HEADER MEMBRANE PROTEIN 01-FEB-24 8Y62 TITLE CRYO-EM STRUCTURE OF THE C16:0 CERAMIDE-BOUND FPR2-GI COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I) SUBUNIT ALPHA-1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: ADENYLATE CYCLASE-INHIBITING G ALPHA PROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 8 BETA-1; COMPND 9 CHAIN: B; COMPND 10 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 14 GAMMA-2; COMPND 15 CHAIN: C; COMPND 16 SYNONYM: G GAMMA-I; COMPND 17 ENGINEERED: YES; COMPND 18 MOL_ID: 4; COMPND 19 MOLECULE: SCFV16; COMPND 20 CHAIN: E; COMPND 21 ENGINEERED: YES; COMPND 22 MOL_ID: 5; COMPND 23 MOLECULE: N-FORMYL PEPTIDE RECEPTOR 2; COMPND 24 CHAIN: R; COMPND 25 SYNONYM: FMLP-RELATED RECEPTOR I; COMPND 26 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: GNAI1; 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: GNB1; SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 GENE: GNG2; SOURCE 20 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 24 ORGANISM_TAXID: 32630; SOURCE 25 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 27 MOL_ID: 5; SOURCE 28 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 29 ORGANISM_COMMON: HUMAN; SOURCE 30 ORGANISM_TAXID: 9606; SOURCE 31 GENE: FPR2; SOURCE 32 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 33 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR J.P.SUN,C.T.JIANG,W.KONG,X.YU,K.CAI,L.L.GUO REVDAT 1 05-FEB-25 8Y62 0 JRNL AUTH J.P.SUN,C.T.JIANG,W.KONG,X.YU,K.CAI,L.L.GUO JRNL TITL CRYO-EM STRUCTURE OF THE C16:0 FATTY ACID-BOUND FPR2-GI JRNL TITL 2 COMPLEX JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.200 REMARK 3 NUMBER OF PARTICLES : 578458 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 8Y62 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-FEB-24. REMARK 100 THE DEPOSITION ID IS D_1300044331. 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 THE C16:0 REMARK 245 CERAMIDE-BOUND FPR2-GI 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 : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 600.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : DIFFRACTION REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 187.50 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, E, R REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 1 REMARK 465 GLY A 2 REMARK 465 CYS A 3 REMARK 465 THR A 4 REMARK 465 ILE A 56 REMARK 465 HIS A 57 REMARK 465 GLU A 58 REMARK 465 ALA A 59 REMARK 465 GLY A 60 REMARK 465 TYR A 61 REMARK 465 SER A 62 REMARK 465 GLU A 63 REMARK 465 GLU A 64 REMARK 465 GLU A 65 REMARK 465 CYS A 66 REMARK 465 LYS A 67 REMARK 465 GLN A 68 REMARK 465 TYR A 69 REMARK 465 LYS A 70 REMARK 465 ALA A 71 REMARK 465 VAL A 72 REMARK 465 VAL A 73 REMARK 465 TYR A 74 REMARK 465 SER A 75 REMARK 465 ASN A 76 REMARK 465 THR A 77 REMARK 465 ILE A 78 REMARK 465 GLN A 79 REMARK 465 SER A 80 REMARK 465 ILE A 81 REMARK 465 ILE A 82 REMARK 465 ALA A 83 REMARK 465 ILE A 84 REMARK 465 ILE A 85 REMARK 465 ARG A 86 REMARK 465 ALA A 87 REMARK 465 MET A 88 REMARK 465 GLY A 89 REMARK 465 ARG A 90 REMARK 465 LEU A 91 REMARK 465 LYS A 92 REMARK 465 ILE A 93 REMARK 465 ASP A 94 REMARK 465 PHE A 95 REMARK 465 GLY A 96 REMARK 465 ASP A 97 REMARK 465 SER A 98 REMARK 465 ALA A 99 REMARK 465 ARG A 100 REMARK 465 ALA A 101 REMARK 465 ASP A 102 REMARK 465 ASP A 103 REMARK 465 ALA A 104 REMARK 465 ARG A 105 REMARK 465 GLN A 106 REMARK 465 LEU A 107 REMARK 465 PHE A 108 REMARK 465 VAL A 109 REMARK 