HEADER MEMBRANE PROTEIN/IMMUNE SYSTEM 05-JUN-24 8ZSV TITLE CRYO-EM STRUCTURE OF THE RO5263397-BOUND MTAAR1-GS 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 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 8 BETA-1; COMPND 9 CHAIN: B; COMPND 10 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 14 GAMMA-2; COMPND 15 CHAIN: G; COMPND 16 SYNONYM: G GAMMA-I; COMPND 17 ENGINEERED: YES; COMPND 18 MOL_ID: 4; COMPND 19 MOLECULE: NB35; COMPND 20 CHAIN: N; COMPND 21 ENGINEERED: YES; COMPND 22 MOL_ID: 5; COMPND 23 MOLECULE: SOLUBLE CYTOCHROME B562,TRACE AMINE-ASSOCIATED RECEPTOR 1; COMPND 24 CHAIN: R; COMPND 25 SYNONYM: CYTOCHROME B-562,TAR-1,TRACE AMINE RECEPTOR 1; COMPND 26 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 GENE: GNG2; SOURCE 19 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 21 MOL_ID: 4; SOURCE 22 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 23 ORGANISM_TAXID: 9844; SOURCE 24 EXPRESSION_SYSTEM: ESCHERICHIA; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 561; SOURCE 26 MOL_ID: 5; SOURCE 27 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI, MUS MUSCULUS; SOURCE 28 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 29 ORGANISM_TAXID: 562, 10090; SOURCE 30 GENE: CYBC, TAAR1, TA1, TAR1, TRAR1; SOURCE 31 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 32 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS GPCR, TAAR1, CRYO-EM, MEMBRANE PROTEIN/IMMUNE SYSTEM, MEMBRANE KEYWDS 2 PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR K.X.JIANG,Y.ZHENG,F.XU JRNL AUTH K.JIANG,Y.ZHENG,L.ZENG,L.WANG,F.LI,J.PU,Y.LU,S.ZHAO,F.XU JRNL TITL THE VERSATILE BINDING LANDSCAPE OF THE TAAR1 POCKET FOR LSD JRNL TITL 2 AND OTHER ANTIPSYCHOTIC DRUG MOLECULES. JRNL REF CELL REP V. 43 14505 2024 JRNL REFN ESSN 2211-1247 JRNL PMID 39002128 JRNL DOI 10.1016/J.CELREP.2024.114505 REMARK 2 REMARK 2 RESOLUTION. 2.96 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) : 2.960 REMARK 3 NUMBER OF PARTICLES : 363775 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 8ZSV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC. REMARK 100 THE DEPOSITION ID IS D_1300048454. 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 : THE LSD-BOUND HTAAR1-GS 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 : 7.40 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 : 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 : DIFFRACTION REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 60.00 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, G, N, 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 7 REMARK 465 GLY A 8 REMARK 465 SER A 9 REMARK 465 THR A 10 REMARK 465 VAL A 11 REMARK 465 ARG A 60A REMARK 465 ILE A 60B REMARK 465 TYR A 60C REMARK 465 HIS A 60D REMARK 465 GLY A 60E REMARK 465 GLY A 60F REMARK 465 SER A 60G REMARK 465 GLY A 60H REMARK 465 GLY A 60I REMARK 465 SER A 60J REMARK 465 GLY A 60K REMARK 465 VAL A 60L REMARK 465 ASN A 60M 