HEADER MEMBRANE PROTEIN 19-JUL-24 9ITB TITLE LPA-BOUND LPAR6 IN COMPLEX WITH MINIGQ COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENGINEERED MINIGAQ; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 7 BETA-1; COMPND 8 CHAIN: B; COMPND 9 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: NB35; COMPND 13 CHAIN: N; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 4; COMPND 16 MOLECULE: LYSOPHOSPHATIDIC ACID RECEPTOR 6; COMPND 17 CHAIN: R; COMPND 18 SYNONYM: LPA RECEPTOR 6,LPA-6,OLEOYL-L-ALPHA-LYSOPHOSPHATIDIC ACID COMPND 19 RECEPTOR,P2Y PURINOCEPTOR 5,P2Y5,PURINERGIC RECEPTOR 5,RB INTRON COMPND 20 ENCODED G-PROTEIN COUPLED RECEPTOR; COMPND 21 ENGINEERED: YES; COMPND 22 MOL_ID: 5; COMPND 23 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 24 GAMMA-2; COMPND 25 CHAIN: G; COMPND 26 SYNONYM: G GAMMA-I; 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 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_COMMON: HUMAN; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 GENE: GNB1; SOURCE 12 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 16 ORGANISM_TAXID: 9844; SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 19 MOL_ID: 4; SOURCE 20 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 21 ORGANISM_COMMON: HUMAN; SOURCE 22 ORGANISM_TAXID: 9606; SOURCE 23 GENE: LPAR6, P2RY5; SOURCE 24 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 26 MOL_ID: 5; SOURCE 27 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 28 ORGANISM_COMMON: HUMAN; SOURCE 29 ORGANISM_TAXID: 9606; SOURCE 30 GENE: GNG2; SOURCE 31 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 32 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS GPCR-G-PROTEIN COMPLEX, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR Y.HE,Y.DUAN REVDAT 1 15-JAN-25 9ITB 0 JRNL AUTH Y.HE,Y.DUAN JRNL TITL LPA-BOUND LPAR6 IN COMPLEX WITH MINIGQ JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.89 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) : 2.890 REMARK 3 NUMBER OF PARTICLES : 211505 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 9ITB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 23-JUL-24. REMARK 100 THE DEPOSITION ID IS D_1300049624. 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 : GPCR/G-PROTEIN 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 : 7.00 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 : FEI TECNAI F30 REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2200.00 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 : 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 APPLY THE