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HEADER HYDROLASE 23-APR-99 1QGE
TITLE NEW CRYSTAL FORM OF PSEUDOMONAS GLUMAE (FORMERLY
TITLE 2 CHROMOBACTERIUM VISCOSUM ATCC 6918) LIPASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRIACYLGLYCEROL HYDROLASE;
COMPND 3 CHAIN: D;
COMPND 4 EC: 3.1.1.3;
COMPND 5 BIOLOGICAL_UNIT: MONOMER;
COMPND 6 OTHER_DETAILS: CHAIN BREAK FROM V 220 - G 222;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: TRIACYLGLYCEROL HYDROLASE;
COMPND 9 CHAIN: E;
COMPND 10 EC: 3.1.1.3;
COMPND 11 BIOLOGICAL_UNIT: MONOMER
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS GLUMAE;
SOURCE 3 STRAIN: CHROMOBACTERIUM VISCOSUM;
SOURCE 4 COLLECTION: 6918;
SOURCE 5 CELLULAR_LOCATION: EXTRACELLULAR;
SOURCE 6 OTHER_DETAILS: ATCC;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: PSEUDOMONAS GLUMAE;
SOURCE 9 STRAIN: CHROMOBACTERIUM VISCOSUM;
SOURCE 10 COLLECTION: 6918;
SOURCE 11 CELLULAR_LOCATION: EXTRACELLULAR;
SOURCE 12 OTHER_DETAILS: ATCC
KEYWDS PSEUDOMONADACEAE, CIS-PEPTIDE, CLOSED CONFORMATION,
KEYWDS 2 HYDROLASE, LID
EXPDTA X-RAY DIFFRACTION
AUTHOR D.A.LANG,P.STADLER,A.KOVACS,F.PALTAUF,B.W.DIJKSTRA
REVDAT 1 06-MAY-99 1QGE 0
JRNL AUTH D.A.LANG,P.STADLER,A.KOVACS,F.PALTAUF,B.W.DIJKSTRA
JRNL TITL STRUCTURAL AND KINETIC INVESTIGATIONS OF
JRNL TITL 2 ENANTIOMERIC BINDING MODE OF SUBCLASS I LIPASES
JRNL TITL 3 FROM THE FAMILY OF PSEUDOMONADACEAE
JRNL REF TO BE PUBLISHED
JRNL REFN 0353
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.LANG,B.HOFMANN,L.HAALCK,H.J.HECHT,F.SPENER,
REMARK 1 AUTH 2 R.D.SCHMID,D.SCHOMBURG
REMARK 1 TITL CRYSTAL STRUCTURE OF A BACTERIAL LIPASE FROM
REMARK 1 TITL 2 CHROMOBACTERIUM VISCOSUM ATCC 6918 REFINED AT 1.6
REMARK 1 TITL 3 ANGSTROMS RESOLUTION
REMARK 1 REF J.MOL.BIOL. V. 259 704 1996
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.E.M.NOBLE,A.CLEASBY,L.N.JOHNSON,M.R.EGMOND,
REMARK 1 AUTH 2 L.G.J.FRENKEN
REMARK 1 TITL CRYSTAL STRUCTURE OF TRIACYLGLYCEROL LIPASE FROM
REMARK 1 TITL 2 PSEUDOMONAS GLUMAE REVEALS A PARTIALLY REDUNDANT
REMARK 1 TITL 3 CATALYTIC ASPARTATE
REMARK 1 REF FEBS LETT. V. 331 123 1993
REMARK 1 REFN ASTM FEBLAL NE ISSN 0014-5793 0165
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.7
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 28058
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 + TEST SET) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1410
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2315
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 324
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.9
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.008 ; 0.02
REMARK 3 ANGLE DISTANCE (A) : 0.025 ; 0.04
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.047 ; 0.05
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.104 ; 0.15
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.171 ; 0.3
REMARK 3 MULTIPLE TORSION (A) : 0.263 ; 0.3
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : 12.2 ; 15.0
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.959 ; 2.0
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.495 ; 3.0
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.193 ; 2.0
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 1.817 ; 3.0
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE DISORDERED REGION (VAL 220,
REMARK 3 LEU 221 AND GLY 223) WAS NOT MODELED OR REFINED.
