HEADER SIGNALING PROTEIN 07-DEC-24 9KXS TITLE STRUCTURE OF EP67 BOUND MOUSE C5AR1 IN COMPLEX WITH GO COMPND MOL_ID: 1; COMPND 2 MOLECULE: MUSCARINIC ACETYLCHOLINE RECEPTOR M4,C5A ANAPHYLATOXIN COMPND 3 CHEMOTACTIC RECEPTOR 1; COMPND 4 CHAIN: A; COMPND 5 SYNONYM: C5A ANAPHYLATOXIN CHEMOTACTIC RECEPTOR,C5A-R,C5AR; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(O) SUBUNIT ALPHA; COMPND 9 CHAIN: B; COMPND 10 EC: 3.6.5.-; COMPND 11 ENGINEERED: YES; COMPND 12 MUTATION: 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: G; COMPND 23 SYNONYM: G GAMMA-I; COMPND 24 ENGINEERED: YES; COMPND 25 MOL_ID: 5; COMPND 26 MOLECULE: ANTIBODY FRAGMENT SCFV16; COMPND 27 CHAIN: H; COMPND 28 ENGINEERED: YES; COMPND 29 MOL_ID: 6; COMPND 30 MOLECULE: EP67 LIGAND; COMPND 31 CHAIN: D; COMPND 32 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HUMAN, HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 9606, 10090; SOURCE 5 GENE: CHRM4, C5AR1, C5AR, C5R1; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 GENE: GNAO1; SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562; 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: SPODOPTERA FRUGIPERDA; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 7108; 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: SPODOPTERA FRUGIPERDA; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 29 MOL_ID: 5; SOURCE 30 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 31 ORGANISM_TAXID: 10090; SOURCE 32 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 33 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 34 MOL_ID: 6; SOURCE 35 SYNTHETIC: YES; SOURCE 36 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 37 ORGANISM_TAXID: 9606 KEYWDS GPCR, G PROTEIN, SIGNALING PROTEIN, SIGNALING PROTEIN-IMMUNE SYSTEM KEYWDS 2 COMPLEX 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 9KXS 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. 3.31 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 : NULL 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) : 3.310 REMARK 3 NUMBER OF PARTICLES : 409104 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 9KXS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1300054503. 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 : EP67 BOUND TO MOUSE C5AR1 IN REMARK 245 COMPLEX WITH GO; MOUSE C5A REMARK 245 ANAPHYLATOXIN CHEMOTACTIC REMARK 245 RECEPTOR 1; GUANINE NUCLEOTIDE- REMARK 245 BINDING PROTEIN G(O) SUBUNIT REMARK 245 ALPHA; GUANINE NUCLEOTIDE- REMARK 245 BINDING PROTEIN G(I)/G(S)/G(T) REMARK 245 SUBUNIT BETA-1; ANTIBODY REMARK 245 FRAGMENT SCFV16; GUANINE REMARK 245 NUCLEOTIDE-BINDING PROTEIN G(I)/ REMARK 245 G(S)/G(O) SUBUNIT GAMMA-2; EP67 REMARK 245 LIGAND 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 : THIS IS A VARIANT OF GUANINE REMARK 245 NUCLEOTIDE-BINDING PROTEIN G(O) SUBUNIT ALPHA CALLED THE "MINI REMARK 245 G(O) ALPHA" 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 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1800.00 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) : 4849.00 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: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, G, H, D 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 -55 REMARK 465 GLY A -54 REMARK 465 LYS A -53 REMARK 465 THR A -52 REMARK 465 ILE A -51 REMARK 465 ILE A -50 REMARK 465 ALA A -49 REMARK 465 LEU A -48 REMARK 465 SER A -47 REMARK 465 TYR A -46 REMARK 465 ILE A -45 REMARK 465 PHE A -44 REMARK 465 CYS A -43 REMARK 465 LEU A -42 REMARK 465 VAL A -41 REMARK 465 PHE A -40 