465 LEU A 110 REMARK 465 ALA A 111 REMARK 465 GLY A 112 REMARK 465 ALA A 113 REMARK 465 ALA A 114 REMARK 465 GLU A 115 REMARK 465 GLU A 116 REMARK 465 GLY A 117 REMARK 465 PHE A 118 REMARK 465 MET A 119 REMARK 465 THR A 120 REMARK 465 ALA A 121 REMARK 465 GLU A 122 REMARK 465 LEU A 123 REMARK 465 ALA A 124 REMARK 465 GLY A 125 REMARK 465 VAL A 126 REMARK 465 ILE A 127 REMARK 465 LYS A 128 REMARK 465 ARG A 129 REMARK 465 LEU A 130 REMARK 465 TRP A 131 REMARK 465 LYS A 132 REMARK 465 ASP A 133 REMARK 465 SER A 134 REMARK 465 GLY A 135 REMARK 465 VAL A 136 REMARK 465 GLN A 137 REMARK 465 ALA A 138 REMARK 465 CYS A 139 REMARK 465 PHE A 140 REMARK 465 ASN A 141 REMARK 465 ARG A 142 REMARK 465 SER A 143 REMARK 465 ARG A 144 REMARK 465 GLU A 145 REMARK 465 TYR A 146 REMARK 465 GLN A 147 REMARK 465 LEU A 148 REMARK 465 ASN A 149 REMARK 465 ASP A 150 REMARK 465 SER A 151 REMARK 465 ALA A 152 REMARK 465 ALA A 153 REMARK 465 TYR A 154 REMARK 465 TYR A 155 REMARK 465 LEU A 156 REMARK 465 ASN A 157 REMARK 465 ASP A 158 REMARK 465 LEU A 159 REMARK 465 ASP A 160 REMARK 465 ARG A 161 REMARK 465 ILE A 162 REMARK 465 ALA A 163 REMARK 465 GLN A 164 REMARK 465 PRO A 165 REMARK 465 ASN A 166 REMARK 465 TYR A 167 REMARK 465 ILE A 168 REMARK 465 PRO A 169 REMARK 465 THR A 170 REMARK 465 GLN A 171 REMARK 465 GLN A 172 REMARK 465 ASP A 173 REMARK 465 VAL A 174 REMARK 465 LEU A 175 REMARK 465 ARG A 176 REMARK 465 THR A 177 REMARK 465 ARG A 178 REMARK 465 VAL A 179 REMARK 465 LYS A 180 REMARK 465 THR A 181 REMARK 465 LEU A 234 REMARK 465 ALA A 235 REMARK 465 GLU A 236 REMARK 465 ASP A 237 REMARK 465 GLU A 238 REMARK 465 GLU A 239 REMARK 465 MET A 240 REMARK 465 ASN A 241 REMARK 465 ARG A 242 REMARK 465 MET B -17 REMARK 465 HIS B -16 REMARK 465 HIS B -15 REMARK 465 HIS B -14 REMARK 465 HIS B -13 REMARK 465 HIS B -12 REMARK 465 HIS B -11 REMARK 465 LEU B -10 REMARK 465 GLU B -9 REMARK 465 VAL B -8 REMARK 465 LEU B -7 REMARK 465 PHE B -6 REMARK 465 GLN B -5 REMARK 465 GLY B -4 REMARK 465 PRO B -3 REMARK 465 GLY B -2 REMARK 465 SER B -1 REMARK 465 SER B 0 REMARK 465 GLY B 1 REMARK 465 SER B 2 REMARK 465 GLU B 3 REMARK 465 LEU B 4 REMARK 465 ASN C 5 REMARK 465 THR C 6 REMARK 465 ALA C 7 REMARK 465 SER C 8 REMARK 465 GLU C 63 REMARK 465 MET E -36 REMARK 465 LEU E -35 REMARK 465 LEU E -34 REMARK 465 VAL E -33 REMARK 465 ASN E -32 REMARK 465 GLN E -31 REMARK 465 SER E -30 REMARK 465 HIS E -29 REMARK 465 GLN E -28 REMARK 465 GLY E -27 REMARK 465 PHE E -26 REMARK 465 ASN E -25 REMARK 465 LYS E -24 REMARK 465 GLU E -23 REMARK 465 HIS E -22 REMARK 465 THR E -21 REMARK 465 SER E -20 REMARK 465 LYS E -19 REMARK 465 MET E -18 REMARK 465 VAL E -17 REMARK 465 SER E -16 REMARK 465 ALA E -15 REMARK 465 ILE E -14 REMARK 465 VAL E -13 REMARK 465 LEU E -12 REMARK 465 TYR E -11 REMARK 465 VAL E -10 REMARK 465 LEU E -9 REMARK 465 LEU E -8 REMARK 465 ALA E -7 REMARK 465 ALA E -6 REMARK 465 ALA E -5 REMARK 465 ALA E -4 REMARK 465 HIS E -3 REMARK 465 SER E -2 REMARK 465 ALA E -1 REMARK 465 PHE E 0 REMARK 465 ALA E 1 REMARK 465 ALA 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 MET R 1 REMARK 465 GLU R 2 REMARK 465 THR R 3 REMARK 465 ASN R 4 REMARK 465 PHE R 5 REMARK 465 SER R 6 REMARK 465 THR R 7 REMARK 465 PRO R 8 REMARK 465 LEU R 9 REMARK 465 ASN R 10 REMARK 465 GLU R 11 REMARK 465 TYR R 12 REMARK 465 GLU R 13 REMARK 465 GLU R 14 REMARK 465 VAL R 15 REMARK 465 SER R 16 REMARK 465 TYR R 17 REMARK 465 GLU R 18 REMARK 465 SER R 19 REMARK 465 