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HEADER BLOOD CLOTTING 09-MAY-03 1P9A TITLE CRYSTAL STRUCTURE OF N-TERMINAL DOMAIN OF HUMAN PLATELET TITLE 2 RECEPTOR GLYCOPROTEIN IB-ALPHA AT 1.7 ANGSTROM RESOLUTION COMPND MOL_ID: 1; COMPND 2 MOLECULE: PLATELET GLYCOPROTEIN IB ALPHA CHAIN PRECURSOR; COMPND 3 CHAIN: G; COMPND 4 FRAGMENT: N-TERMINAL DOMAIN; COMPND 5 SYNONYM: GLYCOPROTEIN IBALPHA, GP-IB ALPHA, GPIBA, GPIB- COMPND 6 ALPHA, CD42B-ALPHA, CD42B, CONTAINS: GLYCOCALICIN; COMPND 7 ENGINEERED: YES; COMPND 8 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 GENE: GP1BA; SOURCE 5 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: S2 KEYWDS PLATELET RECEPTORS, GLYCOCALICIN, LEUCINE RICH REPEATS EXPDTA X-RAY DIFFRACTION AUTHOR K.I.VARUGHESE,R.CELIKEL,Z.M.RUGGERI REVDAT 1 22-JUL-03 1P9A 0 JRNL AUTH R.CELIKEL,R.A.MCCLINTOCK,J.R.ROBERTS, JRNL AUTH 2 G.L.MENDOLICCHIO,J.WARE,K.I.VARUGHESE,Z.M.RUGGERI JRNL TITL MODULATION OF ALPHA-THROMBIN FUNCTION BY DISTINCT JRNL TITL 2 INTERACTIONS WITH PLATELET GLYCOPROTEIN IBALPHA JRNL REF SCIENCE V. 301 218 2003 JRNL REFN ASTM SCIEAS US ISSN 0036-8075 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.5 REMARK 3 NUMBER OF REFLECTIONS : 31316 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.204 REMARK 3 FREE R VALUE : 0.224 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 1521 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2077 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 50 REMARK 3 SOLVENT ATOMS : 207 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.005 REMARK 3 BOND ANGLES (DEGREES) : 1.30 REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : NULL REMARK 3 KSOL : NULL REMARK 3 BSOL : NULL REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1P9A COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.100 (2007-03-17) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB019168. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 14-FEB-2002 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 5.60 REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL11-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0642 REMARK 200 MONOCHROMATOR : CURVED CRYSTAL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 160737 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.4 REMARK 200 DATA REDUNDANCY : 5.100 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.06100 REMARK 200 FOR THE DATA SET : 19.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76 REMARK 200 COMPLETENESS FOR SHELL (%) : 73.6 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.31700 REMARK 200 FOR SHELL : 5.300 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: CNS REMARK 200 STARTING MODEL: 2.7 ANGSTROM P21/GPIB-ALPHA MAD STRUCTURE-TO REMARK 200 BE PUBLISHED REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 47.89 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, SODIUM NITRATE, SODIUM REMARK 280 ACETATE, PH 5.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE REMARK 280 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,1/2+Z REMARK 290 3555 -Y,X,3/4+Z REMARK 290 4555 Y,-X,1/4+Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 57.02050 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 85.53075 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 28.51025 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE 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 APPLY THE FOLLOWING TO CHAINS: G, N 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 LEU G 267 REMARK 465 GLY G 268 REMARK 465 ASP G 269 REMARK 465 GLU G 270 REMARK 465 GLY G 271 REMARK 465 ASP G 272 REMARK 465 THR G 273 REMARK 465 ASP G 274 REMARK 465 LEU G 275 REMARK 465 TYR G 276 REMARK 465 ASP G 277 REMARK 465 TYR G 278 REMARK 465 TYR G 279 REMARK 465 PRO G 280 REMARK 465 GLU G 281 REMARK 465 GLU G 282 REMARK 465 ASP G 283 REMARK 465 THR G 284 REMARK 465 GLU G 285 REMARK 465 GLY G 286 REMARK 465 ASP G 287 