HEADER OXIDOREDUCTASE 26-AUG-03 1QV6
TITLE HORSE LIVER ALCOHOL DEHYDROGENASE HIS51GLN/LYS228ARG MUTANT COMPLEXED
TITLE 2 WITH NAD+ AND 2,4-DIFLUOROBENZYL ALCOHOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALCOHOL DEHYDROGENASE E CHAIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RECOMBINANT WITHOUT THE WILD-TYPE N-ACETYL GROUP;
COMPND 5 EC: 1.1.1.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: EQUUS CABALLUS;
SOURCE 3 ORGANISM_COMMON: HORSE;
SOURCE 4 ORGANISM_TAXID: 9796;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: XL1-BLUE;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PBPP
KEYWDS DEHYDROGENASE, ALCOHOL, NICOTINAMIDE COENZYME, 2, 4-DIFLUOROBENZYL
KEYWDS 2 ALCOHOL, HIS51GLN/LYS228ARG MUTANT, HORSE LIVER, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.A.LEBRUN,D.-H.PARK,S.RAMASWAMY,B.V.PLAPP
REVDAT 5 16-AUG-23 1QV6 1 REMARK
REVDAT 4 27-OCT-21 1QV6 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1QV6 1 VERSN
REVDAT 2 30-MAR-04 1QV6 1 JRNL
REVDAT 1 20-JAN-04 1QV6 0
JRNL AUTH L.A.LEBRUN,D.-H.PARK,S.RAMASWAMY,B.V.PLAPP
JRNL TITL PARTICIPATION OF HISTIDINE-51 IN CATALYSIS BY HORSE LIVER
JRNL TITL 2 ALCOHOL DEHYDROGENASE.
JRNL REF BIOCHEMISTRY V. 43 3014 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15023053
JRNL DOI 10.1021/BI036103M
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.RAMASWAMY,H.EKLUND,B.V.PLAPP
REMARK 1 TITL STRUCTURES OF LIVER ALCOHOL DEHYDROGENASE COMPLEXED WITH
REMARK 1 TITL 2 NAD+ AND SUBSTITUTED BENZYL ALCOHOLS.
REMARK 1 REF BIOCHEMISTRY V. 33 5230 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH L.A.LEBRUN,B.V.PLAPP
REMARK 1 TITL CONTROL OF COENZYME BINDING TO HORSE LIVER ALCOHOL
REMARK 1 TITL 2 DEHYDROGENASE.
REMARK 1 REF BIOCHEMISTRY V. 38 12387 1999
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI991306P
REMARK 1 REFERENCE 3
REMARK 1 AUTH J.K.RUBACH,B.V.PLAPP
REMARK 1 TITL MOBILITY OF FLUOROBENZYL ALCOHOLS BOUND TO LIVER ALCOHOL
REMARK 1 TITL 2 DEHYDROGENASE AS DETERMINED BY NMR AND X-RAY
REMARK 1 TITL 3 CRYSTALLOGRAPHIC STUDIES.