ALA R 20 REMARK 465 GLY R 21 REMARK 465 TYR R 22 REMARK 465 THR R 23 REMARK 465 GLY R 172 REMARK 465 ASP R 173 REMARK 465 PRO R 318 REMARK 465 THR R 319 REMARK 465 SER R 320 REMARK 465 LEU R 321 REMARK 465 GLU R 322 REMARK 465 ARG R 323 REMARK 465 ALA R 324 REMARK 465 LEU R 325 REMARK 465 SER R 326 REMARK 465 GLU R 327 REMARK 465 ASP R 328 REMARK 465 SER R 329 REMARK 465 ALA R 330 REMARK 465 PRO R 331 REMARK 465 THR R 332 REMARK 465 ASN R 333 REMARK 465 ASP R 334 REMARK 465 THR R 335 REMARK 465 ALA R 336 REMARK 465 ALA R 337 REMARK 465 ASN R 338 REMARK 465 SER R 339 REMARK 465 ALA R 340 REMARK 465 SER R 341 REMARK 465 PRO R 342 REMARK 465 PRO R 343 REMARK 465 ALA R 344 REMARK 465 GLU R 345 REMARK 465 THR R 346 REMARK 465 GLU R 347 REMARK 465 LEU R 348 REMARK 465 GLN R 349 REMARK 465 ALA R 350 REMARK 465 MET R 351 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 10 CG CD CE NZ REMARK 470 GLU A 25 CG CD OE1 OE2 REMARK 470 ASP A 26 CG OD1 OD2 REMARK 470 GLU A 28 CG CD OE1 OE2 REMARK 470 LYS A 29 CG CD CE NZ REMARK 470 GLU A 33 CG CD OE1 OE2 REMARK 470 GLU A 43 CG CD OE1 OE2 REMARK 470 SER A 44 OG 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 ILE A 55 CG1 CG2 CD1 REMARK 470 HIS A 188 CG ND1 CD2 CE1 NE2 REMARK 470 ASP A 193 CG OD1 OD2 REMARK 470 ARG A 205 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 207 CG CD OE1 OE2 REMARK 470 LYS A 209 CG CD CE NZ REMARK 470 ASP A 229 CG OD1 OD2 REMARK 470 ASP A 231 CG OD1 OD2 REMARK 470 GLU A 245 CG CD OE1 OE2 REMARK 470 ASP A 261 CG OD1 OD2 REMARK 470 LYS A 270 CG CD CE NZ REMARK 470 ASP A 272 CG OD1 OD2 REMARK 470 LEU A 273 CG CD1 CD2 REMARK 470 GLU A 275 CG CD OE1 OE2 REMARK 470 GLU A 276 CG CD OE1 OE2 REMARK 470 LYS A 277 CG CD CE NZ REMARK 470 LYS A 279 CG CD CE NZ REMARK 470 LYS A 280 CG CD CE NZ REMARK 470 GLU A 297 CG CD OE1 OE2 REMARK 470 GLU A 298 CG CD OE1 OE2 REMARK 470 CYS A 305 SG REMARK 470 LYS A 312 CG CD CE NZ REMARK 470 ASP A 315 CG OD1 OD2 REMARK 470 GLU A 318 CG CD OE1 OE2 REMARK 470 ASP A 328 CG OD1 OD2 REMARK 470 LYS A 330 CG CD CE NZ REMARK 470 LYS A 349 CG CD CE NZ 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 GLN B 13 CG CD OE1 NE2 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 LYS B 23 CG CD CE NZ REMARK 470 ASP B 27 CG OD1 OD2 REMARK 470 GLN B 32 CG CD OE1 NE2 REMARK 470 ASN B 35 CG OD1 ND2 REMARK 470 ASP B 38 CG OD1 OD2 REMARK 470 ARG B 42 CG CD NE CZ NH1 NH2 REMARK 470 GLN B 44 CG CD OE1 NE2 REMARK 470 ASP B 66 CG OD1 OD2 REMARK 470 ASP B 76 CG OD1 OD2 REMARK 470 ARG B 96 CG CD NE CZ NH1 NH2 REMARK 470 ASP B 118 CG OD1 OD2 REMARK 470 SER B 161 OG REMARK 470 ASP B 163 CG OD1 OD2 REMARK 470 ASP B 205 CG OD1 OD2 REMARK 470 GLU B 226 CG CD OE1 OE2 REMARK 470 ASN B 237 CG OD1 ND2 REMARK 470 MET B 262 CG SD CE REMARK 470 ASP B 298 CG OD1 OD2 REMARK 470 LYS B 301 CG CD CE NZ REMARK 470 ASP B 303 CG OD1 OD2 REMARK 470 ASP B 312 CG OD1 OD2 REMARK 470 SER B 331 OG REMARK 470 ASP B 333 CG OD1 OD2 REMARK 470 ARG C 13 CG CD NE CZ NH1 NH2 REMARK 470 LYS C 14 CG CD CE NZ REMARK 470 LEU C 15 CG CD1 CD2 REMARK 470 VAL C 16 CG1 CG2 REMARK 470 GLU C 17 CG CD OE1 OE2 REMARK 470 GLN C 18 CG CD OE1 NE2 REMARK 470 LYS C 20 CG CD CE NZ REMARK 470 GLU C 22 CG CD OE1 OE2 REMARK 470 ASN C 24 CG OD1 ND2 REMARK 470 ASP C 26 CG OD1 OD2 REMARK 470 LYS C 29 CG CD CE NZ REMARK 470 LYS C 32 CG CD CE NZ REMARK 470 ASP C 36 CG OD1 OD2 REMARK 470 GLU C 42 CG CD OE1 OE2 REMARK 470 HIS C 44 CG ND1 CD2 CE1 NE2 REMARK 470 LYS C 46 CG CD