HEADER MEMBRANE PROTEIN 27-AUG-24 9JBH TITLE CRYO-EM STRUCTURE OF THE HUMAN LYCHOS PLD HOMODIMER COMPND MOL_ID: 1; COMPND 2 MOLECULE: LYSOSOMAL CHOLESTEROL SIGNALING PROTEIN; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: LYCHOS,G-PROTEIN COUPLED RECEPTOR PGR22; COMPND 5 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: GPR155, PGR22; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS PERMEASE-LIKE DOMAIN, GPCR-LIKE DOMAIN, CHOLESTEROL, MTORC1, MEMBRANE KEYWDS 2 PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR S.YU,L.LIANG REVDAT 1 16-JUL-25 9JBH 0 JRNL AUTH S.YU,L.LIANG JRNL TITL STRUCTURAL INSIGHTS INTO CHOLESTEROL SENSING BY THE JRNL TITL 2 LYCHOS-MTORC1 PATHWAY JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.73 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) : 2.730 REMARK 3 NUMBER OF PARTICLES : 128416 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 9JBH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-AUG-24. REMARK 100 THE DEPOSITION ID IS D_1300050113. 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 : HOMODIMER OF THE HUMAN GPR155 REMARK 245 PLD REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 2.60 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 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 TITAN KRIOS REMARK 245 DETECTOR TYPE : FEI FALCON IV (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1600.00 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) : 5162.00 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 ASN A 2 REMARK 465 SER A 3 REMARK 465 ASN A 4 REMARK 465 LEU A 5 REMARK 465 PRO A 6 REMARK 465 ALA A 7 REMARK 465 GLU A 8 REMARK 465 ASN A 9 REMARK 465 LEU A 10 REMARK 465 THR A 11 REMARK 465 ILE A 12 REMARK 465 ALA A 13 REMARK 465 VAL A 14 REMARK 465 ASN A 15 REMARK 465 MET A 16 REMARK 465 THR A 17 REMARK 465 LYS A 18 REMARK 465 THR A 19 REMARK 465 LEU A 20 REMARK 465 PRO A 21 REMARK 465 THR A 22 REMARK 465 ALA A 23 REMARK 465 VAL A 24 REMARK 465 THR A 25 REMARK 465 HIS A 26 REMARK 465 GLY A 27 REMARK 465 PHE A 28 REMARK 465 ASN A 29 REMARK 465 SER A 30 REMARK 465 THR A 31 REMARK 465 ASN A 32 REMARK 465 ASP A 33 REMARK 465 PRO A 34 REMARK 465 THR A 369 REMARK 465 MET A 370 REMARK 465 SER A 371 REMARK 465 ARG A 372 REMARK 465 GLU A 373 REMARK 465 ASN A 374 REMARK 465 LEU A 375 REMARK 465 TYR A 376 REMARK 465 PHE A 377 REMARK 465 GLN A 378 REMARK 465 MET B 1 REMARK 465 ASN B 2 REMARK 465 SER B 3 REMARK 465 ASN B 4 REMARK 465 LEU B 5 REMARK 465 PRO B 6 REMARK 465 ALA B 7 REMARK 465 GLU B 8 REMARK 465 ASN B 9 REMARK 465 