| content |
HEADER HYDROLASE 22-AUG-99 1CV2
TITLE HYDROLYTIC HALOALKANE DEHALOGENASE LINB FROM SPHINGOMONAS
TITLE 2 PAUCIMOBILIS UT26 AT 1.6 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LINB, 1,3,4,6-TETRACHLORO-1,4-CYCLOHEXADIENE
COMPND 5 HYDROLASE;
COMPND 6 EC: 3.8.1.5;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SPHINGOMONAS PAUCIMOBILIS;
SOURCE 3 STRAIN: UT26;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_STRAIN: HB101;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PMYLB1
KEYWDS DEHALOGENASE, LINDANE, BIODEGRADATION, ALPHA/BETA-HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.MAREK,J.VEVODOVA,J.DAMBORSKY,I.SMATANOVA,L.A.SVENSSON,
AUTHOR 2 J.NEWMAN,Y.NAGATA,M.TAKAGI
REVDAT 1 11-SEP-00 1CV2 0
JRNL AUTH J.MAREK,J.VEVODOVA,I.SMATANOVA,L.A.SVENSSON,
JRNL AUTH 2 J.NEWMAN,Y.NAGATA,J.DAMBORSKY,M.TAKAGI
JRNL TITL CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE LINB
JRNL TITL 2 FROM SPHINGOMONAS PAUCIMOBILIS UT26 AT 1.6 A
JRNL TITL 3 RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH I.SMATANOVA,Y.NAGATA,L.A.SVENSSON,M.TAKAGI,J.MAREK
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION
REMARK 1 TITL 2 ANALYSIS OF HALOALKANE DEHALOGENASE LINB FROM
REMARK 1 TITL 3 SPHINGOMONAS PAUCIMOBILIS UT26
REMARK 1 REF ACTA CRYSTALLOGR., SECT.D V. 53 1231 1999
REMARK 1 REFN ASTM ABCRE6 DK ISSN 0907-4449
REMARK 2
REMARK 2 RESOLUTION. 1.58 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.58
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.152
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.149
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 1730
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 34513
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.148
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.145
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 1615
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 32485
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2301
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 449
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2749.50
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 0.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 1100
REMARK 3 NUMBER OF RESTRAINTS : 958
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 ANGLE DISTANCES (A) : 0.027
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.027
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.050
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.062
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.014
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : NULL
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.071
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-
REMARK 3 228
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : NULL
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CV2 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-AUG-1999.
REMARK 100 THE RCSB ID CODE IS RCSB009557.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-NOV-1998
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.90
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL 711
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.942
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34649
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.575
REMARK 200 RESOLUTION RANGE LOW (A) : 23.750
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 200 DATA REDUNDANCY : 4.840
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.3100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.57
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.79
REMARK 200 R MERGE FOR SHELL (I) : 0.14600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.980
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: 1BN6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.2
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 19% (W/V) PEG 6000, 100 MM
REMARK 280 TRIS-HCL, 200MM CA ACETATE, PH=8.9