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 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 N 0 REMARK 465 SER N 128 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 465 MET R -155 REMARK 465 LYS R -154 REMARK 465 THR R -153 REMARK 465 ILE R -152 REMARK 465 ILE R -151 REMARK 465 ALA R -150 REMARK 465 LEU R -149 REMARK 465 SER R -148 REMARK 465 TYR R -147 REMARK 465 ILE R -146 REMARK 465 PHE R -145 REMARK 465 CYS R -144 REMARK 465 LEU R -143 REMARK 465 VAL R -142 REMARK 465 PHE R -141 REMARK 465 ALA R -140 REMARK 465 ASP R -139 REMARK 465 TYR R -138 REMARK 465 LYS R -137 REMARK 465 ASP R -136 REMARK 465 ASP R -135 REMARK 465 ASP R -134 REMARK 465 ASP R -133 REMARK 465 LYS R -132 REMARK 465 HIS R -131 REMARK 465 HIS R -130 REMARK 465 HIS R -129 REMARK 465 HIS R -128 REMARK 465 HIS R -127 REMARK 465 HIS R -126 REMARK 465 HIS R -125 REMARK 465 HIS R -124 REMARK 465 HIS R -123 REMARK 465 HIS R -122 REMARK 465 LEU R -121 REMARK 465 GLU R -120 REMARK 465 VAL R -119 REMARK 465 LEU R -118 REMARK 465 PHE R -117 REMARK 465 GLN R -116 REMARK 465 GLY R -115 REMARK 465 PRO R -114 REMARK 465 ALA R -113 REMARK 465 ASP R -112 REMARK 465 LEU R -111 REMARK 465 GLU R -110 REMARK 465 ASP R -109 REMARK 465 ASN R -108 REMARK 465 TRP R -107 REMARK 465 GLU R -106 REMARK 465 THR R -105 REMARK 465 LEU R -104 REMARK 465 ASN R -103 REMARK 465 ASP R -102 REMARK 465 ASN R -101 REMARK 465 LEU R -100 REMARK 465 LYS R -99 REMARK 465 VAL R -98 REMARK 465 ILE R -97 REMARK 465 GLU R -96 REMARK 465 LYS R -95 REMARK 465 ALA R -94 REMARK 465 ASP R -93 REMARK 465 ASN R -92 REMARK 465 ALA R -91 REMARK 465 ALA R -90 REMARK 465 GLN R -89 REMARK 465 VAL R -88 REMARK 465 LYS R -87 REMARK 465 ASP R -86 REMARK 465 ALA R -85 REMARK 465 LEU R -84 REMARK 465 THR R -83 REMARK 465 LYS R -82 REMARK 465 MET R -81 REMARK 465 ARG R -80 REMARK 465 ALA R -79 REMARK 465 ALA R -78 REMARK 465 ALA R -77 REMARK 465 LEU R -76 REMARK 465 ASP R -75 REMARK 465 ALA R -74 REMARK 465 GLN R -73 REMARK 465 LYS R -72 REMARK 465 ALA R -71 REMARK 465 THR R -70 REMARK 465 PRO R -69 REMARK 465 PRO R -68 REMARK 465 LYS R -67 REMARK 465 LEU R -66 REMARK 465 GLU R -65 REMARK 465 ASP R -64 REMARK 465 LYS R -63 REMARK 465 SER R -62 REMARK 465 PRO R -61 REMARK 465 ASP R -60 REMARK 465 SER R -59 REMARK 465 PRO R -58 REMARK 465 GLU R -57 REMARK 465 MET R -56 REMARK 465 LYS R -55 REMARK 465 ASP R -54 REMARK 465 PHE R -53 REMARK 465 ARG R -52 REMARK 465 HIS R -51 REMARK 465 GLY R -50 REMARK 465 PHE R -49 REMARK 465 ASP R -48 REMARK 465 ILE R -47 REMARK 465 LEU R -46 REMARK 465 VAL R -45 REMARK 465 GLY R -44 REMARK 465 GLN R -43 REMARK 465 ILE R -42 REMARK 465 ASP R -41 REMARK 465 ASP R -40 REMARK 465 ALA R -39 REMARK 465 LEU R -38 REMARK 465 LYS R -37 REMARK 465 LEU R -36 REMARK 465 ALA R -35 REMARK 465 ASN R -34 REMARK 465 GLU R -33 REMARK 465 GLY R -32 REMARK 465 LYS R -31 REMARK 465 VAL R -30 REMARK 465 LYS R -29 REMARK 465 GLU R -28 REMARK 465 ALA R -27 REMARK 465 GLN R -26 REMARK 465 ALA R -25 REMARK 465 ALA R -24 REMARK 465 ALA R -23 REMARK 465 GLU R -22 REMARK 465 GLN R -21 REMARK 465 LEU R -20 REMARK 465 LYS R -19 REMARK 465 THR R -18 REMARK 465 THR R -17 REMARK 465 ARG R -16 REMARK 465 ASN R -15 REMARK 465 ALA R -14 REMARK 465 TYR R -13 REMARK 465 ILE R -12 REMARK 465 GLN R -11 REMARK 465 LYS R -10 REMARK 465 TYR R -9 REMARK 465 LEU R -8 REMARK 465 MET R -7 REMARK 465 GLY R -6 REMARK 465 GLN R -5 REMARK 465 PRO R -4 REMARK 465 GLY R -3 REMARK 465 ASN R -2 REMARK 465 GLY R -1 REMARK 465 SER R 0 REMARK 465 ALA R 1 REMARK 465 HIS R 2 REMARK 465 LEU R 3 REMARK 465 CYS R 4 REMARK 465 HIS R 5 REMARK 465 ALA R 6 REMARK 465 ILE R 7 REMARK 465 THR R 8 REMARK 465 ASN R 9 REMARK 465 ILE R 10 REMARK 465 SER R 11 REMARK 465 HIS R 12 REMARK 465 ARG R 13 REMARK 465 ASN R 14 REMARK 465 SER R 15 REMARK 465 ASP R 16 REMARK 465 TRP R 17 REMARK 465 SER R 18 REMARK 465 ARG R 19 REMARK 465 VAL R 228 REMARK 465 GLN R 229 REMARK 465 VAL R 230 REMARK 465 GLY R 231 REMARK 465 LEU R 232 REMARK 465 GLU R 233 REMARK 465 GLY R 234 REMARK 465 LYS R 235 REMARK 465 SER R 236 REMARK 465 GLN R 237 REMARK 465 ALA R 238 REMARK 465 PRO R 239 REMARK 465 GLN R 240 REMARK 465 SER R 241 REMARK 465 LYS R 242 REMARK 465 LEU R 316 REMARK 465 LEU R 317 REMARK 465 GLY R 318 REMARK 465 LYS R 319 REMARK 465 ILE R 320 REMARK 465 PHE R 321 REMARK 465 GLN R 322 REMARK 465 LYS R 323 REMARK 465 ASP R 324 REMARK 465 SER R 325 REMARK 465 SER R 326 REMARK 465 ARG R 327 REMARK 465 SER R 328 REMARK 465 LYS R 329 REMARK 465 LEU R 330 REMARK 465 PHE R 331 REMARK 465 LEU R 332 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 MET A 60 CG SD CE REMARK 470 ARG A 185 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 220 CG OD1 OD2 REMARK 470 LEU B 14 CG CD1 CD2 REMARK 470 LEU B 30 CG CD1 CD2 REMARK 470 LYS B 301 CG CD CE NZ REMARK 470 LYS G 29 CG CD CE NZ REMARK 470 MET N 83 CG SD CE REMARK 470 LEU N 86 CG CD1 CD2 REMARK 470 ARG N 105 CG CD NE CZ NH1 NH2 REMARK 470 ILE R 93 CG1 CG2 CD1 REMARK 470 ARG R 172 CG CD NE CZ NH1 NH2 REMARK 470 SER R 182 OG REMARK 470 PHE R 184 CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR R 291 CG CD1 CD2 CE1 CE2 CZ OH 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 GLU A 71 110.37 -163.82 REMARK 500 VAL A 76 -68.76 -121.39 REMARK 500 ASP A 77 60.78 -104.10 REMARK 500 PHE A 100 51.74 -92.24 REMARK 500 PRO A 165 44.12 -79.16 REMARK 500 ARG A 169 52.72 -92.32 REMARK 500 ASP A 206 -126.23 54.87 REMARK 500 TRP B 99 57.92 -92.03 REMARK 500 THR B 196 14.10 58.00 REMARK 500 ASP B 205 17.56 -141.41 REMARK 500 SER B 227 -168.56 -164.64 REMARK 500 SER B 279 -73.46 -81.86 REMARK 500 LYS B 280 -24.05 -142.64 REMARK 500 ASP B 291 35.51 -84.05 REMARK 500 PHE B 292 -1.62 69.71 REMARK 500 SER B 334 31.91 73.74 REMARK 500 LEU R 53 52.63 -92.53 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG B 314 0.19 SIDE CHAIN REMARK 500 ARG N 98 0.11 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-60427 