HEADER MEMBRANE PROTEIN 19-JUL-24 9ITE TITLE LPA-BOUND LPAR6 IN COMPLEX WITH MINIG13 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENGINEERED MINIGA13; 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: SCFV16; COMPND 13 CHAIN: E; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 4; COMPND 16 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 17 GAMMA-2; COMPND 18 CHAIN: G; COMPND 19 SYNONYM: G GAMMA-I; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 5; COMPND 22 MOLECULE: LYSOPHOSPHATIDIC ACID RECEPTOR 6; COMPND 23 CHAIN: R; COMPND 24 SYNONYM: LPA RECEPTOR 6,LPA-6,OLEOYL-L-ALPHA-LYSOPHOSPHATIDIC ACID COMPND 25 RECEPTOR,P2Y PURINOCEPTOR 5,P2Y5,PURINERGIC RECEPTOR 5,RB INTRON COMPND 26 ENCODED G-PROTEIN COUPLED RECEPTOR; 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: HOMO SAPIENS; SOURCE 16 ORGANISM_COMMON: HUMAN; SOURCE 17 ORGANISM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 20 MOL_ID: 4; SOURCE 21 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 22 ORGANISM_COMMON: HUMAN; SOURCE 23 ORGANISM_TAXID: 9606; SOURCE 24 GENE: GNG2; SOURCE 25 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 27 MOL_ID: 5; SOURCE 28 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 29 ORGANISM_COMMON: HUMAN; SOURCE 30 ORGANISM_TAXID: 9606; SOURCE 31 GENE: LPAR6, P2RY5; SOURCE 32 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 33 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS GPCR-G-PROTEIN COMPLEX, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR Y.HE,Y.DUAN REVDAT 1 15-JAN-25 9ITE 0 JRNL AUTH Y.HE,Y.DUAN JRNL TITL LPA-BOUND LPAR6 IN COMPLEX WITH MINIG13 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.06 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.060 REMARK 3 NUMBER OF PARTICLES : 213708 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 9ITE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 24-JUL-24. REMARK 100 THE DEPOSITION ID IS D_1300049625. 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, 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 SER A 3 REMARK 465 THR A 4 REMARK 465 ILE A 56 REMARK 465 HIS A 57 REMARK 465 GLY A 58 REMARK 465 GLY A 59 REMARK 465 SER A 60 REMARK 465 GLY A 61 REMARK 465 GLY A 62 REMARK 465 SER A 63 REMARK 465 GLY A 64 REMARK 465 GLY A 65 REMARK 465 THR A 66 REMARK 465 LYS A 67 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 ALA E 121 REMARK 465 GLY E 122 REMARK 465 GLY E 123 REMARK 465 GLY E 124 REMARK 465 GLY E 125 REMARK 465 SER E 126 REMARK 465 GLY E 127 REMARK 465 GLY E 128 REMARK 465 GLY E 129 REMARK 465 GLY E 130 REMARK 465 SER E 131 REMARK 465 GLY E 132 REMARK 465 GLY E 133 REMARK 465 GLY E 134 REMARK 465 GLY E 135 