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HEADER HYDROLASE (SERINE ESTERASE) 16-NOV-95 1CUD
TITLE CUTINASE, N172K, R196D MUTANT, MONOCLINIC CRYSTAL FORM WITH
TITLE 2 THREE MOLECULES PER ASYMMETRIC UNIT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: N172K, R196E;
COMPND 7 OTHER_DETAILS: FORM III CRYSTAL (MONOCLINIC, 3 MOLECULES
COMPND 8 PER ASYMMETRIC UNIT)
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: FUSARIUM SOLANI PISI;
SOURCE 3 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 4 EXPRESSION_SYSTEM_PLASMID: PUC19
KEYWDS HYDROLASE, SERINE ESTERASE, GLYCOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.LONGHI,C.CAMBILLAU
REVDAT 1 11-JUL-96 1CUD 0
JRNL AUTH S.LONGHI,A.NICOLAS,L.CREVELD,M.EGMOND,C.T.VERRIPS,
JRNL AUTH 2 J.DE VLIEG,C.MARTINEZ,C.CAMBILLAU
JRNL TITL DYNAMICS OF FUSARIUM SOLANI CUTINASE INVESTIGATED
JRNL TITL 2 THROUGH STRUCTURAL COMPARISON AMONG DIFFERENT
JRNL TITL 3 CRYSTAL FORMS OF ITS VARIANTS
JRNL REF TO BE PUBLISHED REF NOW ASSIGNED AS
JRNL REFN 0353
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.NICOLAS,M.EGMOND,C.T.VERRIPS,J.DE VLIEG,S.LONGHI,
REMARK 1 AUTH 2 C.CAMBILLAU,C.MARTINEZ
REMARK 1 TITL CONTRIBUTION OF CUTINASE SER 42 SIDE-CHAIN TO THE
REMARK 1 TITL 2 STABILIZATION OF THE OXYANION TRANSITION STATE
REMARK 1 REF TO BE PUBLISHED REF NOW ASSIGNED AS
REMARK 1 REFN 0353
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.MARTINEZ,A.NICOLAS,H.VAN TILBEURGH,M.P.EGLOFF,
REMARK 1 AUTH 2 C.CUDREY,R.VERGER,C.CAMBILLAU
REMARK 1 TITL CUTINASE, A LIPOLYTIC ENZYME WITH A PREFORMED
REMARK 1 TITL 2 OXYANION HOLE
REMARK 1 REF BIOCHEMISTRY V. 33 83 1994
REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 0033
REMARK 1 REFERENCE 3
REMARK 1 AUTH C.MARTINEZ,P.DE GEUS,P.STANSSENS,M.LAUWEREYS,
REMARK 1 AUTH 2 C.CAMBILLAU
REMARK 1 TITL ENGINEERING CYSTEINE MUTANTS TO OBTAIN
REMARK 1 TITL 2 CRYSTALLOGRAPHIC PHASES WITH A CUTINASE FROM
REMARK 1 TITL 3 FUSARIUM SOLANI PISI
REMARK 1 REF PROTEIN ENG. V. 6 157 1993
REMARK 1 REFN ASTM PRENE9 UK ISSN 0269-2139 0859
REMARK 1 REFERENCE 4
REMARK 1 AUTH C.MARTINEZ,P.DE GEUS,M.LAUWEREYS,G.MATTHYSSENS,
REMARK 1 AUTH 2 C.CAMBILLAU
REMARK 1 TITL FUSARIUM SOLANI CUTINASE IS A LIPOLYTIC ENZYME
REMARK 1 TITL 2 WITH A CATALYTIC SERINE ACCESSIBLE TO SOLVENT
REMARK 1 REF NATURE V. 356 615 1992
REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 0006
REMARK 2
REMARK 2 RESOLUTION. 2.70 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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 15469
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) : 0.141
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 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 COMPLETENESS IN THIS BIN (%) : 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 : 5322
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 1452
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
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : 1.92
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : 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 0 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 0 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:
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS MOLECULE A (A) : 0.014
REMARK 3 BOND ANGLES MOLECULE A (DEGREES) : 1.92
REMARK 3 BOND LENGTHS MOLECULE B (A) : 0.014
REMARK 3 BOND ANGLES MOLECULE B (DEGREES) : 1.92
REMARK 3 BOND LENGTHS MOLECULE C (A) : 0.014
REMARK 3 BOND ANGLES MOLECULE C (DEGREES) : 1.92
REMARK 3
REMARK 3 MEAN B (ANGSTROMS**2) MOLECULE A : MAIN : 9.7
REMARK 3 MEAN B (ANGSTROMS**2) MOLECULE A : SIDE : 11.3
REMARK 3 MEAN B (ANGSTROMS**2) MOLECULE A : SOLV : 28.9
REMARK 3
REMARK 3 MEAN B (ANGSTROMS**2) MOLECULE B : MAIN : 12.2
REMARK 3 MEAN B (ANGSTROMS**2) MOLECULE B : SIDE : 13.8
REMARK 3 MEAN B (ANGSTROMS**2) MOLECULE B : SOLV : 32.8
REMARK 3
REMARK 3 MEAN B (ANGSTROMS**2) MOLECULE C : MAIN : 25.3
REMARK 3 MEAN B (ANGSTROMS**2) MOLECULE C : SIDE : 26.1
REMARK 3 MEAN B (ANGSTROMS**2) MOLECULE C : SOLV : 38.8
REMARK 4
REMARK 4 1CUD COMPLIES WITH FORMAT V. 2.0, 16-FEB-1996
REMARK 6
REMARK 6 SER 120:
REMARK 6 THE "EPSILON" CONFORMATION OF THE CATALYTIC SERINE IS A
REMARK 6 TYPICAL FEATURE OF THE ALPHA/BETA HYDROLASE FAMILY, WHICH
REMARK 6 CUTINASE BELONGS TO.
