HEADER MEMBRANE PROTEIN 08-NOV-24 9E9S TITLE CRYO-EM STRUCTURE OF THE PGD2-BOUND PROSTAGLANDIN D2 RECEPTOR (DP1)-GS TITLE 2 COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(S) SUBUNIT ALPHA COMPND 3 ISOFORMS SHORT; COMPND 4 CHAIN: A; COMPND 5 SYNONYM: ADENYLATE CYCLASE-STIMULATING G ALPHA PROTEIN; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 9 BETA-1; COMPND 10 CHAIN: B; COMPND 11 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 3; COMPND 14 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 15 GAMMA-2; COMPND 16 CHAIN: C; COMPND 17 SYNONYM: G GAMMA-I; COMPND 18 ENGINEERED: YES; COMPND 19 MOL_ID: 4; COMPND 20 MOLECULE: PROSTAGLANDIN D2 RECEPTOR; COMPND 21 CHAIN: D; COMPND 22 SYNONYM: PGD RECEPTOR,PGD2 RECEPTOR,PROSTANOID DP RECEPTOR; COMPND 23 ENGINEERED: YES; COMPND 24 MOL_ID: 5; COMPND 25 MOLECULE: NANOBODY35|LAMA GLAMA; COMPND 26 CHAIN: N; COMPND 27 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: GNAS, GNAS1, GSP; 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: HOMO SAPIENS; SOURCE 24 ORGANISM_COMMON: HUMAN; SOURCE 25 ORGANISM_TAXID: 9606; SOURCE 26 GENE: PTGDR; SOURCE 27 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 29 MOL_ID: 5; SOURCE 30 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 31 ORGANISM_TAXID: 9844; SOURCE 32 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 33 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS GPCR, DP1, BW245C, PROSTAGLANDIN D2 RECEPTOR, PROSTANOID DP RECEPTOR, KEYWDS 2 PGD RECEPTOR, PTGDR, GS PROTEIN, DP1-SELECTIVE AGONIST, PGD2, KEYWDS 3 MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR B.DAVOUDINASAB,V.CHEREZOV,G.W.HAN,D.KIM REVDAT 1 03-SEP-25 9E9S 0 JRNL AUTH B.DAVOUDINASAB,G.W.HAN,V.CHEREZOV JRNL TITL CRYO-EM STRUCTURE OF INACTIVE AND ACTIVE PROSTAGLANDIN D2 JRNL TITL 2 RECEPTOR JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.68 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, PHENIX, 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 : 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) : 2.680 REMARK 3 NUMBER OF PARTICLES : 363286 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE REMARK 3 CORRECTION REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9E9S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-NOV-24. REMARK 100 THE DEPOSITION ID IS D_1000289965. 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 : PGD2-BOUND PROSTAGLANDIN D2 REMARK 245 RECEPTOR (DP1)-GS PROTEIN-NB35 REMARK 245 COMPLEX REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.50 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K 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) : 6500.