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 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 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 SER R 159 REMARK 465 GLN R 160 REMARK 465 GLY R 161 REMARK 465 ASN R 162 REMARK 465 ASN R 163 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 ASP A 42 CG OD1 OD2 REMARK 470 LYS A 51 CG CD CE NZ REMARK 470 SER A 91 OG REMARK 470 ARG A 93 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 94 CG CD CE NZ REMARK 470 ASP A 111 CG OD1 OD2 REMARK 470 ARG A 132 CG CD NE CZ NH1 NH2 REMARK 470 GLN A 154 CG CD OE1 NE2 REMARK 470 ILE A 158 CG1 CG2 CD1 REMARK 470 LEU A 163 CG CD1 CD2 REMARK 470 GLU A 164 CG CD OE1 OE2 REMARK 470 HIS A 170 CG ND1 CD2 CE1 NE2 REMARK 470 ARG A 173 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 177 CG CD CE NZ REMARK 470 ARG A 188 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 189 CG OD1 OD2 REMARK 470 GLN A 190 CG CD OE1 NE2 REMARK 470 GLN A 192 CG CD OE1 NE2 REMARK 470 ILE A 203 CG1 CG2 CD1 REMARK 470 ASN A 204 CG OD1 ND2 REMARK 470 GLU A 206 CG CD OE1 OE2 REMARK 470 ARG A 209 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 222 CG OD1 OD2 REMARK 470 LYS A 225 CG CD CE NZ REMARK 470 GLU B 3 CG CD OE1 OE2 REMARK 470 LEU B 4 CG CD1 CD2 REMARK 470 ASP B 5 CG OD1 OD2 REMARK 470 GLN B 6 CG CD OE1 NE2 REMARK 470 LEU B 7 CG CD1 CD2 REMARK 470 GLN B 9 CG CD OE1 NE2 REMARK 470 GLN B 13 CG CD OE1 NE2 REMARK 470 LYS B 15 CG CD CE NZ REMARK 470 ARG B 96 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 129 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 172 CG CD OE1 OE2 REMARK 470 GLN B 175 CG CD OE1 NE2 REMARK 470 ARG B 197 CG CD NE CZ NH1 NH2 REMARK 470 ASP B 267 CG OD1 OD2 REMARK 470 ASN B 268 CG OD1 ND2 REMARK 470 GLU E 42 CG CD OE1 OE2 REMARK 470 LYS E 76 CG CD CE NZ REMARK 470 VAL E 150 CG1 CG2 REMARK 470 THR E 151 OG1 CG2 REMARK 470 GLU E 154 CG CD OE1 OE2 REMARK 470 GLU E 221 CG CD OE1 OE2 REMARK 470 GLU E 223 CG CD OE1 OE2 REMARK 470 ILE G 9 CG1 CG2 CD1 REMARK 470 GLN G 11 CG CD OE1 NE2 REMARK 470 LYS G 14 CG CD CE NZ REMARK 470 LYS G 20 CG CD CE NZ REMARK 470 LYS G 46 CG CD CE NZ REMARK 470 GLU G 58 CG CD OE1 OE2 REMARK 470 HIS R 8 CG ND1 CD2 CE1 NE2 REMARK 470 PHE R 10 CG CD1 CD2 CE1 CE2 CZ REMARK 470 MET R 26 CG SD CE REMARK 470 LYS R 47 CG CD CE NZ REMARK 470 LEU R 88 CG CD1 CD2 REMARK 470 MET R 94 CG SD CE REMARK 470 HIS R 158 CG ND1 CD2 CE1 NE2 REMARK 470 ARG R 166 CG CD NE CZ NH1 NH2 REMARK 470 TYR R 180 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLN R 258 CG CD OE1 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 ILE A 76 -164.54 -115.42 REMARK 500 ARG A 93 -70.16 -63.95 REMARK 500 LYS A 94 -1.67 -148.76 REMARK 500 ARG A 