HEADER MEMBRANE PROTEIN 09-SEP-24 9JH5 TITLE ACTIVATION MECHANISM OF CYSLTR2 BY C16:0 CERAMIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: CYSTEINYL LEUKOTRIENE RECEPTOR 2; COMPND 3 CHAIN: R; COMPND 4 SYNONYM: CYSLTR2,G-PROTEIN COUPLED RECEPTOR GPCR21,HGPCR21,G-PROTEIN COMPND 5 COUPLED RECEPTOR HG57,HPN321; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 10 GAMMA-2; COMPND 11 CHAIN: C; COMPND 12 SYNONYM: G GAMMA-I; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 3; COMPND 15 MOLECULE: SCFV16; COMPND 16 CHAIN: S; COMPND 17 ENGINEERED: YES; COMPND 18 MOL_ID: 4; COMPND 19 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I) SUBUNIT ALPHA-1; COMPND 20 CHAIN: A; COMPND 21 ENGINEERED: YES; COMPND 22 MOL_ID: 5; COMPND 23 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 24 BETA-1; COMPND 25 CHAIN: B; COMPND 26 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 27 ENGINEERED: YES; COMPND 28 MOL_ID: 6; COMPND 29 MOLECULE: NB35; COMPND 30 CHAIN: N; COMPND 31 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: CYSLTR2, CYSLT2, CYSLT2R; SOURCE 6 EXPRESSION_SYSTEM: BACULOVIRUS EXPRESSION VECTOR PFASTBAC1-HM; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 274590; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 GENE: GNG2; SOURCE 13 EXPRESSION_SYSTEM: BACULOVIRUS EXPRESSION VECTOR PFASTBAC1-HM; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 274590; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 17 ORGANISM_TAXID: 10090; SOURCE 18 GENE: HOUSE MOUSE; SOURCE 19 EXPRESSION_SYSTEM: BACULOVIRUS EXPRESSION VECTOR PFASTBAC1-HM; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 274590; SOURCE 21 MOL_ID: 4; SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 23 ORGANISM_TAXID: 9606; SOURCE 24 EXPRESSION_SYSTEM: BACULOVIRUS EXPRESSION VECTOR PFASTBAC1-HM; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 274590; SOURCE 26 MOL_ID: 5; SOURCE 27 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 28 ORGANISM_COMMON: HUMAN; SOURCE 29 ORGANISM_TAXID: 9606; SOURCE 30 GENE: GNB1; SOURCE 31 EXPRESSION_SYSTEM: BACULOVIRUS EXPRESSION VECTOR PFASTBAC1-HM; SOURCE 32 EXPRESSION_SYSTEM_TAXID: 274590; SOURCE 33 MOL_ID: 6; SOURCE 34 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 35 ORGANISM_TAXID: 9844; SOURCE 36 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 37 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS GPCR, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR J.L.WANG,J.H.DING,J.P.SUN,X.YU REVDAT 1 23-APR-25 9JH5 0 JRNL AUTH S.ZHANG,H.LIN,J.WANG,J.RUI,T.WANG,Z.CAI,S.HUANG,Y.GAO,T.MA, JRNL AUTH 2 R.FAN,R.DAI,Z.LI,Y.JIA,Q.CHEN,H.HE,J.TAN,S.ZHU,R.GU,Z.DONG, JRNL AUTH 3 M.LI,E.XIE,Y.FU,J.ZHENG,C.JIANG,J.SUN,W.KONG JRNL TITL SENSING CERAMIDES BY CYSLTR2 AND P2RY6 TO AGGRAVATE JRNL TITL 2 ATHEROSCLEROSIS. JRNL REF NATURE 2025 JRNL REFN ESSN 1476-4687 JRNL PMID 40049228 JRNL DOI 10.1038/S41586-025-08792-8 REMARK 2 REMARK 2 RESOLUTION. 2.76 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 2.760 REMARK 3 NUMBER OF PARTICLES : 177531 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 9JH5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-SEP-24. REMARK 100 THE DEPOSITION ID IS D_1300051247. 