REMARK 465 ALA A -39 REMARK 465 ASP A -38 REMARK 465 TYR A -37 REMARK 465 LYS A -36 REMARK 465 ASP A -35 REMARK 465 ASP A -34 REMARK 465 ASP A -33 REMARK 465 ASP A -32 REMARK 465 ALA A -31 REMARK 465 ALA A -30 REMARK 465 ASN A -29 REMARK 465 PHE A -28 REMARK 465 THR A -27 REMARK 465 PRO A -26 REMARK 465 VAL A -25 REMARK 465 ASN A -24 REMARK 465 GLY A -23 REMARK 465 SER A -22 REMARK 465 SER A -21 REMARK 465 GLY A -20 REMARK 465 ASN A -19 REMARK 465 GLN A -18 REMARK 465 SER A -17 REMARK 465 VAL A -16 REMARK 465 ARG A -15 REMARK 465 LEU A -14 REMARK 465 VAL A -13 REMARK 465 THR A -12 REMARK 465 SER A -11 REMARK 465 SER A -10 REMARK 465 SER A -9 REMARK 465 LEU A -8 REMARK 465 GLU A -7 REMARK 465 VAL A -6 REMARK 465 LEU A -5 REMARK 465 PHE A -4 REMARK 465 GLN A -3 REMARK 465 GLY A -2 REMARK 465 PRO A -1 REMARK 465 GLY A 0 REMARK 465 SER A 1 REMARK 465 ASP A 2 REMARK 465 PRO A 3 REMARK 465 ILE A 4 REMARK 465 ASP A 5 REMARK 465 ASN A 6 REMARK 465 SER A 7 REMARK 465 SER A 8 REMARK 465 PHE A 9 REMARK 465 GLU A 10 REMARK 465 ILE A 11 REMARK 465 ASN A 12 REMARK 465 TYR A 13 REMARK 465 ASP A 14 REMARK 465 HIS A 15 REMARK 465 TYR A 16 REMARK 465 GLY A 17 REMARK 465 THR A 18 REMARK 465 MET A 19 REMARK 465 ASP A 20 REMARK 465 PRO A 21 REMARK 465 ASN A 22 REMARK 465 ILE A 23 REMARK 465 PRO A 24 REMARK 465 ALA A 25 REMARK 465 ASP A 26 REMARK 465 GLY A 27 REMARK 465 ILE A 28 REMARK 465 HIS A 29 REMARK 465 LEU A 30 REMARK 465 PRO A 31 REMARK 465 PHE A 180A REMARK 465 TYR A 180B REMARK 465 SER A 180C REMARK 465 GLU A 180D REMARK 465 GLY A 194 REMARK 465 GLY A 195 REMARK 465 SER A 196 REMARK 465 PHE A 197 REMARK 465 LEU A 316 REMARK 465 PRO A 317 REMARK 465 SER A 318 REMARK 465 ILE A 319 REMARK 465 ILE A 320 REMARK 465 ARG A 321 REMARK 465 ASN A 322 REMARK 465 ALA A 323 REMARK 465 LEU A 324 REMARK 465 SER A 325 REMARK 465 GLU A 326 REMARK 465 ASP A 327 REMARK 465 SER A 328 REMARK 465 VAL A 329 REMARK 465 GLY A 330 REMARK 465 ARG A 331 REMARK 465 ASP A 332 REMARK 465 SER A 333 REMARK 465 LYS A 334 REMARK 465 THR A 335 REMARK 465 PHE A 336 REMARK 465 THR A 337 REMARK 465 PRO A 338 REMARK 465 SER A 339 REMARK 465 THR A 340 REMARK 465 THR A 341 REMARK 465 ASP A 342 REMARK 465 THR A 343 REMARK 465 SER A 344 REMARK 465 THR A 345 REMARK 465 ARG A 346 REMARK 465 LYS A 347 REMARK 465 SER A 348 REMARK 465 GLN A 349 REMARK 465 ALA A 350 REMARK 465 VAL A 351 REMARK 465 MET B -11 REMARK 465 GLY B -10 REMARK 465 HIS 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 GLU B -3 REMARK 465 ASN B -2 REMARK 465 LEU B -1 REMARK 465 TYR B 0 REMARK 465 PHE B 1 REMARK 465 GLN B 2 REMARK 465 GLY B 3 REMARK 465 THR B 4 REMARK 465 ILE B 171 REMARK 465 ILE B 172 REMARK 465 HIS B 173 REMARK 465 GLY B 174 REMARK 465 GLY B 175 REMARK 465 SER B 176 REMARK 465 GLY B 177 REMARK 465 GLY B 178 REMARK 465 SER B 179 REMARK 465 GLY B 180 REMARK 465 GLY B 181 REMARK 465 THR B 182 REMARK 465 TYR B 241 REMARK 465 ASN B 242 REMARK 465 ARG B 243 REMARK 465 MET B 244 REMARK 465 ALA B 326 REMARK 465 THR B 327 REMARK 465 MET C -9 REMARK 465 HIS C -8 REMARK 465 HIS C -7 REMARK 465 HIS C -6 REMARK 465 HIS C -5 REMARK 465 HIS C -4 REMARK 465 HIS 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 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 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 GLY H 135 REMARK 465 GLY H 249 REMARK 465 SER H 250 REMARK 465 LEU H 251 REMARK 465 GLU H 252 REMARK 465 VAL H 253 REMARK 465 LEU H 254 REMARK 465 PHE H 255 REMARK 465 GLN H 256 REMARK 465 TYR D 1 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 32 