| content |
HEADER HYDROLASE 01-SEP-97 1AUO
TITLE CARBOXYLESTERASE FROM PSEUDOMONAS FLUORESCENS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 BIOLOGICAL_UNIT: DIMER
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS FLUORESCENS;
SOURCE 3 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 4 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.K.KIM,H.K.SONG,S.W.SUH
REVDAT 1 04-MAR-98 1AUO 0
JRNL AUTH K.K.KIM,H.K.SONG,D.H.SHIN,K.Y.HWANG,S.CHOE,O.J.YOO,
JRNL AUTH 2 S.W.SUH
JRNL TITL CRYSTAL STRUCTURE OF CARBOXYLESTERASE FROM
JRNL TITL 2 PSEUDOMONAS FLUORESCENS, AN ALPHA/BETA HYDROLASE
JRNL TITL 3 WITH BROAD SUBSTRATE SPECIFICITY
JRNL REF STRUCTURE (LONDON) V. 5 1571 1997
JRNL REFN ASTM STRUE6 UK ISSN 0969-2126 2005
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.8 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.843
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.0
REMARK 3 NUMBER OF REFLECTIONS : 40600
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) : 0.208
REMARK 3 FREE R VALUE : 0.273
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.0
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 : 3364
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 247
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.4
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) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.2
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 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 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1AUO COMPLIES WITH FORMAT V. 2.2, 16-DEC-1996
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : MAR-1992
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : 6A2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NONE
REMARK 200 OPTICS : NONE
REMARK 200
REMARK 200 DETECTOR TYPE : IP
REMARK 200 DETECTOR MANUFACTURER : FUJI
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : WEIS
REMARK 200 DATA SCALING SOFTWARE : WEIS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41703
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.80
REMARK 200 RESOLUTION RANGE LOW (A) : 99.0
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.
REMARK 200 DATA REDUNDANCY : 6.3
REMARK 200 R MERGE (I) : 0.071
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MULTIPLE
REMARK 200 ISOMORPHOUS REPLACEMENT
REMARK 200 SOFTWARE USED: CCP4
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: DATA WERE COLLECTED USING THE WEISSENBERG METHOD
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 72.68498
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 41.02059
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 41.02059
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 36.34249
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 41.02059
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 41.02059
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 109.02747
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 41.02059
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 41.02059
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 36.34249
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 41.02059
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 41.02059
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 109.02747
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 72.68498
REMARK 290
REMARK 290 REMARK: NULL
REMARK 295
REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY
REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW
REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS
REMARK 295 IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX
REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD
REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND.
REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH
REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY.
REMARK 295
REMARK 295 APPLIED TO TRANSFORMED TO
REMARK 295 TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD
REMARK 295 SSS
REMARK 295 M 1 B 1 .. 218 A 1 .. 218 0.487
REMARK 295
REMARK 295 WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS
REMARK 295
REMARK 295 REMARK: NULL
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. SOME OF THESE MAY BE ATOMS
REMARK 500 LOCATED ON SPECIAL POSITIONS IN THE CELL. ATOMS WITH
REMARK 500 NON-BLANK ALTERNATE LOCATION INDICATORS ARE NOT INCLUDED
REMARK 500 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 OG1 THR B 53 O HOH 1201 6555 2.13
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 0 HOH 1162 DISTANCE = 5.87 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACA