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, 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 A 1 REMARK 465 GLY A 2 REMARK 465 CYS A 3 REMARK 465 LEU A 4 REMARK 465 GLY A 5 REMARK 465 ASN A 6 REMARK 465 SER A 7 REMARK 465 LYS A 8 REMARK 465 ILE A 62 REMARK 465 LEU A 63 REMARK 465 HIS A 64 REMARK 465 VAL A 65 REMARK 465 ASN A 66 REMARK 465 GLY A 67 REMARK 465 PHE A 68 REMARK 465 ASN A 69 REMARK 465 GLY A 70 REMARK 465 GLU A 71 REMARK 465 GLY A 72 REMARK 465 GLY A 73 REMARK 465 GLU A 74 REMARK 465 GLU A 75 REMARK 465 ASP A 76 REMARK 465 PRO A 77 REMARK 465 GLN A 78 REMARK 465 ALA A 79 REMARK 465 ALA A 80 REMARK 465 ARG A 81 REMARK 465 SER A 82 REMARK 465 ASN A 83 REMARK 465 SER A 84 REMARK 465 ASP A 85 REMARK 465 GLY A 86 REMARK 465 GLU A 87 REMARK 465 LYS A 88 REMARK 465 ALA A 89 REMARK 465 THR A 90 REMARK 465 LYS A 91 REMARK 465 VAL A 92 REMARK 465 GLN A 93 REMARK 465 ASP A 94 REMARK 465 ILE A 95 REMARK 465 LYS A 96 REMARK 465 ASN A 97 REMARK 465 ASN A 98 REMARK 465 LEU A 99 REMARK 465 LYS A 100 REMARK 465 GLU A 101 REMARK 465 ALA A 102 REMARK 465 ILE A 103 REMARK 465 GLU A 104 REMARK 465 THR A 105 REMARK 465 ILE A 106 REMARK 465 VAL A 107 REMARK 465 ALA A 108 REMARK 465 ALA A 109 REMARK 465 MET A 110 REMARK 465 SER A 111 REMARK 465 ASN A 112 REMARK 465 LEU A 113 REMARK 465 VAL A 114 REMARK 465 PRO A 115 REMARK 465 PRO A 116 REMARK 465 VAL A 117 REMARK 465 GLU A 118 REMARK 465 LEU A 119 REMARK 465 ALA A 120 REMARK 465 ASN A 121 REMARK 465 PRO A 122 REMARK 465 GLU A 123 REMARK 465 ASN A 124 REMARK 465 GLN A 125 REMARK 465 PHE A 126 REMARK 465 ARG A 127 REMARK 465 VAL A 128 REMARK 465 ASP A 129 REMARK 465 TYR A 130 REMARK 465 ILE A 131 REMARK 465 LEU A 132 REMARK 465 SER A 133 REMARK 465 VAL A 134 REMARK 465 MET A 135 REMARK 465 ASN A 136 REMARK 465 VAL A 137 REMARK 465 PRO A 138 REMARK 465 ASP A 139 REMARK 465 PHE A 140 REMARK 465 ASP A 141 REMARK 465 PHE A 142 REMARK 465 PRO A 143 REMARK 465 PRO A 144 REMARK 465 GLU A 145 REMARK 465 PHE A 146 REMARK 465 TYR A 147 REMARK 465 GLU A 148 REMARK 465 HIS A 149 REMARK 465 ALA A 150 REMARK 465 LYS A 151 REMARK 465 ALA A 152 REMARK 465 LEU A 153 REMARK 465 TRP A 154 REMARK 465 GLU A 155 REMARK 465 ASP A 156 REMARK 465 GLU A 157 REMARK 465 GLY A 158 REMARK 465 VAL A 159 REMARK 465 ARG A 160 REMARK 465 ALA A 161 REMARK 465 CYS A 162 REMARK 465 TYR A 163 REMARK 465 GLU A 164 REMARK 465 ARG A 165 REMARK 465 SER A 166 REMARK 465 ASN A 167 REMARK 465 GLU A 168 REMARK 465 TYR A 169 REMARK 465 GLN A 170 REMARK 465 LEU A 171 REMARK 465 ILE A 172 REMARK 465 ASP A 173 REMARK 465 CYS A 174 REMARK 465 ALA A 175 REMARK 465 GLN A 176 REMARK 465 TYR A 177 REMARK 465 PHE A 178 REMARK 465 LEU A 179 REMARK 465 ASP A 180 REMARK 465 LYS A 181 REMARK 465 ILE A 182 REMARK 465 ASP A 183 REMARK 465 VAL A 184 REMARK 465 ILE A 185 REMARK 465 LYS A 186 REMARK 465 GLN A 187 REMARK 465 ALA A 188 REMARK 465 ASP A 189 REMARK 465 TYR A 190 REMARK 465 VAL A 191 REMARK 465 