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 : C16:0-CERAMIDE-CYSLTR2-GQ 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 : 7.00 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K2 IS (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00 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 : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 6000.00 REMARK 245 ILLUMINATION MODE : SPOT SCAN 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: R, C, S, A, B, N REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET R 1 REMARK 465 GLU R 2 REMARK 465 ARG R 3 REMARK 465 LYS R 4 REMARK 465 PHE R 5 REMARK 465 MET R 6 REMARK 465 SER R 7 REMARK 465 LEU R 8 REMARK 465 GLN R 9 REMARK 465 PRO R 10 REMARK 465 SER R 11 REMARK 465 ILE R 12 REMARK 465 SER R 13 REMARK 465 VAL R 14 REMARK 465 SER R 15 REMARK 465 GLU R 16 REMARK 465 MET R 17 REMARK 465 GLU R 18 REMARK 465 PRO R 19 REMARK 465 ASN R 20 REMARK 465 GLY R 21 REMARK 465 THR R 22 REMARK 465 PHE R 23 REMARK 465 SER R 24 REMARK 465 ASN R 25 REMARK 465 ASN R 26 REMARK 465 ASN R 27 REMARK 465 SER R 28 REMARK 465 ARG R 29 REMARK 465 ASN R 30 REMARK 465 CYS R 31 REMARK 465 THR R 32 REMARK 465 ILE R 33 REMARK 465 PHE R 41 REMARK 465 SER R 176 REMARK 465 GLY R 177 REMARK 465 SER R 178 REMARK 465 GLU R 179 REMARK 465 GLN R 180 REMARK 465 ASN R 181 REMARK 465 GLY R 182 REMARK 465 SER R 183 REMARK 465 VAL R 184 REMARK 465 THR R 185 REMARK 465 SER R 186 REMARK 465 CYS R 187 REMARK 465 LEU R 188 REMARK 465 GLU R 189 REMARK 465 LEU R 190 REMARK 465 ASN R 191 REMARK 465 LEU R 192 REMARK 465 VAL R 231 REMARK 465 GLU R 232 REMARK 465 VAL R 233 REMARK 465 PRO R 234 REMARK 465 GLU R 235 REMARK 465 SER R 236 REMARK 465 LYS R 317 REMARK 465 SER R 318 REMARK 465 ALA R 319 REMARK 465 LEU R 320 REMARK 465 ARG R 321 REMARK 465 LYS R 322 REMARK 465 GLY R 323 REMARK 465 HIS R 324 REMARK 465 PRO R 325 REMARK 465 GLN R 326 REMARK 465 LYS R 327 REMARK 465 ALA R 328 REMARK 465 LYS R 329 REMARK 465 THR R 330 REMARK 465 LYS R 331 REMARK 465 CYS R 332 REMARK 465 VAL R 333 REMARK 465 PHE R 334 REMARK 465 PRO R 335 REMARK 465 VAL R 336 REMARK 465 SER R 337 REMARK 465 VAL R 338 REMARK 465 TRP R 339 REMARK 465 LEU R 340 REMARK 465 ARG R 341 REMARK 465 LYS R 342 REMARK 465 GLU R 343 REMARK 465 THR R 344 REMARK 465 ARG R 345 REMARK 465 VAL R 346 REMARK 465 ASN C 5 REMARK 465 THR C 6 REMARK 465 ALA C 7 REMARK 465 PRO C 55 REMARK 465 ASP S 1 REMARK 465 GLY S 122 REMARK 465 GLY S 123 REMARK 465 GLY S 124 REMARK 465 GLY S 125 REMARK 465 SER S 126 REMARK 465 GLY S 127 REMARK 465 GLY S 128 REMARK 465 GLY S 129 REMARK 465 GLY S 130 REMARK 465 SER S 131 REMARK 465 GLY S 132 REMARK 465 GLY S 133 REMARK 465 GLY S 134 REMARK 465 LYS S 248 REMARK 465 GLY S 249 REMARK 465 SER S 250 REMARK 465 MET A 1 REMARK 465 GLY A 2 REMARK 465 VAL A 81 REMARK 465 ASN A 82 REMARK 465 GLY A 83 REMARK 465 TYR A 84 REMARK 465 SER A 85 REMARK 465 GLU A 86 REMARK 465 GLU A 87 REMARK 465 GLU A 88 REMARK 465 CYS A 89 REMARK 465 LYS A 90 REMARK 465 GLN A 91 REMARK 465 TYR A 92 REMARK 465 LYS A 93 REMARK 465 ALA A 94 REMARK 465 VAL A 95 REMARK 465 VAL A 96 REMARK 465 TYR A 97 REMARK 465 SER A 98 REMARK 465 ASN A 99 REMARK 465 THR A 100 REMARK 465 ILE A 101 REMARK 465 GLN A 102 REMARK 465 SER A 103 REMARK 465 ILE A 104 REMARK 465 ILE A 105 REMARK 465 ALA A 106 REMARK 465 ILE A 107 REMARK 465 ILE A 108 REMARK 465 ARG A 109 REMARK 465 ALA A 110 REMARK 465 MET A 111 REMARK 465 GLY A 112 REMARK 465 ARG A 113 REMARK 465 LEU A 114 REMARK 465 LYS A 115 REMARK 465 ILE A 116 REMARK 465 ASP A 117 REMARK 465 PHE A 118 REMARK 465 GLY A 119 REMARK 465 ASP A 120 REMARK 465 SER A 121 REMARK 465 ALA A 122 REMARK 465 ARG A 123 REMARK 465 ALA A 124 REMARK 465 ASP A 125 REMARK 465 ASP A 126 REMARK 465 ALA A 