CG CD CE NZ REMARK 470 ARG A 33 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 37 CG OD1 OD2 REMARK 470 ARG A 67 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 68 CG CD NE CZ NH1 NH2 REMARK 470 PHE A 93 CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR A 103 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS A 179 CG CD CE NZ REMARK 470 LYS A 277 CG CD CE NZ REMARK 470 PHE A 308 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG A 314 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 9 CG CD OE1 OE2 REMARK 470 ARG B 10 CG CD NE CZ NH1 NH2 REMARK 470 LEU B 13 CG CD1 CD2 REMARK 470 GLU B 20 CG CD OE1 OE2 REMARK 470 LYS B 21 CG CD CE NZ REMARK 470 LYS B 24 CG CD CE NZ REMARK 470 GLU B 25 CG CD OE1 OE2 REMARK 470 SER B 29 OG REMARK 470 ASP B 42 CB CG OD1 OD2 REMARK 470 ASN B 43 CG OD1 ND2 REMARK 470 VAL B 50 CG1 CG2 REMARK 470 LYS B 51 CG CD CE NZ REMARK 470 GLN B 52 CG CD OE1 NE2 REMARK 470 MET B 53 CG SD CE REMARK 470 LYS B 54 CG CD CE NZ REMARK 470 ILE B 185 CG1 CG2 CD1 REMARK 470 HIS B 196 CG ND1 CD2 CE1 NE2 REMARK 470 GLU B 208 CG CD OE1 OE2 REMARK 470 LYS B 210 CG CD CE NZ REMARK 470 LYS B 211 CG CD CE NZ REMARK 470 ASP B 218 CG OD1 OD2 REMARK 470 ASP B 227 CG OD1 OD2 REMARK 470 SER B 229 OG REMARK 470 ASP B 230 CB CG OD1 OD2 REMARK 470 GLU B 246 CG CD OE1 OE2 REMARK 470 MET B 249 CG SD CE REMARK 470 ASP B 252 CG OD1 OD2 REMARK 470 LYS B 258 CG CD CE NZ REMARK 470 ASP B 262 CG OD1 OD2 REMARK 470 LYS B 272 CG CD CE NZ REMARK 470 LYS B 278 CG CD CE NZ REMARK 470 LYS B 280 CG CD CE NZ REMARK 470 LYS B 281 CG CD CE NZ REMARK 470 GLU B 290 CG CD OE1 OE2 REMARK 470 TYR B 291 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU B 298 CG CD OE1 OE2 REMARK 470 GLN B 307 CG CD OE1 NE2 REMARK 470 LYS B 311 CG CD CE NZ REMARK 470 ARG B 313 CG CD NE CZ NH1 NH2 REMARK 470 ASN B 316 CG OD1 ND2 REMARK 470 LYS B 317 CG CD CE NZ REMARK 470 HIS B 322 CG ND1 CD2 CE1 NE2 REMARK 470 THR B 324 OG1 CG2 REMARK 470 CYS B 325 SG REMARK 470 ASP B 328 CG OD1 OD2 REMARK 470 THR B 329 OG1 CG2 REMARK 470 ILE B 335 CG1 CG2 CD1 REMARK 470 ILE B 342 CG1 CG2 CD1 REMARK 470 ASN B 346 CG OD1 ND2 REMARK 470 LEU B 348 CG CD1 CD2 REMARK 470 GLU C 3 CG CD OE1 OE2 REMARK 470 GLN C 6 CG CD OE1 NE2 REMARK 470 ARG C 8 CG CD NE CZ NH1 NH2 REMARK 470 GLN C 9 CG CD OE1 NE2 REMARK 470 GLU C 12 CG CD OE1 OE2 REMARK 470 GLN C 13 CG CD OE1 NE2 REMARK 470 LEU C 14 CG CD1 CD2 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 ASP C 27 CG OD1 OD2 REMARK 470 THR C 29 OG1 CG2 REMARK 470 THR C 34 OG1 CG2 REMARK 470 ASN C 36 CG OD1 ND2 REMARK 470 ARG C 42 CG CD NE CZ NH1 NH2 REMARK 470 GLN C 44 CG CD OE1 NE2 REMARK 470 ARG C 49 CG CD NE CZ NH1 NH2 REMARK 470 GLN C 75 CG CD OE1 NE2 REMARK 470 ASP C 76 CG OD1 OD2 REMARK 470 ILE C 80 CG1 CG2 CD1 REMARK 470 ILE C 81 CG1 CG2 CD1 REMARK 470 ARG C 96 CG CD NE CZ NH1 NH2 REMARK 470 SER C 98 OG REMARK 470 CYS C 103 SG REMARK 470 LEU C 126 CG CD1 CD2 REMARK 470 GLU C 130 CG CD OE1 OE2 REMARK 470 VAL C 133 CG1 CG2 REMARK 470 ARG C 137 CG CD NE CZ NH1 NH2 REMARK 470 ILE C 157 CG1 CG2 CD1 REMARK 470 SER C 161 OG REMARK 470 ASP C 163 CG OD1 OD2 REMARK 470 GLU C 172 CG CD OE1 OE2 REMARK 470 SER C 189 OG REMARK 470 LEU C 192 CG CD1 CD2 REMARK 470 ARG C 197 CG CD NE CZ NH1 NH2 REMARK 470 VAL C 200 CG1 CG2 REMARK 470 ARG C 214 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 215 CG CD OE1 OE2 REMARK 470 MET C 217 CG SD CE REMARK 470 ASP C 228 CG OD1 OD2 REMARK 470 MET C 262 CG SD CE REMARK 470 ILE C 269 CG1 CG2 CD1 REMARK 470 CYS C 271 SG REMARK 470 ASP C 290 CG OD1 OD2 