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF THE RO5263397-BOUND MTAAR1-GS COMPLEX DBREF 8ZSV A 7 246 PDB 8ZSV 8ZSV 7 246 DBREF 8ZSV B 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 8ZSV G 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 8ZSV N 0 138 PDB 8ZSV 8ZSV 0 138 DBREF 8ZSV R -113 -9 UNP P0ABE7 C562_ECOLX 23 127 DBREF 8ZSV R 2 332 UNP Q923Y8 TAAR1_MOUSE 2 332 SEQADV 8ZSV MET B -4 UNP P62873 INITIATING METHIONINE SEQADV 8ZSV GLY B -3 UNP P62873 EXPRESSION TAG SEQADV 8ZSV SER B -2 UNP P62873 EXPRESSION TAG SEQADV 8ZSV LEU B -1 UNP P62873 EXPRESSION TAG SEQADV 8ZSV LEU B 0 UNP P62873 EXPRESSION TAG SEQADV 8ZSV GLN B 1 UNP P62873 EXPRESSION TAG SEQADV 8ZSV MET R -155 UNP P0ABE7 INITIATING METHIONINE SEQADV 8ZSV LYS R -154 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV THR R -153 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV ILE R -152 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV ILE R -151 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV ALA R -150 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV LEU R -149 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV SER R -148 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV TYR R -147 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV ILE R -146 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV PHE R -145 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV CYS R -144 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV LEU R -143 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV VAL R -142 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV PHE R -141 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV ALA R -140 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV ASP R -139 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV TYR R -138 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV LYS R -137 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV ASP R -136 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV ASP R -135 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV ASP R -134 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV ASP R -133 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV LYS R -132 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV HIS R -131 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV HIS R -130 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV HIS R -129 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV HIS R -128 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV HIS R -127 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV HIS R -126 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV HIS R -125 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV HIS R -124 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV HIS R -123 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV HIS R -122 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV LEU R -121 