HEADER MEMBRANE PROTEIN 05-DEC-24 9KVG TITLE A CRYO_EM STRUCTURE OF 5_HT1A COMPLEX WITH 5-MEO-DMT 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 EC: 3.6.5.-; 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: SCFV16; COMPND 15 CHAIN: E; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 4; COMPND 18 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 19 GAMMA-2; COMPND 20 CHAIN: G; COMPND 21 SYNONYM: G GAMMA-I; COMPND 22 ENGINEERED: YES; COMPND 23 MOL_ID: 5; COMPND 24 MOLECULE: 5-HYDROXYTRYPTAMINE RECEPTOR 1A; COMPND 25 CHAIN: R; COMPND 26 SYNONYM: 5-HT-1A,5-HT1A,G-21,SEROTONIN RECEPTOR 1A; 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: 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 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 21 MOL_ID: 4; SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 23 ORGANISM_COMMON: HUMAN; SOURCE 24 ORGANISM_TAXID: 9606; SOURCE 25 GENE: GNG2; SOURCE 26 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 27 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 28 MOL_ID: 5; SOURCE 29 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 30 ORGANISM_COMMON: HUMAN; SOURCE 31 ORGANISM_TAXID: 9606; SOURCE 32 GENE: HTR1A, ADRB2RL1, ADRBRL1; SOURCE 33 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 34 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS GPCR, 5_HT1A, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR Q.YUAN,S.LI REVDAT 1 03-DEC-25 9KVG 0 JRNL AUTH Q.YUAN,S.LI JRNL TITL A CRYO_EM STRUCTURE OF 5_HT1A COMPLEX WITH 5-MEO-DMT JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.63 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX 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) : 2.630 REMARK 3 NUMBER OF PARTICLES : 180294 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 9KVG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 09-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1300054419. 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 : 5-HT1A COMPLEX WITH 5-MEO-DMT 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 : 7.04 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 : FEI FALCON III (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 8000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 18000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 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, E, G, 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 ALA A 41 REMARK 465 GLY A 42 REMARK 465 GLU A 43 REMARK 465 ILE A 55 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 GLY B 2 REMARK 465 SER B 3 REMARK 