127 REMARK 465 ARG A 128 REMARK 465 GLN A 129 REMARK 465 LEU A 130 REMARK 465 PHE A 131 REMARK 465 VAL A 132 REMARK 465 LEU A 133 REMARK 465 ALA A 134 REMARK 465 GLY A 135 REMARK 465 ALA A 136 REMARK 465 ALA A 137 REMARK 465 GLU A 138 REMARK 465 GLU A 139 REMARK 465 GLY A 140 REMARK 465 PHE A 141 REMARK 465 MET A 142 REMARK 465 THR A 143 REMARK 465 ALA A 144 REMARK 465 GLU A 145 REMARK 465 LEU A 146 REMARK 465 ALA A 147 REMARK 465 GLY A 148 REMARK 465 VAL A 149 REMARK 465 ILE A 150 REMARK 465 LYS A 151 REMARK 465 ARG A 152 REMARK 465 LEU A 153 REMARK 465 TRP A 154 REMARK 465 LYS A 155 REMARK 465 ASP A 156 REMARK 465 SER A 157 REMARK 465 GLY A 158 REMARK 465 VAL A 159 REMARK 465 GLN A 160 REMARK 465 ALA A 161 REMARK 465 CYS A 162 REMARK 465 PHE A 163 REMARK 465 ASN A 164 REMARK 465 ARG A 165 REMARK 465 SER A 166 REMARK 465 ARG A 167 REMARK 465 GLU A 168 REMARK 465 TYR A 169 REMARK 465 GLN A 170 REMARK 465 LEU A 171 REMARK 465 ASN A 172 REMARK 465 ASP A 173 REMARK 465 SER A 174 REMARK 465 ALA A 175 REMARK 465 ALA A 176 REMARK 465 TYR A 177 REMARK 465 TYR A 178 REMARK 465 LEU A 179 REMARK 465 ASN A 180 REMARK 465 ASP A 181 REMARK 465 LEU A 182 REMARK 465 ASP A 183 REMARK 465 ARG A 184 REMARK 465 ILE A 185 REMARK 465 ALA A 186 REMARK 465 GLN A 187 REMARK 465 PRO A 188 REMARK 465 ASN A 189 REMARK 465 TYR A 190 REMARK 465 ILE A 191 REMARK 465 PRO A 192 REMARK 465 THR A 193 REMARK 465 GLN A 194 REMARK 465 GLN A 195 REMARK 465 ASP A 196 REMARK 465 VAL A 197 REMARK 465 LEU A 198 REMARK 465 ARG A 199 REMARK 465 THR A 200 REMARK 465 ARG A 201 REMARK 465 TYR A 263 REMARK 465 ASN A 264 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 GLN B 1 REMARK 465 SER B 2 REMARK 465 MET N -22 REMARK 465 LYS N -21 REMARK 465 TYR N -20 REMARK 465 LEU N -19 REMARK 465 LEU N -18 REMARK 465 PRO N -17 REMARK 465 THR N -16 REMARK 465 ALA N -15 REMARK 465 ALA N -14 REMARK 465 ALA N -13 REMARK 465 GLY N -12 REMARK 465 LEU N -11 REMARK 465 LEU N -10 REMARK 465 LEU N -9 REMARK 465 LEU N -8 REMARK 465 ALA N -7 REMARK 465 ALA N -6 REMARK 465 GLN N -5 REMARK 465 PRO N -4 REMARK 465 ALA N -3 REMARK 465 MET N -2 REMARK 465 ALA N -1 REMARK 465 MET N 0 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 R 34 CG CD OE1 OE2 REMARK 470 PHE R 36 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS R 37 CG CD CE NZ REMARK 470 TYR R 61 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ILE R 152 CG1 CG2 CD1 REMARK 470 TYR R 193 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 MET R 201 CG SD CE REMARK 470 LEU R 206 CG CD1 CD2 REMARK 470 GLU C 63 CG CD OE1 OE2 REMARK 470 GLU S 42 CG CD OE1 OE2 REMARK 470 SER S 121 OG REMARK 470 SER S 136 OG REMARK 470 LYS A 58 CG CD CE NZ REMARK 470 GLN A 59 CG CD OE1 NE2 REMARK 470 HIS A 64 CG ND1 CD2 CE1 NE2 REMARK 470 LYS A 203 CG CD CE NZ REMARK 470 LYS A 216 CG CD CE NZ REMARK 470 ASP A 240 CG OD1 OD2 REMARK 470 GLU A 268 CG CD OE1 OE2 REMARK 470 LYS A 305 CG CD CE NZ REMARK 470 LYS A 307 CG CD CE NZ REMARK 470 GLU A 309 CG CD OE1 OE2 REMARK 470 PRO A 321 CG CD REMARK 470 ASP A 323 CG OD1 OD2 REMARK 470 THR A 325 OG1 CG2 REMARK 470 GLU A 327 CG CD OE1 OE2 REMARK 470 GLU A 330 CG CD OE1 OE2 REMARK 470 ASP A 331 CG OD1 OD2 REMARK 470 GLU A 370 CG CD OE1 OE2 REMARK 470 GLU B 3 CG CD OE1 OE2 REMARK 470 ARG B 42 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 46 CG CD NE CZ NH1 NH2 REMARK 470 SER N 112 OG REMARK 470 THR N 113 OG1 CG2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 CA HIS R 284 CD2 LEU R 