 REMARK 2 RESOLUTION. 3.54 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, EPU, CRYOSPARC, COOT, REMARK 3 PHENIX, CRYOSPARC, CRYOSPARC, CRYOSPARC, REMARK 3 CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 9KV6 REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE FIT 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) : 3.540 REMARK 3 NUMBER OF PARTICLES : 175697 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9KZK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1300054605. 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 : MOUSE C3A BOUND MOUSE C3AR IN REMARK 245 COMPLEX WITH GO; MOUSE C3A REMARK 245 ANAPHYLATOXIN; GUANINE REMARK 245 NUCLEOTIDE-BINDING PROTEIN G(O) REMARK 245 SUBUNIT ALPHA; GUANINE REMARK 245 NUCLEOTIDE-BINDING PROTEIN G(I)/ REMARK 245 G(S)/G(O) SUBUNIT GAMMA-2; REMARK 245 GUANINE NUCLEOTIDE-BINDING REMARK 245 PROTEIN G(I)/G(S)/G(T) SUBUNIT REMARK 245 BETA-1; ANTIBODY FRAGMENT - REMARK 245 SCFV16; MOUSE C3A ANAPHYLATOXIN REMARK 245 CHEMOTACTIC RECEPTOR 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 : 7.40 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 GLACIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 3000.00 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) : 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: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, E, G, H 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 -11 REMARK 465 GLY A -10 REMARK 465 HIS A -9 REMARK 465 HIS A -8 REMARK 465 HIS A -7 REMARK 465 HIS A -6 REMARK 465 HIS A -5 REMARK 465 HIS A -4 REMARK 465 GLU A -3 REMARK 465 ASN A -2 REMARK 465 LEU A -1 REMARK 465 TYR A 0 REMARK 465 PHE A 1 REMARK 465 GLN A 2 REMARK 465 GLY A 3 REMARK 465 THR A 4 REMARK 465 LEU A 5 REMARK 465 ILE A 172 REMARK 465 HIS A 173 REMARK 465 GLY A 174 REMARK 465 GLY A 175 REMARK 465 SER A 176 REMARK 465 GLY A 177 REMARK 465 GLY A 178 REMARK 465 SER A 179 REMARK 465 GLY A 180 REMARK 465 GLY A 181 REMARK 465 THR A 182 REMARK 465 TYR A 231 REMARK 465 ASP A 232 REMARK 465 GLN A 233 REMARK 465 VAL A 234 REMARK 465 LEU A 235 REMARK 465 HIS A 236 REMARK 465 GLU A 237 REMARK 465 ASP A 238 REMARK 465 GLU A 239 REMARK 465 THR A 240 REMARK 465 THR A 241 REMARK 465 ASN A 242 REMARK 465 ARG A 243 REMARK 465 MET A 244 REMARK 465 MET B -9 REMARK 465 HIS B -8 REMARK 465 HIS B -7 REMARK 465 HIS B -6 REMARK 465 HIS B -5 REMARK 465 HIS B -4 REMARK 465 HIS 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 D -1 REMARK 465 LYS D 0 REMARK 465 SER D 1 REMARK 465 VAL D 2 REMARK 465 GLN D 3 REMARK 465 LEU D 4 REMARK 465 MET D 5 REMARK 465 GLU D 6 REMARK 465 ARG D 7 REMARK 465 ARG D 8 REMARK 465 MET D 9 REMARK 465 ASP D 10 REMARK 465 LYS D 11 REMARK 465 ALA D 12 REMARK 465 GLY D 13 REMARK 465 GLN D 14 REMARK 465 TYR D 15 REMARK 465 THR D 16 REMARK 465 ASP D 17 REMARK 465 LYS D 18 REMARK 465 GLY D 19 REMARK 465 LEU D 20 REMARK 465 ARG D 21 REMARK 465 LYS D 22 REMARK 465 CYS D 23 REMARK 465 CYS D 24 REMARK 465 GLU D 25 REMARK 465 ASP D 26 REMARK 465 GLY D 27 REMARK 465 MET D 28 REMARK 465 ARG D 29 REMARK 465 ASP D 30 REMARK 465 ILE D 31 REMARK 465 PRO D 32 REMARK 465 MET D 33 REMARK 465 ARG D 34 REMARK 465 TYR D 35 REMARK 465 SER D 36 REMARK 465 CYS D 37 REMARK 465 GLN D 38 REMARK 465 ARG D 39 REMARK 465 ARG D 40 REMARK 465 ALA D 41 REMARK 465 ARG D 42 REMARK 465 LEU D 43 REMARK 465 ILE D 44 REMARK 465 THR D 45 REMARK 465 GLN D 46 REMARK 465 GLY D 47 REMARK 465 GLU D 48 REMARK 465 ASN D 49 REMARK 465 CYS D 50 REMARK 465 ILE D 51 REMARK 465 LYS D 52 REMARK 465 ALA D 53 REMARK 465 PHE D 54 REMARK 465 ILE D 55 REMARK 465 ASP D 56 REMARK 465 CYS D 57 REMARK 465 CYS D 58 REMARK 465 ASN D 59 REMARK 465 HIS D 60 REMARK 465 ILE D 61 REMARK 465 THR D 62 REMARK 465 LYS D 63 REMARK 465 LEU D 64 REMARK 465 ARG D 65 REMARK 465 GLU D 66 REMARK 465 MET E -55 REMARK 465 GLY E -54 REMARK 465 LYS E -53 REMARK 465 THR E -52 REMARK 465 ILE E -51 REMARK 465 ILE E -50 REMARK 465 ALA E -49 REMARK 465 LEU E -48 REMARK 465 SER E -47 REMARK 465 TYR E -46 REMARK 465 ILE E -45 