REMARK 7
REMARK 7 THE FIRST 16 N-TERMINAL RESIDUES AND LAST C-TERMINAL
REMARK 7 RESIDUE ARE NOT OBSERVED IN THE ELECTRON DENSITY. THEY
REMARK 7 ARE NOT INCLUDED IN THIS ENTRY.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200 ROTATING
REMARK 200 ANODE
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE CRYSTAL
REMARK 200 OPTICS : COLLIMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE (18CM)
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR XDS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16170
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 200 DATA REDUNDANCY : 4.9 %
REMARK 200 R MERGE (I) : 0.173
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: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 280 CRYSTAL FORMS OF THIS MUTANT. THE THREE FORMS ARE
REMARK 280 REFERRED TO AS N172K,R196E_I, N172K,R196E_II,
REMARK 280 N172K,R196E_III BY THE AUTHORS.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
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
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 36.64883
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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 MSSS
REMARK 295 M 1 A 17 .. 213 B 17 .. 213 0.653
REMARK 295 M 2 A 17 .. 213 C 17 .. 213 2.075
REMARK 295 M 3 B 17 .. 213 C 17 .. 213 0.658
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.
REMARK 500
REMARK 500 DISTANCE CUTOFF: 2.2 ANGSTROMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 2H HOH A 969 2HH1 ARG A 211 2556 1.37
REMARK 500 2HH1 ARG A 211 2H HOH A 969 2546 1.37
REMARK 500 1H HOH A 596 3HZ LYS B 206 2545 1.41
REMARK 500 3HZ LYS B 206 1H HOH A 596 2555 1.41
REMARK 500 2HH1 ARG C 96 1H HOH A 949 1564 1.46
REMARK 500 1H HOH A 949 2HH1 ARG C 96 1546 1.46
REMARK 500 2H HOH C 958 2HH1 ARG A 208 1564 1.50
REMARK 500 2HH1 ARG A 208 2H HOH C 958 1546 1.50
REMARK 500 2H HOH C 965 1H HOH A 813 2555 1.60
REMARK 500 1H HOH A 813 2H HOH C 965 2545 1.60
REMARK 500 HE ARG B 78 1H HOH A 814 2556 1.65
REMARK 500 1H HOH A 814 HE ARG B 78 2546 1.65
REMARK 500 1H HOH B 814 O HOH A 597 2555 1.66
REMARK 500 O HOH A 597 1H HOH B 814 2545 1.66
REMARK 500 2H HOH A 553 O HOH B 630 2545 1.70
REMARK 500 O HOH C 982 2H HOH A 680 2655 1.70
REMARK 500 2H HOH A 680 O HOH C 982 2645 1.70
REMARK 500 1H HOH C 642 O HOH B 808 2555 1.70
REMARK 500 O HOH B 630 2H HOH A 553 2555 1.70
REMARK 500 O HOH B 808 1H HOH C 642 2545 1.70
REMARK 500 1HH1 ARG A 78 2H HOH B 814 2545 1.72
REMARK 500 2H HOH B 814 1HH1 ARG A 78 2555 1.72
REMARK 500 HG SER A 213 O THR A 179 2546 1.76
REMARK 500 2HH1 ARG B 158 2HH1 ARG C 208 1455 1.76
REMARK 500 2HH1 ARG C 208 2HH1 ARG B 158 1655 1.76
REMARK 500 O THR A 179 HG SER A 213 2556 1.76
REMARK 500 2H HOH A 596 3HZ LYS B 206 2545 1.78
REMARK 500 3HZ LYS B 206 2H HOH A 596 2555 1.78
REMARK 500 2HZ LYS B 108 1H HOH A 504 1565 1.78
