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HEADER TRANSCRIPTION/DNA 07-NOV-05 2C62 TITLE CRYSTAL STRUCTURE OF THE HUMAN TRANSCRIPTION COFACTOR PC4 TITLE 2 IN COMPLEX WITH SINGLE-STRANDED DNA COMPND MOL_ID: 1; COMPND 2 MOLECULE: 5'-D(*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP COMPND 3 *TP*TP*TP*TP*TP*TP*TP*TP*TP*G)-3'; COMPND 4 CHAIN: C; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: ACTIVATED RNA POLYMERASE II TRANSCRIPTIONAL COMPND 8 COACTIVATOR P15; COMPND 9 CHAIN: A, B; COMPND 10 FRAGMENT: C-TERMINAL SSDNA-BINDING DOMAIN, RESIDUES 62-126; COMPND 11 SYNONYM: PC4, POSITIVE COFACTOR 4, P14; COMPND 12 ENGINEERED: YES; COMPND 13 OTHER_DETAILS: N-TERMINAL ALA RESIDUE RESULTS FROM VECTOR COMPND 14 SEQUENCE SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 MOL_ID: 2; SOURCE 4 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 5 ORGANISM_COMMON: HUMAN; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 9 EXPRESSION_SYSTEM_VARIANT: DE3; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-11A KEYWDS TRANSCRIPTION COFACTOR, SINGLE-STRANDED DNA, PROTEIN-DNA KEYWDS 2 COMPLEX, DNA UNWINDING, ACTIVATOR, DNA-BINDING, NUCLEAR KEYWDS 3 PROTEIN, PHOSPHORYLATION, TRANSCRIPTION, TRANSCRIPTION KEYWDS 4 REGULATION EXPDTA X-RAY DIFFRACTION AUTHOR S.WERTEN,D.MORAS REVDAT 2 20-DEC-06 2C62 1 JRNL REVDAT 1 11-JAN-06 2C62 0 JRNL AUTH S.WERTEN,D.MORAS JRNL TITL A GLOBAL TRANSCRIPTION COFACTOR BOUND TO JRNL TITL 2 JUXTAPOSED STRANDS OF UNWOUND DNA. JRNL REF NAT.STRUCT.MOL.BIOL. V. 13 181 2006 JRNL REFN US ISSN 1545-9993 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.74 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1 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 : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.74 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.97 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) (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 30178 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.229 REMARK 3 FREE R VALUE : 0.240 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 1489 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 10 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.74 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.80 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.70 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.3100 REMARK 3 BIN FREE R VALUE : 0.3670 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10 REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.032 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1090 REMARK 3 NUCLEIC ACID ATOMS : 323 REMARK 3 HETEROGEN ATOMS : 10 REMARK 3 SOLVENT ATOMS : 176 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 29.90 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.10 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.30000 REMARK 3 B22 (A**2) : -0.30000 REMARK 3 B33 (A**2) : 0.59000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.26 REMARK 3 ESD FROM SIGMAA (A) : 0.22 REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.29 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.28 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) : 23.70 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.91 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 1.340 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.090 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 2.170 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.340 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.36 REMARK 3 BSOL : 52.43 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 : PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : NULL REMARK 3 TOPOLOGY FILE 1 : ION.TOP REMARK 3 TOPOLOGY FILE 2 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2C62 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 3.102 (2007-05-31) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI . REMARK 100 THE EBI ID CODE IS EBI-26269 . REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-JUN-2003 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 6.75 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID14-4 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97930 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR REMARK 200 OPTICS : TOROIDAL FOCUSING MIRROR REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31658 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.740 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 6.300 REMARK 200 R MERGE (I) : 0.04000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 21.