REMARK 465 PHE E -44 REMARK 465 CYS E -43 REMARK 465 LEU E -42 REMARK 465 VAL E -41 REMARK 465 PHE E -40 REMARK 465 ALA E -39 REMARK 465 ASP E -38 REMARK 465 TYR E -37 REMARK 465 LYS E -36 REMARK 465 ASP E -35 REMARK 465 ASP E -34 REMARK 465 ASP E -33 REMARK 465 ASP E -32 REMARK 465 ALA E -31 REMARK 465 ALA E -30 REMARK 465 ASN E -29 REMARK 465 PHE E -28 REMARK 465 THR E -27 REMARK 465 PRO E -26 REMARK 465 VAL E -25 REMARK 465 ASN E -24 REMARK 465 GLY E -23 REMARK 465 SER E -22 REMARK 465 SER E -21 REMARK 465 GLY E -20 REMARK 465 ASN E -19 REMARK 465 GLN E -18 REMARK 465 SER E -17 REMARK 465 VAL E -16 REMARK 465 ARG E -15 REMARK 465 LEU E -14 REMARK 465 VAL E -13 REMARK 465 THR E -12 REMARK 465 SER E -11 REMARK 465 SER E -10 REMARK 465 SER E -9 REMARK 465 LEU E -8 REMARK 465 GLU E -7 REMARK 465 VAL E -6 REMARK 465 LEU E -5 REMARK 465 PHE E -4 REMARK 465 GLN E -3 REMARK 465 GLY E -2 REMARK 465 PRO E -1 REMARK 465 GLY E 0 REMARK 465 SER E 1 REMARK 465 GLU E 2 REMARK 465 SER E 3 REMARK 465 PHE E 4 REMARK 465 ASP E 5 REMARK 465 ALA E 6 REMARK 465 ASP E 7 REMARK 465 THR E 8 REMARK 465 ASN E 9 REMARK 465 SER E 10 REMARK 465 THR E 11 REMARK 465 ASP E 12 REMARK 465 LEU E 13 REMARK 465 HIS E 14 REMARK 465 SER E 15 REMARK 465 ARG E 16 REMARK 465 PRO E 17 REMARK 465 ASN E 175 REMARK 465 PHE E 176 REMARK 465 ASP E 177 REMARK 465 SER E 178 REMARK 465 SER E 179 REMARK 465 ARG E 180 REMARK 465 SER E 181 REMARK 465 TYR E 182 REMARK 465 ASP E 183 REMARK 465 TYR E 184 REMARK 465 TRP E 185 REMARK 465 ASP E 186 REMARK 465 TYR E 187 REMARK 465 VAL E 188 REMARK 465 TYR E 189 REMARK 465 LYS E 190 REMARK 465 LEU E 191 REMARK 465 SER E 192 REMARK 465 LEU E 193 REMARK 465 PRO E 194 REMARK 465 GLU E 195 REMARK 465 SER E 196 REMARK 465 ASN E 197 REMARK 465 SER E 198 REMARK 465 THR E 199 REMARK 465 ASP E 200 REMARK 465 ASN E 201 REMARK 465 SER E 202 REMARK 465 THR E 203 REMARK 465 ALA E 204 REMARK 465 GLN E 205 REMARK 465 LEU E 206 REMARK 465 THR E 207 REMARK 465 GLY E 208 REMARK 465 HIS E 209 REMARK 465 MET E 210 REMARK 465 ASN E 211 REMARK 465 ASP E 212 REMARK 465 ARG E 213 REMARK 465 SER E 214 REMARK 465 ALA E 215 REMARK 465 PRO E 216 REMARK 465 SER E 217 REMARK 465 SER E 218 REMARK 465 VAL E 219 REMARK 465 GLN E 220 REMARK 465 ALA E 221 REMARK 465 ARG E 222 REMARK 465 ASP E 223 REMARK 465 TYR E 224 REMARK 465 PHE E 225 REMARK 465 TRP E 226 REMARK 465 THR E 227 REMARK 465 VAL E 228 REMARK 465 THR E 229 REMARK 465 THR E 230 REMARK 465 ALA E 231 REMARK 465 LEU E 232 REMARK 465 GLN E 233 REMARK 465 SER E 234 REMARK 465 GLN E 235 REMARK 465 PRO E 236 REMARK 465 PHE E 237 REMARK 465 LEU E 238 REMARK 465 THR E 239 REMARK 465 SER E 240 REMARK 465 PRO E 241 REMARK 465 GLU E 242 REMARK 465 ASP E 243 REMARK 465 SER E 244 REMARK 465 PHE E 245 REMARK 465 SER E 246 REMARK 465 LEU E 247 REMARK 465 ASP E 248 REMARK 465 SER E 249 REMARK 465 ALA E 250 REMARK 465 ASN E 251 REMARK 465 GLN E 252 REMARK 465 GLN E 253 REMARK 465 PRO E 254 REMARK 465 HIS E 255 REMARK 465 TYR E 256 REMARK 465 GLY E 257 REMARK 465 GLY E 258 REMARK 465 LYS E 259 REMARK 465 PRO E 260 REMARK 465 PRO E 261 REMARK 465 ASN E 262 REMARK 465 VAL E 263 REMARK 465 LEU E 264 REMARK 465 THR E 265 REMARK 465 ALA E 266 REMARK 465 ALA E 267 REMARK 465 VAL E 268 REMARK 465 PRO E 269 REMARK 465 SER E 270 REMARK 465 GLY E 271 REMARK 465 PHE E 272 REMARK 465 PRO E 273 REMARK 465 VAL E 274 REMARK 465 GLU E 275 REMARK 465 ASP E 276 REMARK 465 ARG E 277 REMARK 465 LYS E 278 REMARK 465 SER E 279 REMARK 465 ASN E 280 REMARK 465 THR E 281 REMARK 465 LEU E 282 REMARK 465 ASN E 283 REMARK 465 ALA E 284 REMARK 465 ASP E 285 REMARK 465 ALA E 286 REMARK 465 PHE E 287 REMARK 465 LEU E 288 REMARK 465 SER E 289 REMARK 465 ALA E 290 REMARK 465 HIS E 291 REMARK 465 THR E 292 REMARK 465 GLU E 293 REMARK 465 LEU E 294 REMARK 465 PHE E 295 REMARK 465 PRO E 296 REMARK 465 THR E 297 REMARK 465 ALA E 298 REMARK 465 SER E 299 REMARK 465 SER E 300 REMARK 465 GLY E 301 REMARK 465 HIS E 302 REMARK 465 LEU E 303 REMARK 465 TYR E 304 REMARK 465 PRO E 305 REMARK 465 TYR