REMARK 470 LEU C 308 CG CD1 CD2 REMARK 470 ASP C 312 CG OD1 OD2 REMARK 470 SER C 316 OG REMARK 470 THR C 321 OG1 CG2 REMARK 470 ASP C 323 CG OD1 OD2 REMARK 470 SER C 331 OG REMARK 470 SER C 334 OG REMARK 470 ASN C 340 CG OD1 ND2 REMARK 470 ILE G 9 CG1 CG2 CD1 REMARK 470 ARG G 13 CG CD NE CZ NH1 NH2 REMARK 470 LYS G 14 CG CD CE NZ REMARK 470 GLU G 17 CG CD OE1 OE2 REMARK 470 ILE G 25 CG1 CG2 CD1 REMARK 470 ASP G 36 CG OD1 OD2 REMARK 470 SER G 57 OG REMARK 470 GLU G 58 CG CD OE1 OE2 REMARK 470 ARG G 62 CG CD NE CZ NH1 NH2 REMARK 470 GLU H 6 CG CD OE1 OE2 REMARK 470 GLN H 13 CG CD OE1 NE2 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 LEU H 45 CG CD1 CD2 REMARK 470 GLU H 46 CG CD OE1 OE2 REMARK 470 SER H 52 OG 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 SER H 71 OG REMARK 470 ASP H 73 CG OD1 OD2 REMARK 470 LYS H 76 CG CD CE NZ REMARK 470 ASN H 77 CG OD1 ND2 REMARK 470 LEU H 79 CG CD1 CD2 REMARK 470 GLN H 82 CG CD OE1 NE2 REMARK 470 SER H 85 OG REMARK 470 LEU H 86 CG CD1 CD2 REMARK 470 ARG H 87 CG CD NE CZ NH1 NH2 REMARK 470 GLU H 89 CG CD OE1 OE2 REMARK 470 SER H 121 OG REMARK 470 SER H 136 OG REMARK 470 VAL H 149 CG1 CG2 REMARK 470 GLU H 153 CG CD OE1 OE2 REMARK 470 ILE H 157 CG1 CG2 CD1 REMARK 470 ARG H 160 CG CD NE CZ NH1 NH2 REMARK 470 SER H 161 OG REMARK 470 SER H 162 OG REMARK 470 LEU H 174 CG CD1 CD2 REMARK 470 LEU H 178 CG CD1 CD2 REMARK 470 GLN H 186 CG CD OE1 NE2 REMARK 470 ARG H 218 CG CD NE CZ NH1 NH2 REMARK 470 MET H 230 CG SD CE REMARK 470 GLN H 231 CG CD OE1 NE2 REMARK 470 GLU H 234 CG CD OE1 OE2 REMARK 470 LYS H 244 CG CD CE NZ REMARK 470 LYS H 248 CG CD CE NZ 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 ALA B 7 -61.38 -94.78 REMARK 500 LEU B 228 56.53 -92.48 REMARK 500 TRP C 63 -168.44 -79.22 REMARK 500 ASP C 153 -168.30 -129.17 REMARK 500 SER C 189 159.20 178.02 REMARK 500 SER C 191 115.06 -162.17 REMARK 500 GLU G 58 31.15 -99.27 REMARK 500 PHE G 61 32.92 -98.86 REMARK 500 VAL H 48 -60.45 -124.24 REMARK 500 TYR H 50 148.14 -173.12 REMARK 500 ALA H 92 -169.45 -169.02 REMARK 500 TYR H 102 -169.70 -161.64 REMARK 500 THR H 210 -32.14 -131.07 REMARK 500 HIS H 232 21.10 -140.94 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-62626 RELATED DB: EMDB REMARK 900 STRUCTURE OF EP67 BOUND MOUSE C5AR1 IN COMPLEX WITH GO DBREF 9KXS A -30 -9 UNP P08173 ACM4_HUMAN 2 23 DBREF 9KXS A 2 351 UNP P30993 C5AR1_MOUSE 2 351 DBREF 9KXS B 4 53 UNP P09471 GNAO_HUMAN 4 53 DBREF 9KXS B 182 354 UNP P09471 GNAO_HUMAN 182 354 DBREF 9KXS C 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 9KXS G 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 9KXS H 1 256 PDB 9KXS 9KXS 1 256 DBREF 9KXS D 1 10 PDB 9KXS 9KXS 1 10 SEQADV 9KXS MET A -55 UNP P08173 INITIATING METHIONINE SEQADV 9KXS GLY A -54 UNP P08173 EXPRESSION TAG SEQADV 9KXS LYS A -53 UNP P08173 EXPRESSION TAG SEQADV 9KXS THR A -52 UNP P08173 EXPRESSION TAG SEQADV 9KXS ILE A -51 UNP P08173 EXPRESSION TAG SEQADV 9KXS ILE A -50 UNP P08173 EXPRESSION TAG SEQADV 9KXS ALA A -49 UNP P08173 EXPRESSION TAG SEQADV 9KXS LEU A -48 UNP P08173 EXPRESSION TAG SEQADV 9KXS SER A -47 UNP P08173 EXPRESSION TAG SEQADV 9KXS TYR A -46 UNP P08173 EXPRESSION TAG SEQADV 9KXS ILE A -45 UNP P08173 EXPRESSION TAG SEQADV 9KXS PHE A -44 UNP P08173 EXPRESSION TAG SEQADV 9KXS CYS A -43 UNP P08173 EXPRESSION TAG SEQADV 9KXS LEU A -42 UNP P08173 EXPRESSION TAG SEQADV 9KXS VAL A -41 UNP P08173 EXPRESSION TAG SEQADV 9KXS PHE A -40 UNP P08173 EXPRESSION TAG SEQADV 9KXS ALA A -39 UNP P08173 EXPRESSION TAG SEQADV 9KXS ASP A -38 UNP P08173 EXPRESSION