287 1.04 REMARK 500 O VAL R 269 CG2 THR R 272 1.16 REMARK 500 O ALA R 286 CG1 ILE R 289 1.18 REMARK 500 O HIS R 284 CG LEU R 287 1.18 REMARK 500 CB HIS R 284 CD2 LEU R 287 1.47 REMARK 500 CA TYR R 263 OG1 THR R 290 1.58 REMARK 500 CB TYR R 263 OG1 THR R 290 1.62 REMARK 500 OG1 THR R 216 C27 CLR R 403 1.66 REMARK 500 C HIS R 284 CG LEU R 287 1.79 REMARK 500 O HIS R 284 CD1 LEU R 287 1.80 REMARK 500 ND1 HIS R 284 CD1 LEU R 287 1.80 REMARK 500 CA ALA R 286 CD1 ILE R 289 1.81 REMARK 500 CG HIS R 284 CD2 LEU R 287 1.84 REMARK 500 O ARG A 374 OD1 ASP A 378 1.86 REMARK 500 NE ARG S 38 CE2 TYR S 94 1.87 REMARK 500 C HIS R 284 CD2 LEU R 287 1.87 REMARK 500 NE ARG S 38 CD2 TYR S 94 1.90 REMARK 500 CB LEU R 271 C23 16C R 401 1.92 REMARK 500 CG1 ILE R 195 C32 16C R 401 1.93 REMARK 500 CD1 ILE R 166 C18 16C R 401 1.94 REMARK 500 C23 CLR R 402 C26 CLR R 403 1.95 REMARK 500 O ILE B 58 OG SER B 316 1.98 REMARK 500 NE ARG S 38 CZ TYR S 94 1.98 REMARK 500 C ALA R 286 CG1 ILE R 289 1.98 REMARK 500 CB THR R 216 C27 CLR R 403 2.06 REMARK 500 NE ARG S 38 CE1 TYR S 94 2.08 REMARK 500 NE ARG S 38 CG TYR S 94 2.08 REMARK 500 O SER N 112 NH2 ARG N 118 2.08 REMARK 500 NE ARG S 38 CD1 TYR S 94 2.09 REMARK 500 CG2 ILE R 195 C34 16C R 401 2.10 REMARK 500 C HIS R 270 N THR R 272 2.10 REMARK 500 CB ASN R 202 C21 16C R 401 2.10 REMARK 500 O TYR R 193 CD1 ILE R 195 2.10 REMARK 500 OG SER R 70 OE1 GLU A 390 2.10 REMARK 500 CA HIS R 284 CG LEU R 287 2.12 REMARK 500 CE1 HIS R 284 CD1 LEU R 287 2.12 REMARK 500 NZ LYS C 29 OD1 ASP B 27 2.13 REMARK 500 O VAL C 54 N ALA C 56 2.13 REMARK 500 CE1 HIS R 270 C25 16C R 401 2.13 REMARK 500 O SER S 52 NH1 ARG S 72 2.14 REMARK 500 OG SER S 106 OD2 ASP S 109 2.15 REMARK 500 CG ASN R 202 C21 16C R 401 2.18 REMARK 500 N TYR R 263 OG1 THR R 290 2.18 REMARK 500 O HIS R 284 CD2 LEU R 287 2.18 REMARK 500 OG SER B 245 OD1 ASP B 247 2.19 REMARK 500 CB ALA R 286 CD1 ILE R 289 2.19 REMARK 500 O ARG S 38 N GLU S 46 2.19 REMARK 500 O MET B 325 ND2 ASN B 340 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 TYR R 123 CE1 TYR R 123 CZ -0.095 REMARK 500 VAL C 54 C ALA C 56 N -0.155 REMARK 500 ARG S 38 CD ARG S 38 NE 0.384 REMARK 500 ARG S 38 NE ARG S 38 CZ 0.187 REMARK 500 TYR S 94 CG TYR S 94 CD2 0.405 REMARK 500 TYR S 94 CG TYR S 94 CD1 0.394 REMARK 500 TYR S 94 CD1 TYR S 94 CE1 0.917 REMARK 500 TYR S 94 CE1 TYR S 94 CZ 0.513 REMARK 500 TYR S 94 CZ TYR S 94 CE2 0.517 REMARK 500 TYR S 94 CE2 TYR S 94 CD2 0.853 REMARK 500 ASP A 381 CB ASP A 381 CG -0.146 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ILE R 152 CB - CA - C ANGL. DEV. = 20.9 DEGREES REMARK 500 ARG R 153 CB - CA - C ANGL. DEV. = -29.9 DEGREES REMARK 500 ARG R 153 N - CA - C ANGL. DEV. = 29.8 DEGREES REMARK 500 LEU R 261 CA - CB - CG ANGL. DEV. = -16.5 DEGREES REMARK 500 PRO R 262 C - N - CD ANGL. DEV. = -15.7 DEGREES REMARK 500 LEU R 271 N - CA - C ANGL. DEV. = -22.2 DEGREES REMARK 500 TRP R 274 N - CA - C ANGL. DEV. = 17.9 DEGREES REMARK 500 ARG S 38 CG - CD - NE ANGL. DEV. = 13.2 DEGREES REMARK 500 ARG S 38 CD - NE - CZ ANGL. DEV. = 30.4 DEGREES REMARK 500 ARG S 38 NH1 - CZ - NH2 ANGL. DEV. = -6.8 DEGREES REMARK 500 ARG S 38 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES REMARK 500 ARG S 38 NE - CZ - NH2 ANGL. DEV. = 10.2 DEGREES REMARK 500 MET S 192 CB - CA - C ANGL. DEV. = -14.7 DEGREES REMARK 500 REMARK 500 REMARK: NULL 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 R 69 -77.79 -47.22 REMARK 500 SER R 70 -51.41 -136.71 REMARK 500 THR