465 LEU B 4 REMARK 465 LEU B 5 REMARK 465 GLN B 6 REMARK 465 SER B 7 REMARK 465 GLU B 8 REMARK 465 LEU B 9 REMARK 465 ASP B 10 REMARK 465 GLN B 11 REMARK 465 LEU B 12 REMARK 465 ARG B 13 REMARK 465 ALA E 120 REMARK 465 GLY E 121 REMARK 465 GLY E 122 REMARK 465 GLY E 123 REMARK 465 GLY E 124 REMARK 465 SER E 125 REMARK 465 GLY E 126 REMARK 465 GLY E 127 REMARK 465 GLY E 128 REMARK 465 GLY E 129 REMARK 465 SER E 130 REMARK 465 GLY E 131 REMARK 465 GLY E 132 REMARK 465 GLY E 133 REMARK 465 GLY E 134 REMARK 465 MET G 0 REMARK 465 ALA G 1 REMARK 465 SER G 2 REMARK 465 ASN G 3 REMARK 465 ASN G 4 REMARK 465 THR G 5 REMARK 465 ALA G 6 REMARK 465 SER G 7 REMARK 465 ILE G 8 REMARK 465 GLU G 62 REMARK 465 LYS G 63 REMARK 465 LYS G 64 REMARK 465 PHE G 65 REMARK 465 PHE G 66 REMARK 465 CYS G 67 REMARK 465 ALA G 68 REMARK 465 ILE G 69 REMARK 465 LEU G 70 REMARK 465 THR R 25 REMARK 465 THR R 26 REMARK 465 GLY R 27 REMARK 465 ILE R 28 REMARK 465 SER R 29 REMARK 465 ASP R 30 REMARK 465 VAL R 31 REMARK 465 THR R 32 REMARK 465 VAL R 33 REMARK 465 THR R 229 REMARK 465 VAL R 230 REMARK 465 LYS R 231 REMARK 465 LYS R 232 REMARK 465 VAL R 233 REMARK 465 GLU R 234 REMARK 465 LYS R 235 REMARK 465 THR R 236 REMARK 465 GLY R 237 REMARK 465 ALA R 238 REMARK 465 ASP R 239 REMARK 465 THR R 240 REMARK 465 ARG R 241 REMARK 465 HIS R 242 REMARK 465 GLY R 243 REMARK 465 ALA R 244 REMARK 465 SER R 245 REMARK 465 PRO R 246 REMARK 465 ALA R 247 REMARK 465 PRO R 248 REMARK 465 GLN R 249 REMARK 465 PRO R 250 REMARK 465 LYS R 251 REMARK 465 LYS R 252 REMARK 465 SER R 253 REMARK 465 VAL R 254 REMARK 465 ASN R 255 REMARK 465 GLY R 256 REMARK 465 GLU R 257 REMARK 465 SER R 258 REMARK 465 GLY R 259 REMARK 465 SER R 260 REMARK 465 ARG R 261 REMARK 465 ASN R 262 REMARK 465 TRP R 263 REMARK 465 ARG R 264 REMARK 465 LEU R 265 REMARK 465 GLY R 266 REMARK 465 VAL R 267 REMARK 465 GLU R 268 REMARK 465 SER R 269 REMARK 465 LYS R 270 REMARK 465 ALA R 271 REMARK 465 GLY R 272 REMARK 465 GLY R 273 REMARK 465 ALA R 274 REMARK 465 LEU R 275 REMARK 465 CYS R 276 REMARK 465 ALA R 277 REMARK 465 ASN R 278 REMARK 465 GLY R 279 REMARK 465 ALA R 280 REMARK 465 VAL R 281 REMARK 465 ARG R 282 REMARK 465 GLN R 283 REMARK 465 GLY R 284 REMARK 465 ASP R 285 REMARK 465 ASP R 286 REMARK 465 GLY R 287 REMARK 465 ALA R 288 REMARK 465 ALA R 289 REMARK 465 LEU R 290 REMARK 465 GLU R 291 REMARK 465 VAL R 292 REMARK 465 ILE R 293 REMARK 465 GLU R 294 REMARK 465 VAL R 295 REMARK 465 HIS R 296 REMARK 465 ARG R 297 REMARK 465 VAL R 298 REMARK 465 GLY R 299 REMARK 465 ASN R 300 REMARK 465 SER R 301 REMARK 465 LYS R 302 REMARK 465 