95 -72.46 -57.61 REMARK 500 TRP A 96 31.68 -148.51 REMARK 500 PHE A 134 35.77 -97.27 REMARK 500 ASP B 205 17.64 -140.91 REMARK 500 ALA B 248 36.45 71.20 REMARK 500 MET E 193 -12.95 74.10 REMARK 500 ASP E 224 24.97 -141.17 REMARK 500 PHE G 61 30.56 -98.34 REMARK 500 ALA R 43 -63.24 -94.60 REMARK 500 CYS R 44 41.20 -140.44 REMARK 500 PHE R 68 6.50 -68.97 REMARK 500 SER R 148 49.64 -92.00 REMARK 500 PRO R 214 38.19 -75.39 REMARK 500 SER R 218 40.31 -103.91 REMARK 500 ARG R 219 64.81 64.36 REMARK 500 LEU R 277 -6.78 72.70 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-60859 RELATED DB: EMDB REMARK 900 LPA-BOUND LPAR6 IN COMPLEX WITH MINIG13 DBREF 9ITE A 1 230 PDB 9ITE 9ITE 1 230 DBREF 9ITE B 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 9ITE E 2 248 PDB 9ITE 9ITE 2 248 DBREF 9ITE G 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 9ITE R 1 301 UNP P43657 LPAR6_HUMAN 1 301 SEQADV 9ITE MET B -4 UNP P62873 INITIATING METHIONINE SEQADV 9ITE GLY B -3 UNP P62873 EXPRESSION TAG SEQADV 9ITE SER B -2 UNP P62873 EXPRESSION TAG SEQADV 9ITE LEU B -1 UNP P62873 EXPRESSION TAG SEQADV 9ITE LEU B 0 UNP P62873 EXPRESSION TAG SEQADV 9ITE GLN B 1 UNP P62873 EXPRESSION TAG SEQADV 9ITE ALA R 43 UNP P43657 ILE 43 CONFLICT SEQADV 9ITE ARG R 166 UNP P43657 GLU 166 CONFLICT SEQRES 1 A 230 MET GLY SER THR VAL SER ALA GLU ASP LYS ALA ALA ALA SEQRES 2 A 230 GLU ARG SER LYS GLU ILE ASP LYS CYS LEU SER ARG GLU SEQRES 3 A 230 LYS THR TYR VAL LYS ARG LEU VAL LYS ILE LEU LEU LEU SEQRES 4 A 230 GLY ALA ASP ASN SER GLY LYS SER THR PHE LEU LYS GLN SEQRES 5 A 230 MET ARG ILE ILE HIS GLY GLY SER GLY GLY SER GLY GLY SEQRES 6 A 230 THR LYS GLY ILE HIS GLU TYR ASP PHE GLU ILE LYS ASN SEQRES 7 A 230 VAL PRO PHE LYS MET VAL ASP VAL GLY GLY GLN ARG SER SEQRES 8 A 230 GLU ARG LYS ARG TRP PHE GLU CYS PHE ASP SER VAL THR SEQRES 9 A 230 SER ILE LEU PHE LEU VAL ASP SER SER ASP PHE ASN ARG SEQRES 10 A 230 LEU THR GLU SER LEU ASN ASP PHE GLU THR ILE VAL ASN SEQRES 11 A 230 ASN ARG VAL PHE SER ASN VAL SER ILE ILE LEU PHE LEU SEQRES 12 A 230 ASN LYS THR ASP LEU LEU GLU GLU LYS VAL GLN ILE VAL SEQRES 13 A 230 SER ILE LYS ASP TYR PHE LEU GLU PHE GLU GLY ASP PRO SEQRES 14 A 230 HIS CYS LEU ARG ASP VAL GLN LYS PHE LEU VAL GLU CYS SEQRES 15 A 230 PHE ARG ASN LYS ARG ARG ASP GLN GLN GLN LYS PRO LEU SEQRES 16 A 230 TYR HIS HIS PHE THR THR ALA ILE ASN THR GLU ASN ALA SEQRES 17 A 230 ARG LEU ILE PHE ARG ASP VAL LYS ASP THR ILE LEU HIS SEQRES 18 A 230 ASP ASN LEU LYS GLN LEU MET LEU GLN 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 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 301 MET VAL SER VAL ASN SER SER HIS CYS PHE TYR ASN ASP SEQRES 2 R 301 SER PHE LYS TYR THR LEU TYR GLY