PRO A 192 REMARK 465 SER A 193 REMARK 465 ASP A 194 REMARK 465 GLN A 195 REMARK 465 ASP A 196 REMARK 465 LEU A 197 REMARK 465 LEU A 198 REMARK 465 ARG A 199 REMARK 465 CYS A 200 REMARK 465 ARG A 201 REMARK 465 VAL A 202 REMARK 465 LEU A 203 REMARK 465 ILE A 257 REMARK 465 ARG A 258 REMARK 465 GLU A 259 REMARK 465 ASP A 260 REMARK 465 ASN A 261 REMARK 465 GLN A 262 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 MET C 1 REMARK 465 ALA C 2 REMARK 465 SER C 3 REMARK 465 ASN C 4 REMARK 465 LYS C 64 REMARK 465 LYS C 65 REMARK 465 PHE C 66 REMARK 465 PHE C 67 REMARK 465 CYS C 68 REMARK 465 ALA C 69 REMARK 465 ILE C 70 REMARK 465 LEU C 71 REMARK 465 MET D -25 REMARK 465 LYS D -24 REMARK 465 THR D -23 REMARK 465 ILE D -22 REMARK 465 ILE D -21 REMARK 465 ALA D -20 REMARK 465 LEU D -19 REMARK 465 SER D -18 REMARK 465 TYR D -17 REMARK 465 ILE D -16 REMARK 465 PHE D -15 REMARK 465 CYS D -14 REMARK 465 LEU D -13 REMARK 465 VAL D -12 REMARK 465 PHE D -11 REMARK 465 ALA D -10 REMARK 465 ASP D -9 REMARK 465 TYR D -8 REMARK 465 LYS D -7 REMARK 465 ASP D -6 REMARK 465 ASP D -5 REMARK 465 ASP D -4 REMARK 465 ASP D -3 REMARK 465 GLY D -2 REMARK 465 ALA D -1 REMARK 465 PRO D 0 REMARK 465 MET D 1 REMARK 465 LYS D 2 REMARK 465 TRP D 48 REMARK 465 CYS D 49 REMARK 465 SER D 50 REMARK 465 ARG D 51 REMARK 465 ARG D 52 REMARK 465 PRO D 53 REMARK 465 LEU D 54 REMARK 465 ARG D 55 REMARK 465 PRO D 56 REMARK 465 LEU D 57 REMARK 465 PRO D 236 REMARK 465 ARG D 237 REMARK 465 SER D 238 REMARK 465 CYS D 239 REMARK 465 THR D 240 REMARK 465 ARG D 241 REMARK 465 ASP D 242 REMARK 465 CYS D 243 REMARK 465 ALA D 244 REMARK 465 GLU D 245 REMARK 465 PRO D 246 REMARK 465 ARG D 247 REMARK 465 ALA D 248 REMARK 465 ASP D 249 REMARK 465 GLY D 250 REMARK 465 ARG D 251 REMARK 465 GLU D 252 REMARK 465 ALA D 253 REMARK 465 SER D 254 REMARK 465 PHE D 339 REMARK 465 ILE D 340 REMARK 465 ARG D 341 REMARK 465 PRO D 342 REMARK 465 LEU D 343 REMARK 465 ARG D 344 REMARK 465 TYR D 345 REMARK 465 ARG D 346 REMARK 465 SER D 347 REMARK 465 ARG D 348 REMARK 465 CYS D 349 REMARK 465 SER D 350 REMARK 465 ASN D 351 REMARK 465 SER D 352 REMARK 465 THR D 353 REMARK 465 ASN D 354 REMARK 465 MET D 355 REMARK 465 GLU D 356 REMARK 465 SER D 357 REMARK 465 SER D 358 REMARK 465 LEU D 359 REMARK 465 MET N 0 REMARK 465 HIS N 129 REMARK 465 HIS N 130 REMARK 465 HIS N 131 REMARK 465 HIS N 132 REMARK 465 HIS N 133 REMARK 465 HIS N 134 REMARK 465 GLU N 135 REMARK 465 PRO N 136 REMARK 465 GLU N 137 REMARK 465 ALA N 138 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ASN A 254 CG OD1 ND2 REMARK 470 MET A 255 CG SD CE REMARK 470 VAL A 256 CG1 CG2 REMARK 470 ARG D 234 CG CD NE CZ NH1 NH2 REMARK 470 HIS D 336 CG ND1 CD2 CE1 NE2 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 SER A 306 -160.04 56.18 REMARK 500 PRO A 332 