TAG SEQADV 9KXS TYR A -37 UNP P08173 EXPRESSION TAG SEQADV 9KXS LYS A -36 UNP P08173 EXPRESSION TAG SEQADV 9KXS ASP A -35 UNP P08173 EXPRESSION TAG SEQADV 9KXS ASP A -34 UNP P08173 EXPRESSION TAG SEQADV 9KXS ASP A -33 UNP P08173 EXPRESSION TAG SEQADV 9KXS ASP A -32 UNP P08173 EXPRESSION TAG SEQADV 9KXS ALA A -31 UNP P08173 EXPRESSION TAG SEQADV 9KXS LEU A -8 UNP P08173 LINKER SEQADV 9KXS GLU A -7 UNP P08173 LINKER SEQADV 9KXS VAL A -6 UNP P08173 LINKER SEQADV 9KXS LEU A -5 UNP P08173 LINKER SEQADV 9KXS PHE A -4 UNP P08173 LINKER SEQADV 9KXS GLN A -3 UNP P08173 LINKER SEQADV 9KXS GLY A -2 UNP P08173 LINKER SEQADV 9KXS PRO A -1 UNP P08173 LINKER SEQADV 9KXS GLY A 0 UNP P08173 LINKER SEQADV 9KXS SER A 1 UNP P08173 LINKER SEQADV 9KXS MET B -11 UNP P09471 INITIATING METHIONINE SEQADV 9KXS GLY B -10 UNP P09471 EXPRESSION TAG SEQADV 9KXS HIS B -9 UNP P09471 EXPRESSION TAG SEQADV 9KXS HIS B -8 UNP P09471 EXPRESSION TAG SEQADV 9KXS HIS B -7 UNP P09471 EXPRESSION TAG SEQADV 9KXS HIS B -6 UNP P09471 EXPRESSION TAG SEQADV 9KXS HIS B -5 UNP P09471 EXPRESSION TAG SEQADV 9KXS HIS B -4 UNP P09471 EXPRESSION TAG SEQADV 9KXS GLU B -3 UNP P09471 EXPRESSION TAG SEQADV 9KXS ASN B -2 UNP P09471 EXPRESSION TAG SEQADV 9KXS LEU B -1 UNP P09471 EXPRESSION TAG SEQADV 9KXS TYR B 0 UNP P09471 EXPRESSION TAG SEQADV 9KXS PHE B 1 UNP P09471 EXPRESSION TAG SEQADV 9KXS GLN B 2 UNP P09471 EXPRESSION TAG SEQADV 9KXS GLY B 3 UNP P09471 EXPRESSION TAG SEQADV 9KXS ASP B 42 UNP P09471 GLY 42 ENGINEERED MUTATION SEQADV 9KXS ASN B 43 UNP P09471 GLU 43 ENGINEERED MUTATION SEQADV 9KXS LYS B 54 UNP P09471 LINKER SEQADV 9KXS ILE B 171 UNP P09471 LINKER SEQADV 9KXS ILE B 172 UNP P09471 LINKER SEQADV 9KXS HIS B 173 UNP P09471 LINKER SEQADV 9KXS GLY B 174 UNP P09471 LINKER SEQADV 9KXS GLY B 175 UNP P09471 LINKER SEQADV 9KXS SER B 176 UNP P09471 LINKER SEQADV 9KXS GLY B 177 UNP P09471 LINKER SEQADV 9KXS GLY B 178 UNP P09471 LINKER SEQADV 9KXS SER B 179 UNP P09471 LINKER SEQADV 9KXS GLY B 180 UNP P09471 LINKER SEQADV 9KXS GLY B 181 UNP P09471 LINKER SEQADV 9KXS ASP B 227 UNP P09471 ALA 227 ENGINEERED MUTATION SEQADV 9KXS ASP B 230 UNP P09471 GLY 230 ENGINEERED MUTATION SEQADV 9KXS B UNP P09471 ASP 232 DELETION SEQADV 9KXS B UNP P09471 GLN 233 DELETION SEQADV 9KXS B UNP P09471 VAL 234 DELETION SEQADV 9KXS B UNP P09471 LEU 235 DELETION SEQADV 9KXS B UNP P09471 HIS 236 DELETION SEQADV 9KXS B UNP P09471 GLU 237 DELETION SEQADV 9KXS B UNP P09471 ASP 238 DELETION SEQADV 9KXS B UNP P09471 GLU 239 DELETION SEQADV 9KXS B UNP P09471 THR 240 DELETION SEQADV 9KXS B UNP P09471 THR 241 DELETION SEQADV 9KXS ALA B 332 UNP P09471 ILE 332 ENGINEERED MUTATION SEQADV 9KXS ILE B 335 UNP P09471 VAL 335 ENGINEERED MUTATION SEQADV 9KXS MET C -9 UNP P62873 INITIATING METHIONINE SEQADV 9KXS HIS C -8 UNP P62873 EXPRESSION TAG SEQADV 9KXS HIS C -7 UNP P62873 EXPRESSION TAG SEQADV 9KXS HIS C -6 UNP P62873 EXPRESSION TAG SEQADV 9KXS HIS C -5 UNP P62873 EXPRESSION TAG SEQADV 9KXS HIS C -4 UNP P62873 EXPRESSION TAG SEQADV 9KXS HIS C -3 UNP P62873 EXPRESSION TAG SEQADV 9KXS GLY C -2 UNP P62873 EXPRESSION TAG SEQADV 9KXS SER C -1 UNP P62873 EXPRESSION TAG SEQADV 9KXS SER C 0 UNP P62873 EXPRESSION TAG SEQADV 9KXS GLY C 1 UNP P62873 EXPRESSION TAG SEQRES 1 A 407 MET GLY LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS SEQRES 2 A 407 LEU VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP ALA ALA SEQRES 3 A 407 ASN PHE THR PRO VAL ASN GLY SER SER GLY ASN GLN SER SEQRES 4 A 407 VAL ARG LEU VAL THR SER SER SER LEU GLU VAL LEU PHE SEQRES 5 A 407 GLN GLY PRO GLY SER