GLU R 303 REMARK 465 HIS R 304 REMARK 465 LEU R 305 REMARK 465 PRO R 306 REMARK 465 LEU R 307 REMARK 465 PRO R 308 REMARK 465 SER R 309 REMARK 465 GLU R 310 REMARK 465 ALA R 311 REMARK 465 GLY R 312 REMARK 465 PRO R 313 REMARK 465 THR R 314 REMARK 465 PRO R 315 REMARK 465 CYS R 316 REMARK 465 ALA R 317 REMARK 465 PRO R 318 REMARK 465 ALA R 319 REMARK 465 SER R 320 REMARK 465 PHE R 321 REMARK 465 GLU R 322 REMARK 465 ARG R 323 REMARK 465 LYS R 324 REMARK 465 LYS R 416 REMARK 465 CYS R 417 REMARK 465 LYS R 418 REMARK 465 PHE R 419 REMARK 465 CYS R 420 REMARK 465 ARG R 421 REMARK 465 GLN R 422 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 SER E 135 CB OG 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 OH TYR R 215 O HOH R 601 1.74 REMARK 500 O PHE R 403 O2 J40 R 504 2.08 REMARK 500 OH TYR R 400 O HOH R 601 2.09 REMARK 500 OE1 GLU A 318 NZ LYS A 345 2.17 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 SER A 206 -177.01 -66.07 REMARK 500 ALA A 235 -131.03 52.15 REMARK 500 GLU B 15 52.37 -91.60 REMARK 500 ASN B 124 33.21 -97.65 REMARK 500 ASP B 168 5.11 -68.78 REMARK 500 VAL E 47 -62.56 -106.79 REMARK 500 MET E 192 -8.27 73.62 REMARK 500 PRO E 236 74.28 -62.91 REMARK 500 LYS G 19 -9.88 -54.96 REMARK 500 TRP R 175 -158.34 59.64 REMARK 500 ARG R 176 60.23 60.66 REMARK 500 MET R 377 70.78 53.86 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-62593 RELATED DB: EMDB REMARK 900 A CRYO_EM STRUCTURE OF 5_HT1A COMPLEX WITH 5-MEO-DMT DBREF 9KVG A 1 354 UNP P63096 GNAI1_HUMAN 1 354 DBREF 9KVG B 7 345 UNP P62873 GBB1_HUMAN 2 340 DBREF 9KVG E 1 247 PDB 9KVG 9KVG 1 247 DBREF 9KVG G 0 70 UNP P59768 GBG2_HUMAN 1 71 DBREF 9KVG R 25 422 UNP P08908 5HT1A_HUMAN 25 422 SEQADV 9KVG ASN A 47 UNP P63096 SER 47 CONFLICT SEQADV 9KVG ALA A 203 UNP P63096 GLY 203 CONFLICT SEQADV 9KVG ASP A 236 UNP P63096 GLU 236 CONFLICT SEQADV 9KVG GLU A 237 UNP P63096 ASP 237 CONFLICT SEQADV 9KVG ALA A 238 UNP P63096 GLU 238 CONFLICT SEQADV 9KVG ALA A 245 UNP P63096 GLU 245 CONFLICT SEQADV 9KVG SER A 326 UNP P63096 ALA 326 CONFLICT SEQADV 9KVG GLY B 2 UNP P62873 EXPRESSION TAG SEQADV 9KVG SER B 3 UNP P62873 EXPRESSION TAG SEQADV 9KVG LEU B 4 UNP P62873 EXPRESSION TAG SEQADV 9KVG LEU B 5 UNP P62873 EXPRESSION TAG SEQADV 9KVG GLN B 6 UNP P62873 EXPRESSION TAG SEQADV 9KVG TRP R 125 UNP P08908 LEU 125 CONFLICT 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 ASN 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 ALA 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 ASP GLU ALA GLU MET ASN ARG MET HIS ALA 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 SER 