CE NZ REMARK 470 GLU C 47 CG CD OE1 OE2 REMARK 470 ASP C 48 CG OD1 OD2 REMARK 470 GLU C 58 CG CD OE1 OE2 REMARK 470 ASN C 59 CG OD1 ND2 REMARK 470 ARG C 62 CG CD NE CZ NH1 NH2 REMARK 470 GLU E 6 CG CD OE1 OE2 REMARK 470 GLN E 13 CG CD OE1 NE2 REMARK 470 ARG E 38 CG CD NE CZ NH1 NH2 REMARK 470 GLU E 42 CG CD OE1 OE2 REMARK 470 LYS E 43 CG CD CE NZ REMARK 470 GLU E 46 CG CD OE1 OE2 REMARK 470 TYR E 50 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ASP E 73 CG OD1 OD2 REMARK 470 LYS E 76 CG CD CE NZ REMARK 470 THR E 84 OG1 CG2 REMARK 470 LEU E 86 CG CD1 CD2 REMARK 470 ARG E 87 CG CD NE CZ NH1 NH2 REMARK 470 GLU E 89 CG CD OE1 OE2 REMARK 470 SER E 146 OG REMARK 470 GLU E 153 CG CD OE1 OE2 REMARK 470 ASP E 201 CG OD1 OD2 REMARK 470 ARG E 218 CG CD NE CZ NH1 NH2 REMARK 470 GLU E 220 CG CD OE1 OE2 REMARK 470 GLU E 222 CG CD OE1 OE2 REMARK 470 GLU E 234 CG CD OE1 OE2 REMARK 470 LYS E 244 CG CD CE NZ REMARK 470 GLU E 246 CG CD OE1 OE2 REMARK 470 VAL R 24 CG1 CG2 REMARK 470 LEU R 25 CG CD1 CD2 REMARK 470 ARG R 26 CG CD NE CZ NH1 NH2 REMARK 470 ILE R 27 CG1 CG2 CD1 REMARK 470 LEU R 28 CG CD1 CD2 REMARK 470 LEU R 30 CG CD1 CD2 REMARK 470 VAL R 31 CG1 CG2 REMARK 470 VAL R 32 CG1 CG2 REMARK 470 VAL R 35 CG1 CG2 REMARK 470 THR R 36 OG1 CG2 REMARK 470 VAL R 38 CG1 CG2 REMARK 470 LEU R 39 CG CD1 CD2 REMARK 470 LEU R 42 CG CD1 CD2 REMARK 470 VAL R 50 CG1 CG2 REMARK 470 ARG R 54 CG CD NE CZ NH1 NH2 REMARK 470 ASP R 71 CG OD1 OD2 REMARK 470 THR R 77 OG1 CG2 REMARK 470 LEU R 78 CG CD1 CD2 REMARK 470 ILE R 82 CG1 CG2 CD1 REMARK 470 VAL R 83 CG1 CG2 REMARK 470 MET R 85 CG SD CE REMARK 470 MET R 87 CG SD CE REMARK 470 GLU R 89 CG CD OE1 OE2 REMARK 470 LYS R 90 CG CD CE NZ REMARK 470 TRP R 91 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP R 91 CZ3 CH2 REMARK 470 PHE R 96 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU R 97 CG CD1 CD2 REMARK 470 CYS R 98 SG REMARK 470 LYS R 99 CG CD CE NZ REMARK 470 LEU R 100 CG CD1 CD2 REMARK 470 ILE R 103 CG1 CG2 CD1 REMARK 470 ASP R 106 CG OD1 OD2 REMARK 470 LYS R 144 CG CD CE NZ REMARK 470 LEU R 154 CG CD1 CD2 REMARK 470 LEU R 158 CG CD1 CD2 REMARK 470 VAL R 160 CG1 CG2 REMARK 470 PHE R 161 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU R 162 CG CD1 CD2 REMARK 470 PHE R 163 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU R 164 CG CD1 CD2 REMARK 470 THR R 165 OG1 CG2 REMARK 470 THR R 166 OG1 CG2 REMARK 470 VAL R 167 CG1 CG2 REMARK 470 ILE R 169 CG1 CG2 CD1 REMARK 470 ASN R 171 CG OD1 ND2 REMARK 470 TYR R 175 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 CYS R 176 SG REMARK 470 ASN R 179 CG OD1 ND2 REMARK 470 GLU R 188 CG CD OE1 OE2 REMARK 470 GLU R 189 CG CD OE1 OE2 REMARK 470 ARG R 190 CG CD NE CZ NH1 NH2 REMARK 470 LEU R 191 CG CD1 CD2 REMARK 470 LYS R 192 CG CD CE NZ REMARK 470 VAL R 193 CG1 CG2 REMARK 470 ILE R 195 CG1 CG2 CD1 REMARK 470 THR R 196 OG1 CG2 REMARK 470 MET R 197 CG SD CE REMARK 470 SER R 211 OG REMARK 470 LYS R 230 CG CD CE NZ REMARK 470 ILE R 234 CG1 CG2 CD1 REMARK 470 LYS R 235 CG CD CE NZ REMARK 470 ARG R 241 CG CD NE CZ NH1 NH2 REMARK 470 SER R 249 OG REMARK 470 ILE R 252 CG1 CG2 CD1 REMARK 470 THR R 265 OG1 CG2 REMARK 470 LEU R 268 CG CD1 CD2 REMARK 470 LYS R 269 CG CD CE NZ REMARK 470 GLU R 270 CG CD OE1 OE2 REMARK 470 MET R 271 CG SD CE REMARK 470 LYS R 276 CG CD CE NZ REMARK 470 TYR R 277 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS R 278 CG CD CE NZ REMARK 470 ILE R 279 CG1 CG2 CD1 REMARK 470 ASP R 281 