ASP PRO ILE ASP ASN SER SER PHE SEQRES 6 A 407 GLU ILE ASN TYR ASP HIS TYR GLY THR MET ASP PRO ASN SEQRES 7 A 407 ILE PRO ALA ASP GLY ILE HIS LEU PRO LYS ARG GLN PRO SEQRES 8 A 407 GLY ASP VAL ALA ALA LEU ILE ILE TYR SER VAL VAL PHE SEQRES 9 A 407 LEU VAL GLY VAL PRO GLY ASN ALA LEU VAL VAL TRP VAL SEQRES 10 A 407 THR ALA PHE GLU ALA ARG ARG ALA VAL ASN ALA ILE TRP SEQRES 11 A 407 PHE LEU ASN LEU ALA VAL ALA ASP LEU LEU SER CYS LEU SEQRES 12 A 407 ALA LEU PRO VAL LEU PHE THR THR VAL LEU ASN HIS ASN SEQRES 13 A 407 TYR TRP TYR PHE ASP ALA THR ALA CYS ILE VAL LEU PRO SEQRES 14 A 407 SER LEU ILE LEU LEU ASN MET TYR ALA SER ILE LEU LEU SEQRES 15 A 407 LEU ALA THR ILE SER ALA ASP ARG PHE LEU LEU VAL PHE SEQRES 16 A 407 LYS PRO ILE TRP CYS GLN LYS VAL ARG GLY THR GLY LEU SEQRES 17 A 407 ALA TRP MET ALA CYS GLY VAL ALA TRP VAL LEU ALA LEU SEQRES 18 A 407 LEU LEU THR ILE PRO SER PHE VAL TYR ARG GLU ALA TYR SEQRES 19 A 407 LYS ASP PHE TYR SER GLU HIS THR VAL CYS GLY ILE ASN SEQRES 20 A 407 TYR GLY GLY GLY SER PHE PRO LYS GLU LYS ALA VAL ALA SEQRES 21 A 407 ILE LEU ARG LEU MET VAL GLY PHE VAL LEU PRO LEU LEU SEQRES 22 A 407 THR LEU ASN ILE CYS TYR THR PHE LEU LEU LEU ARG THR SEQRES 23 A 407 TRP SER ARG LYS ALA THR ARG SER THR LYS THR LEU LYS SEQRES 24 A 407 VAL VAL MET ALA VAL VAL ILE CYS PHE PHE ILE PHE TRP SEQRES 25 A 407 LEU PRO TYR GLN VAL THR GLY VAL MET ILE ALA TRP LEU SEQRES 26 A 407 PRO PRO SER SER PRO THR LEU LYS ARG VAL GLU LYS LEU SEQRES 27 A 407 ASN SER LEU CYS VAL SER LEU ALA TYR ILE ASN CYS CYS SEQRES 28 A 407 VAL ASN PRO ILE ILE TYR VAL MET ALA GLY GLN GLY PHE SEQRES 29 A 407 HIS GLY ARG LEU LEU ARG SER LEU PRO SER ILE ILE ARG SEQRES 30 A 407 ASN ALA LEU SER GLU ASP SER VAL GLY ARG ASP SER LYS SEQRES 31 A 407 THR PHE THR PRO SER THR THR ASP THR SER THR ARG LYS SEQRES 32 A 407 SER GLN ALA VAL SEQRES 1 B 240 MET GLY HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE SEQRES 2 B 240 GLN GLY THR LEU SER ALA GLU GLU ARG ALA ALA LEU GLU SEQRES 3 B 240 ARG SER LYS ALA ILE GLU LYS ASN LEU LYS GLU ASP GLY SEQRES 4 B 240 ILE SER ALA ALA LYS ASP VAL LYS LEU LEU LEU LEU GLY SEQRES 5 B 240 ALA ASP ASN SER GLY LYS SER THR ILE VAL LYS GLN MET SEQRES 6 B 240 LYS ILE ILE HIS GLY GLY SER GLY GLY SER GLY GLY THR SEQRES 7 B 240 THR GLY ILE VAL GLU THR HIS PHE THR PHE LYS ASN LEU SEQRES 8 B 240 HIS PHE ARG LEU PHE ASP VAL GLY GLY GLN ARG SER GLU SEQRES 9 B 240 ARG LYS LYS TRP ILE HIS CYS PHE GLU ASP VAL THR ALA SEQRES 10 B 240 ILE ILE PHE CYS VAL ASP LEU SER ASP TYR ASN ARG MET SEQRES 11 B 240 HIS GLU SER LEU MET LEU PHE ASP SER ILE CYS ASN ASN SEQRES 12 B 240 LYS PHE PHE ILE ASP THR SER ILE ILE LEU PHE LEU ASN SEQRES 13 B 240 LYS LYS ASP LEU PHE GLY GLU LYS ILE LYS LYS SER PRO SEQRES 14 B 240 LEU THR ILE CYS PHE PRO GLU TYR THR GLY PRO ASN THR SEQRES 15 B 240 TYR GLU ASP ALA ALA ALA TYR ILE GLN ALA GLN PHE GLU SEQRES 16 B 240 SER LYS ASN ARG SER PRO ASN LYS GLU ILE TYR CYS HIS SEQRES 17 B 240 MET THR CYS ALA THR ASP THR ASN ASN ALA GLN VAL ILE SEQRES 18 B 240 PHE ASP ALA VAL THR ASP ILE ILE ILE ALA ASN ASN LEU SEQRES 19 B 240 ARG GLY CYS GLY LEU TYR SEQRES 1 C 350 MET HIS HIS HIS HIS HIS HIS GLY SER SER GLY SER GLU SEQRES 2 C 350 LEU ASP GLN LEU ARG GLN GLU ALA GLU GLN LEU LYS ASN SEQRES 3 C 350 GLN ILE ARG ASP ALA ARG LYS ALA CYS ALA ASP ALA THR SEQRES 4 C 350 LEU SER GLN ILE THR ASN ASN ILE ASP PRO VAL GLY ARG SEQRES 5 C 350 ILE GLN MET ARG THR ARG ARG THR LEU ARG GLY HIS LEU SEQRES 6 C 350 ALA LYS ILE TYR ALA MET HIS TRP GLY THR ASP SER ARG SEQRES 7 C 350 LEU LEU VAL SER ALA SER GLN ASP GLY LYS