REMARK 500 1H HOH A 504 2HZ LYS B 108 1545 1.78
REMARK 500 O GLY A 174 1H HOH A 981 2556 1.79
REMARK 500 O HOH A 815 1H HOH B 642 2546 1.79
REMARK 500 1H HOH A 981 O GLY A 174 2546 1.79
REMARK 500 1H HOH B 642 O HOH A 815 2556 1.79
REMARK 500 O HOH B 585 H ASP C 21 2645 1.82
REMARK 500 O HOH A 519 1H HOH C 982 2645 1.82
REMARK 500 1H HOH C 982 O HOH A 519 2655 1.82
REMARK 500 1H HOH B 633 O HOH B 959 2555 1.82
REMARK 500 HG1 THR A 113 O HOH A 961 2546 1.82
REMARK 500 O HOH B 959 1H HOH B 633 2545 1.82
REMARK 500 O HOH A 961 HG1 THR A 113 2556 1.82
REMARK 500 H ASP C 21 O HOH B 585 2655 1.82
REMARK 500 O HOH A 813 2H HOH C 960 2545 1.83
REMARK 500 O HOH A 593 1H HOH B 550 2546 1.83
REMARK 500 1H HOH B 550 O HOH A 593 2556 1.83
REMARK 500 2H HOH C 960 O HOH A 813 2555 1.83
REMARK 500 H GLY B 174 O HOH B 966 2545 1.84
REMARK 500 O HOH B 966 H GLY B 174 2555 1.84
REMARK 500 H THR A 45 O ALA C 29 2645 1.85
REMARK 500 2H HOH B 522 O ILE A 24 1565 1.85
REMARK 500 2H HOH C 809 O SER A 213 1564 1.85
REMARK 500 O ILE A 24 2H HOH B 522 1545 1.85
REMARK 500 2H HOH B 537 O HOH B 927 2555 1.85
REMARK 500 O HOH B 927 2H HOH B 537 2545 1.85
REMARK 500 O SER A 213 2H HOH C 809 1546 1.85
REMARK 500 O ALA C 29 H THR A 45 2655 1.85
REMARK 500 2H HOH B 644 O HOH B 588 2555 1.86
REMARK 500 2H HOH B 647 2H HOH C 815 1455 1.86
REMARK 500 2H HOH C 815 2H HOH B 647 1655 1.86
REMARK 500 O HOH B 588 2H HOH B 644 2545 1.86
REMARK 500 1H HOH C 537 O HOH B 691 2645 1.88
REMARK 500 O HOH B 691 1H HOH C 537 2655 1.88
REMARK 500 O GLN A 154 1H HOH C 559 2545 1.89
REMARK 500 1H HOH C 559 O GLN A 154 2555 1.89
REMARK 500 O ALA B 209 1H HOH B 714 2555 1.89
REMARK 500 O HOH C 958 2HH1 ARG A 208 1564 1.89
REMARK 500 1H HOH B 714 O ALA B 209 2545 1.89
REMARK 500 2HH1 ARG A 208 O HOH C 958 1546 1.89
REMARK 500 2HH1 ARG A 211 O HOH A 969 2546 1.90
REMARK 500 3HZ LYS B 206 O HOH A 596 2555 1.90
REMARK 500 O HOH A 596 3HZ LYS B 206 2545 1.90
REMARK 500 1H HOH A 603 O CYS C 31 2645 1.90
REMARK 500 O HOH A 969 2HH1 ARG A 211 2556 1.90
REMARK 500 O CYS C 31 1H HOH A 603 2655 1.90
REMARK 500 O HOH C 518 1H HOH B 585 2655 1.91
REMARK 500 1H HOH B 585 O HOH C 518 2645 1.91
REMARK 500 2H HOH B 588 OG1 THR B 113 2545 1.91
REMARK 500 OG1 THR B 113 2H HOH B 588 2555 1.91
REMARK 500 H GLY A 46 O HOH C 984 2645 1.91
REMARK 500 O HOH C 984 H GLY A 46 2655 1.91
REMARK 500 1H HOH C 560 1HH1 ARG A 156 2555 1.92
REMARK 500 H CYS C 31 OG1 THR A 45 2655 1.92
REMARK 500 1HH1 ARG A 156 1H HOH C 560 2545 1.92
REMARK 500 OG1 THR A 45 H CYS C 31 2645 1.92
REMARK 500 1H HOH A 949 2H HOH C 553 1546 1.93
REMARK 500 1H HOH A 814 1H HOH B 957 2546 1.93
REMARK 500 1H HOH B 957 1H HOH A 814 2556 1.93
REMARK 500 2H HOH C 553 1H HOH A 949 1564 1.93
REMARK 500 O HOH A 609 1H HOH B 694 2546 1.94
REMARK 500 HG1 THR A 18 O HOH C 618 2645 1.94
REMARK 500 OG SER C 92 2H HOH B 808 2555 1.94