CG OD1 OD2 REMARK 470 LEU R 283 CG CD1 CD2 REMARK 470 SER R 288 OG REMARK 470 SER R 289 OG REMARK 470 CYS R 296 SG REMARK 470 MET R 300 CG SD CE REMARK 470 GLN R 307 CG CD OE1 NE2 REMARK 470 GLU R 311 CG CD OE1 OE2 REMARK 470 ILE R 314 CG1 CG2 CD1 REMARK 470 HIS R 315 CG ND1 CD2 CE1 NE2 REMARK 470 SER R 316 OG REMARK 470 LEU R 317 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 209 -8.27 -56.98 REMARK 500 THR B 87 -5.53 69.62 REMARK 500 ASN B 119 45.77 38.82 REMARK 500 ASP B 247 47.33 -91.06 REMARK 500 ASP B 291 33.85 -96.78 REMARK 500 PHE B 292 9.17 81.30 REMARK 500 ALA B 299 4.34 -67.64 REMARK 500 ALA B 302 -0.81 66.51 REMARK 500 TRP B 332 1.00 -67.84 REMARK 500 LEU C 51 -61.01 -95.04 REMARK 500 GLU E 42 14.47 59.93 REMARK 500 VAL E 48 -59.99 -121.61 REMARK 500 TYR E 50 148.25 -172.54 REMARK 500 ARG E 87 -168.45 -79.02 REMARK 500 ALA E 143 18.99 56.17 REMARK 500 MET E 192 -13.05 67.87 REMARK 500 HIS E 232 10.91 -141.33 REMARK 500 LEU E 245 52.85 -90.62 REMARK 500 PHE R 210 -36.71 -130.19 REMARK 500 MET R 233 2.24 59.25 REMARK 500 LEU R 240 44.84 -89.27 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-38964 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF THE C16:0 CERAMIDE-BOUND FPR2-GI COMPLEX DBREF 8Y62 A 1 354 UNP P63096 GNAI1_HUMAN 1 354 DBREF 8Y62 B 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 8Y62 C 5 63 UNP P59768 GBG2_HUMAN 5 63 DBREF 8Y62 E -36 247 PDB 8Y62 8Y62 -36 247 DBREF 8Y62 R 1 351 UNP P25090 FPR2_HUMAN 1 351 SEQADV 8Y62 MET B -17 UNP P62873 INITIATING METHIONINE SEQADV 8Y62 HIS B -16 UNP P62873 EXPRESSION TAG SEQADV 8Y62 HIS B -15 UNP P62873 EXPRESSION TAG SEQADV 8Y62 HIS B -14 UNP P62873 EXPRESSION TAG SEQADV 8Y62 HIS B -13 UNP P62873 EXPRESSION TAG SEQADV 8Y62 HIS B -12 UNP P62873 EXPRESSION TAG SEQADV 8Y62 HIS B -11 UNP P62873 EXPRESSION TAG SEQADV 8Y62 LEU B -10 UNP P62873 EXPRESSION TAG SEQADV 8Y62 GLU B -9 UNP P62873 EXPRESSION TAG SEQADV 8Y62 VAL B -8 UNP P62873 EXPRESSION TAG SEQADV 8Y62 LEU B -7 UNP P62873 EXPRESSION TAG SEQADV 8Y62 PHE B -6 UNP P62873 EXPRESSION TAG SEQADV 8Y62 GLN B -5 UNP P62873 EXPRESSION TAG SEQADV 8Y62 GLY B -4 UNP P62873 EXPRESSION TAG SEQADV 8Y62 PRO B -3 UNP P62873 EXPRESSION TAG SEQADV 8Y62 GLY B -2 UNP P62873 EXPRESSION TAG SEQADV 8Y62 SER B -1 UNP P62873 EXPRESSION TAG SEQADV 8Y62 SER B 0 UNP P62873 EXPRESSION TAG SEQADV 8Y62 GLY B 1 UNP P62873 EXPRESSION TAG SEQRES 1 A 354 MET GLY CYS THR LEU SER ALA GLU ASP LYS ALA ALA VAL SEQRES 2 A 354 GLU ARG SER LYS MET ILE ASP ARG ASN LEU ARG GLU ASP SEQRES 3 A 354 GLY GLU LYS ALA ALA ARG GLU VAL LYS LEU LEU LEU LEU SEQRES 4 A 354 GLY ALA GLY GLU SER GLY LYS SER THR ILE VAL LYS GLN SEQRES 5 A 354 MET LYS ILE ILE HIS GLU ALA GLY TYR SER GLU GLU GLU SEQRES 6 A 354 CYS LYS GLN TYR LYS ALA VAL VAL TYR SER ASN THR ILE SEQRES 7 A 354 GLN SER ILE ILE ALA ILE ILE ARG ALA MET GLY ARG LEU SEQRES 8 A 354 LYS ILE ASP PHE GLY ASP SER ALA ARG ALA ASP ASP ALA SEQRES 9 A 354 ARG GLN LEU PHE VAL LEU ALA GLY ALA ALA GLU GLU GLY SEQRES 10 A 354 PHE MET THR ALA GLU LEU ALA GLY VAL ILE LYS ARG LEU SEQRES 11 A 354 TRP LYS ASP SER GLY VAL GLN ALA CYS PHE ASN ARG SER SEQRES 12 A 354 ARG GLU TYR GLN LEU ASN ASP SER ALA ALA TYR TYR LEU SEQRES 13 A 354 ASN ASP LEU ASP ARG ILE ALA GLN PRO ASN TYR ILE PRO SEQRES 14 A 354 THR GLN GLN ASP VAL LEU ARG THR ARG VAL LYS THR THR SEQRES 15 A 354 GLY ILE VAL GLU THR HIS PHE THR PHE LYS ASP LEU HIS SEQRES 16 A 354 PHE LYS MET PHE ASP VAL GLY GLY GLN ARG SER GLU