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD.
REMARK 800
REMARK 800 SITE_IDENTIFIER: ACB
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD.
DBREF 1AUO A 1 218 GB 244501 S79600 1 218
DBREF 1AUO B 1 218 GB 244501 S79600 1 218
SEQRES 1 A 218 MET THR GLU PRO LEU ILE LEU GLN PRO ALA LYS PRO ALA
SEQRES 2 A 218 ASP ALA CYS VAL ILE TRP LEU HIS GLY LEU GLY ALA ASP
SEQRES 3 A 218 ARG TYR ASP PHE MET PRO VAL ALA GLU ALA LEU GLN GLU
SEQRES 4 A 218 SER LEU LEU THR THR ARG PHE VAL LEU PRO GLN ALA PRO
SEQRES 5 A 218 THR ARG PRO VAL THR ILE ASN GLY GLY TYR GLU MET PRO
SEQRES 6 A 218 SER TRP TYR ASP ILE LYS ALA MET SER PRO ALA ARG SER
SEQRES 7 A 218 ILE SER LEU GLU GLU LEU GLU VAL SER ALA LYS MET VAL
SEQRES 8 A 218 THR ASP LEU ILE GLU ALA GLN LYS ARG THR GLY ILE ASP
SEQRES 9 A 218 ALA SER ARG ILE PHE LEU ALA GLY PHE SER GLN GLY GLY
SEQRES 10 A 218 ALA VAL VAL PHE HIS THR ALA PHE ILE ASN TRP GLN GLY
SEQRES 11 A 218 PRO LEU GLY GLY VAL ILE ALA LEU SER THR TYR ALA PRO
SEQRES 12 A 218 THR PHE GLY ASP GLU LEU GLU LEU SER ALA SER GLN GLN
SEQRES 13 A 218 ARG ILE PRO ALA LEU CYS LEU HIS GLY GLN TYR ASP ASP
SEQRES 14 A 218 VAL VAL GLN ASN ALA MET GLY ARG SER ALA PHE GLU HIS
SEQRES 15 A 218 LEU LYS SER ARG GLY VAL THR VAL THR TRP GLN GLU TYR
SEQRES 16 A 218 PRO MET GLY HIS GLU VAL LEU PRO GLN GLU ILE HIS ASP
SEQRES 17 A 218 ILE GLY ALA TRP LEU ALA ALA ARG LEU GLY
SEQRES 1 B 218 MET THR GLU PRO LEU ILE LEU GLN PRO ALA LYS PRO ALA
SEQRES 2 B 218 ASP ALA CYS VAL ILE TRP LEU HIS GLY LEU GLY ALA ASP
SEQRES 3 B 218 ARG TYR ASP PHE MET PRO VAL ALA GLU ALA LEU GLN GLU
SEQRES 4 B 218 SER LEU LEU THR THR ARG PHE VAL LEU PRO GLN ALA PRO
SEQRES 5 B 218 THR ARG PRO VAL THR ILE ASN GLY GLY TYR GLU MET PRO
SEQRES 6 B 218 SER TRP TYR ASP ILE LYS ALA MET SER PRO ALA ARG SER
SEQRES 7 B 218 ILE SER LEU GLU GLU LEU GLU VAL SER ALA LYS MET VAL
SEQRES 8 B 218 THR ASP LEU ILE GLU ALA GLN LYS ARG THR GLY ILE ASP
SEQRES 9 B 218 ALA SER ARG ILE PHE LEU ALA GLY PHE SER GLN GLY GLY
SEQRES 10 B 218 ALA VAL VAL PHE HIS THR ALA PHE ILE ASN TRP GLN GLY
SEQRES 11 B 218 PRO LEU GLY GLY VAL ILE ALA LEU SER THR TYR ALA PRO
SEQRES 12 B 218 THR PHE GLY ASP GLU LEU GLU LEU SER ALA SER GLN GLN
SEQRES 13 B 218 ARG ILE PRO ALA LEU CYS LEU HIS GLY GLN TYR ASP ASP
SEQRES 14 B 218 VAL VAL GLN ASN ALA MET GLY ARG SER ALA PHE GLU HIS
SEQRES 15 B 218 LEU LYS SER ARG GLY VAL THR VAL THR TRP GLN GLU TYR
SEQRES 16 B 218 PRO MET GLY HIS GLU VAL LEU PRO GLN GLU ILE HIS ASP
SEQRES 17 B 218 ILE GLY ALA TRP LEU ALA ALA ARG LEU GLY
FORMUL 3 HOH *235(H2 O1)
HELIX 1 1 MET A 31 GLN A 38 1 8
HELIX 2 2 THR A 57 ASN A 59 5 3
HELIX 3 3 LEU A 81 ARG A 100 1 20
HELIX 4 4 ALA A 105 ARG A 107 5 3
HELIX 5 5 GLN A 115 PHE A 125 1 11
HELIX 6 6 ALA A 153 ARG A 157 1 5
HELIX 7 7 ASN A 173 ARG A 186 1 14
HELIX 8 8 PRO A 203 ARG A 216 1 14
HELIX 9 9 MET B 31 GLN B 38 1 8
HELIX 10 10 THR B 57 ASN B 59 5 3
HELIX 11 11 LEU B 81 THR B 101 1 21
HELIX 12 12 ALA B 105 ARG B 107 5 3
HELIX 13 13 GLN B 115 PHE B 125 1 11
HELIX 14 14 GLN B 155 ARG B 157 5 3
HELIX 15 15 ASN B 173 ARG B 186 1 14
HELIX 16 16 PRO B 203 ARG B 216 1 14
SHEET 1 A 7 LEU A 5 LEU A 7 0
SHEET 2 A 7 THR A 44 LEU A 48 -1 N LEU A 48 O LEU A 5
SHEET 3 A 7 ALA A 15 LEU A 20 1 N ALA A 15 O ARG A 45
SHEET 4 A 7 ILE A 108 PHE A 113 1 N PHE A 109 O CYS A 16
SHEET 5 A 7 GLY A 134 LEU A 138 1 N GLY A 134 O LEU A 110
SHEET 6 A 7 ALA A 160 GLY A 165 1 N LEU A 161 O VAL A 135
SHEET 7 A 7 VAL A 190 TYR A 195 1 N THR A 191 O ALA A 160
SHEET 1 B 2 THR A 53 VAL A 56 0
SHEET 2 B 2 TYR A 62 PRO A 65 -1 N MET A 64 O ARG A 54
SHEET 1 C 7 LEU B 5 LEU B 7 0
SHEET 2 C 7 THR B 44 LEU B 48 -1 N LEU B 48 O LEU B 5
SHEET 3 C 7 ALA B 15 LEU B 20 1 N ALA B 15 O ARG B 45
SHEET 4 C 7 ILE B 108 PHE B 113 1 N PHE B 109 O CYS B 16
SHEET 5 C 7 GLY B 134 LEU B 138 1 N GLY B 134 O LEU B 110
SHEET 6 C 7 ALA B 160 GLY B 165 1 N LEU B 161 O VAL B 135
SHEET 7 C 7 VAL B 190 TYR B 195 1 N THR B 191 O ALA B 160
SHEET 1 D 2 THR B 53 PRO B 55 0
SHEET 2 D 2 GLU B 63 PRO B 65 -1 N MET B 64 O ARG B 54
CISPEP 1 SER A 74 PRO A 75 0 0.17
CISPEP 2 SER B 74 PRO B 75 0 -8.32
SITE 1 ACA 3 SER A 114 HIS A 199 ASP A 168
SITE 1 ACB 3 SER B 114 HIS B 199 ASP B 168
CRYST1 82.040 82.040 145.380 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 0.012189 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012189 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006879 0.00000
MTRIX1 1 0.669442 -0.070588 0.739503 -26.30750 1
MTRIX2 1 -0.010899 -0.996301 -0.085234 67.13410 1
MTRIX3 1 0.742784 0.048999 -0.667735 62.89660 1 |