LEU ILE ILE SEQRES 8 C 350 TRP ASP SER TYR THR THR ASN LYS VAL HIS ALA ILE PRO SEQRES 9 C 350 LEU ARG SER SER TRP VAL MET THR CYS ALA TYR ALA PRO SEQRES 10 C 350 SER GLY ASN TYR VAL ALA CYS GLY GLY LEU ASP ASN ILE SEQRES 11 C 350 CYS SER ILE TYR ASN LEU LYS THR ARG GLU GLY ASN VAL SEQRES 12 C 350 ARG VAL SER ARG GLU LEU ALA GLY HIS THR GLY TYR LEU SEQRES 13 C 350 SER CYS CYS ARG PHE LEU ASP ASP ASN GLN ILE VAL THR SEQRES 14 C 350 SER SER GLY ASP THR THR CYS ALA LEU TRP ASP ILE GLU SEQRES 15 C 350 THR GLY GLN GLN THR THR THR PHE THR GLY HIS THR GLY SEQRES 16 C 350 ASP VAL MET SER LEU SER LEU ALA PRO ASP THR ARG LEU SEQRES 17 C 350 PHE VAL SER GLY ALA CYS ASP ALA SER ALA LYS LEU TRP SEQRES 18 C 350 ASP VAL ARG GLU GLY MET CYS ARG GLN THR PHE THR GLY SEQRES 19 C 350 HIS GLU SER ASP ILE ASN ALA ILE CYS PHE PHE PRO ASN SEQRES 20 C 350 GLY ASN ALA PHE ALA THR GLY SER ASP ASP ALA THR CYS SEQRES 21 C 350 ARG LEU PHE ASP LEU ARG ALA ASP GLN GLU LEU MET THR SEQRES 22 C 350 TYR SER HIS ASP ASN ILE ILE CYS GLY ILE THR SER VAL SEQRES 23 C 350 SER PHE SER LYS SER GLY ARG LEU LEU LEU ALA GLY TYR SEQRES 24 C 350 ASP ASP PHE ASN CYS ASN VAL TRP ASP ALA LEU LYS ALA SEQRES 25 C 350 ASP ARG ALA GLY VAL LEU ALA GLY HIS ASP ASN ARG VAL SEQRES 26 C 350 SER CYS LEU GLY VAL THR ASP ASP GLY MET ALA VAL ALA SEQRES 27 C 350 THR GLY SER TRP ASP 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 H 256 ASP VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 256 PRO GLY GLY SER ARG LYS LEU SER CYS SER ALA SER GLY SEQRES 3 H 256 PHE ALA PHE SER SER PHE GLY MET HIS TRP VAL ARG GLN SEQRES 4 H 256 ALA PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SEQRES 5 H 256 SER GLY SER GLY THR ILE TYR TYR ALA ASP THR VAL LYS SEQRES 6 H 256 GLY ARG PHE THR ILE SER ARG ASP ASP PRO LYS ASN THR SEQRES 7 H 256 LEU PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR SEQRES 8 H 256 ALA MET TYR TYR CYS VAL ARG SER ILE TYR TYR TYR GLY SEQRES 9 H 256 SER SER PRO PHE ASP PHE TRP GLY GLN GLY THR THR LEU SEQRES 10 H 256 THR VAL SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SEQRES 11 H 256 SER GLY GLY GLY GLY SER ASP ILE VAL MET THR GLN ALA SEQRES 12 H 256 THR SER SER VAL PRO VAL THR PRO GLY GLU SER VAL SER SEQRES 13 H 256 ILE SER CYS ARG SER SER LYS SER LEU LEU HIS SER ASN SEQRES 14 H 256 GLY ASN THR TYR LEU TYR TRP PHE LEU GLN ARG PRO GLY SEQRES 15 H 256 GLN SER PRO GLN LEU LEU ILE TYR ARG MET SER ASN LEU SEQRES 16 H 256 ALA SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SER SEQRES 17 H 256 GLY THR ALA PHE THR LEU THR ILE SER ARG LEU GLU ALA SEQRES 18 H 256 GLU ASP VAL GLY VAL TYR TYR CYS MET GLN HIS LEU GLU SEQRES 19 H 256 TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU LEU SEQRES 20 H 256 LYS GLY SER LEU GLU VAL LEU PHE GLN SEQRES 1 D 10 TYR SER PHE LYS ASP MET PRO MLE DAL ARG HET MLE D 8 9 HET DAL D 9 5 HETNAM MLE N-METHYLLEUCINE HETNAM DAL D-ALANINE FORMUL 6 MLE C7 H15 N O2 FORMUL 6 DAL C3 H7 N O2 HELIX 1 AA1 GLN A 34 ALA A 66 1 33 HELIX 2 AA2 ARG A 67 ARG A 68 5 2 HELIX 3 AA3 ALA A 69 ASN A 71 5 3 HELIX 4 AA4 ALA A 72 ALA A 88 1 17 HELIX 5 AA5 ALA A 88 ASN A 98 1 11 HELIX 6 AA6 THR A 107 ILE A 110 5 4 HELIX 7 AA7 VAL A 111 LYS A 140 1 30 HELIX 8 AA8 LYS A 140 ARG A 148 1 9 HELIX 9 AA9 GLY A 149 ARG A 175 1 27 HELIX 10 AB1 LYS A 199 TRP A 231 1 33 HELIX 11 AB2 THR A 239 ILE A 266 1 28 HELIX 12 AB3 SER A 273 LYS A 281 1 9 HELIX 13 AB4 LEU A 282 TYR A 291 1 10 HELIX 14 AB5 TYR A 291 ALA A 304 1 14 HELIX 15 AB6 PHE A 308 SER A 315 1 8 HELIX 16 AB7 GLU B 8 ALA B 30 1 23 HELIX 17 AB8 GLY B 45 MET B 53 1 9 