ARG SEQRES 17 A 354 LYS LYS TRP ILE HIS CYS PHE GLU GLY VAL THR ALA ILE SEQRES 18 A 354 ILE PHE CYS VAL ALA LEU SER ASP TYR ASP LEU VAL LEU SEQRES 19 A 354 ALA GLU ASP GLU GLU MET ASN ARG MET HIS GLU SER MET SEQRES 20 A 354 LYS LEU PHE ASP SER ILE CYS ASN ASN LYS TRP PHE THR SEQRES 21 A 354 ASP THR SER ILE ILE LEU PHE LEU ASN LYS LYS ASP LEU SEQRES 22 A 354 PHE GLU GLU LYS ILE LYS LYS SER PRO LEU THR ILE CYS SEQRES 23 A 354 TYR PRO GLU TYR ALA GLY SER ASN THR TYR GLU GLU ALA SEQRES 24 A 354 ALA ALA TYR ILE GLN CYS GLN PHE GLU ASP LEU ASN LYS SEQRES 25 A 354 ARG LYS ASP THR LYS GLU ILE TYR THR HIS PHE THR CYS SEQRES 26 A 354 ALA THR ASP THR LYS ASN VAL GLN PHE VAL PHE ASP ALA SEQRES 27 A 354 VAL THR ASP VAL ILE ILE LYS ASN ASN LEU LYS ASP CYS SEQRES 28 A 354 GLY LEU PHE SEQRES 1 B 358 MET HIS HIS HIS HIS HIS HIS LEU GLU VAL LEU PHE GLN SEQRES 2 B 358 GLY PRO GLY SER SER GLY SER GLU LEU ASP GLN LEU ARG SEQRES 3 B 358 GLN GLU ALA GLU GLN LEU LYS ASN GLN ILE ARG ASP ALA SEQRES 4 B 358 ARG LYS ALA CYS ALA ASP ALA THR LEU SER GLN ILE THR SEQRES 5 B 358 ASN ASN ILE ASP PRO VAL GLY ARG ILE GLN MET ARG THR SEQRES 6 B 358 ARG ARG THR LEU ARG GLY HIS LEU ALA LYS ILE TYR ALA SEQRES 7 B 358 MET HIS TRP GLY THR ASP SER ARG LEU LEU VAL SER ALA SEQRES 8 B 358 SER GLN ASP GLY LYS LEU ILE ILE TRP ASP SER TYR THR SEQRES 9 B 358 THR ASN LYS VAL HIS ALA ILE PRO LEU ARG SER SER TRP SEQRES 10 B 358 VAL MET THR CYS ALA TYR ALA PRO SER GLY ASN TYR VAL SEQRES 11 B 358 ALA CYS GLY GLY LEU ASP ASN ILE CYS SER ILE TYR ASN SEQRES 12 B 358 LEU LYS THR ARG GLU GLY ASN VAL ARG VAL SER ARG GLU SEQRES 13 B 358 LEU ALA GLY HIS THR GLY TYR LEU SER CYS CYS ARG PHE SEQRES 14 B 358 LEU ASP ASP ASN GLN ILE VAL THR SER SER GLY ASP THR SEQRES 15 B 358 THR CYS ALA LEU TRP ASP ILE GLU THR GLY GLN GLN THR SEQRES 16 B 358 THR THR PHE THR GLY HIS THR GLY ASP VAL MET SER LEU SEQRES 17 B 358 SER LEU ALA PRO ASP THR ARG LEU PHE VAL SER GLY ALA SEQRES 18 B 358 CYS ASP ALA SER ALA LYS LEU TRP ASP VAL ARG GLU GLY SEQRES 19 B 358 MET CYS ARG GLN THR PHE THR GLY HIS GLU SER ASP ILE SEQRES 20 B 358 ASN ALA ILE CYS PHE PHE PRO ASN GLY ASN ALA PHE ALA SEQRES 21 B 358 THR GLY SER ASP ASP ALA THR CYS ARG LEU PHE ASP LEU SEQRES 22 B 358 ARG ALA ASP GLN GLU LEU MET THR TYR SER HIS ASP ASN SEQRES 23 B 358 ILE ILE CYS GLY ILE THR SER VAL SER PHE SER LYS SER SEQRES 24 B 358 GLY ARG LEU LEU LEU ALA GLY TYR ASP ASP PHE ASN CYS SEQRES 25 B 358 ASN VAL TRP ASP ALA LEU LYS ALA ASP ARG ALA GLY VAL SEQRES 26 B 358 LEU ALA GLY HIS ASP ASN ARG VAL SER CYS LEU GLY VAL SEQRES 27 B 358 THR ASP ASP GLY MET ALA VAL ALA THR GLY SER TRP ASP SEQRES 28 B 358 SER PHE LEU LYS ILE TRP ASN SEQRES 1 C 59 ASN THR ALA SER ILE ALA GLN ALA ARG LYS LEU VAL GLU SEQRES 2 C 59 GLN LEU LYS MET GLU ALA ASN ILE ASP ARG ILE LYS VAL SEQRES 3 C 59 SER LYS ALA ALA ALA ASP LEU MET ALA TYR CYS GLU ALA SEQRES 4 C 59 HIS ALA LYS GLU ASP PRO LEU LEU THR PRO VAL PRO ALA SEQRES 5 C 59 SER GLU ASN PRO PHE ARG GLU SEQRES 1 E 285 MET LEU LEU VAL ASN GLN SER HIS GLN GLY PHE ASN LYS SEQRES 2 E 285 GLU HIS THR SER LYS MET VAL SER ALA ILE VAL LEU TYR SEQRES 3 E 285 VAL LEU LEU ALA ALA ALA ALA HIS SER ALA PHE ALA VAL SEQRES 4 E 285 GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN PRO GLY SEQRES 5 E 285 GLY SER ARG LYS LEU SER CYS SER ALA SER GLY PHE ALA SEQRES 6 E 285 PHE SER SER PHE GLY MET HIS TRP VAL ARG GLN ALA PRO SEQRES 7 E 285 GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SER GLY SEQRES 