E 306 REMARK 465 ASP E 307 REMARK 465 PHE E 308 REMARK 465 GLN E 309 REMARK 465 GLY E 310 REMARK 465 ASP E 311 REMARK 465 TYR E 312 REMARK 465 VAL E 313 REMARK 465 ASP E 314 REMARK 465 GLN E 315 REMARK 465 PHE E 316 REMARK 465 THR E 317 REMARK 465 TYR E 318 REMARK 465 ASP E 319 REMARK 465 ASN E 320 REMARK 465 HIS E 321 REMARK 465 LYS E 444 REMARK 465 GLY E 445 REMARK 465 ILE E 446 REMARK 465 LEU E 447 REMARK 465 GLU E 448 REMARK 465 ALA E 449 REMARK 465 ALA E 450 REMARK 465 PHE E 451 REMARK 465 SER E 452 REMARK 465 GLU E 453 REMARK 465 GLU E 454 REMARK 465 LEU E 455 REMARK 465 THR E 456 REMARK 465 HIS E 457 REMARK 465 SER E 458 REMARK 465 THR E 459 REMARK 465 ASN E 460 REMARK 465 CYS E 461 REMARK 465 THR E 462 REMARK 465 GLN E 463 REMARK 465 ASP E 464 REMARK 465 LYS E 465 REMARK 465 ALA E 466 REMARK 465 SER E 467 REMARK 465 SER E 468 REMARK 465 LYS E 469 REMARK 465 ARG E 470 REMARK 465 ASN E 471 REMARK 465 ASN E 472 REMARK 465 MET E 473 REMARK 465 SER E 474 REMARK 465 THR E 475 REMARK 465 ASP E 476 REMARK 465 VAL E 477 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 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 ARG H 72 REMARK 465 ASP H 73 REMARK 465 ASP H 74 REMARK 465 PRO H 75 REMARK 465 SER H 121 REMARK 465 GLY H 122 REMARK 465 GLY H 123 REMARK 465 GLY H 124 REMARK 465 GLY H 125 REMARK 465 SER H 126 REMARK 465 GLY H 127 REMARK 465 GLY H 128 REMARK 465 GLY H 129 REMARK 465 GLY H 130 REMARK 465 SER H 131 REMARK 465 GLY H 132 REMARK 465 GLY H 133 REMARK 465 GLY H 134 REMARK 465 LYS H 248 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLU A 9 CG CD OE1 OE2 REMARK 470 GLU A 20 CG CD OE1 OE2 REMARK 470 LYS A 24 CG CD CE NZ REMARK 470 GLU A 25 CG CD OE1 OE2 REMARK 470 SER A 29 OG REMARK 470 ASP A 33 CG OD1 OD2 REMARK 470 ASP A 42 CG OD1 OD2 REMARK 470 ASN A 43 CG OD1 ND2 REMARK 470 LYS A 51 CG CD CE NZ REMARK 470 GLN A 52 CG CD OE1 NE2 REMARK 470 LYS A 54 CG CD CE NZ REMARK 470 ARG A 206 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 208 CG CD OE1 OE2 REMARK 470 ASP A 227 CG OD1 OD2 REMARK 470 SER A 229 OG REMARK 470 ASP A 230 CG OD1 OD2 REMARK 470 HIS A 245 CG ND1 CD2 CE1 NE2 REMARK 470 MET A 249 CG SD CE REMARK 470 ASP A 262 CG OD1 OD2 REMARK 470 ILE A 265 CG1 CG2 CD1 REMARK 470 LYS A 272 CG CD CE NZ REMARK 470 LYS A 280 CG CD CE NZ REMARK 470 LYS A 281 CG CD CE NZ REMARK 470 LEU A 284 CG CD1 CD2 REMARK 470 GLU A 298 CG CD OE1 OE2 REMARK 470 SER A 310 OG REMARK 470 SER A 314 OG REMARK 470 ASN A 316 CG OD1 ND2 REMARK 470 THR A 324 OG1 CG2 REMARK 470 CYS A 325 SG REMARK 470 THR A 327 OG1 CG2 REMARK 470 ASP A 328 CG OD1 OD2 REMARK 470 THR A 329 OG1 CG2 REMARK 470 ASN A 346 CG OD1 ND2 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 LEU B 14 CG CD1 CD2 REMARK 470 LYS B 15 CG CD CE NZ 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 ARG B 22 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 23 CG CD CE NZ REMARK 470 CYS B 25 SG REMARK 470 ASP B 27 CG OD1 OD2 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 ILE B 43 CG1 CG2 CD1 REMARK 470 LEU B 51 CG CD1 CD2 REMARK 470 MET B 61 CG SD CE REMARK 470 THR B 65 OG1 CG2 REMARK 470 LEU B 70 CG CD1 CD2 REMARK 470 SER B 72 OG REMARK 470 SER B 74 OG REMARK 470 ASP B 76 CG OD1 OD2 REMARK 470 LEU B 79 CG CD1 CD2 REMARK 470 ILE B 80 CG1 CG2 CD1 REMARK 470 ILE B 81 CG1 CG2 CD1 REMARK 470 THR B 128 OG1 CG2 REMARK 470 GLU B 130 CG CD OE1 OE2 REMARK 470 ARG B 134 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 138 CG CD OE1 OE2 REMARK 470 LEU B 146 CG CD1 CD2 REMARK 470 ILE B 171 CG1 CG2 CD1 REMARK 470 GLU B 172 CG CD OE1 OE2 REMARK 470 VAL B 187 CG1 CG2 REMARK 470 MET B 188 CG SD CE REMARK 470 LEU B 192 CG CD1 CD2 REMARK 470 ARG B 197 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 214 CG CD NE CZ NH1 NH2 REMARK 470 MET B 217 CG SD CE REMARK 470 ASP B 228 CG OD1 OD2 REMARK 470 ASN B 237 CG OD1 ND2 REMARK 470 THR B 243 OG1 CG2 REMARK 470 SER B 245 OG REMARK 470 ASP B 246 CG OD1 OD2 REMARK 470 ASP B 247 CG OD1 OD2 REMARK 470 ASP B 254 CG OD1 OD2 REMARK 470 GLU B 260 CG CD