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 344 GLY SER LEU LEU GLN SER GLU LEU ASP GLN LEU ARG GLN SEQRES 2 B 344 GLU ALA GLU GLN LEU LYS ASN GLN ILE ARG ASP ALA ARG SEQRES 3 B 344 LYS ALA CYS ALA ASP ALA THR LEU SER GLN ILE THR ASN SEQRES 4 B 344 ASN ILE ASP PRO VAL GLY ARG ILE GLN MET ARG THR ARG SEQRES 5 B 344 ARG THR LEU ARG GLY HIS LEU ALA LYS ILE TYR ALA MET SEQRES 6 B 344 HIS TRP GLY THR ASP SER ARG LEU LEU VAL SER ALA SER SEQRES 7 B 344 GLN ASP GLY LYS LEU ILE ILE TRP ASP SER TYR THR THR SEQRES 8 B 344 ASN LYS VAL HIS ALA ILE PRO LEU ARG SER SER TRP VAL SEQRES 9 B 344 MET THR CYS ALA TYR ALA PRO SER GLY ASN TYR VAL ALA SEQRES 10 B 344 CYS GLY GLY LEU ASP ASN ILE CYS SER ILE TYR ASN LEU SEQRES 11 B 344 LYS THR ARG GLU GLY ASN VAL ARG VAL SER ARG GLU LEU SEQRES 12 B 344 ALA GLY HIS THR GLY TYR LEU SER CYS CYS ARG PHE LEU SEQRES 13 B 344 ASP ASP ASN GLN ILE VAL THR SER SER GLY ASP THR THR SEQRES 14 B 344 CYS ALA LEU TRP ASP ILE GLU THR GLY GLN GLN THR THR SEQRES 15 B 344 THR PHE THR GLY HIS THR GLY ASP VAL MET SER LEU SER SEQRES 16 B 344 LEU ALA PRO ASP THR ARG LEU PHE VAL SER GLY ALA CYS SEQRES 17 B 344 ASP ALA SER ALA LYS LEU TRP ASP VAL ARG GLU GLY MET SEQRES 18 B 344 CYS ARG GLN THR PHE THR GLY HIS GLU SER ASP ILE ASN SEQRES 19 B 344 ALA ILE CYS PHE PHE PRO ASN GLY ASN ALA PHE ALA THR SEQRES 20 B 344 GLY SER ASP ASP ALA THR CYS ARG LEU PHE ASP LEU ARG SEQRES 21 B 344 ALA ASP GLN GLU LEU MET THR TYR SER HIS ASP ASN ILE SEQRES 22 B 344 ILE CYS GLY ILE THR SER VAL SER PHE SER LYS SER GLY SEQRES 23 B 344 ARG LEU LEU LEU ALA GLY TYR ASP ASP PHE ASN CYS ASN SEQRES 24 B 344 VAL TRP ASP ALA LEU LYS ALA ASP ARG ALA GLY VAL LEU SEQRES 25 B 344 ALA GLY HIS ASP ASN ARG VAL SER CYS LEU GLY VAL THR SEQRES 26 B 344 ASP ASP GLY MET ALA VAL ALA THR GLY SER TRP ASP SER SEQRES 27 B 344 PHE LEU LYS ILE TRP ASN SEQRES 1 E 247 VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN PRO SEQRES 2 E 247 GLY GLY SER ARG LYS LEU SER CYS SER ALA SER GLY PHE SEQRES 3 E 247 ALA PHE SER SER PHE GLY MET HIS TRP VAL ARG GLN ALA SEQRES 4 E 247 PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SER SEQRES 5 E 247 GLY SER GLY THR ILE TYR TYR ALA ASP THR VAL LYS GLY SEQRES 6 E 247 ARG PHE THR ILE SER ARG ASP ASP PRO LYS ASN THR LEU SEQRES 7 E 247 PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR ALA SEQRES 8 E 247 MET TYR TYR CYS VAL ARG SER ILE TYR TYR TYR GLY SER SEQRES 9 E 247 SER PRO PHE ASP PHE TRP GLY GLN GLY THR THR LEU THR SEQRES 10 E 247 VAL SER ALA GLY GLY GLY GLY SER GLY GLY GLY GLY SER SEQRES 11 E 247 GLY GLY GLY GLY SER ALA ASP ILE VAL MET THR GLN ALA