REMARK 1 REF BIOCHEMISTRY V. 41 15770 2002
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI026581H
REMARK 1 REFERENCE 4
REMARK 1 AUTH H.EKLUND,J.P.SAMAMA,L.WALLEN,C.I.BRANDEN,A.AKESON,T.A.JONES
REMARK 1 TITL STRUCTURE OF A TRICLINIC TERNARY COMPLEX OF HORSE LIVER
REMARK 1 TITL 2 ALCOHOL DEHYDROGENASE AT 2.9 A RESOLUTION
REMARK 1 REF J.MOL.BIOL. V. 146 561 1981
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 5
REMARK 1 AUTH H.EKLUND,B.NORDSTROM,E.ZEPPEZAUER,G.SODERLUND,I.OHLSSON,
REMARK 1 AUTH 2 T.BOIWE,B.O.SODERBERG,O.TAPIA,C.I.BRANDEN,A.AKESON
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF HORSE LIVER ALCOHOL
REMARK 1 TITL 2 DEHYDROGENASE AT 2.4 A RESOLUTION
REMARK 1 REF J.MOL.BIOL. V. 102 27 1976
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 6
REMARK 1 AUTH H.EKLUND,B.V.PLAPP,J.-P.SAMAMA,C.-I.BRANDEN
REMARK 1 TITL BINDING OF SUBSTRATE IN A TERNARY COMPLEX OF HORSE LIVER
REMARK 1 TITL 2 ALCOHOL DEHYDROGENASE
REMARK 1 REF J.BIOL.CHEM. V. 257 14349 1982
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 3 NUMBER OF REFLECTIONS : 62071
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) : 0.158
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.500
REMARK 3 FREE R VALUE TEST SET COUNT : 1572
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4475
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1950
REMARK 3 BIN FREE R VALUE SET COUNT : 109
REMARK 3 BIN FREE R VALUE : 0.2840
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5572
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 120
REMARK 3 SOLVENT ATOMS : 579
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.56
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.26000
REMARK 3 B22 (A**2) : 0.55000
REMARK 3 B33 (A**2) : -1.18000
REMARK 3 B12 (A**2) : -0.72000
REMARK 3 B13 (A**2) : 0.23000
REMARK 3 B23 (A**2) : 0.40000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.120
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.120
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.085
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.701
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5797 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7851 ; 1.736 ; 1.994
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 746 ; 4.643 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1053 ;15.645 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 913 ; 0.125 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4214 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2876 ; 0.209 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 713 ; 0.119 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 23 ; 0.211 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 18 ; 0.151 ; 0.500