45.63 -78.48 REMARK 500 ASP A 354 16.65 59.24 REMARK 500 TRP B 99 42.29 -109.64 REMARK 500 SER C 57 -1.09 67.16 REMARK 500 ASP D 101 -125.48 45.24 REMARK 500 PRO D 179 37.44 -90.02 REMARK 500 ILE D 324 -59.36 -123.88 REMARK 500 LYS D 337 -144.61 52.14 REMARK 500 TYR N 117 38.27 -98.48 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-47802 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF THE BW245C-BOUND PROSTAGLANDIN D2 RECEPTOR REMARK 900 (DP1)-GS COMPLEX REMARK 900 RELATED ID: EMD-71658 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-76159 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-76160 RELATED DB: EMDB DBREF 9E9S A 1 394 UNP P63092 GNAS2_HUMAN 1 394 DBREF 9E9S B 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 9E9S C 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 9E9S D 1 359 UNP Q13258 PD2R_HUMAN 1 359 DBREF 9E9S N 0 138 PDB 9E9S 9E9S 0 138 SEQADV 9E9S ASN A 54 UNP P63092 SER 54 ENGINEERED MUTATION SEQADV 9E9S ALA A 226 UNP P63092 GLY 226 ENGINEERED MUTATION SEQADV 9E9S ALA A 268 UNP P63092 GLU 268 ENGINEERED MUTATION SEQADV 9E9S LYS A 271 UNP P63092 ASN 271 ENGINEERED MUTATION SEQADV 9E9S ASP A 274 UNP P63092 LYS 274 ENGINEERED MUTATION SEQADV 9E9S LYS A 280 UNP P63092 ARG 280 ENGINEERED MUTATION SEQADV 9E9S ASP A 284 UNP P63092 THR 284 ENGINEERED MUTATION SEQADV 9E9S THR A 285 UNP P63092 ILE 285 ENGINEERED MUTATION SEQADV 9E9S GLY B -4 UNP P62873 EXPRESSION TAG SEQADV 9E9S PRO B -3 UNP P62873 EXPRESSION TAG SEQADV 9E9S GLY B -2 UNP P62873 EXPRESSION TAG SEQADV 9E9S SER B -1 UNP P62873 EXPRESSION TAG SEQADV 9E9S SER B 0 UNP P62873 EXPRESSION TAG SEQADV 9E9S GLN B 1 UNP P62873 EXPRESSION TAG SEQADV 9E9S MET D -25 UNP Q13258 EXPRESSION TAG SEQADV 9E9S LYS D -24 UNP Q13258 EXPRESSION TAG SEQADV 9E9S THR D -23 UNP Q13258 EXPRESSION TAG SEQADV 9E9S ILE D -22 UNP Q13258 EXPRESSION TAG SEQADV 9E9S ILE D -21 UNP Q13258 EXPRESSION TAG SEQADV 9E9S ALA D -20 UNP Q13258 EXPRESSION TAG SEQADV 9E9S LEU D -19 UNP Q13258 EXPRESSION TAG SEQADV 9E9S SER D -18 UNP Q13258 EXPRESSION TAG SEQADV 9E9S TYR D -17 UNP Q13258 EXPRESSION TAG SEQADV 9E9S ILE D -16 UNP Q13258 EXPRESSION TAG SEQADV 9E9S PHE D -15 UNP Q13258 EXPRESSION TAG SEQADV 9E9S CYS D -14 UNP Q13258 EXPRESSION TAG SEQADV 9E9S LEU D -13 UNP Q13258 EXPRESSION TAG SEQADV 9E9S VAL D -12 UNP Q13258 EXPRESSION TAG SEQADV 9E9S PHE D -11 UNP Q13258 EXPRESSION TAG SEQADV 9E9S ALA D -10 UNP Q13258 EXPRESSION TAG SEQADV 9E9S ASP D -9 UNP Q13258 EXPRESSION TAG SEQADV 9E9S TYR D -8 UNP Q13258 EXPRESSION TAG SEQADV 9E9S LYS D -7 UNP Q13258 EXPRESSION TAG SEQADV 9E9S ASP D -6 UNP Q13258 EXPRESSION TAG SEQADV 9E9S ASP D -5 UNP Q13258 EXPRESSION TAG SEQADV 9E9S ASP D -4 UNP Q13258 EXPRESSION TAG SEQADV 9E9S ASP D -3 UNP Q13258 EXPRESSION TAG SEQADV 9E9S GLY D -2 UNP Q13258 EXPRESSION