SEQRES 12 E 247 THR SER SER VAL PRO VAL THR PRO GLY GLU SER VAL SER SEQRES 13 E 247 ILE SER CYS ARG SER SER LYS SER LEU LEU HIS SER ASN SEQRES 14 E 247 GLY ASN THR TYR LEU TYR TRP PHE LEU GLN ARG PRO GLY SEQRES 15 E 247 GLN SER PRO GLN LEU LEU ILE TYR ARG MET SER ASN LEU SEQRES 16 E 247 ALA SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SER SEQRES 17 E 247 GLY THR ALA PHE THR LEU THR ILE SER ARG LEU GLU ALA SEQRES 18 E 247 GLU ASP VAL GLY VAL TYR TYR CYS MET GLN HIS LEU GLU SEQRES 19 E 247 TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU LEU SEQRES 1 G 71 MET ALA SER ASN ASN THR ALA SER ILE ALA GLN ALA ARG SEQRES 2 G 71 LYS LEU VAL GLU GLN LEU LYS MET GLU ALA ASN ILE ASP SEQRES 3 G 71 ARG ILE LYS VAL SER LYS ALA ALA ALA ASP LEU MET ALA SEQRES 4 G 71 TYR CYS GLU ALA HIS ALA LYS GLU ASP PRO LEU LEU THR SEQRES 5 G 71 PRO VAL PRO ALA SER GLU ASN PRO PHE ARG GLU LYS LYS SEQRES 6 G 71 PHE PHE CYS ALA ILE LEU SEQRES 1 R 398 THR THR GLY ILE SER ASP VAL THR VAL SER TYR GLN VAL SEQRES 2 R 398 ILE THR SER LEU LEU LEU GLY THR LEU ILE PHE CYS ALA SEQRES 3 R 398 VAL LEU GLY ASN ALA CYS VAL VAL ALA ALA ILE ALA LEU SEQRES 4 R 398 GLU ARG SER LEU GLN ASN VAL ALA ASN TYR LEU ILE GLY SEQRES 5 R 398 SER LEU ALA VAL THR ASP LEU MET VAL SER VAL LEU VAL SEQRES 6 R 398 LEU PRO MET ALA ALA LEU TYR GLN VAL LEU ASN LYS TRP SEQRES 7 R 398 THR LEU GLY GLN VAL THR CYS ASP LEU PHE ILE ALA LEU SEQRES 8 R 398 ASP VAL LEU CYS CYS THR SER SER ILE TRP HIS LEU CYS SEQRES 9 R 398 ALA ILE ALA LEU ASP ARG TYR TRP ALA ILE THR ASP PRO SEQRES 10 R 398 ILE ASP TYR VAL ASN LYS ARG THR PRO ARG ARG ALA ALA SEQRES 11 R 398 ALA LEU ILE SER LEU THR TRP LEU ILE GLY PHE LEU ILE SEQRES 12 R 398 SER ILE PRO PRO MET LEU GLY TRP ARG THR PRO GLU ASP SEQRES 13 R 398 ARG SER ASP PRO ASP ALA CYS THR ILE SER LYS ASP HIS SEQRES 14 R 398 GLY TYR THR ILE TYR SER THR PHE GLY ALA PHE TYR ILE SEQRES 15 R 398 PRO LEU LEU LEU MET LEU VAL LEU TYR GLY ARG ILE PHE SEQRES 16 R 398 ARG ALA ALA ARG PHE ARG ILE ARG LYS THR VAL LYS LYS SEQRES 17 R 398 VAL GLU LYS THR GLY ALA ASP THR ARG HIS GLY ALA SER SEQRES 18 R 398 PRO ALA PRO GLN PRO LYS LYS SER VAL ASN GLY GLU SER SEQRES 19 R 398 GLY SER ARG ASN TRP ARG LEU GLY VAL GLU SER LYS ALA SEQRES 20 R 398 GLY GLY ALA LEU CYS ALA ASN GLY ALA VAL ARG GLN GLY SEQRES 21 R 398 ASP ASP GLY ALA ALA LEU GLU VAL ILE GLU VAL HIS ARG SEQRES 22 R 398 VAL GLY ASN SER LYS GLU HIS LEU PRO LEU PRO SER GLU SEQRES 23 R 398 ALA GLY PRO THR PRO CYS ALA PRO ALA SER PHE GLU ARG SEQRES 24 R 398 LYS ASN GLU ARG ASN ALA GLU ALA LYS ARG LYS MET ALA SEQRES 25 R 398 LEU ALA ARG GLU ARG LYS THR