REMARK 500 1H HOH B 694 O HOH A 609 2556 1.94
REMARK 500 O HOH C 618 HG1 THR A 18 2655 1.94
REMARK 500 2H HOH B 808 OG SER C 92 2545 1.94
REMARK 500 1H HOH B 504 O HOH A 954 1565 1.94
REMARK 500 O HOH A 954 1H HOH B 504 1545 1.94
REMARK 500 1H HOH A 949 O HOH C 553 1546 1.95
REMARK 500 O HOH B 658 2H HOH A 693 2555 1.95
REMARK 500 2H HOH A 693 O HOH B 658 2545 1.95
REMARK 500 O HOH C 553 1H HOH A 949 1564 1.95
REMARK 500 2HE2 GLN C 154 O HOH A 900 2555 1.96
REMARK 500 O HOH B 972 1H HOH C 633 1455 1.96
REMARK 500 1H HOH C 633 O HOH B 972 1655 1.96
REMARK 500 O HOH A 900 2HE2 GLN C 154 2545 1.96
REMARK 500 1H HOH C 601 O HOH B 919 2655 1.97
REMARK 500 1HH1 ARG B 158 2HH1 ARG C 208 1455 1.97
REMARK 500 O HOH B 919 1H HOH C 601 2645 1.97
REMARK 500 2HH1 ARG C 208 1HH1 ARG B 158 1655 1.97
REMARK 500 O HOH A 637 1H HOH C 645 1546 1.98
REMARK 500 1H HOH C 645 O HOH A 637 1564 1.98
REMARK 500 1H HOH C 537 2H HOH B 691 2645 1.98
REMARK 500 2H HOH B 691 1H HOH C 537 2655 1.98
REMARK 500 OD1 ASN A 106 2H HOH A 810 2546 1.99
REMARK 500 2H HOH C 965 O HOH A 813 2555 1.99
REMARK 500 2HH2 ARG B 156 NH2 ARG C 208 1455 1.99
REMARK 500 O HOH A 813 2H HOH C 965 2545 1.99
REMARK 500 O HOH C 965 1H HOH A 813 2555 1.99
REMARK 500 2H HOH A 618 2H HOH C 645 1546 1.99
REMARK 500 2H HOH C 645 2H HOH A 618 1564 1.99
REMARK 500 1H HOH A 813 O HOH C 965 2545 1.99
REMARK 500 2H HOH A 810 OD1 ASN A 106 2556 1.99
REMARK 500 NH2 ARG C 208 2HH2 ARG B 156 1655 1.99
REMARK 500 1H HOH A 953 1H HOH B 677 1545 2.00
REMARK 500 2H HOH B 505 H LYS C 65 1455 2.00
REMARK 500 H LYS C 65 2H HOH B 505 1655 2.00
REMARK 500 1H HOH B 677 1H HOH A 953 1565 2.00
REMARK 500 O HOH B 588 2H HOH B 966 2545 2.01
REMARK 500 2H HOH B 966 O HOH B 588 2555 2.01
REMARK 500 2H HOH B 608 O HOH C 907 2645 2.01
REMARK 500 HG1 THR A 45 O SER C 28 2645 2.01
REMARK 500 O HOH B 966 2H HOH A 976 2555 2.01
REMARK 500 2H HOH A 976 O HOH B 966 2545 2.01
REMARK 500 O HOH C 907 2H HOH B 608 2655 2.01
REMARK 500 O SER C 28 HG1 THR A 45 2655 2.01
REMARK 500 1H HOH B 805 O HOH B 558 2545 2.02
REMARK 500 O HOH A 926 1H HOH A 946 2556 2.02
REMARK 500 1H HOH A 970 O ASP A 139 2556 2.02
REMARK 500 1HH2 ARG C 208 2HH2 ARG B 156 1655 2.02
REMARK 500 O HOH B 943 H ASN C 27 2645 2.02
REMARK 500 O HOH B 558 1H HOH B 805 2555 2.02
REMARK 500 O HOH B 976 2H HOH C 907 2645 2.02
REMARK 500 2H HOH B 655 O SER C 213 2655 2.02
REMARK 500 O SER C 213 2H HOH B 655 2645 2.02
REMARK 500 2H HOH C 907 O HOH B 976 2655 2.02
REMARK 500 1H HOH B 550 1H HOH A 593 2556 2.02
REMARK 500 1H HOH B 810 O ALA B 136 2545 2.02
REMARK 500 1H HOH A 593 1H HOH B 550 2546 2.02
REMARK 500 O ALA B 136 1H HOH B 810 2555 2.02
REMARK 500 O ASP A 139 1H HOH A 970 2546 2.02
REMARK 500 1H HOH A 946 O HOH A 926 2546 2.02
REMARK 500 H ASN C 27 O HOH B 943 2655 2.02
REMARK 500 2HH2 ARG B 156 1HH2 ARG C 208 1455 2.02