OE1 OE2 REMARK 470 MET B 262 CG SD CE REMARK 470 CYS B 271 SG REMARK 470 VAL B 276 CG1 CG2 REMARK 470 LEU B 286 CG CD1 CD2 REMARK 470 ASP B 290 CG OD1 OD2 REMARK 470 ASP B 291 CG OD1 OD2 REMARK 470 ASP B 312 CG OD1 OD2 REMARK 470 ARG B 314 CG CD NE CZ NH1 NH2 REMARK 470 SER B 316 OG REMARK 470 LEU B 318 CG CD1 CD2 REMARK 470 LEU B 336 CG CD1 CD2 REMARK 470 LYS B 337 CG CD CE NZ REMARK 470 ARG D 69 CG CD NE CZ NH1 NH2 REMARK 470 MET E 27 CG SD CE REMARK 470 VAL E 28 CG1 CG2 REMARK 470 LEU E 32 CG CD1 CD2 REMARK 470 LEU E 35 CG CD1 CD2 REMARK 470 LEU E 36 CG CD1 CD2 REMARK 470 LEU E 39 CG CD1 CD2 REMARK 470 LYS E 51 CG CD CE NZ REMARK 470 LEU E 73 CG CD1 CD2 REMARK 470 LEU E 82 CG CD1 CD2 REMARK 470 ILE E 83 CG1 CG2 CD1 REMARK 470 PHE E 93 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS E 96 CG CD CE NZ REMARK 470 LEU E 97 CG CD1 CD2 REMARK 470 LYS E 126 CG CD CE NZ REMARK 470 PHE E 151 CG CD1 CD2 CE1 CE2 CZ REMARK 470 VAL E 152 CG1 CG2 REMARK 470 MET E 153 CG SD CE REMARK 470 VAL E 155 CG1 CG2 REMARK 470 ARG E 161 CG CD NE CZ NH1 NH2 REMARK 470 PHE E 164 CG CD1 CD2 CE1 CE2 CZ REMARK 470 MET E 166 CG SD CE REMARK 470 ASP E 167 CG OD1 OD2 REMARK 470 ASN E 168 CG OD1 ND2 REMARK 470 ARG E 169 CG CD NE CZ NH1 NH2 REMARK 470 ARG E 357 CG CD NE CZ NH1 NH2 REMARK 470 ARG E 365 CG CD NE CZ NH1 NH2 REMARK 470 ARG E 370 CG CD NE CZ NH1 NH2 REMARK 470 VAL E 391 CG1 CG2 REMARK 470 LEU E 392 CG CD1 CD2 REMARK 470 ILE E 395 CG1 CG2 CD1 REMARK 470 LEU E 402 CG CD1 CD2 REMARK 470 SER E 408 OG REMARK 470 MET E 412 CG SD CE REMARK 470 LYS E 433 CG CD CE NZ REMARK 470 ASP E 434 CG OD1 OD2 REMARK 470 ARG E 436 CG CD NE CZ NH1 NH2 REMARK 470 LYS E 437 CG CD CE NZ REMARK 470 LYS E 438 CG CD CE NZ REMARK 470 ARG E 440 CG CD NE CZ NH1 NH2 REMARK 470 GLN E 441 CG CD OE1 NE2 REMARK 470 ILE E 443 CG1 CG2 CD1 REMARK 470 SER G 8 OG REMARK 470 ILE G 9 CG1 CG2 CD1 REMARK 470 GLN G 11 CG CD OE1 NE2 REMARK 470 ARG G 13 CG CD NE CZ NH1 NH2 REMARK 470 LYS G 14 CG CD CE NZ REMARK 470 LEU G 15 CG CD1 CD2 REMARK 470 VAL G 16 CG1 CG2 REMARK 470 GLU G 17 CG CD OE1 OE2 REMARK 470 LYS G 20 CG CD CE NZ REMARK 470 MET G 21 CG SD CE REMARK 470 GLU G 22 CG CD OE1 OE2 REMARK 470 ASN G 24 CG OD1 ND2 REMARK 470 ILE G 25 CG1 CG2 CD1 REMARK 470 ASP G 26 CG OD1 OD2 REMARK 470 LYS G 29 CG CD CE NZ REMARK 470 LYS G 32 CG CD CE NZ REMARK 470 LYS G 46 CG CD CE NZ REMARK 470 GLU G 58 CG CD OE1 OE2 REMARK 470 ARG G 62 CG CD NE CZ NH1 NH2 REMARK 470 ASP H 1 CG OD1 OD2 REMARK 470 GLN H 13 CG CD OE1 NE2 REMARK 470 LEU H 20 CG CD1 CD2 REMARK 470 MET H 34 CG SD CE REMARK 470 GLU H 42 CG CD OE1 OE2 REMARK 470 LYS H 43 CG CD CE NZ REMARK 470 GLU H 46 CG CD OE1 OE2 REMARK 470 ASP H 62 CG OD1 OD2 REMARK 470 LYS H 65 CG CD CE NZ REMARK 470 ARG H 67 CG CD NE CZ NH1 NH2 REMARK 470 ILE H 70 CG1 CG2 CD1 REMARK 470 LYS H 76 CG CD CE NZ REMARK 470 LEU H 79 CG CD1 CD2 REMARK 470 SER H 88 OG REMARK 470 GLU H 89 CG CD OE1 OE2 REMARK 470 MET H 93 CG SD CE REMARK 470 SER H 136 OG REMARK 470 GLU H 153 CG CD OE1 OE2 REMARK 470 VAL H 155 CG1 CG2 REMARK 470 ILE H 157 CG1 CG2 CD1 REMARK 470 LEU H 166 CG CD1 CD2 REMARK 470 LEU H 174 CG CD1 CD2 REMARK 470 GLN H 183 CG CD OE1 NE2 REMARK 470 GLN H 186 CG CD OE1 NE2 REMARK 470 LEU H 188 CG CD1 CD2 REMARK 470 MET H 192 CG SD CE REMARK 470 ASP H 201 CG OD1 OD2 REMARK 470 ARG H 202 CG CD NE CZ NH1 NH2 REMARK 470 SER H 204 OG REMARK 470 LEU H 214 CG CD1 CD2 REMARK 470 ARG H 218 CG CD NE CZ NH1 NH2 REMARK 470 GLU H 220 CG CD OE1 OE2 REMARK 470 GLU H 222 CG CD OE1 OE2 REMARK 470 ASP H 223 CG OD1 OD2 REMARK 470 GLU H 234 CG CD OE1 OE2 REMARK 470 LYS H 244 CG CD CE NZ REMARK 470 LEU H 245 CG CD1 CD2 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 LYS A 54 -168.41 61.95 REMARK 500 LYS B 127 33.97 -97.38 REMARK 500 THR B 196 17.69 57.96 REMARK 500 GLN B 259 -169.86 -165.14 REMARK 500 PHE B 292 -2.91 73.34 REMARK 500 LEU D 76 48.86 -82.54 REMARK 500 LYS E 126 67.39 -158.32 REMARK 500 ILE E 165 -64.37 -122.64 REMARK 500 ASP E 167 -168.72 -167.97 REMARK 500 PRO E 398 -174.91 -68.77 REMARK 500 