FOLLOWING TO CHAINS: A, B, N, R, G 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 7 REMARK 465 MET A 8 REMARK 465 GLY A 9 REMARK 465 CYS A 10 REMARK 465 THR A 11 REMARK 465 LEU A 12 REMARK 465 SER A 13 REMARK 465 ALA A 14 REMARK 465 TYR A 79 REMARK 465 HIS A 80 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 VAL A 202 REMARK 465 LYS A 203 REMARK 465 TYR A 263 REMARK 465 MET B -4 REMARK 465 GLY B -3 REMARK 465 SER B -2 REMARK 465 LEU B -1 REMARK 465 LEU B 0 REMARK 465 GLN B 1 REMARK 465 SER B 2 REMARK 465 ARG B 129 REMARK 465 GLU B 130 REMARK 465 GLY B 131 REMARK 465 ASN B 132 REMARK 465 MET N -21 REMARK 465 LYS N -20 REMARK 465 TYR N -19 REMARK 465 LEU N -18 REMARK 465 LEU N -17 REMARK 465 PRO N -16 REMARK 465 THR N -15 REMARK 465 ALA N -14 REMARK 465 ALA N -13 REMARK 465 ALA N -12 REMARK 465 GLY N -11 REMARK 465 LEU N -10 REMARK 465 LEU N -9 REMARK 465 LEU N -8 REMARK 465 LEU N -7 REMARK 465 ALA N -6 REMARK 465 ALA N -5 REMARK 465 GLN N -4 REMARK 465 PRO N -3 REMARK 465 ALA N -2 REMARK 465 MET N -1 REMARK 465 ALA N 0 REMARK 465 ALA N 129 REMARK 465 ALA N 130 REMARK 465 ALA N 131 REMARK 465 LEU N 132 REMARK 465 GLU N 133 REMARK 465 HIS N 134 REMARK 465 HIS N 135 REMARK 465 HIS N 136 REMARK 465 HIS N 137 REMARK 465 HIS N 138 REMARK 465 HIS N 139 REMARK 465 MET R 1 REMARK 465 VAL R 2 REMARK 465 SER R 3 REMARK 465 VAL R 4 REMARK 465 ASN R 5 REMARK 465 SER R 6 REMARK 465 SER R 7 REMARK 465 HIS R 8 REMARK 465 SER R 159 REMARK 465 GLN R 160 REMARK 465 GLY R 161 REMARK 465 ASN R 162 REMARK 465 ASN R 163 REMARK 465 ALA R 164 REMARK 465 SER R 165 REMARK 465 VAL R 215 REMARK 465 THR R 216 REMARK 465 LEU R 217 REMARK 465 SER R 218 REMARK 465 ARG R 219 REMARK 465 SER R 220 REMARK 465 LYS R 221 REMARK 465 ILE R 222 REMARK 465 MET G 1 REMARK 465 ALA G 2 REMARK 465 SER G 3 REMARK 465 ASN G 4 REMARK 465 ASN G 5 REMARK 465 THR G 6 REMARK 465 GLU G 63 REMARK 465 LYS G 64 REMARK 465 LYS G 65 REMARK 465 PHE G 66 REMARK 465 PHE G 67 REMARK 465 CYS G 68 REMARK 465 ALA G 69 REMARK 465 ILE G 70 REMARK 465 LEU G 71 REMARK 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 17 CG CD CE NZ REMARK 470 LYS A 58 CG CD CE NZ REMARK 470 ARG A 61 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 216 CG CD CE NZ REMARK 470 GLU A 299 CG CD OE1 OE2 REMARK 470 LYS A 300 CG CD CE NZ REMARK 470 LYS A 305 CG CD CE NZ REMARK 470 LYS A 307 CG CD CE NZ REMARK 470 ARG A 317 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 322 CG CD OE1 OE2 REMARK 470 ASP A 323 CG OD1 OD2 REMARK 470 SER A 352 OG REMARK 470 ASP A 354 CG OD1 OD2 REMARK 470 ARG A 356 CG CD NE CZ NH1 NH2 REMARK 470 MET A 386 CG SD CE REMARK 470 GLU B 3 CG CD OE1 OE2 REMARK 470 ASP B 5 CG OD1 OD2 REMARK 470 GLN B 6 CG CD OE1 NE2 REMARK 470 ARG B 8 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 12 CG CD OE1 OE2 REMARK 470 ARG B 46 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 96 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 127 CG CD CE NZ REMARK 470 ARG B 134 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 197 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 214 CG CD NE CZ NH1 NH2 REMARK 470 GLU N 89 CG CD OE1 OE2 REMARK 470 ARG N 105 CG CD NE CZ NH1 NH2 REMARK 470 PHE R 10 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASN R 12 CG OD1 ND2 REMARK 470 HIS R 158 CG ND1 CD2 CE1 NE2 REMARK 470 ARG R 166 CG CD NE CZ NH1 NH2 REMARK 470 GLU R 174 CG CD OE1 OE2 REMARK 470 LYS R 178 CG CD CE NZ REMARK 470 THR R 179 OG1 CG2 REMARK 470 ASN R 223 CG OD1 ND2 REMARK 470 LYS R 229 CG CD CE NZ REMARK 470 GLN R 258 CG CD OE1 NE2 REMARK 470 VAL R 261 CG1 CG2 REMARK 470 ARG G 13 CG CD NE CZ NH1 NH2 REMARK 470 LYS G 14 CG CD CE NZ REMARK 470 ASN G 24 CG OD1 ND2 REMARK 470 ASP G 26 CG OD1 OD2 REMARK 470 ARG G 62 CG CD NE CZ NH1 NH2 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 O ASN R 50 OG1 THR R 53 2.15 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 ARG A 231 25.83 -141.28 REMARK 500 TYR A 311 -30.65 -130.28 REMARK 500 SER A 352 -79.64 -82.96 REMARK 500 ASP A 354 -21.81 -146.92 REMARK 500 ARG B 68 -35.54 -130.19 REMARK 500 ASP B 291 -79.88 -69.93 REMARK 500 PHE B 292 0.68 -160.48 REMARK 500 SER B 334 12.04 81.02 REMARK 500 THR N 114 92.11 -69.82 REMARK 500 CYS R 44 89.39 -168.59 REMARK 500 PRO R 83 43.76 -71.45 REMARK 500 ALA R 151 -9.53 -57.47 REMARK 500 GLN R 155 -65.22 -95.06 REMARK 500 PHE R 193 -37.69 -130.59 REMARK 500 GLN R 258 62.34 62.03 REMARK 500 LEU R 277 -6.23 70.20 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-60857 RELATED DB: EMDB REMARK 900 LPA-BOUND LPAR6 IN COMPLEX WITH MINIGQ DBREF 9ITB A 7 394 PDB 9ITB 9ITB 7 394 DBREF 9ITB B 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 9ITB N -21 139 PDB 9ITB 9ITB -21 139 DBREF 9ITB R 1 294 UNP P43657 LPAR6_HUMAN 1 294 DBREF 9ITB G 1 71 UNP P59768 GBG2_HUMAN 1 71 SEQADV 9ITB MET B -4 UNP P62873 INITIATING METHIONINE SEQADV 9ITB GLY B -3 UNP P62873 EXPRESSION TAG SEQADV 9ITB SER B -2 UNP P62873 EXPRESSION TAG SEQADV 9ITB LEU B -1 UNP P62873 EXPRESSION TAG SEQADV 9ITB LEU B 0 UNP P62873 EXPRESSION TAG SEQADV 9ITB GLN B 1 UNP P62873 EXPRESSION TAG SEQADV 9ITB ALA R 43 UNP P43657 ILE 43 CONFLICT SEQADV 9ITB ARG R 166 UNP P43657 