REMARK 500 1H HOH C 553 1H HOH A 949 1564 2.05
REMARK 500 O HOH B 647 2H HOH C 815 1455 2.05
REMARK 500 1H HOH A 949 1H HOH C 553 1546 2.05
REMARK 500 2H HOH C 815 O HOH B 647 1655 2.05
REMARK 500 2H HOH C 982 2H HOH A 680 2655 2.05
REMARK 500 2H HOH A 680 2H HOH C 982 2645 2.05
REMARK 500 1H HOH B 677 O HOH A 953 1565 2.06
REMARK 500 2H HOH C 602 2H HOH B 980 2655 2.06
REMARK 500 1H HOH A 969 2HH1 ARG A 211 2556 2.06
REMARK 500 2H HOH B 980 2H HOH C 602 2645 2.06
REMARK 500 O HOH A 953 1H HOH B 677 1545 2.06
REMARK 500 2HH1 ARG A 211 1H HOH A 969 2546 2.06
REMARK 500 1H HOH B 957 O HOH A 814 2556 2.07
REMARK 500 O HOH A 814 1H HOH B 957 2546 2.07
REMARK 500 1H HOH A 940 O HOH B 677 1545 2.08
REMARK 500 O HOH B 677 1H HOH A 940 1565 2.08
REMARK 500 1H HOH B 588 2H HOH B 644 2545 2.08
REMARK 500 2H HOH B 644 1H HOH B 588 2555 2.08
REMARK 500 1H HOH B 658 2H HOH A 693 2555 2.09
REMARK 500 O HOH A 571 2H HOH C 808 2545 2.09
REMARK 500 2H HOH C 808 O HOH A 571 2555 2.09
REMARK 500 2H HOH A 693 1H HOH B 658 2545 2.09
REMARK 500 OD1 ASN A 161 1H HOH C 564 2545 2.09
REMARK 500 1H HOH C 564 OD1 ASN A 161 2555 2.09
REMARK 500 O HOH C 963 1H HOH A 539 2655 2.10
REMARK 500 2H HOH C 950 O SER A 61 1564 2.10
REMARK 500 O SER A 61 2H HOH C 950 1546 2.10
REMARK 500 1H HOH A 539 O HOH C 963 2645 2.10
REMARK 500 O ALA B 29 HG SER C 213 2655 2.10
REMARK 500 HG SER C 213 O ALA B 29 2645 2.10
REMARK 500 2H HOH B 551 O HOH A 669 2556 2.10
REMARK 500 3HZ LYS A 168 2H HOH B 694 2546 2.10
REMARK 500 NH1 ARG B 158 2HH1 ARG C 208 1455 2.10
REMARK 500 O HOH A 669 2H HOH B 551 2546 2.10
REMARK 500 2H HOH B 694 3HZ LYS A 168 2556 2.10
REMARK 500 2HH1 ARG C 208 NH1 ARG B 158 1655 2.10
REMARK 500 1H HOH A 519 1H HOH C 982 2645 2.11
REMARK 500 1H HOH C 982 1H HOH A 519 2655 2.11
REMARK 500 O HOH C 602 2H HOH B 980 2655 2.11
REMARK 500 NZ LYS B 206 1H HOH A 596 2555 2.11
REMARK 500 HE ARG B 208 O HOH B 959 2555 2.11
REMARK 500 1H HOH A 596 NZ LYS B 206 2545 2.11
REMARK 500 O HOH B 959 HE ARG B 208 2545 2.11
REMARK 500 2H HOH B 980 O HOH C 602 2645 2.11
REMARK 500 O HOH A 814 HE ARG B 78 2546 2.12
REMARK 500 2H HOH A 645 2H HOH B 975 2545 2.12
REMARK 500 2H HOH B 975 2H HOH A 645 2555 2.12
REMARK 500 1H HOH A 949 NH1 ARG C 96 1546 2.12
REMARK 500 NH1 ARG C 96 1H HOH A 949 1564 2.12
REMARK 500 1HH1 ARG A 156 O HOH C 560 2545 2.12
REMARK 500 O HOH C 560 1HH1 ARG A 156 2555 2.12
REMARK 500 HE ARG B 78 O HOH A 814 2556 2.12
REMARK 500 2H HOH B 663 O HOH C 638 1455 2.13
REMARK 500 H LYS C 65 O HOH B 505 1655 2.13
REMARK 500 O HOH B 505 H LYS C 65 1455 2.13
REMARK 500 2HH2 ARG C 208 1HH1 ARG B 158 1655 2.13
REMARK 500 1HH1 ARG B 158 2HH2 ARG C 208 1455 2.13
REMARK 500 2H HOH A 618 O HOH C 645 1546 2.13
REMARK 500 O HOH C 645 2H HOH A 618 1564 2.13
REMARK 500 O HOH C 638 2H HOH B 663 1655 2.13
REMARK 500 1H HOH B 551 O HOH A 590 2556 2.14
REMARK 500 1H HOH B 677 1H HOH A 695 1565 2.14