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3704 ; 0.962 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5990 ; 1.643 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2093 ; 2.904 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1861 ; 4.751 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1QV6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-AUG-03.
REMARK 100 THE DEPOSITION ID IS D_1000020109.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAY-99
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9315
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63963
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 10.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.3
REMARK 200 DATA REDUNDANCY : 1.940
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.6
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.22000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1HLD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM AMMONIUM N
REMARK 280 -[TRIS(HYDROXYMETHYL)METHYL)]-2-AMINOETHANESULFONATE BUFFER, 1
REMARK 280 MM NAD+, 10 MM 2,4-DIFLUOROBENZYL ALCOHOL, 2-METHYL-2,4-
REMARK 280 PENTANEDIOL, PH 7.0, DIALYSIS, TEMPERATURE 278K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -116.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 218 NE - CZ - NH1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ASP B 153 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP B 360 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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
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 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 HIS A 67 -7.44 -147.70
REMARK 500 THR A 143 -65.18 -124.28
REMARK 500 SER A 144 73.42 55.56
REMARK 500 CYS A 174 -77.53 -157.75
REMARK 500 ILE A 269 -53.98 -126.51
REMARK 500 SER A 298 19.15 58.74
REMARK 500 ILE A 368 -70.90 -93.78
REMARK 500 HIS B 67 -11.23 -145.36
REMARK 500 THR B 143 -68.61 -124.86
REMARK 500 SER B 144 76.84 59.59
REMARK 500 CYS B 174 -79.13 -157.48
REMARK 500 ILE B 269 -55.36 -125.52
REMARK 500 ILE B 368 -80.94 -91.41
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 375 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 46 SG
REMARK 620 2 HIS A 67 NE2 107.5
REMARK 620 3 CYS A 174 SG 127.6 117.3
REMARK 620 4 24B A 378 O1 105.3 82.1 106.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 376 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 97 SG
REMARK 620 2 CYS A 100 SG 107.6
REMARK 620 3 CYS A 103 SG 116.6 105.7
REMARK 620 4 CYS A 111 SG 104.0 118.5 105.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 375 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 46 SG
REMARK 620 2 HIS B 67 NE2 103.2
REMARK 620 3 CYS B 174 SG 126.4 120.3
REMARK 620 4 24B B 378 O1 106.2 88.7 104.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 376 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 97 SG
REMARK 620 2 CYS B 100 SG 109.1
REMARK 620 3 CYS B 103 SG 117.2 104.8
REMARK 620 4 CYS B 111 SG 103.2 118.0 105.1