HELIX 18 AB9 GLU B 208 ILE B 213 1 6 HELIX 19 AC1 HIS B 214 GLU B 217 5 4 HELIX 20 AC2 GLU B 246 ASN B 256 1 11 HELIX 21 AC3 LYS B 271 SER B 282 1 12 HELIX 22 AC4 TYR B 297 SER B 310 1 14 HELIX 23 AC5 ASN B 330 CYS B 351 1 22 HELIX 24 AC6 LEU C 4 ALA C 26 1 23 HELIX 25 AC7 LEU C 30 ASN C 35 1 6 HELIX 26 AC8 SER G 8 ILE G 25 1 18 HELIX 27 AC9 LYS G 29 HIS G 44 1 16 HELIX 28 AD1 ALA G 45 ASP G 48 5 4 HELIX 29 AD2 GLU H 220 VAL H 224 5 5 SHEET 1 AA1 6 VAL B 186 THR B 191 0 SHEET 2 AA1 6 HIS B 196 ASP B 201 -1 O PHE B 197 N PHE B 190 SHEET 3 AA1 6 ASP B 33 LEU B 38 1 N LEU B 36 O ARG B 198 SHEET 4 AA1 6 ALA B 221 ASP B 227 1 O ILE B 223 N LEU B 37 SHEET 5 AA1 6 SER B 264 ASN B 270 1 O ILE B 266 N ILE B 222 SHEET 6 AA1 6 ILE B 319 MET B 323 1 O TYR B 320 N LEU B 267 SHEET 1 AA2 4 ARG C 49 LEU C 51 0 SHEET 2 AA2 4 LEU C 336 ILE C 338 -1 O LEU C 336 N LEU C 51 SHEET 3 AA2 4 VAL C 327 SER C 331 -1 N THR C 329 O LYS C 337 SHEET 4 AA2 4 VAL C 315 VAL C 320 -1 N SER C 316 O GLY C 330 SHEET 1 AA3 4 ILE C 58 MET C 61 0 SHEET 2 AA3 4 SER C 72 SER C 74 -1 O ALA C 73 N ALA C 60 SHEET 3 AA3 4 LYS C 78 TRP C 82 -1 O ILE C 80 N SER C 72 SHEET 4 AA3 4 LYS C 89 PRO C 94 -1 O ILE C 93 N LEU C 79 SHEET 1 AA4 4 THR C 102 TYR C 105 0 SHEET 2 AA4 4 TYR C 111 GLY C 115 -1 O ALA C 113 N ALA C 104 SHEET 3 AA4 4 CYS C 121 ASN C 125 -1 O SER C 122 N CYS C 114 SHEET 4 AA4 4 ARG C 134 LEU C 139 -1 O LEU C 139 N CYS C 121 SHEET 1 AA5 4 LEU C 146 PHE C 151 0 SHEET 2 AA5 4 ILE C 157 SER C 161 -1 O VAL C 158 N ARG C 150 SHEET 3 AA5 4 CYS C 166 LEU C 168 -1 O ALA C 167 N THR C 159 SHEET 4 AA5 4 THR C 178 PHE C 180 -1 O PHE C 180 N CYS C 166 SHEET 1 AA6 3 LEU C 198 GLY C 202 0 SHEET 2 AA6 3 SER C 207 ASP C 212 -1 O TRP C 211 N PHE C 199 SHEET 3 AA6 3 THR C 221 THR C 223 -1 O PHE C 222 N ALA C 208 SHEET 1 AA7 4 ILE C 229 PHE C 234 0 SHEET 2 AA7 4 ALA C 240 SER C 245 -1 O GLY C 244 N ASN C 230 SHEET 3 AA7 4 CYS C 250 ASP C 254 -1 O PHE C 253 N PHE C 241 SHEET 4 AA7 4 MET C 262 TYR C 264 -1 O TYR C 264 N CYS C 250 SHEET 1 AA8 4 VAL C 276 PHE C 278 0 SHEET 2 AA8 4 LEU C 284 ALA C 287 -1 O LEU C 286 N SER C 277 SHEET 3 AA8 4 ASN C 295 ASP C 298 -1 O TRP C 297 N LEU C 285 SHEET 4 AA8 4 ARG C 304 GLY C 306 -1 O ALA C 305 N VAL C 296 SHEET 1 AA9 4 GLN H 3 SER H 7 0 SHEET 2 AA9 4 SER H 17 SER H 25 -1 O SER H 21 N SER H 7 SHEET 3 AA9 4 THR H 78 THR H 84 -1 O MET H 83 N ARG H 18 SHEET 4 AA9 4 PHE H 68 ASP H 73 -1 N SER H 71 O PHE H 80 SHEET 1 AB1 6 LEU H 11 VAL H 12 0 SHEET 2 AB1 6 THR H 115 VAL H 119 1 O THR H 118 N VAL H 12 SHEET 3 AB1 6 ALA H 92 VAL H 97 -1 N ALA H 92 O LEU H 117 SHEET 4 AB1 6 MET H 34 GLN H 39 -1 N GLN H 39 O MET H 93 SHEET 5 AB1 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AB1 6 ILE H 58 TYR H 60 -1 O TYR H 59 N TYR H 50 SHEET 1 AB2 6 SER H 146 VAL H 149 0 SHEET 2 AB2 6 THR H 243 LEU H 247 1 O GLU H 246 N VAL H 149 SHEET 3 AB2 6 GLY H 225 GLN H 231 -1 N GLY H 225 O LEU H 245 SHEET 4 AB2 6 LEU H 174 GLN H 179 -1 N PHE H 177 O TYR H 228 SHEET 5 AB2 6 GLN H 186 TYR H 190 -1 O GLN H 186 N LEU H 178 SHEET 6 AB2 6 ASN H 194 LEU H 195 -1 O ASN H 194 N TYR H 190 SHEET 1 AB3 3 SER H 154 ARG H 160 0 SHEET 2 AB3 3 ALA H 211 SER H 217 -1 O ILE H 216 N VAL H 155 SHEET 3 AB3 3 PHE H 203 SER H 208 -1 N SER H 206 O THR H 213 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 2 CYS H 159 CYS H 229 1555 1555 2.03 LINK C PRO D 7 N MLE D 8 1555 1555 1.33 LINK C MLE D 8 N DAL D 9 1555 1555 1.33 LINK C DAL D 9 N ARG D 10 1555 1555 1.33 CISPEP 1 TYR H 235 PRO H 236 0 0.32 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