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV GLU R -120 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV VAL R -119 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV LEU R -118 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV PHE R -117 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV GLN R -116 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV GLY R -115 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV PRO R -114 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZSV TRP R -107 UNP P0ABE7 MET 29 CONFLICT SEQADV 8ZSV ILE R -12 UNP P0ABE7 HIS 124 CONFLICT SEQADV 8ZSV LEU R -8 UNP P0ABE7 LINKER SEQADV 8ZSV MET R -7 UNP P0ABE7 LINKER SEQADV 8ZSV GLY R -6 UNP P0ABE7 LINKER SEQADV 8ZSV GLN R -5 UNP P0ABE7 LINKER SEQADV 8ZSV PRO R -4 UNP P0ABE7 LINKER SEQADV 8ZSV GLY R -3 UNP P0ABE7 LINKER SEQADV 8ZSV ASN R -2 UNP P0ABE7 LINKER SEQADV 8ZSV GLY R -1 UNP P0ABE7 LINKER SEQADV 8ZSV SER R 0 UNP P0ABE7 LINKER SEQADV 8ZSV ALA R 1 UNP P0ABE7 LINKER SEQRES 1 A 247 MET GLY SER THR VAL SER ALA GLU ASP LYS ALA ALA ALA SEQRES 2 A 247 GLU ARG SER LYS MET ILE ASP LYS ASN LEU ARG GLU ASP SEQRES 3 A 247 GLY GLU LYS ALA ALA ALA ALA THR HIS ARG LEU LEU LEU SEQRES 4 A 247 LEU GLY ALA ASP ASN SER GLY LYS SER THR ILE VAL LYS SEQRES 5 A 247 GLN MET ARG ILE TYR HIS GLY GLY SER GLY GLY SER GLY SEQRES 6 A 247 VAL ASN SER GLY ILE PHE GLU THR LYS PHE GLN VAL ASP SEQRES 7 A 247 LYS VAL ASN PHE HIS MET PHE ASP VAL GLY ALA GLN ARG SEQRES 8 A 247 ASP GLU ARG ARG LYS TRP ILE GLN CYS PHE ASN ASP VAL SEQRES 9 A 247 THR ALA ILE ILE PHE VAL VAL ASP SER SER ASP TYR ASN SEQRES 10 A 247 ARG LEU GLN GLU ALA LEU ASN ASP PHE LYS SER ILE TRP SEQRES 11 A 247 ASN ASN ARG TRP LEU ARG THR ILE SER VAL ILE LEU PHE SEQRES 12 A 247 LEU ASN LYS GLN ASP LEU LEU ALA GLU LYS VAL LEU ALA SEQRES 13 A 247 GLY LYS SER LYS ILE GLU ASP TYR PHE PRO GLU PHE ALA SEQRES 14 A 247 ARG TYR THR THR PRO GLU ASP ALA THR PRO GLU PRO GLY SEQRES 15 A 247 GLU ASP PRO ARG VAL THR ARG ALA LYS TYR PHE ILE ARG SEQRES 16 A 247 ASP GLU PHE LEU ARG ILE SER THR ALA SER GLY ASP GLY SEQRES 17 A 247 ARG HIS TYR CYS TYR PRO HIS PHE THR CYS SER VAL ASP SEQRES 18 A 247 THR GLU ASN ALA ARG ARG ILE PHE ASN ASP CYS ARG ASP SEQRES 19 A 247 ILE ILE GLN ARG MET HIS LEU ARG GLN TYR GLU LEU LEU 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 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 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 SEQRES 1 R 488 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU SEQRES 2 R 488 VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP LYS HIS HIS SEQRES 3 R 488 HIS HIS HIS HIS HIS HIS HIS HIS LEU GLU VAL LEU PHE SEQRES 4 R 488 GLN GLY PRO ALA ASP LEU GLU ASP ASN TRP GLU THR LEU SEQRES 5 R 488 ASN ASP ASN LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA SEQRES 6 R 488 ALA GLN VAL LYS ASP ALA LEU THR LYS MET ARG ALA ALA SEQRES 7 R 488 ALA LEU ASP ALA GLN LYS ALA THR PRO PRO LYS LEU GLU SEQRES 8 R 488 ASP LYS