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 375
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 376
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 375
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 376
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 377
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 377
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 24B A 378
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 24B B 378
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HLD RELATED DB: PDB
REMARK 900 HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED WITH 2,3,4,5,6-
REMARK 900 PENTAFLUOROBENZYL ALCOHOL
REMARK 900 RELATED ID: 1MG0 RELATED DB: PDB
REMARK 900 HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED WITH 2,3-DIFLUOROBENZYL
REMARK 900 ALCOHOL
REMARK 900 RELATED ID: 1QV7 RELATED DB: PDB
REMARK 900 HORSE LIVER ALCOHOL DEHYDROGENASE HIS51GLN/LYS228ARG MUTANT
REMARK 900 COMPLEXED WITH 2,3-DIFLUOROBENZYL ALCOHOL
DBREF 1QV6 A 1 374 UNP P00327 ADHE_HORSE 1 374
DBREF 1QV6 B 1 374 UNP P00327 ADHE_HORSE 1 374
SEQADV 1QV6 GLN A 51 UNP P00327 HIS 51 ENGINEERED MUTATION
SEQADV 1QV6 ARG A 228 UNP P00327 LYS 228 ENGINEERED MUTATION
SEQADV 1QV6 GLN B 51 UNP P00327 HIS 51 ENGINEERED MUTATION
SEQADV 1QV6 ARG B 228 UNP P00327 LYS 228 ENGINEERED MUTATION
SEQRES 1 A 374 SER THR ALA GLY LYS VAL ILE LYS CYS LYS ALA ALA VAL
SEQRES 2 A 374 LEU TRP GLU GLU LYS LYS PRO PHE SER ILE GLU GLU VAL
SEQRES 3 A 374 GLU VAL ALA PRO PRO LYS ALA HIS GLU VAL ARG ILE LYS
SEQRES 4 A 374 MET VAL ALA THR GLY ILE CYS ARG SER ASP ASP GLN VAL
SEQRES 5 A 374 VAL SER GLY THR LEU VAL THR PRO LEU PRO VAL ILE ALA
SEQRES 6 A 374 GLY HIS GLU ALA ALA GLY ILE VAL GLU SER ILE GLY GLU
SEQRES 7 A 374 GLY VAL THR THR VAL ARG PRO GLY ASP LYS VAL ILE PRO
SEQRES 8 A 374 LEU PHE THR PRO GLN CYS GLY LYS CYS ARG VAL CYS LYS
SEQRES 9 A 374 HIS PRO GLU GLY ASN PHE CYS LEU LYS ASN ASP LEU SER
SEQRES 10 A 374 MET PRO ARG GLY THR MET GLN ASP GLY THR SER ARG PHE
SEQRES 11 A 374 THR CYS ARG GLY LYS PRO ILE HIS HIS PHE LEU GLY THR
SEQRES 12 A 374 SER THR PHE SER GLN TYR THR VAL VAL ASP GLU ILE SER
SEQRES 13 A 374 VAL ALA LYS ILE ASP ALA ALA SER PRO LEU GLU LYS VAL
SEQRES 14 A 374 CYS LEU ILE GLY CYS GLY PHE SER THR GLY TYR GLY SER
SEQRES 15 A 374 ALA VAL LYS VAL ALA LYS VAL THR GLN GLY SER THR CYS
SEQRES 16 A 374 ALA VAL PHE GLY LEU GLY GLY VAL GLY LEU SER VAL ILE
SEQRES 17 A 374 MET GLY CYS LYS ALA ALA GLY ALA ALA ARG ILE ILE GLY
SEQRES 18 A 374 VAL ASP ILE ASN LYS ASP ARG PHE ALA LYS ALA LYS GLU
SEQRES 19 A 374 VAL GLY ALA THR GLU CYS VAL ASN PRO GLN ASP TYR LYS
SEQRES 20 A 374 LYS PRO ILE GLN GLU VAL LEU THR GLU MET SER ASN GLY
SEQRES 21 A 374 GLY VAL ASP PHE SER PHE GLU VAL ILE GLY ARG LEU ASP
SEQRES 22 A 374 THR MET VAL THR ALA LEU SER CYS CYS GLN GLU ALA TYR
SEQRES 23 A 374 GLY VAL SER VAL ILE VAL GLY VAL PRO PRO ASP SER GLN