REMARK 4
REMARK 4 1QGE COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 7
REMARK 7 PARTLY DEGRADED LIPASE AS A RESULT OF UNSPECIFIC
REMARK 7 PROTEOLYTIC DIGESTION DURING PURIFICATION AND/OR STORAGE
REMARK 7 PROVEN BY MALDI-TOF MASS SPECTROSCOPY MOLECULAR WEIGHT:
REMARK 7 CALCULATED -- 33091 DALTON, MEASURED -- 32839 DALTON
REMARK 8
REMARK 8 NO OXYANION LOOP FORMATION, BUT A SLIGHT MOVEMENT OF THE
REMARK 8 LID REGION ALREADY OCCURED. THE STRUCTURE STILL REPRESENTS
REMARK 8 THE CLOSED, INACTIVE CONFORMATIONAL STATES OF THE LIPASE
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-APR-1999.
REMARK 100 THE RCSB ID CODE IS RCSB000931.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-1996
REMARK 200 TEMPERATURE (KELVIN) : 90.0
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW6
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 : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28124
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.7
REMARK 200 RESOLUTION RANGE LOW (A) : 100.0
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 3.4
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.067
REMARK 200 FOR THE DATA SET : 10.5
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.7
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.5
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.27
REMARK 200 FOR SHELL : 4.1
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1CVL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.0
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.9
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM
REMARK 280 10 % PEG 6000, 5 % PEG 1000, 100 MM HEPES BUFFER, PH 7.8
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 20.49000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.34500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 21.67500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.34500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.49000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 21.67500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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 VAL D 220
REMARK 465 LEU D 221
REMARK 465 GLY D 222
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 4*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 GLY D 200 N - CA - C ANGL. DEV. =-12.0 DEGREES
REMARK 500 GLY D 201 N - CA - C ANGL. DEV. =-10.5 DEGREES
REMARK 500 TRP D 209 CA - CB - CG ANGL. DEV. = 8.3 DEGREES
REMARK 500 ASP E 241 CB - CG - OD1 ANGL. DEV. = 11.1 DEGREES
REMARK 500 GLN E 291 CA - C - N ANGL. DEV. = 12.9 DEGREES
REMARK 500 GLN E 291 O - C - N ANGL. DEV. =-16.7 DEGREES
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLN E 291 LEU E 292 -67.45
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACT
REMARK 800 SITE_DESCRIPTION:
REMARK 800 THE CATALYTIC TRIAD OF THE ACTIVE
REMARK 800 CENTER CONSISTS OF THE RESIDUES SER 87 - HIS 285 - ASP
REMARK 800 263, ALTHOUGH THEY ARE NOT EXPOSED TO THE SOLVENT.
REMARK 800
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1QGE SWS Q05489 1 - 39 NOT IN ATOMS LIST
REMARK 999
REMARK 999 REFERENCE: THE SEQUENCE FOR PSEUDOMONAS GLUMAE DESCRIBED
REMARK 999 IN FRENKEN ET AL. (1992), APPL. ENVIR. MICROBIOL. 58
REMARK 999 3787-3791; IS IDENTICAL TO THE AMINO ACID SEQUENCE OF
REMARK 999 CHROMOBACTERIUM VISCOSUM DESCRIBED IN SHIZUOKA ET AL.,
REMARK 999 1989 (GERMAN PATENT 3908131 A1).