TAG SEQADV 9E9S ALA D -1 UNP Q13258 EXPRESSION TAG SEQADV 9E9S PRO D 0 UNP Q13258 EXPRESSION TAG SEQRES 1 A 394 MET GLY CYS LEU GLY ASN SER LYS THR GLU ASP GLN ARG SEQRES 2 A 394 ASN GLU GLU LYS ALA GLN ARG GLU ALA ASN LYS LYS ILE SEQRES 3 A 394 GLU LYS GLN LEU GLN LYS ASP LYS GLN VAL TYR ARG ALA SEQRES 4 A 394 THR HIS ARG LEU LEU LEU LEU GLY ALA GLY GLU SER GLY SEQRES 5 A 394 LYS ASN THR ILE VAL LYS GLN MET ARG ILE LEU HIS VAL SEQRES 6 A 394 ASN GLY PHE ASN GLY GLU GLY GLY GLU GLU ASP PRO GLN SEQRES 7 A 394 ALA ALA ARG SER ASN SER ASP GLY GLU LYS ALA THR LYS SEQRES 8 A 394 VAL GLN ASP ILE LYS ASN ASN LEU LYS GLU ALA ILE GLU SEQRES 9 A 394 THR ILE VAL ALA ALA MET SER ASN LEU VAL PRO PRO VAL SEQRES 10 A 394 GLU LEU ALA ASN PRO GLU ASN GLN PHE ARG VAL ASP TYR SEQRES 11 A 394 ILE LEU SER VAL MET ASN VAL PRO ASP PHE ASP PHE PRO SEQRES 12 A 394 PRO GLU PHE TYR GLU HIS ALA LYS ALA LEU TRP GLU ASP SEQRES 13 A 394 GLU GLY VAL ARG ALA CYS TYR GLU ARG SER ASN GLU TYR SEQRES 14 A 394 GLN LEU ILE ASP CYS ALA GLN TYR PHE LEU ASP LYS ILE SEQRES 15 A 394 ASP VAL ILE LYS GLN ALA ASP TYR VAL PRO SER ASP GLN SEQRES 16 A 394 ASP LEU LEU ARG CYS ARG VAL LEU THR SER GLY ILE PHE SEQRES 17 A 394 GLU THR LYS PHE GLN VAL ASP LYS VAL ASN PHE HIS MET SEQRES 18 A 394 PHE ASP VAL GLY ALA GLN ARG ASP GLU ARG ARG LYS TRP SEQRES 19 A 394 ILE GLN CYS PHE ASN ASP VAL THR ALA ILE ILE PHE VAL SEQRES 20 A 394 VAL ALA SER SER SER TYR ASN MET VAL ILE ARG GLU ASP SEQRES 21 A 394 ASN GLN THR ASN ARG LEU GLN ALA ALA LEU LYS LEU PHE SEQRES 22 A 394 ASP SER ILE TRP ASN ASN LYS TRP LEU ARG ASP THR SER SEQRES 23 A 394 VAL ILE LEU PHE LEU ASN LYS GLN ASP LEU LEU ALA GLU SEQRES 24 A 394 LYS VAL LEU ALA GLY LYS SER LYS ILE GLU ASP TYR PHE SEQRES 25 A 394 PRO GLU PHE ALA ARG TYR THR THR PRO GLU ASP ALA THR SEQRES 26 A 394 PRO GLU PRO GLY GLU ASP PRO ARG VAL THR ARG ALA LYS SEQRES 27 A 394 TYR PHE ILE ARG ASP GLU PHE LEU ARG ILE SER THR ALA SEQRES 28 A 394 SER GLY ASP GLY ARG HIS TYR CYS TYR PRO HIS PHE THR SEQRES 29 A 394 CYS ALA VAL ASP THR GLU ASN ILE ARG ARG VAL PHE ASN SEQRES 30 A 394 ASP CYS ARG ASP ILE ILE GLN ARG MET HIS LEU ARG GLN SEQRES 31 A 394 TYR GLU LEU LEU SEQRES 1 B 345 GLY PRO GLY SER SER GLN SER GLU LEU ASP GLN LEU ARG SEQRES 2 B 345 GLN GLU ALA GLU GLN LEU LYS ASN GLN ILE ARG ASP ALA SEQRES 3 B 345 ARG LYS ALA CYS ALA ASP ALA THR LEU SER GLN ILE THR SEQRES 4 B 345 ASN ASN ILE ASP PRO VAL GLY ARG ILE GLN MET ARG THR SEQRES 5 B 345 ARG ARG THR LEU ARG GLY HIS LEU ALA LYS ILE TYR ALA SEQRES 6 B 345 MET HIS TRP GLY THR ASP SER ARG LEU LEU VAL SER ALA SEQRES 7 B 345 SER GLN ASP GLY LYS LEU ILE ILE TRP ASP SER TYR THR SEQRES 8 B 345 THR ASN LYS VAL HIS ALA ILE PRO LEU ARG SER SER TRP SEQRES 9 B 345 VAL MET THR CYS ALA TYR ALA PRO SER GLY ASN TYR VAL SEQRES 10 B 345 ALA CYS GLY GLY LEU ASP