LEU B 10 REMARK 465 THR B 11 REMARK 465 ILE B 12 REMARK 465 ALA B 13 REMARK 465 VAL B 14 REMARK 465 ASN B 15 REMARK 465 MET B 16 REMARK 465 THR B 17 REMARK 465 LYS B 18 REMARK 465 THR B 19 REMARK 465 LEU B 20 REMARK 465 PRO B 21 REMARK 465 THR B 22 REMARK 465 ALA B 23 REMARK 465 VAL B 24 REMARK 465 THR B 25 REMARK 465 HIS B 26 REMARK 465 GLY B 27 REMARK 465 PHE B 28 REMARK 465 ASN B 29 REMARK 465 SER B 30 REMARK 465 THR B 31 REMARK 465 ASN B 32 REMARK 465 ASP B 33 REMARK 465 PRO B 34 REMARK 465 THR B 369 REMARK 465 MET B 370 REMARK 465 SER B 371 REMARK 465 ARG B 372 REMARK 465 GLU B 373 REMARK 465 ASN B 374 REMARK 465 LEU B 375 REMARK 465 TYR B 376 REMARK 465 PHE B 377 REMARK 465 GLN B 378 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 ASN B 202 60.84 37.74 REMARK 500 ASP B 302 119.52 -160.07 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9JBE RELATED DB: PDB REMARK 900 RELATED ID: EMD-61314 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF THE HUMAN LYCHOS PLD HOMODIMER DBREF 9JBH A 1 370 UNP Q7Z3F1 LYCHS_HUMAN 1 370 DBREF 9JBH B 1 370 UNP Q7Z3F1 LYCHS_HUMAN 1 370 SEQADV 9JBH SER A 371 UNP Q7Z3F1 EXPRESSION TAG SEQADV 9JBH ARG A 372 UNP Q7Z3F1 EXPRESSION TAG SEQADV 9JBH GLU A 373 UNP Q7Z3F1 EXPRESSION TAG SEQADV 9JBH ASN A 374 UNP Q7Z3F1 EXPRESSION TAG SEQADV 9JBH LEU A 375 UNP Q7Z3F1 EXPRESSION TAG SEQADV 9JBH TYR A 376 UNP Q7Z3F1 EXPRESSION TAG SEQADV 9JBH PHE A 377 UNP Q7Z3F1 EXPRESSION TAG SEQADV 9JBH GLN A 378 UNP Q7Z3F1 EXPRESSION TAG SEQADV 9JBH SER B 371 UNP Q7Z3F1 EXPRESSION TAG SEQADV 9JBH ARG B 372 UNP Q7Z3F1 EXPRESSION TAG SEQADV 9JBH GLU B 373 UNP Q7Z3F1 EXPRESSION TAG SEQADV 9JBH ASN B 374 UNP Q7Z3F1 EXPRESSION TAG SEQADV 9JBH LEU B 375 UNP Q7Z3F1 EXPRESSION TAG SEQADV 9JBH TYR B 376 UNP Q7Z3F1 EXPRESSION TAG SEQADV 9JBH PHE B 377 UNP Q7Z3F1 EXPRESSION TAG SEQADV 9JBH GLN B 378 UNP Q7Z3F1 EXPRESSION TAG SEQRES 1 A 378 MET ASN SER ASN LEU PRO ALA GLU ASN LEU THR ILE ALA SEQRES 2 A 378 VAL ASN MET THR LYS THR LEU PRO THR ALA VAL THR HIS SEQRES 3 A 378 GLY PHE ASN SER THR ASN ASP PRO PRO SER MET SER ILE SEQRES 4 A 378 THR ARG LEU PHE PRO ALA LEU LEU GLU CYS PHE GLY ILE SEQRES 5 A 378 VAL LEU CYS GLY TYR ILE ALA GLY ARG ALA ASN VAL ILE SEQRES 6 A 378 THR SER THR GLN ALA LYS GLY LEU GLY ASN PHE VAL SER SEQRES 7 A 378 ARG PHE ALA LEU PRO ALA LEU LEU PHE LYS ASN MET VAL SEQRES 8 A 378 VAL LEU ASN PHE SER ASN VAL ASP TRP SER PHE LEU TYR SEQRES 9 A 378 SER ILE LEU ILE ALA LYS ALA SER VAL PHE PHE ILE VAL SEQRES 10 A 378 CYS VAL LEU THR LEU LEU VAL ALA SER PRO ASP SER ARG SEQRES 11 A 378 PHE