ALA H 92 -175.18 -171.79 REMARK 500 MET H 192 -5.23 67.76 REMARK 500 ASP H 201 3.40 -69.30 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-62665 RELATED DB: EMDB REMARK 900 STRUCTURE OF MOUSE C3A BOUND MOUSE C3AR IN COMPLEX WITH GO DBREF 9KZK A 4 173 UNP P09471 GNAO_HUMAN 4 57 DBREF 9KZK A 182 354 UNP P09471 GNAO_HUMAN 182 354 DBREF 9KZK B 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 9KZK D 1 78 UNP P01027 CO3_MOUSE 671 748 DBREF 9KZK E -30 -9 UNP P08173 ACM4_HUMAN 2 23 DBREF 9KZK E 2 477 UNP O09047 C3AR_MOUSE 2 477 DBREF 9KZK G 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 9KZK H 1 248 PDB 9KZK 9KZK 1 248 SEQADV 9KZK MET A -11 UNP P09471 INITIATING METHIONINE SEQADV 9KZK GLY A -10 UNP P09471 EXPRESSION TAG SEQADV 9KZK HIS A -9 UNP P09471 EXPRESSION TAG SEQADV 9KZK HIS A -8 UNP P09471 EXPRESSION TAG SEQADV 9KZK HIS A -7 UNP P09471 EXPRESSION TAG SEQADV 9KZK HIS A -6 UNP P09471 EXPRESSION TAG SEQADV 9KZK HIS A -5 UNP P09471 EXPRESSION TAG SEQADV 9KZK HIS A -4 UNP P09471 EXPRESSION TAG SEQADV 9KZK GLU A -3 UNP P09471 EXPRESSION TAG SEQADV 9KZK ASN A -2 UNP P09471 EXPRESSION TAG SEQADV 9KZK LEU A -1 UNP P09471 EXPRESSION TAG SEQADV 9KZK TYR A 0 UNP P09471 EXPRESSION TAG SEQADV 9KZK PHE A 1 UNP P09471 EXPRESSION TAG SEQADV 9KZK GLN A 2 UNP P09471 EXPRESSION TAG SEQADV 9KZK GLY A 3 UNP P09471 EXPRESSION TAG SEQADV 9KZK ASP A 42 UNP P09471 GLY 42 ENGINEERED MUTATION SEQADV 9KZK ASN A 43 UNP P09471 GLU 43 ENGINEERED MUTATION SEQADV 9KZK GLY A 174 UNP P09471 LINKER SEQADV 9KZK GLY A 175 UNP P09471 LINKER SEQADV 9KZK SER A 176 UNP P09471 LINKER SEQADV 9KZK GLY A 177 UNP P09471 LINKER SEQADV 9KZK GLY A 178 UNP P09471 LINKER SEQADV 9KZK SER A 179 UNP P09471 LINKER SEQADV 9KZK GLY A 180 UNP P09471 LINKER SEQADV 9KZK GLY A 181 UNP P09471 LINKER SEQADV 9KZK ASP A 227 UNP P09471 ALA 227 ENGINEERED MUTATION SEQADV 9KZK ASP A 230 UNP P09471 GLY 230 ENGINEERED MUTATION SEQADV 9KZK ALA A 332 UNP P09471 ILE 332 ENGINEERED MUTATION SEQADV 9KZK ILE A 335 UNP P09471 VAL 335 ENGINEERED MUTATION SEQADV 9KZK MET B -9 UNP P62873 INITIATING METHIONINE SEQADV 9KZK HIS B -8 UNP P62873 EXPRESSION TAG SEQADV 9KZK HIS B -7 UNP P62873 EXPRESSION TAG SEQADV 9KZK HIS B -6 UNP P62873 EXPRESSION TAG SEQADV 9KZK HIS B -5 UNP P62873 EXPRESSION TAG SEQADV 9KZK HIS B -4 UNP P62873 EXPRESSION TAG SEQADV 9KZK HIS B -3 UNP P62873 EXPRESSION TAG SEQADV 9KZK GLY B -2 UNP P62873 EXPRESSION TAG SEQADV 9KZK SER B -1 UNP P62873 EXPRESSION TAG SEQADV 9KZK SER B 0 UNP P62873 EXPRESSION TAG SEQADV 9KZK GLY B 1 UNP P62873 EXPRESSION TAG SEQADV 9KZK GLY D -1 UNP P01027 EXPRESSION TAG SEQADV 9KZK LYS D 0 UNP P01027 EXPRESSION TAG SEQADV 9KZK MET E -55 UNP P08173 INITIATING METHIONINE SEQADV 9KZK GLY E -54 UNP P08173 EXPRESSION TAG SEQADV 9KZK LYS E -53 UNP P08173 EXPRESSION TAG SEQADV 9KZK THR E -52 UNP P08173 EXPRESSION TAG SEQADV 9KZK ILE E -51 UNP P08173 EXPRESSION TAG SEQADV 9KZK ILE E -50 UNP P08173 EXPRESSION TAG SEQADV 9KZK ALA E -49 UNP P08173 EXPRESSION TAG SEQADV 9KZK LEU E -48 UNP P08173 EXPRESSION TAG SEQADV 9KZK SER E -47 UNP P08173 EXPRESSION TAG SEQADV 9KZK TYR E -46 UNP P08173 EXPRESSION TAG SEQADV 9KZK ILE E -45 UNP P08173 EXPRESSION TAG SEQADV 9KZK PHE E -44 UNP P08173 EXPRESSION TAG SEQADV 9KZK CYS E -43 UNP P08173 EXPRESSION TAG SEQADV 9KZK LEU E -42 UNP P08173 EXPRESSION TAG SEQADV 9KZK VAL E -41 UNP P08173 EXPRESSION TAG SEQADV 9KZK PHE E -40 UNP P08173 EXPRESSION TAG SEQADV 9KZK ALA E -39 UNP P08173 EXPRESSION TAG SEQADV 9KZK ASP E -38 UNP P08173 EXPRESSION TAG SEQADV 9KZK TYR E -37 UNP P08173 EXPRESSION TAG SEQADV 9KZK LYS E -36 UNP P08173 EXPRESSION TAG SEQADV 9KZK ASP E -35 UNP P08173 EXPRESSION TAG SEQADV 9KZK ASP E -34 UNP P08173 EXPRESSION TAG SEQADV 9KZK ASP E -33 UNP P08173 EXPRESSION TAG SEQADV 9KZK ASP E -32 UNP P08173 EXPRESSION TAG SEQADV 9KZK ALA E -31 UNP P08173 EXPRESSION TAG SEQADV 9KZK LEU E -8 UNP P08173 LINKER SEQADV 9KZK GLU E -7 UNP P08173 LINKER SEQADV 9KZK VAL E -6 UNP P08173 LINKER SEQADV 9KZK LEU E -5 UNP P08173 LINKER SEQADV 9KZK PHE E -4 UNP