SER PRO ASP SER PRO GLU MET LYS ASP PHE ARG SEQRES 9 R 488 HIS GLY PHE ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA SEQRES 10 R 488 LEU LYS LEU ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN SEQRES 11 R 488 ALA ALA ALA GLU GLN LEU LYS THR THR ARG ASN ALA TYR SEQRES 12 R 488 ILE GLN LYS TYR LEU MET GLY GLN PRO GLY ASN GLY SER SEQRES 13 R 488 ALA HIS LEU CYS HIS ALA ILE THR ASN ILE SER HIS ARG SEQRES 14 R 488 ASN SER ASP TRP SER ARG GLU VAL GLN ALA SER LEU TYR SEQRES 15 R 488 SER LEU MET SER LEU ILE ILE LEU ALA THR LEU VAL GLY SEQRES 16 R 488 ASN LEU ILE VAL ILE ILE SER ILE SER HIS PHE LYS GLN SEQRES 17 R 488 LEU HIS THR PRO THR ASN TRP LEU LEU HIS SER MET ALA SEQRES 18 R 488 ILE VAL ASP PHE LEU LEU GLY CYS LEU ILE MET PRO CYS SEQRES 19 R 488 SER MET VAL ARG THR VAL GLU ARG CYS TRP TYR PHE GLY SEQRES 20 R 488 GLU ILE LEU CYS LYS VAL HIS THR SER THR ASP ILE MET SEQRES 21 R 488 LEU SER SER ALA SER ILE PHE HIS LEU ALA PHE ILE SER SEQRES 22 R 488 ILE ASP ARG TYR CYS ALA VAL CYS ASP PRO LEU ARG TYR SEQRES 23 R 488 LYS ALA LYS ILE ASN ILE SER THR ILE LEU VAL MET ILE SEQRES 24 R 488 LEU VAL SER TRP SER LEU PRO ALA VAL TYR ALA PHE GLY SEQRES 25 R 488 MET ILE PHE LEU GLU LEU ASN LEU LYS GLY VAL GLU GLU SEQRES 26 R 488 LEU TYR ARG SER GLN VAL SER ASP LEU GLY GLY CYS SER SEQRES 27 R 488 PRO PHE PHE SER LYS VAL SER GLY VAL LEU ALA PHE MET SEQRES 28 R 488 THR SER PHE TYR ILE PRO GLY SER VAL MET LEU PHE VAL SEQRES 29 R 488 TYR TYR ARG ILE TYR PHE ILE ALA LYS GLY GLN ALA ARG SEQRES 30 R 488 SER ILE ASN ARG THR ASN VAL GLN VAL GLY LEU GLU GLY SEQRES 31 R 488 LYS SER GLN ALA PRO GLN SER LYS GLU THR LYS ALA ALA SEQRES 32 R 488 LYS THR LEU GLY ILE MET VAL GLY VAL PHE LEU VAL CYS SEQRES 33 R 488 TRP CYS PRO PHE PHE LEU CYS THR VAL LEU ASP PRO PHE SEQRES 34 R 488 LEU GLY TYR VAL ILE PRO PRO SER LEU ASN ASP ALA LEU SEQRES 35 R 488 TYR TRP PHE GLY TYR LEU ASN SER ALA LEU ASN PRO MET SEQRES 36 R 488 VAL TYR ALA PHE PHE TYR PRO TRP PHE ARG ARG ALA LEU SEQRES 37 R 488 LYS MET VAL LEU LEU GLY LYS ILE PHE GLN LYS ASP SER SEQRES 38 R 488 SER ARG SER LYS LEU PHE LEU HET D8X R 401 14 FORMUL 6 D8X HELIX 1 AA1 SER A 12 ALA A 37 1 26 HELIX 2 AA2 LYS A 95 PHE A 100 5 6 HELIX 3 AA3 ARG A 117 ASN A 130 1 14 HELIX 4 AA4 TRP A 133 ILE A 137 5 5 HELIX 5 AA5 LYS A 145 GLY A 156 1 12 HELIX 6 AA6 LYS A 159 PHE A 164 1 6 HELIX 7 AA7 ASP A 183 SER A 204 1 22 HELIX 8 AA8 GLU A 222 TYR A 243 1 22 HELIX 9 AA9 LEU B 4 ALA B 26 1 23 HELIX 10 AB1 THR B 29 THR B 34 1 6 HELIX 11 AB2 ASN B 35 ILE B 37 5 3 HELIX 12 AB3 ALA G 7 ASN G 24 1 18 HELIX 13 AB4 LYS G 29 HIS G 44 1 16 HELIX 14 AB5 THR N 28 TYR N 32 5 5 HELIX 15 AB6 GLY N 62 LYS N 65 5 4 HELIX 16 AB7 LYS N 87 THR N 91 5 5 HELIX 17 AB8 VAL R 21 PHE R 50 1 30 HELIX 18 AB9 PRO R 56 ILE R 75 1 20 HELIX 19 AC1 ILE R 75 ARG R 86 1 12 HELIX 20 AC2 GLY R 91 ASP R 126 1 36 HELIX 21 AC3 ARG R 129 ILE R 134 1 6 HELIX 22 AC4 ASN R 135 ILE R 158 1 24 HELIX 23 AC5 VAL R 167 VAL R 175 1 9 HELIX 24 