R 71 -169.06 -168.79 REMARK 500 ASP R 108 -172.53 -174.17 REMARK 500 PHE R 144 46.76 -91.37 REMARK 500 ARG R 153 -19.10 -144.74 REMARK 500 CYS R 259 -75.24 -61.43 REMARK 500 LEU R 271 2.34 -69.66 REMARK 500 ALA R 298 -27.15 -37.95 REMARK 500 SER C 57 -16.81 -142.44 REMARK 500 SER S 30 45.10 -87.78 REMARK 500 GLU S 42 47.12 -97.86 REMARK 500 SER S 55 103.75 -51.12 REMARK 500 THR S 69 73.51 43.80 REMARK 500 MET S 83 135.94 -170.33 REMARK 500 SER S 88 -8.48 63.53 REMARK 500 ALA S 92 -166.84 -162.98 REMARK 500 THR S 116 42.18 -101.75 REMARK 500 ASP S 137 -165.01 -75.67 REMARK 500 VAL S 147 77.04 45.29 REMARK 500 SER S 156 48.13 -141.16 REMARK 500 PRO S 181 85.07 -67.60 REMARK 500 LEU S 188 -61.31 -102.60 REMARK 500 MET S 192 8.78 53.01 REMARK 500 SER S 193 -48.16 -137.29 REMARK 500 ALA S 196 -168.61 -76.67 REMARK 500 SER S 197 -70.58 -75.06 REMARK 500 ASP S 201 1.54 -65.62 REMARK 500 SER S 217 -56.93 -121.09 REMARK 500 TYR S 235 63.74 -110.54 REMARK 500 LEU S 237 62.33 37.94 REMARK 500 GLU A 209 113.15 -165.35 REMARK 500 VAL A 214 -61.86 -100.88 REMARK 500 ALA A 243 78.44 62.28 REMARK 500 TRP A 281 -5.75 71.37 REMARK 500 TYR A 311 -6.51 70.02 REMARK 500 PHE A 312 79.56 -161.46 REMARK 500 GLU A 314 47.01 -81.75 REMARK 500 TYR A 318 -60.68 -109.52 REMARK 500 THR A 319 78.56 56.28 REMARK 500 THR A 320 134.84 -29.40 REMARK 500 THR A 325 78.11 -160.42 REMARK 500 ASP A 354 -70.31 -66.11 REMARK 500 THR B 47 97.66 -69.79 REMARK 500 ARG B 68 -38.47 -131.06 REMARK 500 SER B 84 9.14 59.96 REMARK 500 CYS B 204 21.52 -78.49 REMARK 500 ARG B 214 -35.70 -135.05 REMARK 500 SER B 227 -169.31 -114.92 REMARK 500 SER B 279 -81.54 -84.71 REMARK 500 REMARK 500 THIS ENTRY HAS 61 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 LYS R 68 LYS R 69 -144.18 REMARK 500 TYR S 235 PRO S 236 141.26 REMARK 500 TYR B 85 THR B 86 148.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 TRP R 274 -11.74 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-61472 RELATED DB: EMDB REMARK 900 ACTIVATION MECHANISM OF GPR132 BY COMPOUND NOX-6-7 DBREF 9JH5 R 1 346 UNP Q9NS75 CLTR2_HUMAN 1 346 DBREF 9JH5 C 5 63 UNP P59768 GBG2_HUMAN 5 63 DBREF 9JH5 S 1 250 PDB 9JH5 9JH5 1 250 DBREF 9JH5 A 1 394 PDB 9JH5 9JH5 1 394 DBREF 9JH5 B 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 9JH5 N -22 128 PDB 9JH5 9JH5 -22 128 SEQADV 9JH5 MET B -17 UNP P62873 INITIATING METHIONINE SEQADV 9JH5 HIS B -16 UNP P62873 EXPRESSION TAG SEQADV 9JH5 HIS B -15 UNP P62873 EXPRESSION TAG SEQADV 9JH5 HIS B -14 UNP P62873 EXPRESSION TAG SEQADV 9JH5 HIS B -13 UNP P62873 EXPRESSION TAG SEQADV 9JH5 HIS B -12 UNP P62873 EXPRESSION TAG SEQADV 9JH5 HIS B -11 UNP P62873 EXPRESSION TAG SEQADV 9JH5 LEU B -10 UNP P62873 EXPRESSION TAG SEQADV 9JH5 GLU B -9 UNP P62873 EXPRESSION TAG SEQADV 9JH5 VAL B -8 UNP P62873 EXPRESSION TAG SEQADV 9JH5 LEU B -7 UNP P62873 EXPRESSION TAG SEQADV 9JH5 PHE B -6 UNP P62873 EXPRESSION TAG SEQADV 9JH5 GLN B -5 UNP P62873 EXPRESSION TAG SEQADV 9JH5 GLY B -4 UNP P62873 EXPRESSION TAG SEQADV 9JH5 PRO B -3 UNP P62873 EXPRESSION TAG SEQADV 9JH5 GLY B -2 UNP P62873 EXPRESSION TAG SEQADV 9JH5 SER B -1 UNP P62873 EXPRESSION TAG SEQADV 9JH5 SER B 0 UNP P62873 EXPRESSION TAG SEQADV 9JH5 GLN B 1 UNP P62873 EXPRESSION TAG SEQRES 1 R 346 MET GLU ARG LYS PHE MET SER LEU GLN PRO SER ILE SER SEQRES 2 R 346 VAL SER GLU MET GLU PRO ASN GLY THR PHE SER ASN ASN SEQRES 3 R 346 ASN SER ARG ASN CYS THR ILE GLU ASN PHE LYS ARG GLU SEQRES 4 R 346 PHE PHE PRO ILE VAL TYR LEU ILE ILE