P08173 LINKER SEQADV 9KZK GLN E -3 UNP P08173 LINKER SEQADV 9KZK GLY E -2 UNP P08173 LINKER SEQADV 9KZK PRO E -1 UNP P08173 LINKER SEQADV 9KZK GLY E 0 UNP P08173 LINKER SEQADV 9KZK SER E 1 UNP P08173 LINKER SEQRES 1 A 250 MET GLY HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE SEQRES 2 A 250 GLN GLY THR LEU SER ALA GLU GLU ARG ALA ALA LEU GLU SEQRES 3 A 250 ARG SER LYS ALA ILE GLU LYS ASN LEU LYS GLU ASP GLY SEQRES 4 A 250 ILE SER ALA ALA LYS ASP VAL LYS LEU LEU LEU LEU GLY SEQRES 5 A 250 ALA ASP ASN SER GLY LYS SER THR ILE VAL LYS GLN MET SEQRES 6 A 250 LYS ILE ILE HIS GLY GLY SER GLY GLY SER GLY GLY THR SEQRES 7 A 250 THR GLY ILE VAL GLU THR HIS PHE THR PHE LYS ASN LEU SEQRES 8 A 250 HIS PHE ARG LEU PHE ASP VAL GLY GLY GLN ARG SER GLU SEQRES 9 A 250 ARG LYS LYS TRP ILE HIS CYS PHE GLU ASP VAL THR ALA SEQRES 10 A 250 ILE ILE PHE CYS VAL ASP LEU SER ASP TYR ASP GLN VAL SEQRES 11 A 250 LEU HIS GLU ASP GLU THR THR ASN ARG MET HIS GLU SER SEQRES 12 A 250 LEU MET LEU PHE ASP SER ILE CYS ASN ASN LYS PHE PHE SEQRES 13 A 250 ILE ASP THR SER ILE ILE LEU PHE LEU ASN LYS LYS ASP SEQRES 14 A 250 LEU PHE GLY GLU LYS ILE LYS LYS SER PRO LEU THR ILE SEQRES 15 A 250 CYS PHE PRO GLU TYR THR GLY PRO ASN THR TYR GLU ASP SEQRES 16 A 250 ALA ALA ALA TYR ILE GLN ALA GLN PHE GLU SER LYS ASN SEQRES 17 A 250 ARG SER PRO ASN LYS GLU ILE TYR CYS HIS MET THR CYS SEQRES 18 A 250 ALA THR ASP THR ASN ASN ALA GLN VAL ILE PHE ASP ALA SEQRES 19 A 250 VAL THR ASP ILE ILE ILE ALA ASN ASN LEU ARG GLY CYS SEQRES 20 A 250 GLY LEU TYR SEQRES 1 B 350 MET HIS HIS HIS HIS HIS HIS GLY SER SER GLY SER GLU SEQRES 2 B 350 LEU ASP GLN LEU ARG GLN GLU ALA GLU GLN LEU LYS ASN SEQRES 3 B 350 GLN ILE ARG ASP ALA ARG LYS ALA CYS ALA ASP ALA THR SEQRES 4 B 350 LEU SER GLN ILE THR ASN ASN ILE ASP PRO VAL GLY ARG SEQRES 5 B 350 ILE GLN MET ARG THR ARG ARG THR LEU ARG GLY HIS LEU SEQRES 6 B 350 ALA LYS ILE TYR ALA MET HIS TRP GLY THR ASP SER ARG SEQRES 7 B 350 LEU LEU VAL SER ALA SER GLN ASP GLY LYS LEU ILE ILE SEQRES 8 B 350 TRP ASP SER TYR THR THR ASN LYS VAL HIS ALA ILE PRO SEQRES 9 B 350 LEU ARG SER SER TRP VAL MET THR CYS ALA TYR ALA PRO SEQRES 10 B 350 SER GLY ASN TYR VAL ALA CYS GLY GLY LEU ASP ASN ILE SEQRES 11 B 350 CYS SER ILE TYR ASN LEU LYS THR ARG GLU GLY ASN VAL SEQRES 12 B 350 ARG VAL SER ARG GLU LEU ALA GLY HIS THR GLY TYR LEU SEQRES 13 B 350 SER CYS CYS ARG PHE LEU ASP ASP ASN GLN ILE VAL THR SEQRES 14 B 350 SER SER GLY ASP THR THR CYS ALA LEU TRP ASP ILE GLU SEQRES 15 B 350 THR GLY GLN GLN THR THR THR PHE THR GLY HIS THR GLY SEQRES 16 B 350 ASP VAL MET SER LEU SER LEU ALA PRO ASP THR ARG LEU SEQRES 17 B 350 PHE VAL SER GLY ALA CYS ASP ALA SER ALA LYS LEU TRP SEQRES 18 B 350 ASP VAL ARG GLU GLY MET CYS ARG GLN THR PHE THR GLY SEQRES 19 B 350 HIS GLU SER ASP ILE ASN ALA ILE CYS PHE PHE PRO ASN SEQRES 20 B 350 GLY ASN ALA PHE ALA THR GLY SER ASP ASP ALA THR CYS SEQRES 21 B 350 ARG LEU PHE ASP LEU ARG ALA ASP GLN GLU LEU MET THR SEQRES 22 B 350 TYR SER HIS ASP ASN ILE ILE CYS GLY ILE THR SER VAL SEQRES 23 B 350 SER PHE SER LYS SER GLY ARG LEU LEU LEU ALA GLY TYR SEQRES 24 B 350 ASP ASP PHE ASN CYS ASN VAL TRP ASP ALA LEU LYS ALA SEQRES 25 B 350 ASP ARG ALA GLY VAL LEU ALA GLY HIS ASP ASN ARG VAL SEQRES 26 B 350 SER CYS LEU GLY VAL THR ASP ASP GLY MET ALA VAL ALA SEQRES 27 B 350 THR GLY SER TRP ASP SER PHE LEU LYS ILE TRP ASN SEQRES 1 D 80 GLY LYS SER VAL GLN LEU MET GLU ARG ARG MET ASP LYS SEQRES 2 D 80 ALA GLY GLN TYR THR ASP LYS GLY LEU ARG LYS CYS CYS SEQRES 3 D 80 GLU ASP GLY MET ARG ASP ILE PRO MET ARG TYR SER CYS SEQRES 4 D 80 GLN ARG ARG ALA ARG LEU ILE THR GLN GLY GLU ASN CYS SEQRES 5 D 80 ILE LYS ALA PHE ILE ASP CYS CYS ASN HIS ILE THR LYS SEQRES 6 D 80 LEU ARG GLU GLN HIS ARG ARG ASP HIS VAL LEU GLY LEU SEQRES 7 D 80 ALA ARG SEQRES 1 E 533 MET GLY LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS SEQRES 2 E 533 LEU VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP ALA ALA SEQRES 3 E 533 ASN PHE THR PRO VAL ASN GLY SER SER GLY ASN GLN SER SEQRES 4 E 533 VAL ARG LEU