VAL LYS THR LEU GLY ILE SEQRES 26 R 398 ILE MET GLY THR PHE ILE LEU CYS TRP LEU PRO PHE PHE SEQRES 27 R 398 ILE VAL ALA LEU VAL LEU PRO PHE CYS GLU SER SER CYS SEQRES 28 R 398 HIS MET PRO THR LEU LEU GLY ALA ILE ILE ASN TRP LEU SEQRES 29 R 398 GLY TYR SER ASN SER LEU LEU ASN PRO VAL ILE TYR ALA SEQRES 30 R 398 TYR PHE ASN LYS ASP PHE GLN ASN ALA PHE LYS LYS ILE SEQRES 31 R 398 ILE LYS CYS LYS PHE CYS ARG GLN HET YFW R 501 16 HET CHO R 502 32 HET Y01 R 503 35 HET J40 R 504 57 HETNAM YFW 2-(5-METHOXY-1H-INDOL-3-YL)-N,N-DIMETHYLETHAN-1-AMINE HETNAM CHO GLYCOCHENODEOXYCHOLIC ACID HETNAM Y01 CHOLESTEROL HEMISUCCINATE HETNAM J40 [(2R)-1-[OXIDANYL-[(2R,3R,5S,6R)-2,3,5,6- HETNAM 2 J40 TETRAKIS(OXIDANYL)-4-PHOSPHONOOXY-CYCLOHEXYL]OXY- HETNAM 3 J40 PHOSPHORYL]OXY-3-TETRADECANOYLOXY-PROPAN-2-YL] (5E, HETNAM 4 J40 8E)-HEXADECA-5,8,11,14-TETRAENOATE FORMUL 6 YFW C13 H18 N2 O FORMUL 7 CHO C26 H43 N O5 FORMUL 8 Y01 C31 H50 O4 FORMUL 9 J40 C39 H68 O16 P2 FORMUL 10 HOH *6(H2 O) HELIX 1 AA1 SER A 6 ARG A 32 1 27 HELIX 2 AA2 GLY A 45 LYS A 54 1 10 HELIX 3 AA3 GLU A 207 GLU A 216 5 10 HELIX 4 AA4 SER A 228 ASP A 231 5 4 HELIX 5 AA5 ALA A 235 GLU A 239 5 5 HELIX 6 AA6 ASN A 241 ASN A 255 1 15 HELIX 7 AA7 ASN A 256 THR A 260 5 5 HELIX 8 AA8 LYS A 270 LYS A 279 1 10 HELIX 9 AA9 PRO A 282 CYS A 286 5 5 HELIX 10 AB1 THR A 295 LEU A 310 1 16 HELIX 11 AB2 THR A 329 CYS A 351 1 23 HELIX 12 AB3 ALA B 16 CYS B 30 1 15 HELIX 13 AB4 THR B 34 THR B 39 1 6 HELIX 14 AB5 ASN B 40 ILE B 42 5 3 HELIX 15 AB6 SER E 52 GLY E 55 5 4 HELIX 16 AB7 ARG E 86 THR E 90 5 5 HELIX 17 AB8 GLU E 220 VAL E 224 5 5 HELIX 18 AB9 GLN G 10 LYS G 19 1 10 HELIX 19 AC1 LYS G 19 ILE G 24 1 6 HELIX 20 AC2 LYS G 28 HIS G 43 1 16 HELIX 21 AC3 ALA G 44 ASP G 47 5 4 HELIX 22 AC4 PRO G 54 ASN G 58 5 5 HELIX 23 AC5 TYR R 35 GLU R 64 1 30 HELIX 24 AC6 ASN R 69 LEU R 99 1 31 HELIX 25 AC7 GLY R 105 ASP R 140 1 36 HELIX 26 AC8 ASP R 140 ASN R 146 1 7 HELIX 27 AC9 THR R 149 ILE R 169 1 21 HELIX 28 AD1 ILE R 169 GLY R 174 1 6 HELIX 29 AD2 ASP R 192 PHE R 204 1 13 HELIX 30 AD3 PHE R 204 LYS R 228 1 25 HELIX 31 AD4 GLU R 326 CYS R 371 1 46 HELIX 32 AD5 PRO R 378 ALA R 401 1 24 HELIX 33 AD6 ASN R 404 ILE R 415 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 ASP A 200 N VAL A 185 SHEET 3 AA1 6 VAL A 34 LEU A 39 1 N VAL A 34 O LYS A 197 SHEET 4 AA1 6 ALA A 220 ALA A 226 1 O ILE A 222 N LEU A 37 SHEET 5 AA1 6 SER A 263 ASN A 269 1 O ILE A 265 N ILE A 221 SHEET 6 AA1 6 ILE A 319 PHE A 323 1 O TYR A 320 N ILE A 264 SHEET 1 AA2 4 THR B 52 LEU B 56 0 SHEET 2 AA2 4 LEU B 341 TRP B 344 -1 O LEU B 341 N LEU B 56 SHEET 3 AA2 4 VAL