GLU 166 CONFLICT SEQRES 1 A 362 MET MET GLY CYS THR LEU SER ALA GLU ASP LYS ALA ALA SEQRES 2 A 362 VAL GLU ARG SER LYS MET ILE GLU LYS GLN LEU GLN LYS SEQRES 3 A 362 ASP LYS GLN VAL TYR ARG ARG THR LEU ARG LEU LEU LEU SEQRES 4 A 362 LEU GLY ALA ASP ASN SER GLY LYS SER THR ILE VAL LYS SEQRES 5 A 362 GLN MET ARG ILE TYR HIS VAL ASN GLY TYR SER GLU GLU SEQRES 6 A 362 GLU CYS LYS GLN TYR LYS ALA VAL VAL TYR SER ASN THR SEQRES 7 A 362 ILE GLN SER ILE ILE ALA ILE ILE ARG ALA MET GLY ARG SEQRES 8 A 362 LEU LYS ILE ASP PHE GLY ASP SER ALA ARG ALA ASP ASP SEQRES 9 A 362 ALA ARG GLN LEU PHE VAL LEU ALA GLY ALA ALA GLU GLU SEQRES 10 A 362 GLY PHE MET THR ALA GLU LEU ALA GLY VAL ILE LYS ARG SEQRES 11 A 362 LEU TRP LYS ASP SER GLY VAL GLN ALA CYS PHE ASN ARG SEQRES 12 A 362 SER ARG GLU TYR GLN LEU ASN ASP SER ALA ALA TYR TYR SEQRES 13 A 362 LEU ASN ASP LEU ASP ARG ILE ALA GLN PRO ASN TYR ILE SEQRES 14 A 362 PRO THR GLN GLN ASP VAL LEU ARG THR ARG VAL LYS THR SEQRES 15 A 362 SER GLY ILE PHE GLU THR LYS PHE GLN VAL ASP LYS VAL SEQRES 16 A 362 ASN PHE HIS MET PHE ASP VAL GLY ALA GLN ARG ASP GLU SEQRES 17 A 362 ARG ARG LYS TRP ILE GLN CYS PHE ASN ASP VAL THR ALA SEQRES 18 A 362 ILE ILE PHE VAL VAL ASP SER SER ASP TYR ASN ARG LEU SEQRES 19 A 362 GLN GLU ALA LEU ASN ASP PHE LYS SER ILE TRP ASN ASN SEQRES 20 A 362 ARG TRP LEU ARG THR ILE SER VAL ILE LEU PHE LEU ASN SEQRES 21 A 362 LYS GLN ASP LEU LEU ALA GLU LYS VAL LEU ALA GLY LYS SEQRES 22 A 362 SER LYS ILE GLU ASP TYR PHE PRO GLU PHE ALA ARG TYR SEQRES 23 A 362 THR THR PRO GLU ASP ALA THR PRO GLU PRO GLY GLU ASP SEQRES 24 A 362 PRO ARG VAL THR ARG ALA LYS TYR PHE ILE ARG LYS GLU SEQRES 25 A 362 PHE VAL ASP ILE SER THR ALA SER GLY ASP GLY ARG HIS SEQRES 26 A 362 ILE CYS TYR PRO HIS PHE THR CYS SER VAL ASP THR GLU SEQRES 27 A 362 ASN ALA ARG ARG ILE PHE ASN ASP CYS LYS ASP ILE ILE SEQRES 28 A 362 LEU GLN MET ASN LEU ARG GLU TYR ASN LEU VAL SEQRES 1 B 345 MET GLY SER LEU LEU 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 N 161 MET LYS TYR LEU LEU PRO THR ALA ALA ALA GLY LEU LEU SEQRES 2 N 161 LEU LEU ALA ALA GLN PRO ALA MET ALA GLN VAL GLN LEU SEQRES 3 N 161 GLN GLU SER GLY GLY GLY LEU VAL GLN PRO GLY GLY SER SEQRES 4 N 161 LEU ARG LEU SER CYS ALA ALA SER GLY PHE THR PHE SER SEQRES 5 N 161 ASN TYR LYS MET ASN TRP VAL ARG GLN ALA PRO GLY LYS SEQRES 6 N 161 GLY LEU GLU TRP VAL SER ASP ILE SER GLN SER GLY ALA SEQRES 7 N 161 SER ILE SER TYR THR GLY SER VAL LYS GLY ARG PHE THR SEQRES 8 N 161 ILE SER ARG ASP ASN ALA LYS ASN THR LEU TYR LEU GLN SEQRES 9 N 161 MET ASN SER LEU LYS PRO GLU ASP THR ALA VAL