VAL THR SER SER SER LEU GLU VAL LEU PHE SEQRES 5 E 533 GLN GLY PRO GLY SER GLU SER PHE ASP ALA ASP THR ASN SEQRES 6 E 533 SER THR ASP LEU HIS SER ARG PRO LEU PHE GLN PRO GLN SEQRES 7 E 533 ASP ILE ALA SER MET VAL ILE LEU GLY LEU THR CYS LEU SEQRES 8 E 533 LEU GLY LEU LEU GLY ASN GLY LEU VAL LEU TRP VAL ALA SEQRES 9 E 533 GLY VAL LYS MET LYS THR THR VAL ASN THR VAL TRP PHE SEQRES 10 E 533 LEU HIS LEU THR LEU ALA ASP PHE LEU CYS CYS LEU SER SEQRES 11 E 533 LEU PRO PHE SER LEU ALA HIS LEU ILE LEU GLN GLY HIS SEQRES 12 E 533 TRP PRO TYR GLY LEU PHE LEU CYS LYS LEU ILE PRO SER SEQRES 13 E 533 ILE ILE ILE LEU ASN MET PHE ALA SER VAL PHE LEU LEU SEQRES 14 E 533 THR ALA ILE SER LEU ASP ARG CYS LEU ILE VAL HIS LYS SEQRES 15 E 533 PRO ILE TRP CYS GLN ASN HIS ARG ASN VAL ARG THR ALA SEQRES 16 E 533 PHE ALA ILE CYS GLY CYS VAL TRP VAL VAL ALA PHE VAL SEQRES 17 E 533 MET CYS VAL PRO VAL PHE VAL TYR ARG ASP LEU PHE ILE SEQRES 18 E 533 MET ASP ASN ARG SER ILE CYS ARG TYR ASN PHE ASP SER SEQRES 19 E 533 SER ARG SER TYR ASP TYR TRP ASP TYR VAL TYR LYS LEU SEQRES 20 E 533 SER LEU PRO GLU SER ASN SER THR ASP ASN SER THR ALA SEQRES 21 E 533 GLN LEU THR GLY HIS MET ASN ASP ARG SER ALA PRO SER SEQRES 22 E 533 SER VAL GLN ALA ARG ASP TYR PHE TRP THR VAL THR THR SEQRES 23 E 533 ALA LEU GLN SER GLN PRO PHE LEU THR SER PRO GLU ASP SEQRES 24 E 533 SER PHE SER LEU ASP SER ALA ASN GLN GLN PRO HIS TYR SEQRES 25 E 533 GLY GLY LYS PRO PRO ASN VAL LEU THR ALA ALA VAL PRO SEQRES 26 E 533 SER GLY PHE PRO VAL GLU ASP ARG LYS SER ASN THR LEU SEQRES 27 E 533 ASN ALA ASP ALA PHE LEU SER ALA HIS THR GLU LEU PHE SEQRES 28 E 533 PRO THR ALA SER SER GLY HIS LEU TYR PRO TYR ASP PHE SEQRES 29 E 533 GLN GLY ASP TYR VAL ASP GLN PHE THR TYR ASP ASN HIS SEQRES 30 E 533 VAL PRO THR PRO LEU MET ALA ILE THR ILE THR ARG LEU SEQRES 31 E 533 VAL VAL GLY PHE LEU VAL PRO PHE PHE ILE MET VAL ILE SEQRES 32 E 533 CYS TYR SER LEU ILE VAL PHE ARG MET ARG LYS THR ASN SEQRES 33 E 533 PHE THR LYS SER ARG ASN LYS THR PHE ARG VAL ALA VAL SEQRES 34 E 533 ALA VAL VAL THR VAL PHE PHE ILE CYS TRP THR PRO TYR SEQRES 35 E 533 HIS LEU VAL GLY VAL LEU LEU LEU ILE THR ASP PRO GLU SEQRES 36 E 533 SER SER LEU GLY GLU ALA VAL MET SER TRP ASP HIS MET SEQRES 37 E 533 SER ILE ALA LEU ALA SER ALA ASN SER CYS PHE ASN PRO SEQRES 38 E 533 PHE LEU TYR ALA LEU LEU GLY LYS ASP PHE ARG LYS LYS SEQRES 39 E 533 ALA ARG GLN SER ILE LYS GLY ILE LEU GLU ALA ALA PHE SEQRES 40 E 533 SER GLU GLU LEU THR HIS SER THR ASN CYS THR GLN ASP SEQRES 41 E 533 LYS ALA SER SER LYS ARG ASN ASN MET SER THR ASP VAL 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 H 248 ASP VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 248 PRO GLY GLY SER ARG LYS LEU SER CYS SER ALA SER GLY SEQRES 3 H 248 PHE ALA PHE SER SER PHE GLY MET HIS TRP VAL ARG GLN SEQRES 4 H 248 ALA PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SEQRES 5 H 248 SER GLY SER GLY THR ILE TYR TYR ALA ASP THR VAL LYS SEQRES 6 H 248 GLY ARG PHE THR ILE SER ARG ASP ASP PRO LYS ASN THR SEQRES 7 H 248 LEU PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR SEQRES 8 H 248 ALA MET TYR TYR CYS VAL ARG SER ILE TYR TYR TYR GLY SEQRES 9 H 248 SER SER PRO PHE ASP PHE TRP GLY GLN GLY THR THR LEU SEQRES 10 H 248 THR VAL SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SEQRES 11 H 248 SER GLY GLY GLY GLY SER ASP ILE VAL MET THR GLN ALA SEQRES 12 H 248 THR SER SER VAL PRO VAL THR PRO GLY GLU SER VAL SER SEQRES 13 H 248 ILE SER CYS ARG SER SER LYS SER LEU LEU HIS SER ASN SEQRES 14 H 248 GLY ASN THR TYR LEU TYR TRP PHE LEU GLN ARG PRO GLY SEQRES 15 H 248 GLN SER PRO GLN LEU LEU ILE TYR ARG MET SER ASN LEU SEQRES 16 H 248 ALA SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SER SEQRES 17 H 248 GLY THR ALA PHE THR LEU THR ILE SER ARG LEU GLU ALA SEQRES 18 H 248 GLU ASP VAL GLY VAL TYR TYR CYS MET GLN HIS LEU GLU SEQRES 19 H 248 TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU LEU SEQRES 20 H 248 LYS HELIX 1 AA1 GLU A 8 ALA A 31 1 24 HELIX 2 AA2 GLY A 45 MET A 53 1 9 HELIX 3 AA3 GLU A 208 