DBREF 1QGE D 1 222 SWS Q05489 LIP_PSEGL 40 261
DBREF 1QGE E 223 319 SWS Q05489 LIP_PSEGL 262 358
SEQRES 1 D 222 ALA ASP THR TYR ALA ALA THR ARG TYR PRO VAL ILE LEU
SEQRES 2 D 222 VAL HIS GLY LEU ALA GLY THR ASP LYS PHE ALA ASN VAL
SEQRES 3 D 222 VAL ASP TYR TRP TYR GLY ILE GLN SER ASP LEU GLN SER
SEQRES 4 D 222 HIS GLY ALA LYS VAL TYR VAL ALA ASN LEU SER GLY PHE
SEQRES 5 D 222 GLN SER ASP ASP GLY PRO ASN GLY ARG GLY GLU GLN LEU
SEQRES 6 D 222 LEU ALA TYR VAL LYS GLN VAL LEU ALA ALA THR GLY ALA
SEQRES 7 D 222 THR LYS VAL ASN LEU ILE GLY HIS SER GLN GLY GLY LEU
SEQRES 8 D 222 THR SER ARG TYR VAL ALA ALA VAL ALA PRO GLN LEU VAL
SEQRES 9 D 222 ALA SER VAL THR THR ILE GLY THR PRO HIS ARG GLY SER
SEQRES 10 D 222 GLU PHE ALA ASP PHE VAL GLN ASP VAL LEU LYS THR ASP
SEQRES 11 D 222 PRO THR GLY LEU SER SER THR VAL ILE ALA ALA PHE VAL
SEQRES 12 D 222 ASN VAL PHE GLY THR LEU VAL SER SER SER HIS ASN THR
SEQRES 13 D 222 ASP GLN ASP ALA LEU ALA ALA LEU ARG THR LEU THR THR
SEQRES 14 D 222 ALA GLN THR ALA THR TYR ASN ARG ASN PHE PRO SER ALA
SEQRES 15 D 222 GLY LEU GLY ALA PRO GLY SER CYS GLN THR GLY ALA ALA
SEQRES 16 D 222 THR GLU THR VAL GLY GLY SER GLN HIS LEU LEU TYR SER
SEQRES 17 D 222 TRP GLY GLY THR ALA ILE GLN PRO THR SER THR VAL LEU
SEQRES 18 D 222 GLY
SEQRES 1 E 97 VAL VAL GLY ALA THR ASP THR SER THR GLY THR LEU ASP
SEQRES 2 E 97 VAL ALA ASN VAL THR ASP PRO SER THR LEU ALA LEU LEU
SEQRES 3 E 97 ALA THR GLY ALA VAL MET ILE ASN ARG ALA SER GLY GLN
SEQRES 4 E 97 ASN ASP GLY LEU VAL SER ARG CYS SER SER LEU PHE GLY
SEQRES 5 E 97 GLN VAL ILE SER THR SER TYR HIS TRP ASN HIS LEU ASP
SEQRES 6 E 97 GLU ILE ASN GLN LEU LEU GLY VAL ARG GLY ALA ASN ALA
SEQRES 7 E 97 GLU ASP PRO VAL ALA VAL ILE ARG THR HIS VAL ASN ARG
SEQRES 8 E 97 LEU LYS LEU GLN GLY VAL
HET CA 320 1
HETNAM CA CALCIUM ION
FORMUL 3 CA CA1 2+
FORMUL 4 HOH *324(H2 O1)
HELIX 1 1 ILE D 33 HIS D 40 1 8
HELIX 2 2 ARG D 61 THR D 76 1 16
HELIX 3 3 SER D 87 VAL D 99 5 13
HELIX 4 4 PRO D 101 LEU D 103 5 3
HELIX 5 5 GLU D 118 THR D 129 1 12
HELIX 6 6 THR D 137 LEU D 149 1 13
HELIX 7 7 THR D 156 LEU D 167 1 12
HELIX 8 8 THR D 169 ASN D 178 1 10
HELIX 9 9 VAL E 236 THR E 240 5 5
HELIX 10 10 PRO E 242 ARG E 257 1 16
HELIX 11 11 ARG E 268 SER E 271 1 4
HELIX 12 12 ASP E 287 ILE E 289 5 3
HELIX 13 13 PRO E 303 GLN E 317 1 15
SHEET 1 A 6 VAL D 44 VAL D 46 0
SHEET 2 A 6 PRO D 10 VAL D 14 1 N VAL D 11 O TYR D 45
SHEET 3 A 6 VAL D 81 HIS D 86 1 N ASN D 82 O PRO D 10
SHEET 4 A 6 VAL D 104 ILE D 110 1 N ALA D 105 O VAL D 81
SHEET 5 A 6 GLN D 203 TRP D 209 1 N LEU D 205 O VAL D 107
SHEET 6 A 6 THR D 196 THR D 198 -1 N GLU D 197 O HIS D 204
SSBOND 1 CYS D 190 CYS E 269
SITE 1 ACT 3 SER D 87 HIS E 285 ASP E 263
CRYST1 40.980 43.350 140.690 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 0.024402 0.000000 0.000000 0.00000
SCALE2 0.000000 0.023068 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007108 0.00000
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