PHE PHE TRP GLY SEQRES 5 R 346 VAL LEU GLY ASN GLY LEU SER ILE TYR VAL PHE LEU GLN SEQRES 6 R 346 PRO TYR LYS LYS SER THR SER VAL ASN VAL PHE MET LEU SEQRES 7 R 346 ASN LEU ALA ILE SER ASP LEU LEU PHE ILE SER THR LEU SEQRES 8 R 346 PRO PHE ARG ALA ASP TYR TYR LEU ARG GLY SER ASN TRP SEQRES 9 R 346 ILE PHE GLY ASP LEU ALA CYS ARG ILE MET SER TYR SER SEQRES 10 R 346 LEU TYR VAL ASN MET TYR SER SER ILE TYR PHE LEU THR SEQRES 11 R 346 VAL LEU SER VAL VAL ARG PHE LEU ALA MET VAL HIS PRO SEQRES 12 R 346 PHE ARG LEU LEU HIS VAL THR SER ILE ARG SER ALA TRP SEQRES 13 R 346 ILE LEU CYS GLY ILE ILE TRP ILE LEU ILE MET ALA SER SEQRES 14 R 346 SER ILE MET LEU LEU ASP SER GLY SER GLU GLN ASN GLY SEQRES 15 R 346 SER VAL THR SER CYS LEU GLU LEU ASN LEU TYR LYS ILE SEQRES 16 R 346 ALA LYS LEU GLN THR MET ASN TYR ILE ALA LEU VAL VAL SEQRES 17 R 346 GLY CYS LEU LEU PRO PHE PHE THR LEU SER ILE CYS TYR SEQRES 18 R 346 LEU LEU ILE ILE ARG VAL LEU LEU LYS VAL GLU VAL PRO SEQRES 19 R 346 GLU SER GLY LEU ARG VAL SER HIS ARG LYS ALA LEU THR SEQRES 20 R 346 THR ILE ILE ILE THR LEU ILE ILE PHE PHE LEU CYS PHE SEQRES 21 R 346 LEU PRO TYR HIS THR LEU ARG THR VAL HIS LEU THR THR SEQRES 22 R 346 TRP LYS VAL GLY LEU CYS LYS ASP ARG LEU HIS LYS ALA SEQRES 23 R 346 LEU VAL ILE THR LEU ALA LEU ALA ALA ALA ASN ALA CYS SEQRES 24 R 346 PHE ASN PRO LEU LEU TYR TYR PHE ALA GLY GLU ASN PHE SEQRES 25 R 346 LYS ASP ARG LEU LYS SER ALA LEU ARG LYS GLY HIS PRO SEQRES 26 R 346 GLN LYS ALA LYS THR LYS CYS VAL PHE PRO VAL SER VAL SEQRES 27 R 346 TRP LEU ARG LYS GLU THR ARG VAL 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 S 250 ASP VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 S 250 PRO GLY GLY SER ARG LYS LEU SER CYS SER ALA SER GLY SEQRES 3 S 250 PHE ALA PHE SER SER PHE GLY MET HIS TRP VAL ARG GLN SEQRES 4 S 250 ALA PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SEQRES 5 S 250 SER GLY SER GLY THR ILE TYR TYR ALA ASP THR VAL LYS SEQRES 6 S 250 GLY ARG PHE THR ILE SER ARG ASP ASP PRO LYS ASN THR SEQRES 7 S 250 LEU PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR SEQRES 8 S 250 ALA MET TYR TYR CYS VAL ARG SER ILE TYR TYR TYR GLY SEQRES 9 S 250 SER SER PRO PHE ASP PHE TRP GLY GLN GLY THR THR LEU SEQRES 10 S 250 THR VAL SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SEQRES 11 S 250 SER GLY GLY GLY SER SER ASP ILE VAL MET THR GLN ALA SEQRES 12 S 250 THR SER SER VAL PRO VAL THR PRO GLY GLU SER VAL SER SEQRES 13 S 250 ILE SER CYS ARG SER SER LYS SER LEU LEU HIS SER ASN SEQRES 14 S 250 GLY ASN THR TYR LEU TYR TRP PHE LEU GLN ARG PRO GLY SEQRES 15 S 250 GLN SER PRO GLN LEU LEU ILE TYR ARG MET SER ASN LEU SEQRES 16 S 250 ALA SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SER SEQRES 17 S 250 GLY THR ALA PHE THR LEU THR ILE SER ARG LEU GLU ALA SEQRES 18 S 250 GLU ASP VAL GLY VAL TYR TYR CYS MET GLN HIS LEU GLU SEQRES 19 S 250 TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU LEU SEQRES 20 S 250 LYS GLY SER SEQRES 1 A 361 MET GLY CYS THR LEU SER ALA GLU ASP LYS ALA ALA VAL SEQRES 2 A 361 GLU ARG SER LYS MET ILE GLU LYS GLN LEU GLN LYS ASP SEQRES 3 A 361 LYS GLN VAL TYR ARG ARG THR LEU ARG LEU LEU LEU LEU SEQRES 4 A 361 GLY ALA ASP ASN SER GLY LYS SER THR ILE VAL LYS GLN SEQRES 5 A 361 MET ARG ILE TYR HIS VAL ASN GLY TYR SER GLU GLU GLU SEQRES 6 A 361 CYS LYS GLN TYR LYS ALA VAL VAL TYR SER ASN THR ILE SEQRES 7 A 361 GLN SER ILE ILE ALA ILE ILE ARG ALA MET GLY ARG LEU SEQRES 8 A 361 LYS ILE ASP PHE GLY ASP SER ALA ARG ALA