SER LYS ALA GLY LEU PHE PRO ILE PHE ALA THR GLN SEQRES 12 A 378 SER ASN ASP PHE ALA LEU GLY TYR PRO ILE VAL GLU ALA SEQRES 13 A 378 LEU TYR GLN THR THR TYR PRO GLU TYR LEU GLN TYR ILE SEQRES 14 A 378 TYR LEU VAL ALA PRO ILE SER LEU MET MET LEU ASN PRO SEQRES 15 A 378 ILE GLY PHE ILE PHE CYS GLU ILE GLN LYS TRP LYS ASP SEQRES 16 A 378 THR GLN ASN ALA SER GLN ASN LYS ILE LYS ILE VAL GLY SEQRES 17 A 378 LEU GLY LEU LEU ARG VAL LEU GLN ASN PRO ILE VAL PHE SEQRES 18 A 378 MET VAL PHE ILE GLY ILE ALA PHE ASN PHE ILE LEU ASP SEQRES 19 A 378 ARG LYS VAL PRO VAL TYR VAL GLU ASN PHE LEU ASP GLY SEQRES 20 A 378 LEU GLY ASN SER PHE SER GLY SER ALA LEU PHE TYR LEU SEQRES 21 A 378 GLY LEU THR MET VAL GLY LYS ILE LYS ARG LEU LYS LYS SEQRES 22 A 378 SER ALA PHE VAL VAL LEU ILE LEU LEU ILE THR ALA LYS SEQRES 23 A 378 LEU LEU VAL LEU PRO LEU LEU CYS ARG GLU MET VAL GLU SEQRES 24 A 378 LEU LEU ASP LYS GLY ASP SER VAL VAL ASN HIS THR SER SEQRES 25 A 378 LEU SER ASN TYR ALA PHE LEU TYR GLY VAL PHE PRO VAL SEQRES 26 A 378 ALA PRO GLY VAL ALA ILE PHE ALA THR GLN PHE ASN MET SEQRES 27 A 378 GLU VAL GLU ILE ILE THR SER GLY MET VAL ILE SER THR SEQRES 28 A 378 PHE VAL SER ALA PRO ILE MET TYR VAL SER ALA TRP LEU SEQRES 29 A 378 LEU THR PHE PRO THR MET SER ARG GLU ASN LEU TYR PHE SEQRES 30 A 378 GLN SEQRES 1 B 378 MET ASN SER ASN LEU PRO ALA GLU ASN LEU THR ILE ALA SEQRES 2 B 378 VAL ASN MET THR LYS THR LEU PRO THR ALA VAL THR HIS SEQRES 3 B 378 GLY PHE ASN SER THR ASN ASP PRO PRO SER MET SER ILE SEQRES 4 B 378 THR ARG LEU PHE PRO ALA LEU LEU GLU CYS PHE GLY ILE SEQRES 5 B 378 VAL LEU CYS GLY TYR ILE ALA GLY ARG ALA ASN VAL ILE SEQRES 6 B 378 THR SER THR GLN ALA LYS GLY LEU GLY ASN PHE VAL SER SEQRES 7 B 378 ARG PHE ALA LEU PRO ALA LEU LEU PHE LYS ASN MET VAL SEQRES 8 B 378 VAL LEU ASN PHE SER ASN VAL ASP TRP SER PHE LEU TYR SEQRES 9 B 378 SER ILE LEU ILE ALA LYS ALA SER VAL PHE PHE ILE VAL SEQRES 10 B 378 CYS VAL LEU THR LEU LEU VAL ALA SER PRO ASP SER ARG SEQRES 11 B 378 PHE SER LYS ALA GLY LEU PHE PRO ILE PHE ALA THR GLN SEQRES 12 B 378 SER ASN ASP PHE ALA LEU GLY TYR PRO ILE VAL GLU ALA SEQRES 13 B 378 LEU TYR GLN THR THR TYR PRO GLU TYR LEU GLN TYR ILE SEQRES 14 B 378 TYR LEU VAL ALA PRO ILE SER LEU MET MET LEU ASN PRO SEQRES 15 B 378 ILE GLY PHE ILE PHE CYS GLU ILE GLN LYS TRP LYS ASP SEQRES 16 B 378 THR GLN ASN ALA SER GLN ASN LYS ILE LYS ILE VAL GLY SEQRES 17 B 378 LEU GLY LEU LEU ARG VAL LEU GLN ASN PRO ILE VAL PHE SEQRES 18 B 378 MET VAL PHE ILE GLY ILE ALA PHE ASN PHE ILE LEU ASP SEQRES 19 B 378 ARG LYS VAL PRO VAL TYR VAL GLU ASN PHE