REMARK 500 O HOH A 590 1H HOH B 551 2546 2.14
REMARK 500 1H HOH A 695 1H HOH B 677 1545 2.14
REMARK 500 1H HOH C 642 1H HOH B 808 2555 2.16
REMARK 500 1H HOH B 808 1H HOH C 642 2545 2.16
REMARK 500 1H HOH B 633 1H HOH B 959 2555 2.16
REMARK 500 1H HOH B 959 1H HOH B 633 2545 2.16
REMARK 500 O GLY C 75 2H HOH B 686 2655 2.16
REMARK 500 2H HOH B 686 O GLY C 75 2645 2.16
REMARK 500 2H HOH B 966 2H HOH B 588 2555 2.17
REMARK 500 O SER C 213 1H HOH B 649 1655 2.17
REMARK 500 1H HOH B 649 O SER C 213 1455 2.17
REMARK 500 2H HOH B 588 2H HOH B 966 2545 2.17
REMARK 500 1H HOH B 708 O GLU C 60 1455 2.19
REMARK 500 O GLU C 60 1H HOH B 708 1655 2.19
REMARK 500 1H HOH B 585 H ASP C 21 2645 2.19
REMARK 500 H ASP C 21 1H HOH B 585 2655 2.19
REMARK 500 1HH2 ARG B 208 O HOH B 959 2555 2.20
REMARK 500 O HOH B 959 1HH2 ARG B 208 2545 2.20
REMARK 500 2H HOH B 608 2H HOH C 907 2645 2.20
REMARK 500 2H HOH C 907 2H HOH B 608 2655 2.20
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAA
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD, CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: CAB
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD, CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: CAC
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD, CHAIN C
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1CUD A SWS P00590 1 - 32 NOT IN ATOMS LIST
REMARK 999 1CUD A SWS P00590 230 - 230 NOT IN ATOMS LIST
REMARK 999 1CUD B SWS P00590 1 - 32 NOT IN ATOMS LIST
REMARK 999 1CUD B SWS P00590 230 - 230 NOT IN ATOMS LIST
REMARK 999 1CUD C SWS P00590 1 - 32 NOT IN ATOMS LIST
REMARK 999 1CUD C SWS P00590 230 - 230 NOT IN ATOMS LIST
DBREF 1CUD A 17 213 SWS P00590 CUTI_FUSSO 33 229
DBREF 1CUD B 17 213 SWS P00590 CUTI_FUSSO 33 229
DBREF 1CUD C 17 213 SWS P00590 CUTI_FUSSO 33 229
SEQADV 1CUD ALA A 32 SWS P00590 ARG 48 CONFLICT
SEQADV 1CUD LYS A 172 SWS P00590 ASN 188 ENGINEERED
SEQADV 1CUD GLU A 196 SWS P00590 ARG 212 ENGINEERED
SEQADV 1CUD ALA B 32 SWS P00590 ARG 48 CONFLICT
SEQADV 1CUD LYS B 172 SWS P00590 ASN 188 ENGINEERED
SEQADV 1CUD GLU B 196 SWS P00590 ARG 212 ENGINEERED
SEQADV 1CUD ALA C 32 SWS P00590 ARG 48 CONFLICT
SEQADV 1CUD LYS C 172 SWS P00590 ASN 188 ENGINEERED
SEQADV 1CUD GLU C 196 SWS P00590 ARG 212 ENGINEERED
SEQRES 1 A 214 LEU PRO THR SER ASN PRO ALA GLN GLU LEU GLU ALA ARG
SEQRES 2 A 214 GLN LEU GLY ARG THR THR ARG ASP ASP LEU ILE ASN GLY
SEQRES 3 A 214 ASN SER ALA SER CYS ALA ASP VAL ILE PHE ILE TYR ALA
SEQRES 4 A 214 ARG GLY SER THR GLU THR GLY ASN LEU GLY THR LEU GLY
SEQRES 5 A 214 PRO SER ILE ALA SER ASN LEU GLU SER ALA PHE GLY LYS
SEQRES 6 A 214 ASP GLY VAL TRP ILE GLN GLY VAL GLY GLY ALA TYR ARG
SEQRES 7 A 214 ALA THR LEU GLY ASP ASN ALA LEU PRO ARG GLY THR SER
SEQRES 8 A 214 SER ALA ALA ILE ARG GLU MET LEU GLY LEU PHE GLN GLN
SEQRES 9 A 214 ALA ASN THR LYS CYS PRO ASP ALA THR LEU ILE ALA GLY