8 E 285 SER GLY THR ILE TYR TYR ALA ASP THR VAL LYS GLY ARG SEQRES 9 E 285 PHE THR ILE SER ARG ASP ASP PRO LYS ASN THR LEU PHE SEQRES 10 E 285 LEU GLN MET THR SER LEU ARG SER GLU ASP THR ALA MET SEQRES 11 E 285 TYR TYR CYS VAL ARG SER ILE TYR TYR TYR GLY SER SER SEQRES 12 E 285 PRO PHE ASP PHE TRP GLY GLN GLY THR THR LEU THR VAL SEQRES 13 E 285 SER ALA GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLY SEQRES 14 E 285 GLY GLY GLY SER ALA ASP ILE VAL MET THR GLN ALA THR SEQRES 15 E 285 SER SER VAL PRO VAL THR PRO GLY GLU SER VAL SER ILE SEQRES 16 E 285 SER CYS ARG SER SER LYS SER LEU LEU HIS SER ASN GLY SEQRES 17 E 285 ASN THR TYR LEU TYR TRP PHE LEU GLN ARG PRO GLY GLN SEQRES 18 E 285 SER PRO GLN LEU LEU ILE TYR ARG MET SER ASN LEU ALA SEQRES 19 E 285 SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SER GLY SEQRES 20 E 285 THR ALA PHE THR LEU THR ILE SER ARG LEU GLU ALA GLU SEQRES 21 E 285 ASP VAL GLY VAL TYR TYR CYS MET GLN HIS LEU GLU TYR SEQRES 22 E 285 PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU LEU SEQRES 1 R 351 MET GLU THR ASN PHE SER THR PRO LEU ASN GLU TYR GLU SEQRES 2 R 351 GLU VAL SER TYR GLU SER ALA GLY TYR THR VAL LEU ARG SEQRES 3 R 351 ILE LEU PRO LEU VAL VAL LEU GLY VAL THR PHE VAL LEU SEQRES 4 R 351 GLY VAL LEU GLY ASN GLY LEU VAL ILE TRP VAL ALA GLY SEQRES 5 R 351 PHE ARG MET THR ARG THR VAL THR THR ILE CYS TYR LEU SEQRES 6 R 351 ASN LEU ALA LEU ALA ASP PHE SER PHE THR ALA THR LEU SEQRES 7 R 351 PRO PHE LEU ILE VAL SER MET ALA MET GLY GLU LYS TRP SEQRES 8 R 351 PRO PHE GLY TRP PHE LEU CYS LYS LEU ILE HIS ILE VAL SEQRES 9 R 351 VAL ASP ILE ASN LEU PHE GLY SER VAL PHE LEU ILE GLY SEQRES 10 R 351 PHE ILE ALA LEU ASP ARG CYS ILE CYS VAL LEU HIS PRO SEQRES 11 R 351 VAL TRP ALA GLN ASN HIS ARG THR VAL SER LEU ALA MET SEQRES 12 R 351 LYS VAL ILE VAL GLY PRO TRP ILE LEU ALA LEU VAL LEU SEQRES 13 R 351 THR LEU PRO VAL PHE LEU PHE LEU THR THR VAL THR ILE SEQRES 14 R 351 PRO ASN GLY ASP THR TYR CYS THR PHE ASN PHE ALA SER SEQRES 15 R 351 TRP GLY GLY THR PRO GLU GLU ARG LEU LYS VAL ALA ILE SEQRES 16 R 351 THR MET LEU THR ALA ARG GLY ILE ILE ARG PHE VAL ILE SEQRES 17 R 351 GLY PHE SER LEU PRO MET SER ILE VAL ALA ILE CYS TYR SEQRES 18 R 351 GLY LEU ILE ALA ALA LYS ILE HIS LYS LYS GLY MET ILE SEQRES 19 R 351 LYS SER SER ARG PRO LEU ARG VAL LEU THR ALA VAL VAL SEQRES 20 R 351 ALA SER PHE PHE ILE CYS TRP PHE PRO PHE GLN LEU VAL SEQRES 21 R 351 ALA LEU LEU GLY THR VAL TRP LEU LYS GLU MET LEU PHE SEQRES 22 R 351 TYR GLY LYS TYR LYS ILE ILE ASP ILE LEU VAL ASN PRO SEQRES 23 R 351 THR SER SER LEU ALA PHE PHE ASN SER CYS LEU ASN PRO SEQRES 24 R 351 MET LEU TYR VAL PHE VAL GLY GLN ASP PHE ARG GLU ARG SEQRES 25 R 351 LEU ILE HIS SER LEU PRO THR SER LEU GLU ARG ALA LEU SEQRES 26 R 351 SER GLU ASP SER ALA PRO THR ASN ASP THR ALA ALA ASN SEQRES 27 R 351 SER ALA SER PRO PRO ALA GLU THR GLU LEU GLN ALA MET HET 16C R 401 38 HETNAM 16C N-((E,2S,3R)-1,3-DIHYDROXYOCTADEC-4-EN-2-YL)PALMITAMIDE HETSYN 16C C16-CERAMIDE; N-PALMITOYL-D-ERYTHRO-SPHINGOSINE; (2S, HETSYN 2 16C 3R,4E)-2-PALMITOYLAMINOOCTADEC-4-ENE-1,3-DIOL; (2S,3R, HETSYN 3 16C 4E)-2-PALMITOYLAMINO-1,3-OCTADEC-4-ENEDIOL FORMUL 6 16C C34 H67 N O3 HELIX 1 AA1 GLU A 8 ALA A 31 1 24 HELIX 2 AA2 GLY A 45 GLN A 52 1 8 HELIX 3 AA3 GLU A 207 ILE A 212 1 6 HELIX 4 AA4 HIS A 213 GLU A 216 5 4 HELIX 5 AA5 HIS A 244 ASN A 255 1 12 HELIX 6 AA6 LYS A 270 LYS A 279 1 10 HELIX 7 AA7 THR A 295 ASP A 309 1 15 HELIX 8 AA8 LYS A 330 GLY A 352 1 23 