ASN ILE CYS SER ILE TYR ASN SEQRES 11 B 345 LEU LYS THR ARG GLU GLY ASN VAL ARG VAL SER ARG GLU SEQRES 12 B 345 LEU ALA GLY HIS THR GLY TYR LEU SER CYS CYS ARG PHE SEQRES 13 B 345 LEU ASP ASP ASN GLN ILE VAL THR SER SER GLY ASP THR SEQRES 14 B 345 THR CYS ALA LEU TRP ASP ILE GLU THR GLY GLN GLN THR SEQRES 15 B 345 THR THR PHE THR GLY HIS THR GLY ASP VAL MET SER LEU SEQRES 16 B 345 SER LEU ALA PRO ASP THR ARG LEU PHE VAL SER GLY ALA SEQRES 17 B 345 CYS ASP ALA SER ALA LYS LEU TRP ASP VAL ARG GLU GLY SEQRES 18 B 345 MET CYS ARG GLN THR PHE THR GLY HIS GLU SER ASP ILE SEQRES 19 B 345 ASN ALA ILE CYS PHE PHE PRO ASN GLY ASN ALA PHE ALA SEQRES 20 B 345 THR GLY SER ASP ASP ALA THR CYS ARG LEU PHE ASP LEU SEQRES 21 B 345 ARG ALA ASP GLN GLU LEU MET THR TYR SER HIS ASP ASN SEQRES 22 B 345 ILE ILE CYS GLY ILE THR SER VAL SER PHE SER LYS SER SEQRES 23 B 345 GLY ARG LEU LEU LEU ALA GLY TYR ASP ASP PHE ASN CYS SEQRES 24 B 345 ASN VAL TRP ASP ALA LEU LYS ALA ASP ARG ALA GLY VAL SEQRES 25 B 345 LEU ALA GLY HIS ASP ASN ARG VAL SER CYS LEU GLY VAL SEQRES 26 B 345 THR ASP ASP GLY MET ALA VAL ALA THR GLY SER TRP ASP SEQRES 27 B 345 SER PHE LEU LYS ILE TRP ASN SEQRES 1 C 71 MET ALA SER ASN ASN THR ALA SER ILE ALA GLN ALA ARG SEQRES 2 C 71 LYS LEU VAL GLU GLN LEU LYS MET GLU ALA ASN ILE ASP SEQRES 3 C 71 ARG ILE LYS VAL SER LYS ALA ALA ALA ASP LEU MET ALA SEQRES 4 C 71 TYR CYS GLU ALA HIS ALA LYS GLU ASP PRO LEU LEU THR SEQRES 5 C 71 PRO VAL PRO ALA SER GLU ASN PRO PHE ARG GLU LYS LYS SEQRES 6 C 71 PHE PHE CYS ALA ILE LEU SEQRES 1 D 385 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU SEQRES 2 D 385 VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO SEQRES 3 D 385 MET LYS SER PRO PHE TYR ARG CYS GLN ASN THR THR SER SEQRES 4 D 385 VAL GLU LYS GLY ASN SER ALA VAL MET GLY GLY VAL LEU SEQRES 5 D 385 PHE SER THR GLY LEU LEU GLY ASN LEU LEU ALA LEU GLY SEQRES 6 D 385 LEU LEU ALA ARG SER GLY LEU GLY TRP CYS SER ARG ARG SEQRES 7 D 385 PRO LEU ARG PRO LEU PRO SER VAL PHE TYR MET LEU VAL SEQRES 8 D 385 CYS GLY LEU THR VAL THR ASP LEU LEU GLY LYS CYS LEU SEQRES 9 D 385 LEU SER PRO VAL VAL LEU ALA ALA TYR ALA GLN ASN ARG SEQRES 10 D 385 SER LEU ARG VAL LEU ALA PRO ALA LEU ASP ASN SER LEU SEQRES 11 D 385 CYS GLN ALA PHE ALA PHE PHE MET SER PHE PHE GLY LEU SEQRES 12 D 385 SER SER THR LEU GLN LEU LEU ALA MET ALA LEU GLU CYS SEQRES 13 D 385 TRP LEU SER LEU GLY HIS PRO PHE PHE TYR ARG ARG HIS SEQRES 14 D 385 ILE THR LEU ARG LEU GLY ALA LEU VAL ALA PRO VAL VAL SEQRES 15 D 385 SER ALA PHE SER LEU ALA PHE CYS ALA LEU PRO PHE MET SEQRES 16 D 385 GLY PHE GLY LYS PHE VAL GLN TYR CYS PRO GLY THR TRP SEQRES 17 D 385 CYS PHE ILE GLN MET VAL HIS GLU GLU GLY SER LEU SER SEQRES 18 D 385 VAL LEU GLY TYR SER VAL LEU TYR SER SER LEU MET ALA SEQRES 19 D 385 LEU LEU VAL LEU ALA THR VAL LEU CYS