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 1/2-X,1/2+Y,-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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 25.13200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.83450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.13200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.83450
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH 1047 LIES ON A SPECIAL POSITION.
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 MET A 1
REMARK 465 SER A 2
REMARK 465 LEU A 3
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 GLU A 10 CB CG CD OE1 OE2
REMARK 470 ASP A 73 CG OD1 OD2
REMARK 470 GLU A 145 CG CD OE1 OE2
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 PRO A 295 N ALA A 296 C -0.058
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 ARG A 19 CA - C - N ANGL. DEV. = 14.4 DEGREES
REMARK 500 THR A 40 CB - CA - C ANGL. DEV. = 16.6 DEGREES
REMARK 500 THR A 40 N - CA - CB ANGL. DEV. =-23.0 DEGREES
REMARK 500 LEU A 44 CA - CB - CG ANGL. DEV. = 14.4 DEGREES
REMARK 500 ALA A 296 C - N - CA ANGL. DEV. = 41.3 DEGREES
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 1420 DISTANCE = 7.08 ANGSTROMS
REMARK 999
REMARK 999 SEQUENCE REFERENCE :
REMARK 999 NAGATA, Y. ET AL., (1994) J. BACTERIOL. 176, PP 3117-3125
REMARK 999
DBREF 1CV2 A 1 296 GB 4521186 BAA03443 1 296
SEQRES 1 A 296 MET SER LEU GLY ALA LYS PRO PHE GLY GLU LYS LYS PHE
SEQRES 2 A 296 ILE GLU ILE LYS GLY ARG ARG MET ALA TYR ILE ASP GLU
SEQRES 3 A 296 GLY THR GLY ASP PRO ILE LEU PHE GLN HIS GLY ASN PRO
SEQRES 4 A 296 THR SER SER TYR LEU TRP ARG ASN ILE MET PRO HIS CYS
SEQRES 5 A 296 ALA GLY LEU GLY ARG LEU ILE ALA CYS ASP LEU ILE GLY
SEQRES 6 A 296 MET GLY ASP SER ASP LYS LEU ASP PRO SER GLY PRO GLU
SEQRES 7 A 296 ARG TYR ALA TYR ALA GLU HIS ARG ASP TYR LEU ASP ALA
SEQRES 8 A 296 LEU TRP GLU ALA LEU ASP LEU GLY ASP ARG VAL VAL LEU
SEQRES 9 A 296 VAL VAL HIS ASP TRP GLY SER ALA LEU GLY PHE ASP TRP
SEQRES 10 A 296 ALA ARG ARG HIS ARG GLU ARG VAL GLN GLY ILE ALA TYR
SEQRES 11 A 296 MET GLU ALA ILE ALA MET PRO ILE GLU TRP ALA ASP PHE
SEQRES 12 A 296 PRO GLU GLN ASP ARG ASP LEU PHE GLN ALA PHE ARG SER
SEQRES 13 A 296 GLN ALA GLY GLU GLU LEU VAL LEU GLN ASP ASN VAL PHE
SEQRES 14 A 296 VAL GLU GLN VAL LEU PRO GLY LEU ILE LEU ARG PRO LEU
SEQRES 15 A 296 SER GLU ALA GLU MET ALA ALA TYR ARG GLU PRO PHE LEU
SEQRES 16 A 296 ALA ALA GLY GLU ALA ARG ARG PRO THR LEU SER TRP PRO
SEQRES 17 A 296 ARG GLN ILE PRO ILE ALA GLY THR PRO ALA ASP VAL VAL
SEQRES 18 A 296 ALA ILE ALA ARG ASP TYR ALA GLY TRP LEU SER GLU SER
SEQRES 19 A 296 PRO ILE PRO LYS LEU PHE ILE ASN ALA GLU PRO GLY ALA
SEQRES 20 A 296 LEU THR THR GLY ARG MET ARG ASP PHE CYS ARG THR TRP
SEQRES 21 A 296 PRO ASN GLN THR GLU ILE THR VAL ALA GLY ALA HIS PHE
SEQRES 22 A 296 ILE GLN GLU ASP SER PRO ASP GLU ILE GLY ALA ALA ILE
SEQRES 23 A 296 ALA ALA PHE VAL ARG ARG LEU ARG PRO ALA
FORMUL 2 HOH *449(H2 O1)
HELIX 1 1 SER A 42 ALA A 53 5 12
HELIX 2 2 TYR A 82 LEU A 96 1 15
HELIX 3 3 TRP A 109 ARG A 120 1 12
HELIX 4 4 GLU A 145 ARG A 155 1 11
HELIX 5 5 GLY A 159 LEU A 164 1 6
HELIX 6 6 VAL A 168 LEU A 177 1 10
HELIX 7 7 GLU A 184 GLU A 192 1 9
HELIX 8 8 ARG A 202 ILE A 211 1 10
HELIX 9 9 ALA A 218 SER A 234 1 17
HELIX 10 10 THR A 250 ARG A 258 1 9
HELIX 11 11 ILE A 274 ASP A 277 5 4
HELIX 12 12 SER A 278 LEU A 293 1 16
SHEET 1 S1 8 LYS A 12 ILE A 14 0
SHEET 2 S1 8 MET A 21 GLU A 26 -1 N MET A 21 O ILE A 14
SHEET 3 S1 8 ARG A 57 ASP A 62 -1 N ALA A 60 O ILE A 24
SHEET 4 S1 8 ASP A 30 HIS A 36 1 N ILE A 32 O ARG A 57
SHEET 5 S1 8 VAL A 102 HIS A 107 1 N VAL A 103 O PRO A 31
SHEET 6 S1 8 VAL A 125 MET A 131 1 N ALA A 129 O LEU A 104
SHEET 7 S1 8 LYS A 238 PRO A 245 1 N ILE A 241 O TYR A 130
SHEET 8 S1 8 GLN A 263 GLY A 270 1 N THR A 264 O LYS A 238
CISPEP 1 ASN A 38 PRO A 39 0 -2.50
CISPEP 2 ASP A 73 PRO A 74 0 -2.40
CISPEP 3 THR A 216 PRO A 217 0 -3.84
CISPEP 4 GLU A 244 PRO A 245 0 3.01
CISPEP 5 PRO A 295 ALA A 296 0 20.14
CRYST1 50.264 71.669 72.698 90.00 90.00 90.00 P 21 21 2 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 0.019895 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013953 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013755 0.00000
END |