ASP ASP ALA SEQRES 9 A 361 ARG GLN LEU PHE VAL LEU ALA GLY ALA ALA GLU GLU GLY SEQRES 10 A 361 PHE MET THR ALA GLU LEU ALA GLY VAL ILE LYS ARG LEU SEQRES 11 A 361 TRP LYS ASP SER GLY VAL GLN ALA CYS PHE ASN ARG SER SEQRES 12 A 361 ARG GLU TYR GLN LEU ASN ASP SER ALA ALA TYR TYR LEU SEQRES 13 A 361 ASN ASP LEU ASP ARG ILE ALA GLN PRO ASN TYR ILE PRO SEQRES 14 A 361 THR GLN GLN ASP VAL LEU ARG THR ARG VAL LYS THR SER SEQRES 15 A 361 GLY ILE PHE GLU THR LYS PHE GLN VAL ASP LYS VAL ASN SEQRES 16 A 361 PHE HIS MET PHE ASP VAL GLY ALA GLN ARG ASP GLU ARG SEQRES 17 A 361 ARG LYS TRP ILE GLN CYS PHE ASN ASP VAL THR ALA ILE SEQRES 18 A 361 ILE PHE VAL VAL ASP SER SER ASP TYR ASN ARG LEU GLN SEQRES 19 A 361 GLU ALA LEU ASN ASP PHE LYS SER ILE TRP ASN ASN ARG SEQRES 20 A 361 TRP LEU ARG THR ILE SER VAL ILE LEU PHE LEU ASN LYS SEQRES 21 A 361 GLN ASP LEU LEU ALA GLU LYS VAL LEU ALA GLY LYS SER SEQRES 22 A 361 LYS ILE GLU ASP TYR PHE PRO GLU PHE ALA ARG TYR THR SEQRES 23 A 361 THR PRO GLU ASP ALA THR PRO GLU PRO GLY GLU ASP PRO SEQRES 24 A 361 ARG VAL THR ARG ALA LYS TYR PHE ILE ARG LYS GLU PHE SEQRES 25 A 361 VAL ASP ILE SER THR ALA SER GLY ASP GLY ARG HIS ILE SEQRES 26 A 361 CYS TYR PRO HIS PHE THR CYS SER VAL ASP THR GLU ASN SEQRES 27 A 361 ALA ARG ARG ILE PHE ASN ASP CYS LYS ASP ILE ILE LEU SEQRES 28 A 361 GLN MET ASN LEU ARG GLU TYR ASN LEU VAL SEQRES 1 B 358 MET HIS HIS HIS HIS HIS HIS LEU GLU VAL LEU PHE GLN SEQRES 2 B 358 GLY PRO GLY SER SER GLN 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 N 151 MET LYS TYR LEU LEU PRO THR ALA ALA ALA GLY LEU LEU SEQRES 2 N 151 LEU LEU ALA ALA GLN PRO ALA MET ALA MET GLN VAL GLN SEQRES 3 N 151 LEU GLN GLU SER GLY GLY GLY LEU VAL GLN PRO GLY GLY SEQRES 4 N 151 SER LEU ARG LEU SER CYS ALA ALA SER GLY PHE THR PHE SEQRES 5 N 151 SER ASN TYR LYS MET ASN TRP VAL ARG GLN ALA PRO GLY SEQRES 6 N 151 LYS GLY LEU GLU TRP VAL SER ASP ILE SER GLN SER GLY SEQRES 7 N 151 ALA SER ILE SER TYR THR GLY SER VAL LYS GLY ARG PHE SEQRES 8 N 151 THR ILE SER ARG ASP ASN ALA LYS ASN THR LEU TYR LEU SEQRES 9 N 151 GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA VAL TYR SEQRES 10 N 151 TYR CYS ALA ARG CYS PRO ALA PRO PHE THR ARG ASP CYS SEQRES 11 N 151 PHE ASP VAL THR SER THR THR TYR ALA TYR ARG GLY GLN SEQRES 12 N 151 GLY THR GLN VAL THR VAL SER SER HET 16C R 401 38 HET CLR R 402 28 HET CLR R 403 28 HETNAM 16C N-((E,2S,3R)-1,3-DIHYDROXYOCTADEC-4-EN-2-YL)PALMITAMIDE HETNAM CLR CHOLESTEROL 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 7 16C C34 H67 N O3 FORMUL 8 CLR 2(C27 H46 O) HELIX 1 AA1 ILE R 43 LEU R 64 1 22 HELIX 2 AA2 VAL R 73 ARG R 100 1 28 HELIX 3 AA3 ASN R 103 ASP R 108 1 6 HELIX 4 AA4 LEU R 109 TYR R 119 1 11 HELIX 5 AA5 TYR R 119 HIS R 142 1 24 HELIX 6 AA6 ALA R 155 ILE R 171 1 17 HELIX 7 AA7 LEU R 198 CYS R 210 1 13 HELIX 8 AA8 CYS R 210 LYS R 230 1 21 HELIX 9 AA9 LEU R 238 HIS R 270 1 33 HELIX 10 AB1 LYS R 280 PHE R 307 1 28 HELIX 11 AB2 GLY R 309 LEU R 316 1 8 HELIX 12 AB3 ILE C 9 ASN C 24 1 16 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 ALA S 28 PHE S 32 5 5 HELIX 16 AB7 ARG S 191 SER S 193 5 3 HELIX 17 AB8 SER A 6 ARG A 39 1 27 HELIX 18 AB9 GLY A 52 HIS A 64 1 13 HELIX 19 AC1 LYS A 233 ASN A 239 5 7 HELIX 20 AC2 LEU A 266 ASN A 278 1 13 HELIX 21 AC3 LYS A 293 ALA A 303 1 11 HELIX 22 AC4 ASP A 331 GLY A 353 1 23 HELIX 23 AC5 GLU A 370 TYR A 391 1 22 HELIX 24 AC6 LEU B 4 CYS B 25 1 22 HELIX 25 AC7 THR B 29 THR B 34 1 6 HELIX 26 AC8 THR N 28 TYR N 32 5 5 HELIX 27 AC9 