GLU A 217 5 10 HELIX 4 AA4 SER A 247 ASN A 256 1 10 HELIX 5 AA5 LYS A 271 SER A 282 1 12 HELIX 6 AA6 PRO A 283 CYS A 287 5 5 HELIX 7 AA7 THR A 296 SER A 310 1 15 HELIX 8 AA8 ASN A 330 CYS A 351 1 22 HELIX 9 AA9 LEU B 4 CYS B 25 1 22 HELIX 10 AB1 THR B 29 THR B 34 1 6 HELIX 11 AB2 ASN B 35 ILE B 37 5 3 HELIX 12 AB3 HIS D 68 VAL D 73 1 6 HELIX 13 AB4 GLN E 20 LYS E 51 1 32 HELIX 14 AB5 ASN E 57 GLN E 85 1 29 HELIX 15 AB6 GLY E 91 LYS E 126 1 36 HELIX 16 AB7 LYS E 126 ARG E 134 1 9 HELIX 17 AB8 ASN E 135 ARG E 161 1 27 HELIX 18 AB9 PRO E 323 ARG E 357 1 35 HELIX 19 AC1 ASN E 366 THR E 396 1 31 HELIX 20 AC2 SER E 400 TYR E 428 1 29 HELIX 21 AC3 GLY E 432 ILE E 443 1 12 HELIX 22 AC4 SER G 8 ASN G 24 1 17 HELIX 23 AC5 LYS G 29 HIS G 44 1 16 HELIX 24 AC6 ALA H 28 PHE H 32 5 5 HELIX 25 AC7 SER H 53 GLY H 56 5 4 HELIX 26 AC8 ARG H 87 THR H 91 5 5 HELIX 27 AC9 GLU H 220 VAL H 224 5 5 SHEET 1 AA1 5 VAL A 186 PHE A 192 0 SHEET 2 AA1 5 LEU A 195 ASP A 201 -1 O LEU A 199 N THR A 188 SHEET 3 AA1 5 ASP A 33 GLY A 40 1 N LEU A 36 O ARG A 198 SHEET 4 AA1 5 ALA A 221 ASP A 227 1 O ILE A 223 N LEU A 37 SHEET 5 AA1 5 SER A 264 ASN A 270 1 O ILE A 266 N ILE A 222 SHEET 1 AA2 4 THR B 47 LEU B 51 0 SHEET 2 AA2 4 LEU B 336 TRP B 339 -1 O LEU B 336 N LEU B 51 SHEET 3 AA2 4 VAL B 327 SER B 331 -1 N VAL B 327 O TRP B 339 SHEET 4 AA2 4 VAL B 315 VAL B 320 -1 N CYS B 317 O GLY B 330 SHEET 1 AA3 4 ILE B 58 TRP B 63 0 SHEET 2 AA3 4 LEU B 69 SER B 74 -1 O ALA B 73 N TYR B 59 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 ILE B 93 N LEU B 79 SHEET 1 AA4 4 VAL B 100 TYR B 105 0 SHEET 2 AA4 4 TYR B 111 GLY B 116 -1 O ALA B 113 N ALA B 104 SHEET 3 AA4 4 CYS B 121 ASN B 125 -1 O TYR B 124 N VAL B 112 SHEET 4 AA4 4 ARG B 134 LEU B 139 -1 O ARG B 137 N ILE B 123 SHEET 1 AA5 4 LEU B 146 PHE B 151 0 SHEET 2 AA5 4 GLN B 156 SER B 161 -1 O SER B 160 N CYS B 148 SHEET 3 AA5 4 CYS B 166 ASP B 170 -1 O TRP B 169 N ILE B 157 SHEET 4 AA5 4 GLN B 176 PHE B 180 -1 O PHE B 180 N CYS B 166 SHEET 1 AA6 4 VAL B 187 LEU B 192 0 SHEET 2 AA6 4 LEU B 198 ALA B 203 -1 O GLY B 202 N SER B 189 SHEET 3 AA6 4 ALA B 208 ASP B 212 -1 O LYS B 209 N SER B 201 SHEET 4 AA6 4 THR B 221 PHE B 222 -1 O PHE B 222 N ALA B 208 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 LEU B 284 ALA B 287 0 SHEET 2 AA8 3 ASN B 295 ASP B 298 -1 O TRP B 297 N LEU B 285 SHEET 3 AA8 3 ASP B 303 VAL B 307 -1 O ASP B 303 N ASP B 298 SHEET 1 AA9 2 ASP E 162 PHE E 164 0 SHEET 2 AA9 2 ILE E 171 ARG E 173 -1 O ARG E 173 N ASP E 162 SHEET 1 AB1 4 GLN H 3 SER H 7 0 SHEET 2 AB1 4 SER H 17 SER H 25 -1 O SER H 23 N VAL H 5 SHEET 3 AB1 4 THR H 78 THR H 84 -1 O LEU H 79 N CYS H 22 SHEET 4 AB1 4 PHE H 68 ILE H 70 -1 N THR H 69 O GLN H 82 SHEET 1 AB2 6 LEU H 11 VAL H 12 0 SHEET 2 AB2 6 THR H 115 VAL H 119 1 O THR H 118 N VAL H 12 SHEET 3 AB2 6 ALA H 92 ARG H 98 -1 N TYR H 94 O THR H 115 SHEET 4 AB2 6 HIS H 35 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AB2 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AB2 6 ILE H 58 TYR H 60 -1 O TYR H 59 N TYR H 50 SHEET 1 AB3 4 LEU H 11 VAL H 12 0 SHEET 2 AB3 4 THR H 115 VAL H 119 1 O THR H 118 N VAL H 12 SHEET 3 AB3 4 ALA H 92 ARG H 98 -1 N TYR H 94 O THR H 115 SHEET 4 AB3 4 PHE H 110 TRP H 111 -1 O PHE H 110 N ARG H 98 SHEET 1 AB4 4 MET H 140 THR H 141 0 SHEET 2 AB4 4 VAL H 155 SER H 161 -1 O ARG H 160 N THR H 141 SHEET 3 AB4 4 ALA H 211 ILE H 216 -1 O LEU H 214 N ILE H 157 SHEET 4 AB4 4 PHE H 203 SER H 208 -1 N SER H 206 O THR H 213 SHEET 1 AB5 6 SER H 146 PRO H 148 0 SHEET 2 AB5 6 THR H 243 GLU H 246 1 O LYS H 244 N VAL H 147 SHEET 3 AB5 6 GLY H 225 GLN H 231 -1 N TYR H 227 O THR H 243 SHEET 4 AB5 6 LEU H 174 GLN H 179 -1 N TYR H 175 O MET H 230 SHEET 5 AB5 6 GLN H 186 TYR H 190 -1 O ILE H 189 N TRP H 176 SHEET 6 AB5 6 ASN H 194 LEU H 195 -1 O ASN H 194 N TYR H 190 SSBOND 1 CYS E 95 CYS E 172 1555 1555 2.03 SSBOND 2 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 3 CYS H 159 CYS H 229 1555 1555 2.03 CISPEP 1 TYR H 235 PRO H 236 0 0.37 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