SEQRES 24 A 374 ASN LEU SER MET ASN PRO MET LEU LEU LEU SER GLY ARG
SEQRES 25 A 374 THR TRP LYS GLY ALA ILE PHE GLY GLY PHE LYS SER LYS
SEQRES 26 A 374 ASP SER VAL PRO LYS LEU VAL ALA ASP PHE MET ALA LYS
SEQRES 27 A 374 LYS PHE ALA LEU ASP PRO LEU ILE THR HIS VAL LEU PRO
SEQRES 28 A 374 PHE GLU LYS ILE ASN GLU GLY PHE ASP LEU LEU ARG SER
SEQRES 29 A 374 GLY GLU SER ILE ARG THR ILE LEU THR PHE
SEQRES 1 B 374 SER THR ALA GLY LYS VAL ILE LYS CYS LYS ALA ALA VAL
SEQRES 2 B 374 LEU TRP GLU GLU LYS LYS PRO PHE SER ILE GLU GLU VAL
SEQRES 3 B 374 GLU VAL ALA PRO PRO LYS ALA HIS GLU VAL ARG ILE LYS
SEQRES 4 B 374 MET VAL ALA THR GLY ILE CYS ARG SER ASP ASP GLN VAL
SEQRES 5 B 374 VAL SER GLY THR LEU VAL THR PRO LEU PRO VAL ILE ALA
SEQRES 6 B 374 GLY HIS GLU ALA ALA GLY ILE VAL GLU SER ILE GLY GLU
SEQRES 7 B 374 GLY VAL THR THR VAL ARG PRO GLY ASP LYS VAL ILE PRO
SEQRES 8 B 374 LEU PHE THR PRO GLN CYS GLY LYS CYS ARG VAL CYS LYS
SEQRES 9 B 374 HIS PRO GLU GLY ASN PHE CYS LEU LYS ASN ASP LEU SER
SEQRES 10 B 374 MET PRO ARG GLY THR MET GLN ASP GLY THR SER ARG PHE
SEQRES 11 B 374 THR CYS ARG GLY LYS PRO ILE HIS HIS PHE LEU GLY THR
SEQRES 12 B 374 SER THR PHE SER GLN TYR THR VAL VAL ASP GLU ILE SER
SEQRES 13 B 374 VAL ALA LYS ILE ASP ALA ALA SER PRO LEU GLU LYS VAL
SEQRES 14 B 374 CYS LEU ILE GLY CYS GLY PHE SER THR GLY TYR GLY SER
SEQRES 15 B 374 ALA VAL LYS VAL ALA LYS VAL THR GLN GLY SER THR CYS
SEQRES 16 B 374 ALA VAL PHE GLY LEU GLY GLY VAL GLY LEU SER VAL ILE
SEQRES 17 B 374 MET GLY CYS LYS ALA ALA GLY ALA ALA ARG ILE ILE GLY
SEQRES 18 B 374 VAL ASP ILE ASN LYS ASP ARG PHE ALA LYS ALA LYS GLU
SEQRES 19 B 374 VAL GLY ALA THR GLU CYS VAL ASN PRO GLN ASP TYR LYS
SEQRES 20 B 374 LYS PRO ILE GLN GLU VAL LEU THR GLU MET SER ASN GLY
SEQRES 21 B 374 GLY VAL ASP PHE SER PHE GLU VAL ILE GLY ARG LEU ASP
SEQRES 22 B 374 THR MET VAL THR ALA LEU SER CYS CYS GLN GLU ALA TYR
SEQRES 23 B 374 GLY VAL SER VAL ILE VAL GLY VAL PRO PRO ASP SER GLN
SEQRES 24 B 374 ASN LEU SER MET ASN PRO MET LEU LEU LEU SER GLY ARG
SEQRES 25 B 374 THR TRP LYS GLY ALA ILE PHE GLY GLY PHE LYS SER LYS
SEQRES 26 B 374 ASP SER VAL PRO LYS LEU VAL ALA ASP PHE MET ALA LYS
SEQRES 27 B 374 LYS PHE ALA LEU ASP PRO LEU ILE THR HIS VAL LEU PRO
SEQRES 28 B 374 PHE GLU LYS ILE ASN GLU GLY PHE ASP LEU LEU ARG SER
SEQRES 29 B 374 GLY GLU SER ILE ARG THR ILE LEU THR PHE
HET ZN A 375 1
HET ZN A 376 1
HET NAD A 377 44
HET 24B A 378 10
HET MPD A 601 8
HET ZN B 375 1
HET ZN B 376 1
HET NAD B 377 44
HET 24B B 378 10
HETNAM ZN ZINC ION
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 24B (2,4-DIFLUOROPHENYL)METHANOL
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETSYN 24B 2,4-DIFLUOROBENZYL ALCOHOL 2,4-DIFLUORO-1-
HETSYN 2 24B (HYDROXYMETHYL)BENZENE
FORMUL 3 ZN 4(ZN 2+)
FORMUL 5 NAD 2(C21 H27 N7 O14 P2)
FORMUL 6 24B 2(C7 H6 F2 O)
FORMUL 7 MPD C6 H14 O2