CYS MET PHE SER MET SEQRES 3 R 301 VAL PHE VAL LEU GLY LEU ILE SER ASN CYS VAL ALA ILE SEQRES 4 R 301 TYR ILE PHE ALA CYS VAL LEU LYS VAL ARG ASN GLU THR SEQRES 5 R 301 THR THR TYR MET ILE ASN LEU ALA MET SER ASP LEU LEU SEQRES 6 R 301 PHE VAL PHE THR LEU PRO PHE ARG ILE PHE TYR PHE THR SEQRES 7 R 301 THR ARG ASN TRP PRO PHE GLY ASP LEU LEU CYS LYS ILE SEQRES 8 R 301 SER VAL MET LEU PHE TYR THR ASN MET TYR GLY SER ILE SEQRES 9 R 301 LEU PHE LEU THR CYS ILE SER VAL ASP ARG PHE LEU ALA SEQRES 10 R 301 ILE VAL TYR PRO PHE LYS SER LYS THR LEU ARG THR LYS SEQRES 11 R 301 ARG ASN ALA LYS ILE VAL CYS THR GLY VAL TRP LEU THR SEQRES 12 R 301 VAL ILE GLY GLY SER ALA PRO ALA VAL PHE VAL GLN SER SEQRES 13 R 301 THR HIS SER GLN GLY ASN ASN ALA SER ARG ALA CYS PHE SEQRES 14 R 301 GLU ASN PHE PRO GLU ALA THR TRP LYS THR TYR LEU SER SEQRES 15 R 301 ARG ILE VAL ILE PHE ILE GLU ILE VAL GLY PHE PHE ILE SEQRES 16 R 301 PRO LEU ILE LEU ASN VAL THR CYS SER SER MET VAL LEU SEQRES 17 R 301 LYS THR LEU THR LYS PRO VAL THR LEU SER ARG SER LYS SEQRES 18 R 301 ILE ASN LYS THR LYS VAL LEU LYS MET ILE PHE VAL HIS SEQRES 19 R 301 LEU ILE ILE PHE CYS PHE CYS PHE VAL PRO TYR ASN ILE SEQRES 20 R 301 ASN LEU ILE LEU TYR SER LEU VAL ARG THR GLN THR PHE SEQRES 21 R 301 VAL ASN CYS SER VAL VAL ALA ALA VAL ARG THR MET TYR SEQRES 22 R 301 PRO ILE THR LEU CYS ILE ALA VAL SER ASN CYS CYS PHE SEQRES 23 R 301 ASP PRO ILE VAL TYR TYR PHE THR SER ASP THR ILE GLN SEQRES 24 R 301 ASN SER HET NKP R 401 29 HET CLR R 501 28 HET CLR R 601 28 HET CLR R 701 28 HET PLM R 801 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 SER A 6 LYS A 31 1 26 HELIX 2 AA2 GLY A 45 GLN A 52 1 8 HELIX 3 AA3 ASP A 114 ASN A 116 5 3 HELIX 4 AA4 ARG A 117 VAL A 129 1 13 HELIX 5 AA5 ASN A 131 SER A 135 5 5 HELIX 6 AA6 LYS A 145 VAL A 156 1 12 HELIX 7 AA7 SER A 157 TYR A 161 5 5 HELIX 8 AA8 CYS A 171 ASN A 185 1 15 HELIX 9 AA9 GLU A 206 LEU A 227 1 22 HELIX 10 AB1 LEU B 4 CYS B 25 1 22 HELIX 11 AB2 THR B 29 THR B 34 1 6 HELIX 12 AB3 ALA E 28 PHE E 32 5 5 HELIX 13 AB4 ARG E 87 THR E 91 5 5 HELIX 14 AB5 ALA G 7 ALA G 23 1 17 HELIX 15 AB6 LYS G 29 HIS G 44 1 16 HELIX 16 AB7 ALA G 45 ASP G 48 5 4 HELIX 17 AB8 PRO G 55 ASN G 59 5 5 HELIX 18 AB9 PHE R 15 VAL R 45 1 31 HELIX 19 AC1 ASN R 50 PHE R 68 1 19 HELIX 20 AC2 THR R 69 ARG R 80 1 12 HELIX 21 AC3 GLY R 85 TYR R 120 1 36 HELIX 22 AC4 THR R 129 GLY R 146 1 18 HELIX 23 AC5 ALA R 149 PHE R 153 5 5 HELIX 24 AC6 PRO R 173 LYS R 178 1 6 HELIX 25 AC7 TYR R 180 GLY R 192 1 13 HELIX 26 AC8 PHE R 193 THR R 212 1 20 HELIX 27 AC9 ASN R 223 PHE R 242 1 20 HELIX 28 AD1 PHE R 242 ARG R 256 1 15 HELIX 29 AD2 ASN R 262 TYR R 273 1 12 HELIX 30 AD3 ALA R 280 CYS R 285 5 6 HELIX 31 AD4 