| content |
HEADER LYASE 11-MAR-99 2YAS
TITLE HYDROXYNITRILE LYASE FROM HEVEA BRASILIENSIS COMPLEXED WITH
TITLE 2 RHODANIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYDROXYNITRILE LYASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: OXYNITRILE LYASE;
COMPND 5 EC: 4.2.1.39;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HEVEA BRASILIENSIS;
SOURCE 3 ORGANISM_COMMON: PARA RUBBER TREE;
SOURCE 4 ORGAN: LEAF;
SOURCE 5 GENE: HNL;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: BHIL-D2;
SOURCE 8 EXPRESSION_SYSTEM_GENE: HNL
KEYWDS OXYNITRILASE, CYANOGENESIS, CYANHYDRIN FORMATION, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.GRUBER,M.GUGGANIG,C.KRATKY,K.GRUBER,M.GUGGANIG,C.KRATKY
REVDAT 1 13-OCT-99 2YAS 0
JRNL AUTH J.ZUEGG,K.GRUBER,M.GUGGANIG,U.G.WAGNER,C.KRATKY
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF ENZYME-SUBSTRATE
JRNL TITL 2 COMPLEXES OF THE HYDROXYNITRILE LYASE FROM HEVEA
JRNL TITL 3 BRASILIENSIS
JRNL REF PROTEIN SCI. V. 8 1990 1999
JRNL REFN ASTM PRCIEI US ISSN 0961-8368 0795
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH U.G.WAGNER,M.HASSLACHER,H.GRIENGL,H.SCHWAB,C.KRATKY
REMARK 1 TITL MECHANISM OF CYANOGENESIS: THE CRYSTAL STRUCTURE
REMARK 1 TITL 2 OF HYDROXYNITRILE LYASE FROM HEVEA BRASILIENSIS
REMARK 1 REF STRUCTURE (LONDON) V. 4 811 1996
REMARK 1 REFN ASTM STRUE6 UK ISSN 0969-2126 2005
REMARK 1 REFERENCE 2
REMARK 1 AUTH U.G.WAGNER,M.SCHALL,M.HAYN,M.HASSLACHER,H.SCHWAB,
REMARK 1 AUTH 2 H.S.GRIENGL,C.KRATKY
REMARK 1 TITL CRYSTALLIZATION OF A HYDROXYNITRILE LYASE
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 52 591 1996
REMARK 1 REFN ASTM ABCRE6 DK ISSN 0907-4449 0766
REMARK 1 REFERENCE 3
REMARK 1 AUTH M.HASSLACHER,M.SCHALL,M.HAYN,H.GRIENGL,
REMARK 1 AUTH 2 S.D.KOHLWEIN,H.SCHWAB
REMARK 1 TITL MOLECULAR CLONING OF THE FULL-LENGTH CDNA OF
REMARK 1 TITL 2 (S)-HYDROXYNITRILE LYASE FROM HEVEA BRASILIENSIS.
REMARK 1 TITL 3 FUNCTIONAL EXPRESSION IN ESCHERICHIA COLI AND
REMARK 1 TITL 4 SACCHAROMYCES CEREVISIAE AND IDENTIFICATION OF AN
REMARK 1 TITL 5 ACTIVE SITE RESIDUE
REMARK 1 REF J.BIOL.CHEM. V. 271 5884 1996
REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 0071
REMARK 2
REMARK 2 RESOLUTION. 1.72 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) : 1.72
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 14.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 CROSS-VALIDATION METHOD : FREE R
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) : 0.154
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.150
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 11.100
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 3465
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 31167
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)) : 0.144
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.183
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 11.200
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 3198
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 28574
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2080
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 23
REMARK 3 SOLVENT ATOMS : 334
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2411.50
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 2049.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 5
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 9757
REMARK 3 NUMBER OF RESTRAINTS : 8672
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 ANGLE DISTANCES (A) : 0.025
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.026
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.050
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.052
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.027
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.000
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.054
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-2
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ANISOTROPIC SCALING APPLIED BY
REMARK 3 THE METHOD OF PARKIN, MOEZZI & HOPE, J.APPL.CRYST.28
REMARK 3 (1995)53-56
REMARK 4
REMARK 4 2YAS COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAR-1999.
REMARK 100 THE RCSB ID CODE IS RCSB000639.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-OCT-1998
REMARK 200 TEMPERATURE (KELVIN) : 105.0
REMARK 200 PH : 7.50
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 : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9076
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 : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34663
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.720
REMARK 200 RESOLUTION RANGE LOW (A) : 14.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06600
REMARK 200 FOR THE DATA SET : 18.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.72
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.23700
REMARK 200 FOR SHELL : 5.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: SHELXL-97
REMARK 200 STARTING MODEL: 1YAS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.0
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH=7.5 2 % PEG 400, 2.0 M
REMARK 280 AMMONIUM SULFATE, 20 DEGREES.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,1/2-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 1/2+X,1/2+Y,Z
REMARK 290 6555 1/2-X,1/2-Y,1/2+Z
REMARK 290 7555 1/2-X,1/2+Y,1/2-Z
REMARK 290 8555 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 64.37650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 64.37650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 23.71150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 53.38550
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 23.71150
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 53.38550
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 64.37650
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 23.71150
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 53.38550
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 64.37650
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 23.71150
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 53.38550
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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 509 LIES ON A SPECIAL POSITION.
REMARK 375 HOH 630 LIES ON A SPECIAL POSITION.
REMARK 375 HOH 632 LIES ON A SPECIAL POSITION.
REMARK 375 HOH 689 LIES ON A SPECIAL POSITION.