LEU ASP GLY SEQRES 20 B 378 LEU GLY ASN SER PHE SER GLY SER ALA LEU PHE TYR LEU SEQRES 21 B 378 GLY LEU THR MET VAL GLY LYS ILE LYS ARG LEU LYS LYS SEQRES 22 B 378 SER ALA PHE VAL VAL LEU ILE LEU LEU ILE THR ALA LYS SEQRES 23 B 378 LEU LEU VAL LEU PRO LEU LEU CYS ARG GLU MET VAL GLU SEQRES 24 B 378 LEU LEU ASP LYS GLY ASP SER VAL VAL ASN HIS THR SER SEQRES 25 B 378 LEU SER ASN TYR ALA PHE LEU TYR GLY VAL PHE PRO VAL SEQRES 26 B 378 ALA PRO GLY VAL ALA ILE PHE ALA THR GLN PHE ASN MET SEQRES 27 B 378 GLU VAL GLU ILE ILE THR SER GLY MET VAL ILE SER THR SEQRES 28 B 378 PHE VAL SER ALA PRO ILE MET TYR VAL SER ALA TRP LEU SEQRES 29 B 378 LEU THR PHE PRO THR MET SER ARG GLU ASN LEU TYR PHE SEQRES 30 B 378 GLN HET 3PE A 401 51 HET CDL A 402 100 HET 3PE A 403 51 HET 3PE A 404 51 HET 3PE B 401 51 HET CDL B 402 100 HET 3PE B 403 51 HET 3PE B 404 51 HETNAM 3PE 1,2-DISTEAROYL-SN-GLYCEROPHOSPHOETHANOLAMINE HETNAM CDL CARDIOLIPIN HETSYN 3PE 3-SN-PHOSPHATIDYLETHANOLAMINE; 1,2-DIACYL-SN-GLYCERO-3- HETSYN 2 3PE PHOSPHOETHANOLAMINE HETSYN CDL DIPHOSPHATIDYL GLYCEROL; BIS-(1,2-DIACYL-SN-GLYCERO-3- HETSYN 2 CDL PHOSPHO)-1',3'-SN-GLYCEROL FORMUL 3 3PE 6(C41 H82 N O8 P) FORMUL 4 CDL 2(C81 H156 O17 P2 2-) HELIX 1 AA1 SER A 38 ALA A 62 1 25 HELIX 2 AA2 THR A 66 PHE A 80 1 15 HELIX 3 AA3 PHE A 80 LEU A 93 1 14 HELIX 4 AA4 ASP A 99 ALA A 125 1 27 HELIX 5 AA5 ARG A 130 ALA A 141 1 12 HELIX 6 AA6 LEU A 149 TYR A 158 1 10 HELIX 7 AA7 TYR A 162 GLN A 167 5 6 HELIX 8 AA8 TYR A 168 THR A 196 1 29 HELIX 9 AA9 ASN A 202 ASN A 217 1 16 HELIX 10 AB1 ASN A 217 LEU A 233 1 17 HELIX 11 AB2 PRO A 238 ASN A 250 1 13 HELIX 12 AB3 SER A 251 MET A 264 1 14 HELIX 13 AB4 LYS A 272 LEU A 288 1 17 HELIX 14 AB5 LEU A 288 ASP A 302 1 15 HELIX 15 AB6 SER A 306 TYR A 320 1 15 HELIX 16 AB7 ALA A 326 ASN A 337 1 12 HELIX 17 AB8 GLU A 341 PHE A 367 1 27 HELIX 18 AB9 ARG B 41 ALA B 62 1 22 HELIX 19 AC1 THR B 66 PHE B 80 1 15 HELIX 20 AC2 PHE B 80 LEU B 93 1 14 HELIX 21 AC3 ASP B 99 ALA B 125 1 27 HELIX 22 AC4 SER B 126 ASP B 128 5 3 HELIX 23 AC5 SER B 129 ALA B 141 1 13 HELIX 24 AC6 LEU B 149 TYR B 158 1 10 HELIX 25 AC7 TYR B 162 GLN B 167 5 6 HELIX 26 AC8 TYR B 168 ASP B 195 1 28 HELIX 27 AC9 ASN B 202 ASN B 217 1 16 HELIX 28 AD1 ASN B 217 LEU B 233 1 17 HELIX 29 AD2 PRO B 238 GLY B 249 1 12 HELIX 30 AD3 SER B 251 MET B 264 1 14 HELIX 31 AD4 LYS B 272 LEU B 288 1 17 HELIX 32 AD5 LEU B 288 LEU B 301 1 14 HELIX 33 AD6 SER B 306 TYR B 320 1 15 HELIX 34 AD7 ALA B 326 ASN B 337 1 12 HELIX 35 AD8 GLU B 341 PHE B 367 1 27 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