REMARK 465 LYS G 288 REMARK 465 VAL G 289 REMARK 465 ARG G 290 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 THR G 55 N - CA - C ANGL. DEV. = 8.0 DEGREES REMARK 500 LEU G 76 N - CA - C ANGL. DEV. = -9.5 DEGREES REMARK 500 PRO G 77 N - CA - C ANGL. DEV. = 8.6 DEGREES REMARK 500 LEU G 95 N - CA - C ANGL. DEV. = 8.9 DEGREES REMARK 500 ALA G 119 N - CA - C ANGL. DEV. = 10.5 DEGREES REMARK 500 GLN G 247 N - CA - C ANGL. DEV. = 9.1 DEGREES 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 M RES CSSEQI PSI PHI REMARK 500 VAL G 9 129.92 85.08 REMARK 500 ALA G 10 -116.58 39.90 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 100K RELATED DB: PDB REMARK 900 COMPLEX OF PLATELET RECEPTOR GPIB-ALPHA AND HUMAN ALPHA- REMARK 900 THROMBIN DBREF 1P9A G 1 290 UNP P07359 GPBA_HUMAN 17 306 SEQADV 1P9A ALA G 65 UNP P07359 CYS 81 ENGINEERED SEQRES 1 G 290 HIS PRO ILE CYS GLU VAL SER LYS VAL ALA SER HIS LEU SEQRES 2 G 290 GLU VAL ASN CYS ASP LYS ARG ASN LEU THR ALA LEU PRO SEQRES 3 G 290 PRO ASP LEU PRO LYS ASP THR THR ILE LEU HIS LEU SER SEQRES 4 G 290 GLU ASN LEU LEU TYR THR PHE SER LEU ALA THR LEU MET SEQRES 5 G 290 PRO TYR THR ARG LEU THR GLN LEU ASN LEU ASP ARG ALA SEQRES 6 G 290 GLU LEU THR LYS LEU GLN VAL ASP GLY THR LEU PRO VAL SEQRES 7 G 290 LEU GLY THR LEU ASP LEU SER HIS ASN GLN LEU GLN SER SEQRES 8 G 290 LEU PRO LEU LEU GLY GLN THR LEU PRO ALA LEU THR VAL SEQRES 9 G 290 LEU ASP VAL SER PHE ASN ARG LEU THR SER LEU PRO LEU SEQRES 10 G 290 GLY ALA LEU ARG GLY LEU GLY GLU LEU GLN GLU LEU TYR SEQRES 11 G 290 LEU LYS GLY ASN GLU LEU LYS THR LEU PRO PRO GLY LEU SEQRES 12 G 290 LEU THR PRO THR PRO LYS LEU GLU LYS LEU SER LEU ALA SEQRES 13 G 290 ASN ASN ASN LEU THR GLU LEU PRO ALA GLY LEU LEU ASN SEQRES 14 G 290 GLY LEU GLU ASN LEU ASP THR LEU LEU LEU GLN GLU ASN SEQRES 15 G 290 SER LEU TYR THR ILE PRO LYS GLY PHE PHE GLY SER HIS SEQRES 16 G 290 LEU LEU PRO PHE ALA PHE LEU HIS GLY ASN PRO TRP LEU SEQRES 17 G 290 CYS ASN CYS GLU ILE LEU TYR PHE ARG ARG TRP LEU GLN SEQRES 18 G 290 ASP ASN ALA GLU ASN VAL TYR VAL TRP LYS GLN GLY VAL SEQRES 19 G 290 ASP VAL LYS ALA MET THR SER ASN VAL ALA SER VAL GLN SEQRES 20 G 290 CYS ASP ASN SER ASP LYS PHE PRO VAL TYR LYS TYR PRO SEQRES 21 G 290 GLY LYS GLY CYS PRO THR LEU GLY ASP GLU GLY ASP THR SEQRES 22 G 290 ASP LEU TYR ASP TYR TYR PRO GLU GLU ASP THR GLU GLY SEQRES 23 G 290 ASP LYS VAL ARG MODRES 1P9A ASN G 159 ASN GLYCOSYLATION SITE HET NAG N 601 14 HET NAG N 602 14 HET BMA N 603 11 HET BMA N 604 11 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETSYN NAG NAG FORMUL 2 NAG 2(C8 H15 N O6) FORMUL 2 BMA 2(C6 H12 O6) FORMUL 3 HOH *207(H2 O) HELIX 1 1 ALA G 49 MET G 52 5 4 HELIX 2 2 ASN G 210 GLU G 212 5 3 HELIX 3 3 ILE G 213 ASN G 223 1 11 HELIX 4 4 ALA G 224 VAL G 227 5 4 HELIX 5 5 ASN G 242 VAL G 246 5 5 HELIX 6 6 GLN G 247 SER G 251 5 5 HELIX 7 7 PRO G 255 TYR G 259 5 5 SHEET 1 A10 GLU G 5 SER G 7 0 SHEET 2 A10 GLU G 14 ASN G 16 -1 O ASN G 16 N GLU G 5 SHEET 3 A10 ILE G 35 HIS G 37 1 O ILE G 35 N VAL G 15 SHEET 4 A10 GLN G 59 ASN G 61 1 O GLN G 59 N LEU G 36 SHEET 5 A10 THR G 81 ASP G 83 1 O THR G 81 N LEU G 60 SHEET 6 A10 VAL G 104 ASP G 106 1 O ASP G 106 N LEU G 82 SHEET 7 A10 GLU G 128 TYR G 130 1 O TYR G 130 N LEU G 105 SHEET 8 A10 LYS G 152 SER G 154 1 O SER G 154 N LEU G 129 SHEET 9 A10 THR G 176 LEU G 178 1 O LEU G 178 N LEU G 153 SHEET 10 A10 PHE G 199 PHE G 201 1 O PHE G 199 N LEU G 177 SHEET 1 B 2 THR G 45 SER G 47 0 SHEET 2 B 2 LYS G 69 GLN G 71 1 O GLN G 71 N PHE G 46 SSBOND 1 CYS G 4 CYS G 17 SSBOND 2 CYS G 209 CYS G 248 SSBOND 3 CYS G 211 CYS G 264 LINK ND2 ASN G 159 C1 NAG N 601 LINK O4 NAG N 601 C1 NAG N 602 LINK O4 NAG N 602 C1 BMA N 603 LINK O3 BMA N 603 C1 BMA N 604 CRYST1 51.734 51.734 114.041 90.00 90.00 90.00 P 43 4 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 0.019330 0.000000 0.000000 0.00000 SCALE2 0.000000 0.019330 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008769 0.00000