REMARK 375 HOH 752 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 1
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 SER A 80 CA - C - N ANGL. DEV. = 8.2 DEGREES
REMARK 500 SER A 80 O - C - N ANGL. DEV. =-12.7 DEGREES
REMARK 500 GLY A 193 C - N - CA ANGL. DEV. = 10.8 DEGREES
REMARK 500 GLN A 218 CG - CD - OE1 ANGL. DEV. = 13.7 DEGREES
REMARK 500 GLN A 218 OE1 - CD - NE2 ANGL. DEV. = -8.0 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 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
REMARK 500 SER A 80 55.50 -112.45
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: DSSP, AUTHOR-DETERMINED
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP, AUTHOR-DETERMINED
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 SITE_DESCRIPTION:
REMARK 800 ACTIVE SITE
REMARK 800
DBREF 2YAS A 1 257 SWS P52704 HNL_HEVBR 1 257
SEQRES 1 A 257 MET ALA PHE ALA HIS PHE VAL LEU ILE HIS THR ILE CYS
SEQRES 2 A 257 HIS GLY ALA TRP ILE TRP HIS LYS LEU LYS PRO LEU LEU
SEQRES 3 A 257 GLU ALA LEU GLY HIS LYS VAL THR ALA LEU ASP LEU ALA
SEQRES 4 A 257 ALA SER GLY VAL ASP PRO ARG GLN ILE GLU GLU ILE GLY
SEQRES 5 A 257 SER PHE ASP GLU TYR SER GLU PRO LEU LEU THR PHE LEU
SEQRES 6 A 257 GLU ALA LEU PRO PRO GLY GLU LYS VAL ILE LEU VAL GLY
SEQRES 7 A 257 GLU SER CYS GLY GLY LEU ASN ILE ALA ILE ALA ALA ASP
SEQRES 8 A 257 LYS TYR CYS GLU LYS ILE ALA ALA ALA VAL PHE HIS ASN
SEQRES 9 A 257 SER VAL LEU PRO ASP THR GLU HIS CYS PRO SER TYR VAL
SEQRES 10 A 257 VAL ASP LYS LEU MET GLU VAL PHE PRO ASP TRP LYS ASP
SEQRES 11 A 257 THR THR TYR PHE THR TYR THR LYS ASP GLY LYS GLU ILE
SEQRES 12 A 257 THR GLY LEU LYS LEU GLY PHE THR LEU LEU ARG GLU ASN
SEQRES 13 A 257 LEU TYR THR LEU CYS GLY PRO GLU GLU TYR GLU LEU ALA
SEQRES 14 A 257 LYS MET LEU THR ARG LYS GLY SER LEU PHE GLN ASN ILE
SEQRES 15 A 257 LEU ALA LYS ARG PRO PHE PHE THR LYS GLU GLY TYR GLY
SEQRES 16 A 257 SER ILE LYS LYS ILE TYR VAL TRP THR ASP GLN ASP GLU
SEQRES 17 A 257 ILE PHE LEU PRO GLU PHE GLN LEU TRP GLN ILE GLU ASN
SEQRES 18 A 257 TYR LYS PRO ASP LYS VAL TYR LYS VAL GLU GLY GLY ASP
SEQRES 19 A 257 HIS LYS LEU GLN LEU THR LYS THR LYS GLU ILE ALA GLU
SEQRES 20 A 257 ILE LEU GLN GLU VAL ALA ASP THR TYR ASN
HET SCN 300 3
HET SO4 400 5
HET SO4 401 5
HET SO4 402 5
HET SO4 403 5
HETNAM SCN THIOCYANATE ION
HETNAM SO4 SULFATE ION
FORMUL 2 SCN C1 N1 S1 1-
FORMUL 3 SO4 4(O4 S1 2-)
FORMUL 7 HOH *334(H2 O1)
HELIX 1 1 ALA A 16 TRP A 19 5 4
HELIX 2 2 LEU A 22 LEU A 29 1 8
HELIX 3 3 ILE A 48 GLU A 50 5 3
HELIX 4 4 PHE A 54 TYR A 57 1 4
HELIX 5 5 GLU A 59 GLU A 66 1 8
HELIX 6 6 SER A 80 LYS A 96 5 17
HELIX 7 7 TYR A 116 VAL A 124 1 9
HELIX 8 8 PHE A 150 ASN A 156 1 7
HELIX 9 9 PRO A 163 LEU A 172 1 10
HELIX 10 10 GLN A 180 LYS A 185 1 6
HELIX 11 11 TYR A 194 SER A 196 5 3
HELIX 12 12 PRO A 212 ASN A 221 1 10
HELIX 13 13 LEU A 237 THR A 240 1 4
HELIX 14 14 THR A 242 THR A 255 1 14
SHEET 1 A 6 LYS A 32 ALA A 35 0
SHEET 2 A 6 HIS A 5 ILE A 9 1 N PHE A 6 O LYS A 32
SHEET 3 A 6 VAL A 74 GLU A 79 1 N ILE A 75 O VAL A 7
SHEET 4 A 6 ILE A 97 HIS A 103 1 N ALA A 98 O VAL A 74
SHEET 5 A 6 LYS A 199 TRP A 203 1 N ILE A 200 O ALA A 100
SHEET 6 A 6 LYS A 226 LYS A 229 1 N LYS A 226 O TYR A 201
SHEET 1 B 2 THR A 132 LYS A 138 0
SHEET 2 B 2 LYS A 141 LYS A 147 -1 N LYS A 147 O THR A 132
SITE 1 CAT 3 SER A 80 ASP A 207 HIS A 235
CRYST1 47.423 106.771 128.753 90.00 90.00 90.00 C 2 2 21 8
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 0.021087 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009366 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007767 0.00000 |