FORMUL 12 HOH *579(H2 O)
HELIX 1 1 CYS A 46 SER A 54 1 9
HELIX 2 2 CYS A 100 HIS A 105 1 6
HELIX 3 3 PRO A 165 CYS A 170 1 6
HELIX 4 4 LEU A 171 GLY A 173 5 3
HELIX 5 5 CYS A 174 LYS A 185 1 12
HELIX 6 6 GLY A 201 ALA A 214 1 14
HELIX 7 7 ASN A 225 ASP A 227 5 3
HELIX 8 8 ARG A 228 VAL A 235 1 8
HELIX 9 9 ASN A 242 TYR A 246 5 5
HELIX 10 10 PRO A 249 SER A 258 1 10
HELIX 11 11 ARG A 271 CYS A 282 1 12
HELIX 12 12 PRO A 305 SER A 310 1 6
HELIX 13 13 ILE A 318 PHE A 322 5 5
HELIX 14 14 LYS A 323 ALA A 337 1 15
HELIX 15 15 LEU A 342 PRO A 344 5 3
HELIX 16 16 LYS A 354 SER A 364 1 11
HELIX 17 17 CYS B 46 GLY B 55 1 10
HELIX 18 18 CYS B 100 HIS B 105 1 6
HELIX 19 19 PRO B 165 CYS B 170 1 6
HELIX 20 20 LEU B 171 GLY B 173 5 3
HELIX 21 21 CYS B 174 LYS B 185 1 12
HELIX 22 22 GLY B 201 ALA B 214 1 14
HELIX 23 23 ASN B 225 ASP B 227 5 3
HELIX 24 24 ARG B 228 GLY B 236 1 9
HELIX 25 25 ASN B 242 TYR B 246 5 5
HELIX 26 26 PRO B 249 SER B 258 1 10
HELIX 27 27 ARG B 271 CYS B 282 1 12
HELIX 28 28 PRO B 305 SER B 310 1 6
HELIX 29 29 ILE B 318 PHE B 322 5 5
HELIX 30 30 LYS B 323 ALA B 337 1 15
HELIX 31 31 LEU B 342 PRO B 344 5 3
HELIX 32 32 LYS B 354 SER B 364 1 11
SHEET 1 A 5 VAL A 63 ILE A 64 0
SHEET 2 A 5 ILE A 7 LEU A 14 -1 N LEU A 14 O VAL A 63
SHEET 3 A 5 SER A 22 VAL A 28 -1 O VAL A 28 N ILE A 7
SHEET 4 A 5 PHE A 130 CYS A 132 -1 O THR A 131 N GLU A 27
SHEET 5 A 5 LYS A 135 ILE A 137 -1 O LYS A 135 N CYS A 132
SHEET 1 B 5 TYR A 149 ASP A 153 0
SHEET 2 B 5 GLU A 35 GLY A 44 -1 N VAL A 36 O VAL A 152
SHEET 3 B 5 GLU A 68 ILE A 76 -1 O ILE A 72 N LYS A 39
SHEET 4 B 5 LYS A 88 PRO A 91 -1 O VAL A 89 N GLY A 71
SHEET 5 B 5 VAL A 157 ILE A 160 -1 O ILE A 160 N LYS A 88
SHEET 1 C 4 TYR A 149 ASP A 153 0
SHEET 2 C 4 GLU A 35 GLY A 44 -1 N VAL A 36 O VAL A 152
SHEET 3 C 4 ARG A 369 THR A 373 -1 O LEU A 372 N THR A 43
SHEET 4 C 4 ILE A 346 PRO A 351 1 N HIS A 348 O ILE A 371
SHEET 1 D12 GLU A 239 VAL A 241 0
SHEET 2 D12 ARG A 218 VAL A 222 1 N GLY A 221 O VAL A 241
SHEET 3 D12 THR A 194 PHE A 198 1 N CYS A 195 O ILE A 220
SHEET 4 D12 PHE A 264 GLU A 267 1 O PHE A 266 N PHE A 198
SHEET 5 D12 VAL A 288 ILE A 291 1 O VAL A 288 N SER A 265
SHEET 6 D12 THR A 313 GLY A 316 1 O LYS A 315 N ILE A 291
SHEET 7 D12 THR B 313 GLY B 316 -1 O TRP B 314 N TRP A 314
SHEET 8 D12 VAL B 288 ILE B 291 1 N ILE B 291 O LYS B 315
SHEET 9 D12 PHE B 264 GLU B 267 1 N GLU B 267 O VAL B 290
SHEET 10 D12 THR B 194 PHE B 198 1 N PHE B 198 O PHE B 266
SHEET 11 D12 ARG B 218 VAL B 222 1 O ILE B 220 N CYS B 195
SHEET 12 D12 GLU B 239 VAL B 241 1 O VAL B 241 N GLY B 221
SHEET 1 E 2 LEU A 301 MET A 303 0
SHEET 2 E 2 LEU B 301 MET B 303 -1 O LEU B 301 N MET A 303
SHEET 1 F 4 ILE B 7 VAL B 13 0
SHEET 2 F 4 SER B 22 VAL B 28 -1 O SER B 22 N VAL B 13
SHEET 3 F 4 PHE B 130 CYS B 132 -1 O THR B 131 N GLU B 27
SHEET 4 F 4 LYS B 135 ILE B 137 -1 O LYS B 135 N CYS B 132