ASN LEU GLY ALA SEQRES 20 D 385 MET ARG ASN LEU TYR ALA MET HIS ARG ARG LEU GLN ARG SEQRES 21 D 385 HIS PRO ARG SER CYS THR ARG ASP CYS ALA GLU PRO ARG SEQRES 22 D 385 ALA ASP GLY ARG GLU ALA SER PRO GLN PRO LEU GLU GLU SEQRES 23 D 385 LEU ASP HIS LEU LEU LEU LEU ALA LEU MET THR VAL LEU SEQRES 24 D 385 PHE THR MET CYS SER LEU PRO VAL ILE TYR ARG ALA TYR SEQRES 25 D 385 TYR GLY ALA PHE LYS ASP VAL LYS GLU LYS ASN ARG THR SEQRES 26 D 385 SER GLU GLU ALA GLU ASP LEU ARG ALA LEU ARG PHE LEU SEQRES 27 D 385 SER VAL ILE SER ILE VAL ASP PRO TRP ILE PHE ILE ILE SEQRES 28 D 385 PHE ARG SER PRO VAL PHE ARG ILE PHE PHE HIS LYS ILE SEQRES 29 D 385 PHE ILE ARG PRO LEU ARG TYR ARG SER ARG CYS SER ASN SEQRES 30 D 385 SER THR ASN MET GLU SER SER LEU SEQRES 1 N 139 MET GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL SEQRES 2 N 139 GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER SEQRES 3 N 139 GLY PHE THR PHE SER ASN TYR LYS MET ASN TRP VAL ARG SEQRES 4 N 139 GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ASP ILE SEQRES 5 N 139 SER GLN SER GLY ALA SER ILE SER TYR THR GLY SER VAL SEQRES 6 N 139 LYS GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SEQRES 7 N 139 THR LEU TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP SEQRES 8 N 139 THR ALA VAL TYR TYR CYS ALA ARG CYS PRO ALA PRO PHE SEQRES 9 N 139 THR ARG ASP CYS PHE ASP VAL THR SER THR THR TYR ALA SEQRES 10 N 139 TYR ARG GLY GLN GLY THR GLN VAL THR VAL SER SER HIS SEQRES 11 N 139 HIS HIS HIS HIS HIS GLU PRO GLU ALA HET PG2 D 401 25 HET NAG D 402 14 HET Y01 D 403 35 HETNAM PG2 PROSTAGLANDIN D2 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM Y01 CHOLESTEROL HEMISUCCINATE HETSYN PG2 (5E,13E)-9,15-DIHYDROXY-11-OXOPROSTA-5,13-DIEN-1-OIC HETSYN 2 PG2 ACID HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE FORMUL 6 PG2 C20 H32 O5 FORMUL 7 NAG C8 H15 N O6 FORMUL 8 Y01 C31 H50 O4 FORMUL 9 HOH *90(H2 O) HELIX 1 AA1 THR A 9 ALA A 39 1 31 HELIX 2 AA2 GLY A 52 GLN A 59 1 8 HELIX 3 AA3 LYS A 233 ASN A 239 5 7 HELIX 4 AA4 ASN A 264 ASN A 279 1 16 HELIX 5 AA5 LYS A 293 GLY A 304 1 12 HELIX 6 AA6 PHE A 312 ALA A 316 5 5 HELIX 7 AA7 ARG A 333 THR A 350 1 18 HELIX 8 AA8 GLU A 370 ARG A 389 1 20 HELIX 9 AA9 GLN A 390 GLU A 392 5 3 HELIX 10 AB1 GLU B 3 ALA B 26 1 24 HELIX 11 AB2 THR B 29 THR B 34 1 6 HELIX 12 AB3 THR C 6 ASN C 24 1 19 HELIX 13 AB4 LYS C 29 HIS C 44 1 16 HELIX 14 AB5 ALA C 45 ASP C 48 5 4 HELIX 15 AB6 ALA D 20 LEU D 46 1 27 HELIX 16 AB7 SER D 59 ASN D 90 1 32 HELIX 17 AB8 ASN D 102 HIS D 136 1 35 HELIX 18 AB9 HIS D 136 ILE D 144 1 9 HELIX 19 AC1 THR D 145 LEU D 151 1 7 HELIX 20 AC2 LEU D 151 CYS D 164 1 14 HELIX 21 AC3 ALA D 165 GLY D 170 5 6 HELIX 22 AC4 SER D 193 HIS D 235 1 43 HELIX 23 AC5 GLU D 260 LYS D 291 1 32 HELIX 24 AC6 ASP D 292 LYS D 296 5 5 HELIX 25 AC7 ASN D 297 