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.74 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 4.80 REMARK 200 R MERGE FOR SHELL (I) : 0.30000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 5.430 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: EPMR REMARK 200 STARTING MODEL: PDB ENTRY 1PCF, CHAINS A AND B REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 62.77 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.33 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M ADA PH 6.75, 1.9 M AMMONIUM REMARK 280 SULFATE REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2 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 1/2-Y,1/2+X,1/4+Z REMARK 290 4555 1/2+Y,1/2-X,3/4+Z REMARK 290 5555 1/2-X,1/2+Y,1/4-Z REMARK 290 6555 1/2+X,1/2-Y,3/4-Z REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,1/2-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 65.94950 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 33.62100 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 33.62100 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 32.97475 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 33.62100 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 33.62100 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 98.92425 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 33.62100 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 33.62100 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 32.97475 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 33.62100 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 33.62100 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 98.92425 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 65.94950 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 3 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: C, A, B, X, Y, Z 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 DT C 1 REMARK 465 DT C 2 REMARK 465 DT C 3 REMARK 465 DT C 4 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 MET B 69 SD MET B 69 CE -0.034 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 VAL A 72 N - CA - C ANGL. DEV. =-13.3 DEGREES REMARK 500 ILE A 83 N - CA - C ANGL. DEV. =-10.0 DEGREES REMARK 500 ILE A 85 N - CA - C ANGL. DEV. =-10.1 DEGREES REMARK 500 VAL B 72 N - CA - C ANGL. DEV. =-12.5 DEGREES REMARK 500 ASP B 76 N - CA - C ANGL. DEV. = -8.3 DEGREES REMARK 500 ILE B 83 N - CA - C ANGL. DEV. = -7.9 DEGREES REMARK 500 ILE B 85 N - CA - C ANGL. DEV. =-12.8 DEGREES REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR CHAIN A DBREF 2C62 A 62 62 PDB 2C62 2C62 62 62 DBREF 2C62 A 63 127 UNP P53999 TCP4_HUMAN 62 126 DBREF 2C62 B 62 62 PDB 2C62 2C62 62 62 DBREF 2C62 B 63 127 UNP P53999 TCP4_HUMAN 62 126 DBREF 2C62 C 1 20 PDB 2C62 2C62 1 20 SEQRES 1 C 20 DT DT DT DT DT DT DT DT DT DT DT DT DT SEQRES 2 C 20 DT DT DT DT DT DT DG SEQRES 1 A 66 ALA MET PHE GLN ILE GLY LYS MET ARG TYR VAL SER VAL SEQRES 2 A 66 ARG ASP PHE LYS GLY LYS VAL LEU ILE ASP ILE ARG GLU SEQRES 3 A 66 TYR TRP MET ASP PRO GLU GLY GLU MET LYS PRO GLY ARG SEQRES 4 A 66 LYS GLY ILE SER LEU ASN PRO GLU GLN TRP SER GLN LEU SEQRES 5 A 66 LYS GLU GLN ILE SER ASP ILE ASP ASP ALA VAL ARG LYS SEQRES 6 A 66 LEU SEQRES 1 B 66 ALA MET PHE GLN ILE GLY LYS MET ARG TYR VAL SER VAL SEQRES 2 B 66 ARG ASP PHE LYS GLY LYS VAL LEU ILE ASP ILE ARG GLU SEQRES 3 B 66 TYR TRP MET ASP PRO GLU GLY GLU MET LYS PRO GLY ARG SEQRES 4 B 66 LYS GLY ILE SER LEU ASN PRO GLU GLN TRP SER GLN LEU SEQRES 5 B 66 LYS GLU GLN ILE SER ASP ILE ASP ASP ALA VAL ARG LYS SEQRES 6 B 66 LEU HET SO4 A1128 5 HET SO4 C1021 5 HETNAM SO4 SULFATE ION FORMUL 4 SO4 2(O4 S 2-) FORMUL 6 HOH *176(H2 O) HELIX 1 1 ASN A 106 GLN A 116 1 11 HELIX 2 2 GLN A 116 LYS A 126 1 11 HELIX 3 3 ASN B 106 GLN B 116 1 11 HELIX 4 4 GLN B 116 LEU B 127 1 12 SHEET 1 AA 4 MET A 63 GLY A 67 0 SHEET 2 AA 4 ARG A 70 PHE A 77 -1 O ARG A 70 N ILE A 66 SHEET 3 AA 4 LYS A 80 MET A 90 -1 O LYS A 80 N PHE A 77 SHEET 4 AA 4 MET A 96 LEU A 105 -1 O LYS A 97 N TRP A 89 SHEET 1 BA 4 MET B 63 GLY B 67 0 SHEET 2 BA 4 ARG B 70 PHE B 77 -1 O ARG B 70 N ILE B 66 SHEET 3 BA 4 LYS B 80 MET B 90 -1 O LYS B 80 N PHE B 77 SHEET 4 BA 4 MET B 96 LEU B 105 -1 O LYS B 97 N TRP B 89 SITE 1 AC1 2 DG C 20 HOH X 47 SITE 1 AC2 2 ALA A 62 HOH Z 55 CRYST1 67.242 67.242 131.899 90.00 90.00 90.00 P 41 21 2 16 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 0.014872 0.000000 0.000000 0.00000 SCALE2 0.000000 0.014872 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007582 0.00000