SHEET 1 G 5 TYR B 149 ASP B 153 0
SHEET 2 G 5 GLU B 35 GLY B 44 -1 N VAL B 36 O VAL B 152
SHEET 3 G 5 ALA B 69 ILE B 76 -1 O GLU B 74 N ARG B 37
SHEET 4 G 5 LYS B 88 PRO B 91 -1 O VAL B 89 N GLY B 71
SHEET 5 G 5 VAL B 157 LYS B 159 -1 O ALA B 158 N ILE B 90
SHEET 1 H 4 TYR B 149 ASP B 153 0
SHEET 2 H 4 GLU B 35 GLY B 44 -1 N VAL B 36 O VAL B 152
SHEET 3 H 4 ARG B 369 THR B 373 -1 O LEU B 372 N THR B 43
SHEET 4 H 4 ILE B 346 PRO B 351 1 N HIS B 348 O ILE B 371
LINK SG CYS A 46 ZN ZN A 375 1555 1555 2.27
LINK NE2 HIS A 67 ZN ZN A 375 1555 1555 2.15
LINK SG CYS A 97 ZN ZN A 376 1555 1555 2.36
LINK SG CYS A 100 ZN ZN A 376 1555 1555 2.36
LINK SG CYS A 103 ZN ZN A 376 1555 1555 2.30
LINK SG CYS A 111 ZN ZN A 376 1555 1555 2.34
LINK SG CYS A 174 ZN ZN A 375 1555 1555 2.24
LINK ZN ZN A 375 O1 24B A 378 1555 1555 2.33
LINK SG CYS B 46 ZN ZN B 375 1555 1555 2.28
LINK NE2 HIS B 67 ZN ZN B 375 1555 1555 2.19
LINK SG CYS B 97 ZN ZN B 376 1555 1555 2.34
LINK SG CYS B 100 ZN ZN B 376 1555 1555 2.36
LINK SG CYS B 103 ZN ZN B 376 1555 1555 2.31
LINK SG CYS B 111 ZN ZN B 376 1555 1555 2.34
LINK SG CYS B 174 ZN ZN B 375 1555 1555 2.16
LINK ZN ZN B 375 O1 24B B 378 1555 1555 2.14
CISPEP 1 LEU A 61 PRO A 62 0 4.15
CISPEP 2 LEU B 61 PRO B 62 0 0.62
SITE 1 AC1 5 CYS A 46 HIS A 67 CYS A 174 NAD A 377
SITE 2 AC1 5 24B A 378
SITE 1 AC2 4 CYS A 97 CYS A 100 CYS A 103 CYS A 111
SITE 1 AC3 5 CYS B 46 HIS B 67 CYS B 174 NAD B 377
SITE 2 AC3 5 24B B 378
SITE 1 AC4 4 CYS B 97 CYS B 100 CYS B 103 CYS B 111
SITE 1 AC5 28 ARG A 47 SER A 48 GLN A 51 CYS A 174
SITE 2 AC5 28 THR A 178 GLY A 199 GLY A 201 GLY A 202
SITE 3 AC5 28 VAL A 203 ASP A 223 ILE A 224 ARG A 228
SITE 4 AC5 28 VAL A 268 ILE A 269 VAL A 292 GLY A 293
SITE 5 AC5 28 VAL A 294 ALA A 317 ILE A 318 PHE A 319
SITE 6 AC5 28 ARG A 369 ZN A 375 24B A 378 HOH A 604
SITE 7 AC5 28 HOH A 647 HOH A 675 HOH A 767 HOH A 845
SITE 1 AC6 27 ARG B 47 SER B 48 GLN B 51 CYS B 174
SITE 2 AC6 27 THR B 178 GLY B 199 GLY B 201 GLY B 202
SITE 3 AC6 27 VAL B 203 ASP B 223 ILE B 224 ARG B 228
SITE 4 AC6 27 VAL B 268 ILE B 269 VAL B 292 GLY B 293
SITE 5 AC6 27 VAL B 294 ALA B 317 ILE B 318 PHE B 319
SITE 6 AC6 27 ARG B 369 ZN B 375 24B B 378 HOH B 386
SITE 7 AC6 27 HOH B 514 HOH B 540 HOH B 562
SITE 1 AC7 12 CYS A 46 SER A 48 LEU A 57 HIS A 67
SITE 2 AC7 12 PHE A 93 LEU A 116 LEU A 141 CYS A 174
SITE 3 AC7 12 VAL A 294 ZN A 375 NAD A 377 LEU B 309
SITE 1 AC8 12 LEU A 309 CYS B 46 SER B 48 LEU B 57
SITE 2 AC8 12 HIS B 67 PHE B 93 LEU B 116 LEU B 141
SITE 3 AC8 12 CYS B 174 VAL B 294 ZN B 375 NAD B 377
SITE 1 AC9 4 ARG A 218 THR A 238 GLU A 239 GLU B 239
CRYST1 44.255 51.115 92.722 91.61 103.05 109.90 P 1 2
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 0.022596 0.008180 0.006216 0.00000
SCALE2 0.000000 0.020806 0.002400 0.00000
SCALE3 0.000000 0.000000 0.011144 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
