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HEADER HYDROLASE 27-SEP-00 1GGV
TITLE CRYSTAL STRUCTURE OF THE C123S MUTANT OF DIENELACTONE
TITLE 2 HYDROLASE (DLH) BOUND WITH THE PMS MOIETY OF THE PROTEASE
TITLE 3 INHIBITOR, PHENYLMETHYLSULFONYL FLUORIDE (PMSF)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIENELACTONE HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.45;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS PUTIDA;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR: LAMBDA TEMPERATURE SENSITIVE
SOURCE 7 VECTOR SYSTEM (RSC, ANU);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PAC27
KEYWDS ALPHA/BETA HYDROLASE FOLD, DIENELACTONE HYDROLASE, PMSF,
KEYWDS 2 PSEUDOMONAS PUTIDA (PAC27)
EXPDTA X-RAY DIFFRACTION
AUTHOR A.ROBINSON,K.J.EDWARDS,P.D.CARR,J.D.BARTON,G.D.EWART,
AUTHOR 2 D.L.OLLIS
REVDAT 1 13-DEC-00 1GGV 0
JRNL AUTH A.ROBINSON,K.J.EDWARDS,P.D.CARR,J.D.BARTON,
JRNL AUTH 2 G.D.EWART,D.L.OLLIS
JRNL TITL STRUCTURE OF THE C123S MUTANT OF DIENELACTONE
JRNL TITL 2 HYDROLASE (DLH) BOUND WITH THE PMS MOIETY OF THE
JRNL TITL 3 PROTEASE INHIBITOR PHENYLMETHYLSULFONYL FLUORIDE
JRNL TITL 4 (PMSF)
JRNL REF ACTA CRYSTALLOGR., SECT.D V. 56 1376 2000
JRNL REFN ASTM ABCRE6 DK ISSN 0907-4449
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
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 : 6459
REMARK 3
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.151
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 : 2254
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 64
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) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.51
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.24
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.29
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
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 1GGV COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-OCT-2000.
REMARK 100 THE RCSB ID CODE IS RCSB001500.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-1994
REMARK 200 TEMPERATURE (KELVIN) : 277.0
REMARK 200 PH : 6.30
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MANUFACTURER SUPPLIED
REMARK 200 (MSC)
REMARK 200 DATA SCALING SOFTWARE : MANUFACTURER SUPPLIED
REMARK 200 (MSC)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12109
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 78.7
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.09
REMARK 200 COMPLETENESS FOR SHELL (%) : 65.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: DIENELACTONE HYDROLASE (WILD-TYPE)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: (K+/NA+) PHOSPHATE, PMSF
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-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 25.55000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.85000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.95000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.85000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.55000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 25.95000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: A
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 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 1 CG SD CE
REMARK 470 GLU A 4 CG CD OE1 OE2
REMARK 470 LYS A 25 CG CD CE NZ
REMARK 470 ARG A 45 CD NE CZ NH1 NH2
REMARK 470 ASN A 154 CG OD1 ND2
REMARK 470 HIS A 172 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 199 CG CD OE1 OE2
REMARK 470 HIS A 202 CG ND1 CD2 CE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NE2 HIS A 161 NE2 GLN A 180 4557 1.50
REMARK 500 CE1 HIS A 161 NE2 GLN A 180 4557 1.83
REMARK 500 CA GLY A 136 OE1 GLU A 184 4557 2.05
REMARK 500 OH TYR A 11 CG1 VAL A 156 4557 2.06
REMARK 500 OE2 GLU A 184 O GLY A 136 4457 2.12
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 LEU A 19 N - CA - C ANGL. DEV. = -9.0 DEGREES
REMARK 500 ALA A 57 N - CA - C ANGL. DEV. =-12.2 DEGREES
REMARK 500 HIS A 161 N - CA - C ANGL. DEV. = -8.9 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 SEB A 123 51.40 -110.01
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD:
REMARK 650 AUTHOR-DETERMINED
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD:
REMARK 700 AUTHOR-DETERMINED
REMARK 999
REMARK 999 SEQUENCE
REMARK 999
REMARK 999 THE PROTEIN IN THIS ENTRY IS A C123S MUTANT WITH
REMARK 999 THE PMS MOIETY OF THE PROTEASE INHIBITOR,
REMARK 999 PHENYLMETHYLSULFONYL FLUORIDE (PMSF), BOUND TO
REMARK 999 SER 123.