TYR TYR SEQRES 10 N 161 CYS ALA ARG CYS PRO ALA PRO PHE THR ARG ASP CYS PHE SEQRES 11 N 161 ASP VAL THR SER THR THR TYR ALA TYR ARG GLY GLN GLY SEQRES 12 N 161 THR GLN VAL THR VAL SER SER ALA ALA ALA LEU GLU HIS SEQRES 13 N 161 HIS HIS HIS HIS HIS SEQRES 1 R 294 MET VAL SER VAL ASN SER SER HIS CYS PHE TYR ASN ASP SEQRES 2 R 294 SER PHE LYS TYR THR LEU TYR GLY CYS MET PHE SER MET SEQRES 3 R 294 VAL PHE VAL LEU GLY LEU ILE SER ASN CYS VAL ALA ILE SEQRES 4 R 294 TYR ILE PHE ALA CYS VAL LEU LYS VAL ARG ASN GLU THR SEQRES 5 R 294 THR THR TYR MET ILE ASN LEU ALA MET SER ASP LEU LEU SEQRES 6 R 294 PHE VAL PHE THR LEU PRO PHE ARG ILE PHE TYR PHE THR SEQRES 7 R 294 THR ARG ASN TRP PRO PHE GLY ASP LEU LEU CYS LYS ILE SEQRES 8 R 294 SER VAL MET LEU PHE TYR THR ASN MET TYR GLY SER ILE SEQRES 9 R 294 LEU PHE LEU THR CYS ILE SER VAL ASP ARG PHE LEU ALA SEQRES 10 R 294 ILE VAL TYR PRO PHE LYS SER LYS THR LEU ARG THR LYS SEQRES 11 R 294 ARG ASN ALA LYS ILE VAL CYS THR GLY VAL TRP LEU THR SEQRES 12 R 294 VAL ILE GLY GLY SER ALA PRO ALA VAL PHE VAL GLN SER SEQRES 13 R 294 THR HIS SER GLN GLY ASN ASN ALA SER ARG ALA CYS PHE SEQRES 14 R 294 GLU ASN PHE PRO GLU ALA THR TRP LYS THR TYR LEU SER SEQRES 15 R 294 ARG ILE VAL ILE PHE ILE GLU ILE VAL GLY PHE PHE ILE SEQRES 16 R 294 PRO LEU ILE LEU ASN VAL THR CYS SER SER MET VAL LEU SEQRES 17 R 294 LYS THR LEU THR LYS PRO VAL THR LEU SER ARG SER LYS SEQRES 18 R 294 ILE ASN LYS THR LYS VAL LEU LYS MET ILE PHE VAL HIS SEQRES 19 R 294 LEU ILE ILE PHE CYS PHE CYS PHE VAL PRO TYR ASN ILE SEQRES 20 R 294 ASN LEU ILE LEU TYR SER LEU VAL ARG THR GLN THR PHE SEQRES 21 R 294 VAL ASN CYS SER VAL VAL ALA ALA VAL ARG THR MET TYR SEQRES 22 R 294 PRO ILE THR LEU CYS ILE ALA VAL SER ASN CYS CYS PHE SEQRES 23 R 294 ASP PRO ILE VAL TYR TYR PHE THR 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 HET NKP R 401 29 HET CLR R 402 28 HET CLR R 403 28 HET CLR R 404 28 HET PLM R 405 18 HETNAM NKP (2R)-2-HYDROXY-3-(PHOSPHONOOXY)PROPYL (9E)-OCTADEC-9- HETNAM 2 NKP ENOATE HETNAM CLR CHOLESTEROL HETNAM PLM PALMITIC ACID HETSYN NKP 18:1 LPA; OLEOYL LYSOPHOSPHATIDIC ACID FORMUL 6 NKP C21 H41 O7 P FORMUL 7 CLR 3(C27 H46 O) FORMUL 10 PLM C16 H32 O2 HELIX 1 AA1 GLU A 15 ARG A 38 1 24 HELIX 2 AA2 GLY A 52 LYS A 58 1 7 HELIX 3 AA3 TRP A 234 ASN A 239 5 6 HELIX 4 AA4 ARG A 265 ASN A 278 1 14 HELIX 5 AA5 LYS A 293 GLY A 304 1 12 HELIX 6 AA6 PHE A 312 TYR A 318 5 7 HELIX 7 AA7 ASP A 331 SER A 352 1 22 HELIX 8 AA8 GLU A 370 TYR A 391 1 22 HELIX 9 AA9 LEU B 4 ALA B 24 1 21 HELIX 10 AB1 THR B 29 THR B 34 1 6 HELIX 11 AB2 THR N 28 TYR N 32 5 5 HELIX 12 