HELIX 9 AA9 GLN B 6 ALA B 26 1 21 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 ALA C 10 ALA C 23 1 14 HELIX 13 AB4 LYS C 29 ALA C 45 1 17 HELIX 14 AB5 LYS C 46 ASP C 48 5 3 HELIX 15 AB6 PRO C 53 SER C 57 5 5 HELIX 16 AB7 ALA E 28 PHE E 32 5 5 HELIX 17 AB8 SER E 53 GLY E 56 5 4 HELIX 18 AB9 ASP E 62 LYS E 65 5 4 HELIX 19 AC1 GLU E 220 VAL E 224 5 5 HELIX 20 AC2 ILE R 27 ALA R 51 1 25 HELIX 21 AC3 THR R 58 GLY R 88 1 31 HELIX 22 AC4 GLY R 94 HIS R 129 1 36 HELIX 23 AC5 HIS R 129 HIS R 136 1 8 HELIX 24 AC6 THR R 138 PHE R 163 1 26 HELIX 25 AC7 THR R 186 GLY R 209 1 24 HELIX 26 AC8 PHE R 210 LYS R 231 1 22 HELIX 27 AC9 ARG R 238 GLY R 275 1 38 HELIX 28 AD1 LYS R 278 LEU R 283 1 6 HELIX 29 AD2 LEU R 283 VAL R 303 1 21 HELIX 30 AD3 GLY R 306 LEU R 317 1 12 SHEET 1 AA1 6 VAL A 185 PHE A 191 0 SHEET 2 AA1 6 LEU A 194 ASP A 200 -1 O PHE A 196 N PHE A 189 SHEET 3 AA1 6 VAL A 34 LEU A 38 1 N LEU A 36 O PHE A 199 SHEET 4 AA1 6 ALA A 220 ALA A 226 1 O ILE A 222 N LEU A 37 SHEET 5 AA1 6 LEU A 266 ASN A 269 1 O PHE A 267 N PHE A 223 SHEET 6 AA1 6 THR A 321 PHE A 323 1 O HIS A 322 N LEU A 268 SHEET 1 AA2 4 ARG B 46 THR B 50 0 SHEET 2 AA2 4 LEU B 336 ASN B 340 -1 O ILE B 338 N ARG B 48 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 HIS B 91 PRO B 94 -1 O HIS B 91 N ILE B 81 SHEET 1 AA4 4 THR B 102 TYR B 105 0 SHEET 2 AA4 4 TYR B 111 GLY B 115 -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 134 N ASN B 125 SHEET 1 AA5 4 LEU B 146 PHE B 151 0 SHEET 2 AA5 4 ILE B 157 SER B 161 -1 O SER B 160 N SER B 147 SHEET 3 AA5 4 CYS B 166 LEU B 168 -1 O ALA B 167 N THR B 159 SHEET 4 AA5 4 THR B 178 PHE B 180 -1 O PHE B 180 N CYS B 166 SHEET 1 AA6 4 VAL B 187 LEU B 192 0 SHEET 2 AA6 4 PHE B 199 ALA B 203 -1 O GLY B 202 N MET B 188 SHEET 3 AA6 4 ALA B 208 LEU B 210 -1 O LYS B 209 N SER B 201 SHEET 4 AA6 4 GLN B 220 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 ASN B 230 SHEET 3 AA7 4 CYS B 250 ASP B 254 -1 O ARG B 251 N THR B 243 SHEET 4 AA7 4 GLN B 259 TYR B 264 -1 O TYR B 264 N CYS B 250 SHEET 1 AA8 4 ILE B 273 PHE B 278 0 SHEET 2 AA8 4 LEU B 284 TYR B 289 -1 O GLY B 288 N SER B 275 SHEET 3 AA8 4 CYS B 294 ASP B 298 -1 O TRP B 297 N LEU B 285 SHEET 4 AA8 4 ARG B 304 LEU B 308 -1 O ALA B 305 N VAL B 296 SHEET 1 AA9 4 LEU E 4 SER E 7 0 SHEET 2 AA9 4 SER E 17 ALA E 24 -1 O SER E 23 N VAL E 5 SHEET 3 AA9 4 THR E 78 THR E 84 -1 O MET E 83 N ARG E 18 SHEET 4 AA9 4 PHE E 68 ASP E 73 -1 N SER E 71 O PHE E 80 SHEET 1 AB1 3 GLY E 10 VAL E 12 0 SHEET 2 AB1 3 THR E 115 VAL E 119 1 O THR E 118 N GLY E 10 SHEET 3 AB1 3 ALA E 92 TYR E 94 -1 N ALA E 92 O LEU E 117 SHEET 1 AB2 4 ILE E 58 TYR E 60 0 SHEET 2 AB2 4 GLU E 46 ILE E 51 -1 N TYR E 50 O TYR E 59 SHEET 3 AB2 4 GLY E 33 ARG E 38 -1 N TRP E 36 O VAL E 48 SHEET 4 AB2 4 ARG E 98 SER E 99 -1 O SER E 99 N GLY E 33 SHEET 1 AB3 3 VAL E 155 ARG E 160 0 SHEET 2 AB3 3 ALA E 211 ILE E 216 -1 O LEU E 214 N ILE E 157 SHEET 3 AB3 3 GLY E 205 SER E 208 -1 N SER E 206 O THR E 213 SHEET 1 AB4 5 ASN E 194 LEU E 195 0 SHEET 2 AB4 5 GLN E 186 TYR E 190 -1 N TYR E 190 O ASN E 194 SHEET 3 AB4 5 LEU E 174 GLN E 179 -1 N LEU E 178 O GLN E 186 SHEET 4 AB4 5 VAL E 226 GLN E 231 -1 O MET E 230 N TYR E 175 SHEET 5 AB4 5 THR E 243 LYS E 244 -1 O THR E 243 N TYR E 227 SHEET 1 AB5 2 LEU R 164 THR R 166 0 SHEET 2 AB5 2 CYS R 176 PHE R 178 -1 O THR R 177 N THR R 165 SSBOND 1 CYS E 22 CYS E 96 1555 1555 2.03 SSBOND 2 CYS E 159 CYS E 229 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