THR N 61 LYS N 65 5 5 SHEET 1 AA1 2 VAL S 5 GLU S 6 0 SHEET 2 AA1 2 CYS S 22 SER S 23 -1 O SER S 23 N VAL S 5 SHEET 1 AA2 2 LEU S 11 VAL S 12 0 SHEET 2 AA2 2 THR S 118 VAL S 119 1 O THR S 118 N VAL S 12 SHEET 1 AA3 3 LEU S 45 ILE S 51 0 SHEET 2 AA3 3 GLY S 33 GLN S 39 -1 N ARG S 38 O GLU S 46 SHEET 3 AA3 3 MET S 93 TYR S 95 -1 O MET S 93 N GLN S 39 SHEET 1 AA4 4 LEU S 45 ILE S 51 0 SHEET 2 AA4 4 GLY S 33 GLN S 39 -1 N ARG S 38 O GLU S 46 SHEET 3 AA4 4 VAL S 97 SER S 99 -1 O SER S 99 N GLY S 33 SHEET 4 AA4 4 PHE S 110 TRP S 111 -1 O PHE S 110 N ARG S 98 SHEET 1 AA5 4 MET S 140 GLN S 142 0 SHEET 2 AA5 4 SER S 158 SER S 161 -1 O ARG S 160 N THR S 141 SHEET 3 AA5 4 ALA S 211 THR S 215 -1 O PHE S 212 N CYS S 159 SHEET 4 AA5 4 SER S 204 SER S 206 -1 N SER S 206 O THR S 213 SHEET 1 AA6 2 PHE S 177 LEU S 178 0 SHEET 2 AA6 2 GLN S 186 LEU S 187 -1 O GLN S 186 N LEU S 178 SHEET 1 AA7 2 ILE S 189 TYR S 190 0 SHEET 2 AA7 2 ASN S 194 LEU S 195 -1 O ASN S 194 N TYR S 190 SHEET 1 AA8 2 GLY S 225 TYR S 227 0 SHEET 2 AA8 2 THR S 243 LEU S 245 -1 O THR S 243 N TYR S 227 SHEET 1 AA9 6 THR A 210 GLN A 213 0 SHEET 2 AA9 6 ASN A 218 ASP A 223 -1 O PHE A 219 N PHE A 212 SHEET 3 AA9 6 THR A 40 LEU A 46 1 N LEU A 43 O PHE A 222 SHEET 4 AA9 6 ILE A 245 ASP A 249 1 O ILE A 245 N LEU A 44 SHEET 5 AA9 6 PHE A 290 ASN A 292 1 O PHE A 290 N PHE A 246 SHEET 6 AA9 6 HIS A 362 PHE A 363 1 O HIS A 362 N LEU A 291 SHEET 1 AB1 4 THR B 47 ARG B 52 0 SHEET 2 AB1 4 PHE B 335 TRP B 339 -1 O LEU B 336 N LEU B 51 SHEET 3 AB1 4 VAL B 327 SER B 331 -1 N VAL B 327 O TRP B 339 SHEET 4 AB1 4 VAL B 315 VAL B 320 -1 N GLY B 319 O ALA B 328 SHEET 1 AB2 4 ILE B 58 TRP B 63 0 SHEET 2 AB2 4 LEU B 70 SER B 74 -1 O ALA B 73 N ALA B 60 SHEET 3 AB2 4 LYS B 78 TRP B 82 -1 O TRP B 82 N LEU B 70 SHEET 4 AB2 4 LYS B 89 PRO B 94 -1 O ILE B 93 N LEU B 79 SHEET 1 AB3 4 ALA B 104 TYR B 105 0 SHEET 2 AB3 4 TYR B 111 ALA B 113 -1 O ALA B 113 N ALA B 104 SHEET 3 AB3 4 ILE B 120 ASN B 125 -1 O TYR B 124 N VAL B 112 SHEET 4 AB3 4 ARG B 134 ALA B 140 -1 O SER B 136 N ILE B 123 SHEET 1 AB4 4 LEU B 146 PHE B 151 0 SHEET 2 AB4 4 GLN B 156 SER B 161 -1 O VAL B 158 N ARG B 150 SHEET 3 AB4 4 CYS B 166 ASP B 170 -1 O ALA B 167 N THR B 159 SHEET 4 AB4 4 GLN B 175 PHE B 180 -1 O PHE B 180 N CYS B 166 SHEET 1 AB5 4 VAL B 187 LEU B 192 0 SHEET 2 AB5 4 LEU B 198 ALA B 203 -1 O GLY B 202 N MET B 188 SHEET 3 AB5 4 ALA B 208 ASP B 212 -1 O LYS B 209 N SER B 201 SHEET 4 AB5 4 CYS B 218 PHE B 222 -1 O PHE B 222 N ALA B 208 SHEET 1 AB6 4 ILE B 229 PHE B 234 0 SHEET 2 AB6 4 ALA B 240 SER B 245 -1 O GLY B 244 N ALA B 231 SHEET 3 AB6 4 CYS B 250 ASP B 254 -1 O PHE B 253 N PHE B 241 SHEET 4 AB6 4 GLN B 259 TYR B 264 -1 O TYR B 264 N CYS B 250 SHEET 1 AB7 4 ILE B 273 PHE B 278 0 SHEET 2 AB7 4 LEU B 284 TYR B 289 -1 O LEU B 286 N SER B 277 SHEET 3 AB7 4 CYS B 294 ASP B 298 -1 O TRP B 297 N LEU B 285 SHEET 4 AB7 4 ASP B 303 LEU B 308 -1 O LEU B 308 N CYS B 294 SHEET 1 AB8 4 GLN N 3 SER N 7 0 SHEET 2 AB8 4 LEU N 18 SER N 25 -1 O ALA N 23 N GLN N 5 SHEET 3 AB8 4 THR N 78 MET N 83 -1 O LEU N 81 N LEU N 20 SHEET 4 AB8 4 PHE N 68 ASP N 73 -1 N THR N 69 O GLN N 82 SHEET 1 AB9 4 GLU N 46 SER N 49 0 SHEET 2 AB9 4 ASN N 35 GLN N 39 -1 N TRP N 36 O VAL N 48 SHEET 3 AB9 4 VAL N 93 ALA N 97 -1 O TYR N 95 N VAL N 37 SHEET 4 AB9 4 THR N 122 GLN N 123 -1 O THR N 122 N TYR N 94 SSBOND 1 CYS N 22 CYS N 96 1555 1555 2.03 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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