AB3 LYS N 87 THR N 91 5 5 HELIX 13 AB4 PHE R 15 VAL R 45 1 31 HELIX 14 AB5 ASN R 50 PHE R 68 1 19 HELIX 15 AB6 THR R 69 ARG R 80 1 12 HELIX 16 AB7 GLY R 85 TYR R 120 1 36 HELIX 17 AB8 THR R 129 GLY R 146 1 18 HELIX 18 AB9 SER R 148 PHE R 153 5 6 HELIX 19 AC1 PRO R 173 TYR R 180 1 8 HELIX 20 AC2 TYR R 180 PHE R 193 1 14 HELIX 21 AC3 PHE R 193 THR R 210 1 18 HELIX 22 AC4 VAL R 227 GLN R 258 1 32 HELIX 23 AC5 ASN R 262 THR R 276 1 15 HELIX 24 AC6 LEU R 277 ASN R 283 1 7 HELIX 25 AC7 PHE R 286 TYR R 291 1 6 HELIX 26 AC8 SER G 8 ALA G 23 1 16 HELIX 27 AC9 LYS G 29 HIS G 44 1 16 HELIX 28 AD1 ALA G 45 ASP G 48 5 4 HELIX 29 AD2 PRO G 55 ASN G 59 5 5 SHEET 1 AA1 6 ILE A 207 VAL A 214 0 SHEET 2 AA1 6 VAL A 217 VAL A 224 -1 O PHE A 219 N PHE A 212 SHEET 3 AA1 6 LEU A 41 GLY A 47 1 N LEU A 41 O HIS A 220 SHEET 4 AA1 6 ALA A 243 ASP A 249 1 O ILE A 245 N LEU A 46 SHEET 5 AA1 6 SER A 286 ASN A 292 1 O ASN A 292 N VAL A 248 SHEET 6 AA1 6 CYS A 359 PHE A 363 1 O HIS A 362 N LEU A 291 SHEET 1 AA2 4 ARG B 46 LEU B 51 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 ILE B 80 N SER B 72 SHEET 4 AA3 4 LYS B 89 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 ILE B 120 ASN B 125 -1 O TYR B 124 N VAL B 112 SHEET 4 AA4 4 VAL B 135 ALA B 140 -1 O ARG B 137 N ILE B 123 SHEET 1 AA5 4 LEU B 146 ASP B 153 0 SHEET 2 AA5 4 GLN B 156 SER B 161 -1 O SER B 160 N SER B 147 SHEET 3 AA5 4 CYS B 166 ASP B 170 -1 O TRP B 169 N ILE B 157 SHEET 4 AA5 4 GLN B 175 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 LEU B 198 ALA B 203 -1 O GLY B 202 N MET B 188 SHEET 3 AA6 4 ALA B 208 ASP B 212 -1 O TRP B 211 N PHE B 199 SHEET 4 AA6 4 CYS B 218 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 GLY B 244 N ASN B 230 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 LEU B 261 N LEU B 252 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 THR B 274 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 GLY B 306 N VAL B 296 SHEET 1 AA9 4 GLN N 3 SER N 7 0 SHEET 2 AA9 4 SER N 17 SER N 25 -1 O SER N 25 N GLN N 3 SHEET 3 AA9 4 THR N 78 ASN N 84 -1 O MET N 83 N LEU N 18 SHEET 4 AA9 4 PHE N 68 ASP N 73 -1 N THR N 69 O GLN N 82 SHEET 1 AB1 6 GLY N 10 VAL N 12 0 SHEET 2 AB1 6 THR N 122 VAL N 126 1 O THR N 125 N GLY N 10 SHEET 3 AB1 6 ALA N 92 ARG N 98 -1 N TYR N 94 O THR N 122 SHEET 4 AB1 6 MET N 34 GLN N 39 -1 N VAL N 37 O TYR N 95 SHEET 5 AB1 6 LEU N 45 ILE N 51 -1 O GLU N 46 N ARG N 38 SHEET 6 AB1 6 ILE N 58 TYR N 60 -1 O SER N 59 N ASP N 50 SSBOND 1 CYS R 9 CYS R 263 1555 1555 2.03 SSBOND 2 CYS R 89 CYS R 168 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