AC6 SER R 186 PHE R 198 1 13 HELIX 25 AC7 TYR R 199 ASN R 227 1 29 HELIX 26 AC8 LYS R 245 GLY R 251 1 7 HELIX 27 AC9 GLY R 251 GLY R 275 1 25 HELIX 28 AD1 PRO R 279 PHE R 303 1 25 HELIX 29 AD2 TYR R 305 LYS R 313 1 9 SHEET 1 AA1 5 THR A 72 GLN A 75 0 SHEET 2 AA1 5 ASN A 80 PHE A 84 -1 O MET A 83 N THR A 72 SHEET 3 AA1 5 THR A 40 LEU A 46 1 N LEU A 43 O HIS A 82 SHEET 4 AA1 5 ALA A 105 ASP A 111 1 O ILE A 107 N LEU A 44 SHEET 5 AA1 5 SER A 138 VAL A 139 1 O SER A 138 N ILE A 106 SHEET 1 AA2 6 THR A 72 GLN A 75 0 SHEET 2 AA2 6 ASN A 80 PHE A 84 -1 O MET A 83 N THR A 72 SHEET 3 AA2 6 THR A 40 LEU A 46 1 N LEU A 43 O HIS A 82 SHEET 4 AA2 6 ALA A 105 ASP A 111 1 O ILE A 107 N LEU A 44 SHEET 5 AA2 6 PHE A 142 ASN A 144 1 O PHE A 142 N PHE A 108 SHEET 6 AA2 6 HIS A 214 PHE A 215 1 O HIS A 214 N LEU A 143 SHEET 1 AA3 4 THR B 47 ARG B 52 0 SHEET 2 AA3 4 PHE B 335 TRP B 339 -1 O LEU B 336 N LEU B 51 SHEET 3 AA3 4 VAL B 327 GLY B 330 -1 N VAL B 327 O TRP B 339 SHEET 4 AA3 4 GLY B 319 VAL B 320 -1 N GLY B 319 O ALA B 328 SHEET 1 AA4 4 ILE B 58 TRP B 63 0 SHEET 2 AA4 4 LEU B 69 SER B 74 -1 O ALA B 73 N ALA B 60 SHEET 3 AA4 4 LYS B 78 ASP B 83 -1 O TRP B 82 N LEU B 70 SHEET 4 AA4 4 ASN B 88 PRO B 94 -1 O ILE B 93 N LEU B 79 SHEET 1 AA5 4 VAL B 100 TYR B 105 0 SHEET 2 AA5 4 TYR B 111 GLY B 116 -1 O GLY B 115 N MET B 101 SHEET 3 AA5 4 ILE B 120 ASN B 125 -1 O TYR B 124 N VAL B 112 SHEET 4 AA5 4 ARG B 134 ALA B 140 -1 O SER B 136 N ILE B 123 SHEET 1 AA6 4 LEU B 146 PHE B 151 0 SHEET 2 AA6 4 GLN B 156 SER B 161 -1 O VAL B 158 N ARG B 150 SHEET 3 AA6 4 CYS B 166 ASP B 170 -1 O TRP B 169 N ILE B 157 SHEET 4 AA6 4 GLN B 175 PHE B 180 -1 O PHE B 180 N CYS B 166 SHEET 1 AA7 4 SER B 191 LEU B 192 0 SHEET 2 AA7 4 LEU B 198 GLY B 202 -1 O VAL B 200 N SER B 191 SHEET 3 AA7 4 ALA B 208 ASP B 212 -1 O TRP B 211 N PHE B 199 SHEET 4 AA7 4 CYS B 218 PHE B 222 -1 O PHE B 222 N ALA B 208 SHEET 1 AA8 4 ILE B 229 PHE B 234 0 SHEET 2 AA8 4 ALA B 240 SER B 245 -1 O GLY B 244 N ASN B 230 SHEET 3 AA8 4 CYS B 250 ASP B 254 -1 O PHE B 253 N PHE B 241 SHEET 4 AA8 4 GLN B 259 TYR B 264 -1 O TYR B 264 N CYS B 250 SHEET 1 AA9 4 ILE B 273 PHE B 278 0 SHEET 2 AA9 4 LEU B 284 TYR B 289 -1 O GLY B 288 N THR B 274 SHEET 3 AA9 4 CYS B 294 ASP B 298 -1 O TRP B 297 N LEU B 285 SHEET 4 AA9 4 ASP B 303 LEU B 308 -1 O GLY B 306 N VAL B 296 SHEET 1 AB1 4 GLN N 3 SER N 7 0 SHEET 2 AB1 4 ARG N 19 SER N 25 -1 O SER N 21 N SER N 7 SHEET 3 AB1 4 THR N 78 MET N 83 -1 O LEU N 79 N CYS N 22 SHEET 4 AB1 4 PHE N 68 ASP N 73 -1 N ASP N 73 O THR N 78 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 TYR N 95 -1 N ALA N 92 O VAL N 124 SHEET 4 AB2 6 ASN N 35 GLN N 39 -1 N VAL N 37 O TYR N 95 SHEET 5 AB2 6 LEU N 45 ASP N 50 -1 O GLU N 46 N ARG N 38 SHEET 6 AB2 6 SER N 59 TYR N 60 -1 O SER N 59 N ASP N 50 SSBOND 1 CYS N 22 CYS N 96 1555 1555 2.03 SSBOND 2 CYS N 99 CYS N 107 1555 1555 2.02 SSBOND 3 CYS R 95 CYS R 181 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