SER D 313 1 17 HELIX 26 AC8 SER D 313 ILE D 324 1 12 HELIX 27 AC9 ILE D 325 ARG D 327 5 3 HELIX 28 AD1 SER D 328 HIS D 336 1 9 HELIX 29 AD2 THR N 28 TYR N 32 5 5 HELIX 30 AD3 LYS N 87 THR N 91 5 5 SHEET 1 AA1 6 ILE A 207 GLN A 213 0 SHEET 2 AA1 6 ASN A 218 VAL A 224 -1 O ASP A 223 N PHE A 208 SHEET 3 AA1 6 THR A 40 GLY A 47 1 N LEU A 43 O HIS A 220 SHEET 4 AA1 6 ALA A 243 ALA A 249 1 O ILE A 245 N LEU A 44 SHEET 5 AA1 6 SER A 286 ASN A 292 1 O PHE A 290 N PHE A 246 SHEET 6 AA1 6 CYS A 359 HIS A 362 1 O HIS A 362 N LEU A 291 SHEET 1 AA2 4 THR B 47 LEU B 51 0 SHEET 2 AA2 4 LEU B 336 TRP B 339 -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 GLY B 319 O ALA B 328 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 ALA B 60 SHEET 3 AA3 4 LYS B 78 ASP B 83 -1 O TRP B 82 N LEU B 70 SHEET 4 AA3 4 ASN B 88 PRO B 94 -1 O ILE B 93 N LEU B 79 SHEET 1 AA4 4 VAL B 100 TYR B 105 0 SHEET 2 AA4 4 TYR B 111 GLY B 116 -1 O GLY B 115 N MET B 101 SHEET 3 AA4 4 CYS B 121 ASN B 125 -1 O SER B 122 N CYS B 114 SHEET 4 AA4 4 ARG B 134 LEU B 139 -1 O ARG B 137 N ILE B 123 SHEET 1 AA5 4 LEU B 146 PHE B 151 0 SHEET 2 AA5 4 GLN B 156 SER B 161 -1 O SER B 160 N CYS B 148 SHEET 3 AA5 4 THR B 165 ASP B 170 -1 O ALA B 167 N THR B 159 SHEET 4 AA5 4 GLN B 175 THR B 181 -1 O PHE B 180 N CYS B 166 SHEET 1 AA6 4 VAL B 187 LEU B 192 0 SHEET 2 AA6 4 LEU B 198 ALA B 203 -1 O VAL B 200 N SER B 191 SHEET 3 AA6 4 ALA B 208 ASP B 212 -1 O TRP B 211 N PHE B 199 SHEET 4 AA6 4 MET B 217 PHE B 222 -1 O ARG B 219 N LEU B 210 SHEET 1 AA7 4 ILE B 229 PHE B 234 0 SHEET 2 AA7 4 ALA B 240 SER B 245 -1 O ALA B 242 N CYS B 233 SHEET 3 AA7 4 CYS B 250 ASP B 254 -1 O PHE B 253 N PHE B 241 SHEET 4 AA7 4 GLN B 259 TYR B 264 -1 O TYR B 264 N CYS B 250 SHEET 1 AA8 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 ASN B 295 N ALA B 287 SHEET 4 AA8 4 ARG B 304 LEU B 308 -1 O ALA B 305 N VAL B 296 SHEET 1 AA9 2 PHE D 174 TYR D 177 0 SHEET 2 AA9 2 TRP D 182 ILE D 185 -1 O PHE D 184 N VAL D 175 SHEET 1 AB1 4 GLN N 3 SER N 7 0 SHEET 2 AB1 4 LEU N 18 SER N 25 -1 O SER N 21 N SER N 7 SHEET 3 AB1 4 THR N 78 MET N 83 -1 O MET N 83 N LEU N 18 SHEET 4 AB1 4 PHE N 68 ASP N 73 -1 N THR N 69 O GLN N 82 SHEET 1 AB2 6 LEU N 11 VAL N 12 0 SHEET 2 AB2 6 THR N 122 VAL N 126 1 O THR N 125 N VAL N 12 SHEET 3 AB2 6 ALA N 92 ARG N 98 -1 N ALA N 92 O VAL N 124 SHEET 4 AB2 6 MET N 34 GLN N 39 -1 N VAL N 37 O TYR N 95 SHEET 5 AB2 6 LEU N 45 ILE N 51 -1 O GLU N 46 N ARG N 38 SHEET 6 AB2 6 ILE N 58 TYR N 60 -1 O SER N 59 N ASP N 50 SSBOND 1 CYS D 8 CYS D 178 1555 1555 2.03 SSBOND 2 CYS D 105 CYS D 183 1555 1555 2.03 SSBOND 3 CYS N 22 CYS N 96 1555 1555 2.03 SSBOND 4 CYS N 99 CYS N 107 1555 1555 2.03 LINK ND2 ASN D 10 C1 NAG D 402 1555 1555 1.44 CISPEP 1 CYS D 178 PRO D 179 0 0.99 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