SEQRES 10 A 214 GLY TYR SER GLN GLY ALA ALA LEU ALA ALA ALA SER ILE
SEQRES 11 A 214 GLU ASP LEU ASP SER ALA ILE ARG ASP LYS ILE ALA GLY
SEQRES 12 A 214 THR VAL LEU PHE GLY TYR THR LYS ASN LEU GLN ASN ARG
SEQRES 13 A 214 GLY ARG ILE PRO ASN TYR PRO ALA ASP ARG THR LYS VAL
SEQRES 14 A 214 PHE CYS LYS THR GLY ASP LEU VAL CYS THR GLY SER LEU
SEQRES 15 A 214 ILE VAL ALA ALA PRO HIS LEU ALA TYR GLY PRO ASP ALA
SEQRES 16 A 214 GLU GLY PRO ALA PRO GLU PHE LEU ILE GLU LYS VAL ARG
SEQRES 17 A 214 ALA VAL ARG GLY SER ALA
SEQRES 1 B 214 LEU PRO THR SER ASN PRO ALA GLN GLU LEU GLU ALA ARG
SEQRES 2 B 214 GLN LEU GLY ARG THR THR ARG ASP ASP LEU ILE ASN GLY
SEQRES 3 B 214 ASN SER ALA SER CYS ALA ASP VAL ILE PHE ILE TYR ALA
SEQRES 4 B 214 ARG GLY SER THR GLU THR GLY ASN LEU GLY THR LEU GLY
SEQRES 5 B 214 PRO SER ILE ALA SER ASN LEU GLU SER ALA PHE GLY LYS
SEQRES 6 B 214 ASP GLY VAL TRP ILE GLN GLY VAL GLY GLY ALA TYR ARG
SEQRES 7 B 214 ALA THR LEU GLY ASP ASN ALA LEU PRO ARG GLY THR SER
SEQRES 8 B 214 SER ALA ALA ILE ARG GLU MET LEU GLY LEU PHE GLN GLN
SEQRES 9 B 214 ALA ASN THR LYS CYS PRO ASP ALA THR LEU ILE ALA GLY
SEQRES 10 B 214 GLY TYR SER GLN GLY ALA ALA LEU ALA ALA ALA SER ILE
SEQRES 11 B 214 GLU ASP LEU ASP SER ALA ILE ARG ASP LYS ILE ALA GLY
SEQRES 12 B 214 THR VAL LEU PHE GLY TYR THR LYS ASN LEU GLN ASN ARG
SEQRES 13 B 214 GLY ARG ILE PRO ASN TYR PRO ALA ASP ARG THR LYS VAL
SEQRES 14 B 214 PHE CYS LYS THR GLY ASP LEU VAL CYS THR GLY SER LEU
SEQRES 15 B 214 ILE VAL ALA ALA PRO HIS LEU ALA TYR GLY PRO ASP ALA
SEQRES 16 B 214 GLU GLY PRO ALA PRO GLU PHE LEU ILE GLU LYS VAL ARG
SEQRES 17 B 214 ALA VAL ARG GLY SER ALA
SEQRES 1 C 214 LEU PRO THR SER ASN PRO ALA GLN GLU LEU GLU ALA ARG
SEQRES 2 C 214 GLN LEU GLY ARG THR THR ARG ASP ASP LEU ILE ASN GLY
SEQRES 3 C 214 ASN SER ALA SER CYS ALA ASP VAL ILE PHE ILE TYR ALA
SEQRES 4 C 214 ARG GLY SER THR GLU THR GLY ASN LEU GLY THR LEU GLY
SEQRES 5 C 214 PRO SER ILE ALA SER ASN LEU GLU SER ALA PHE GLY LYS
SEQRES 6 C 214 ASP GLY VAL TRP ILE GLN GLY VAL GLY GLY ALA TYR ARG
SEQRES 7 C 214 ALA THR LEU GLY ASP ASN ALA LEU PRO ARG GLY THR SER
SEQRES 8 C 214 SER ALA ALA ILE ARG GLU MET LEU GLY LEU PHE GLN GLN
SEQRES 9 C 214 ALA ASN THR LYS CYS PRO ASP ALA THR LEU ILE ALA GLY
SEQRES 10 C 214 GLY TYR SER GLN GLY ALA ALA LEU ALA ALA ALA SER ILE
SEQRES 11 C 214 GLU ASP LEU ASP SER ALA ILE ARG ASP LYS ILE ALA GLY
SEQRES 12 C 214 THR VAL LEU PHE GLY TYR THR LYS ASN LEU GLN ASN ARG
SEQRES 13 C 214 GLY ARG ILE PRO ASN TYR PRO ALA ASP ARG THR LYS VAL
SEQRES 14 C 214 PHE CYS LYS THR GLY ASP LEU VAL CYS THR GLY SER LEU
SEQRES 15 C 214 ILE VAL ALA ALA PRO HIS LEU ALA TYR GLY PRO ASP ALA
SEQRES 16 C 214 GLU GLY PRO ALA PRO GLU PHE LEU ILE GLU LYS VAL ARG
SEQRES 17 C 214 ALA VAL ARG GLY SER ALA
FORMUL 4 HOH *484(H2 O1)
HELIX 1 1 SER A 28 SER A 30 5 3
HELIX 2 2 GLY A 52 PHE A 63 1 12