PHE R 286 TYR R 291 1 6 HELIX 32 AD5 SER R 295 GLN R 299 5 5 SHEET 1 AA1 6 HIS A 70 GLU A 75 0 SHEET 2 AA1 6 PRO A 80 ASP A 85 -1 O MET A 83 N TYR A 72 SHEET 3 AA1 6 VAL A 34 LEU A 39 1 N LEU A 38 O VAL A 84 SHEET 4 AA1 6 SER A 105 ASP A 111 1 O LEU A 107 N LEU A 37 SHEET 5 AA1 6 SER A 138 ASN A 144 1 O ILE A 140 N PHE A 108 SHEET 6 AA1 6 LEU A 195 PHE A 199 1 O HIS A 198 N LEU A 143 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 TYR B 59 SHEET 3 AA3 4 LYS B 78 ASP B 83 -1 O TRP B 82 N LEU B 70 SHEET 4 AA3 4 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 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 LEU B 139 N CYS B 121 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 SER B 147 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 176 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 GLY B 202 N MET B 188 SHEET 3 AA6 4 SER B 207 ASP B 212 -1 O TRP B 211 N PHE B 199 SHEET 4 AA6 4 CYS B 218 THR B 223 -1 O PHE B 222 N ALA B 208 SHEET 1 AA7 4 ILE B 229 PHE B 234 0 SHEET 2 AA7 4 ALA B 240 SER B 245 -1 O GLY B 244 N ASN B 230 SHEET 3 AA7 4 CYS B 250 ASP B 254 -1 O PHE B 253 N PHE B 241 SHEET 4 AA7 4 GLU B 260 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 E 3 SER E 7 0 SHEET 2 AA9 4 SER E 17 SER E 25 -1 O SER E 23 N VAL E 5 SHEET 3 AA9 4 THR E 78 THR E 84 -1 O MET E 83 N ARG E 18 SHEET 4 AA9 4 PHE E 68 ASP E 73 -1 N ASP E 73 O THR E 78 SHEET 1 AB1 6 GLY E 10 VAL E 12 0 SHEET 2 AB1 6 THR E 115 VAL E 119 1 O THR E 118 N VAL E 12 SHEET 3 AB1 6 ALA E 92 SER E 99 -1 N ALA E 92 O LEU E 117 SHEET 4 AB1 6 GLY E 33 GLN E 39 -1 N GLY E 33 O SER E 99 SHEET 5 AB1 6 LEU E 45 ILE E 51 -1 O GLU E 46 N ARG E 38 SHEET 6 AB1 6 ILE E 58 TYR E 60 -1 O TYR E 59 N TYR E 50 SHEET 1 AB2 4 GLY E 10 VAL E 12 0 SHEET 2 AB2 4 THR E 115 VAL E 119 1 O THR E 118 N VAL E 12 SHEET 3 AB2 4 ALA E 92 SER E 99 -1 N ALA E 92 O LEU E 117 SHEET 4 AB2 4 PHE E 110 TRP E 111 -1 O PHE E 110 N ARG E 98 SHEET 1 AB3 6 SER E 147 PRO E 149 0 SHEET 2 AB3 6 THR E 244 GLU E 247 1 O LYS E 245 N VAL E 148 SHEET 3 AB3 6 GLY E 226 GLN E 232 -1 N TYR E 228 O THR E 244 SHEET 4 AB3 6 LEU E 175 GLN E 180 -1 N GLN E 180 O VAL E 227 SHEET 5 AB3 6 GLN E 187 TYR E 191 -1 O LEU E 189 N TRP E 177 SHEET 6 AB3 6 ASN E 195 LEU E 196 -1 O ASN E 195 N TYR E 191 SHEET 1 AB4 3 VAL E 156 ARG E 161 0 SHEET 2 AB4 3 ALA E 212 ILE E 217 -1 O ILE E 217 N VAL E 156 SHEET 3 AB4 3 PHE E 204 GLY E 208 -1 N SER E 207 O THR E 214 SHEET 1 AB5 2 THR R 157 HIS R 158 0 SHEET 2 AB5 2 ALA R 167 CYS R 168 -1 O ALA R 167 N HIS R 158 SSBOND 1 CYS R 9 CYS R 263 1555 1555 2.03 SSBOND 2 CYS R 89 CYS R 168 1555 1555 2.03 CISPEP 1 TYR E 236 PRO E 237 0 -0.33 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