B 332 SER B 336 -1 N VAL B 332 O TRP B 344 SHEET 4 AA2 4 VAL B 320 VAL B 325 -1 N CYS B 322 O GLY B 335 SHEET 1 AA3 4 ILE B 63 TRP B 68 0 SHEET 2 AA3 4 LEU B 74 SER B 79 -1 O VAL B 76 N HIS B 67 SHEET 3 AA3 4 LYS B 83 ASP B 88 -1 O TRP B 87 N LEU B 75 SHEET 4 AA3 4 ASN B 93 PRO B 99 -1 O ILE B 98 N LEU B 84 SHEET 1 AA4 4 VAL B 105 TYR B 110 0 SHEET 2 AA4 4 TYR B 116 GLY B 121 -1 O GLY B 120 N MET B 106 SHEET 3 AA4 4 CYS B 126 ASN B 130 -1 O TYR B 129 N VAL B 117 SHEET 4 AA4 4 ARG B 139 LEU B 144 -1 O SER B 141 N ILE B 128 SHEET 1 AA5 4 LEU B 151 PHE B 156 0 SHEET 2 AA5 4 GLN B 161 SER B 166 -1 O VAL B 163 N ARG B 155 SHEET 3 AA5 4 CYS B 171 ASP B 175 -1 O ALA B 172 N THR B 164 SHEET 4 AA5 4 GLN B 180 PHE B 185 -1 O THR B 183 N LEU B 173 SHEET 1 AA6 4 VAL B 192 LEU B 197 0 SHEET 2 AA6 4 LEU B 203 ALA B 208 -1 O VAL B 205 N SER B 196 SHEET 3 AA6 4 ALA B 213 ASP B 217 -1 O TRP B 216 N PHE B 204 SHEET 4 AA6 4 CYS B 223 PHE B 227 -1 O PHE B 227 N ALA B 213 SHEET 1 AA7 4 ILE B 234 PHE B 239 0 SHEET 2 AA7 4 ALA B 245 SER B 250 -1 O GLY B 249 N ASN B 235 SHEET 3 AA7 4 CYS B 255 ASP B 259 -1 O PHE B 258 N PHE B 246 SHEET 4 AA7 4 GLU B 265 TYR B 269 -1 O TYR B 269 N CYS B 255 SHEET 1 AA8 4 ILE B 278 PHE B 283 0 SHEET 2 AA8 4 LEU B 289 TYR B 294 -1 O GLY B 293 N SER B 280 SHEET 3 AA8 4 CYS B 299 ASP B 303 -1 O TRP B 302 N LEU B 290 SHEET 4 AA8 4 ARG B 309 LEU B 313 -1 O LEU B 313 N CYS B 299 SHEET 1 AA9 4 GLN E 2 SER E 6 0 SHEET 2 AA9 4 ARG E 17 SER E 24 -1 O SER E 20 N SER E 6 SHEET 3 AA9 4 THR E 77 MET E 82 -1 O LEU E 78 N CYS E 21 SHEET 4 AA9 4 PHE E 67 ASP E 72 -1 N SER E 70 O PHE E 79 SHEET 1 AB1 6 GLY E 9 VAL E 11 0 SHEET 2 AB1 6 THR E 114 VAL E 118 1 O THR E 117 N VAL E 11 SHEET 3 AB1 6 ALA E 91 SER E 98 -1 N TYR E 93 O THR E 114 SHEET 4 AB1 6 GLY E 32 GLN E 38 -1 N GLY E 32 O SER E 98 SHEET 5 AB1 6 LEU E 44 ILE E 50 -1 O VAL E 47 N TRP E 35 SHEET 6 AB1 6 ILE E 57 TYR E 59 -1 O TYR E 58 N TYR E 49 SHEET 1 AB2 4 MET E 140 GLN E 142 0 SHEET 2 AB2 4 VAL E 155 SER E 161 -1 O ARG E 160 N THR E 141 SHEET 3 AB2 4 ALA E 211 ILE E 216 -1 O LEU E 214 N ILE E 157 SHEET 4 AB2 4 PHE E 203 GLY E 207 -1 N SER E 206 O THR E 213 SHEET 1 AB3 5 SER E 146 PRO E 148 0 SHEET 2 AB3 5 THR E 243 GLU E 246 1 O LYS E 244 N VAL E 147 SHEET 3 AB3 5 GLY E 225 GLN E 231 -1 N GLY E 225 O LEU E 245 SHEET 4 AB3 5 LEU E 174 GLN E 179 -1 N PHE E 177 O TYR E 228 SHEET 5 AB3 5 GLN E 186 ILE E 189 -1 O ILE E 189 N TRP E 176 SSBOND 1 CYS B 126 CYS B 154 1555 1555 2.04 SSBOND 2 CYS R 109 CYS R 187 1555 1555 2.03 SSBOND 3 CYS R 371 CYS R 375 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