HELIX 3 3 LYS A 65 GLY A 67 5 3
HELIX 4 4 ASP A 83 ALA A 85 5 3
HELIX 5 5 SER A 92 LYS A 108 1 17
HELIX 6 6 GLN A 121 ASP A 132 1 12
HELIX 7 7 SER A 135 ARG A 138 1 4
HELIX 8 8 ALA A 164 ARG A 166 5 3
HELIX 9 9 LEU A 176 CYS A 178 5 3
HELIX 10 10 ALA A 186 LEU A 189 5 4
HELIX 11 11 GLY A 192 GLU A 196 1 5
HELIX 12 12 PRO A 198 ARG A 211 1 14
HELIX 13 13 SER B 28 SER B 30 5 3
HELIX 14 14 GLY B 49 PHE B 63 1 15
HELIX 15 15 LEU B 81 ALA B 85 5 5
HELIX 16 16 SER B 92 LYS B 108 1 17
HELIX 17 17 GLN B 121 ILE B 130 1 10
HELIX 18 18 SER B 135 ARG B 138 1 4
HELIX 19 19 ALA B 186 LEU B 189 5 4
HELIX 20 20 GLY B 192 GLU B 196 1 5
HELIX 21 21 PRO B 198 ARG B 211 1 14
HELIX 22 22 SER C 28 SER C 30 5 3
HELIX 23 23 GLY C 52 PHE C 63 1 12
HELIX 24 24 LYS C 65 GLY C 67 5 3
HELIX 25 25 LEU C 81 ALA C 85 5 5
HELIX 26 26 SER C 92 LYS C 108 1 17
HELIX 27 27 SER C 120 ASP C 132 5 13
HELIX 28 28 SER C 135 LYS C 140 1 6
HELIX 29 29 ALA C 164 ARG C 166 5 3
HELIX 30 30 VAL C 177 THR C 179 5 3
HELIX 31 31 ALA C 186 LEU C 189 5 4
HELIX 32 32 GLY C 192 GLU C 196 1 5
HELIX 33 33 PRO C 198 VAL C 210 1 13
SHEET 1 A 5 VAL A 68 GLY A 72 0
SHEET 2 A 5 VAL A 34 ALA A 39 1 N VAL A 34 O TRP A 69
SHEET 3 A 5 THR A 113 TYR A 119 1 N THR A 113 O ILE A 35
SHEET 4 A 5 ILE A 141 PHE A 147 1 N ALA A 142 O LEU A 114
SHEET 5 A 5 THR A 167 PHE A 170 1 N LYS A 168 O THR A 144
SHEET 1 B 5 VAL B 68 GLY B 72 0
SHEET 2 B 5 VAL B 34 ALA B 39 1 N VAL B 34 O TRP B 69
SHEET 3 B 5 THR B 113 TYR B 119 1 N THR B 113 O ILE B 35
SHEET 4 B 5 THR B 144 PHE B 147 1 N VAL B 145 O ALA B 116
SHEET 5 B 5 THR B 167 PHE B 170 1 N LYS B 168 O THR B 144
SHEET 1 C 5 VAL C 68 GLY C 72 0
SHEET 2 C 5 VAL C 34 ALA C 39 1 N VAL C 34 O TRP C 69
SHEET 3 C 5 THR C 113 TYR C 119 1 N THR C 113 O ILE C 35
SHEET 4 C 5 ILE C 141 PHE C 147 1 N ALA C 142 O LEU C 114
SHEET 5 C 5 THR C 167 PHE C 170 1 N LYS C 168 O THR C 144
SSBOND 1 CYS A 31 CYS A 109
SSBOND 2 CYS A 171 CYS A 178
SSBOND 3 CYS B 31 CYS B 109
SSBOND 4 CYS B 171 CYS B 178
SSBOND 5 CYS C 31 CYS C 109
SSBOND 6 CYS C 171 CYS C 178
SITE 1 CAA 3 SER A 120 ASP A 175 HIS A 188
SITE 1 CAB 3 SER B 120 ASP B 175 HIS B 188
SITE 1 CAC 3 SER C 120 ASP C 175 HIS C 188
CRYST1 65.900 73.300 71.200 90.00 112.70 90.00 P 1 21 1 6
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 0.015175 0.000000 0.006348 0.00000
SCALE2 0.000000 0.013643 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015224 0.00000
MTRIX1 1 0.696600 0.027630 0.716930 -14.67947 1
MTRIX2 1 0.033380 -0.999420 0.006080 38.67043 1
MTRIX3 1 0.716680 0.019700 -0.697120 32.76411 1
MTRIX1 2 0.622139 -0.672915 0.400162 30.58514 1
MTRIX2 2 0.692448 0.234448 -0.682312 69.71629 1
MTRIX3 2 0.365321 0.701584 0.611818 -26.07318 1
MTRIX1 3 0.792539 0.608716 0.036698 12.90325 1
MTRIX2 3 0.037400 -0.108583 0.993384 41.88312 1
MTRIX3 3 0.608673 -0.785923 -0.108823 19.29346 1 |