DBREF 1GGV A 1 232 SWS P11453 CLCD_PSEPU 1 232
SEQADV 1GGV ALA A 79 SWS P11453 ARG 79 CONFLICT
SEQADV 1GGV SEB A 123 SWS P11453 CYS 123 SEE REMARK 999
SEQADV 1GGV ASN A 154 SWS P11453 LYS 154 CONFLICT
SEQADV 1GGV THR A 224 SWS P11453 ARG 224 CONFLICT
SEQRES 1 A 232 MET LEU THR GLU GLY ILE SER ILE GLN SER TYR ASP GLY
SEQRES 2 A 232 HIS THR PHE GLY ALA LEU VAL GLY SER PRO ALA LYS ALA
SEQRES 3 A 232 PRO ALA PRO VAL ILE VAL ILE ALA GLN GLU ILE PHE GLY
SEQRES 4 A 232 VAL ASN ALA PHE MET ARG GLU THR VAL SER TRP LEU VAL
SEQRES 5 A 232 ASP GLN GLY TYR ALA ALA VAL CYS PRO ASP LEU TYR ALA
SEQRES 6 A 232 ARG GLN ALA PRO GLY THR ALA LEU ASP PRO GLN ASP GLU
SEQRES 7 A 232 ALA GLN ARG GLU GLN ALA TYR LYS LEU TRP GLN ALA PHE
SEQRES 8 A 232 ASP MET GLU ALA GLY VAL GLY ASP LEU GLU ALA ALA ILE
SEQRES 9 A 232 ARG TYR ALA ARG HIS GLN PRO TYR SER ASN GLY LYS VAL
SEQRES 10 A 232 GLY LEU VAL GLY TYR SEB LEU GLY GLY ALA LEU ALA PHE
SEQRES 11 A 232 LEU VAL ALA ALA LYS GLY TYR VAL ASP ARG ALA VAL GLY
SEQRES 12 A 232 TYR TYR GLY VAL GLY LEU GLU LYS GLN LEU ASN LYS VAL
SEQRES 13 A 232 PRO GLU VAL LYS HIS PRO ALA LEU PHE HIS MET GLY GLY
SEQRES 14 A 232 GLN ASP HIS PHE VAL PRO ALA PRO SER ARG GLN LEU ILE
SEQRES 15 A 232 THR GLU GLY PHE GLY ALA ASN PRO LEU LEU GLN VAL HIS
SEQRES 16 A 232 TRP TYR GLU GLU ALA GLY HIS SER PHE ALA ARG THR SER
SEQRES 17 A 232 SER SER GLY TYR VAL ALA SER ALA ALA ALA LEU ALA ASN
SEQRES 18 A 232 GLU ARG THR LEU ASP PHE LEU ALA PRO LEU GLN
MODRES 1GGV SEB A 123 O-BENZYLSULFONYL-SERINE
HET SEB A 123 16
HETNAM SEB O-BENZYLSULFONYL-SERINE
FORMUL 1 SEB C10 H13 N1 O5 S1
FORMUL 2 HOH *64(H2 O1)
HELIX 1 1 ASN A 41 GLN A 54 1 14
HELIX 2 2 ASP A 62 GLN A 67 5 6
HELIX 3 3 ASP A 77 PHE A 91 1 15
HELIX 4 4 ASP A 92 HIS A 109 1 18
HELIX 5 5 LEU A 124 GLY A 136 1 13
HELIX 6 6 GLY A 148 LEU A 153 5 6
HELIX 7 7 GLN A 152 VAL A 159 5 8
HELIX 8 8 PRO A 175 ASN A 189 1 15
HELIX 9 9 VAL A 213 ALA A 229 1 17
HELIX 10 10 PRO A 230 GLN A 232 5 3
SHEET 1 B 7 ALA A 18 GLY A 21 0
SHEET 2 B 7 ALA A 28 ALA A 34 0
SHEET 3 B 7 ALA A 57 PRO A 61 0
SHEET 4 B 7 SER A 113 TYR A 122 0
SHEET 5 B 7 ARG A 140 TYR A 144 0
SHEET 6 B 7 ALA A 163 GLY A 168 0
SHEET 7 B 7 LEU A 192 TYR A 197 0
CISPEP 1 ALA A 26 PRO A 27 0 -0.26
CRYST1 51.100 51.900 81.700 90.00 90.00 90.00 P 21 21 21 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 0.019569 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019268 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012240 0.00000
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