HEADER TRANSFERASE 29-JUL-10 3O6W
TITLE CRYSTAL STRUCTURE OF MONOMERIC KLHXK1 IN CRYSTAL FORM VIII (OPEN
TITLE 2 STATE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEXOKINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.7.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 28985;
SOURCE 5 STRAIN: CBS2359/152;
SOURCE 6 GENE: KLLA0D11352G, RAG5;
SOURCE 7 EXPRESSION_SYSTEM: KLUYVEROMYCES LACTIS;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 28985;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: JA6-DELTA-RAG5;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PTS32X;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PTSRAG5
KEYWDS RNASEH-LIKE FOLD, HEXOKINASE, GLYCOLYSIS, GLUCOSE REPRESSION, ATP
KEYWDS 2 BINDING, MIG1 BINDING, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.B.KUETTNER,K.KETTNER,A.KEIM,T.M.KRIEGEL,N.STRATER
REVDAT 4 06-SEP-23 3O6W 1 REMARK
REVDAT 3 08-NOV-17 3O6W 1 REMARK
REVDAT 2 29-DEC-10 3O6W 1 JRNL
REVDAT 1 13-OCT-10 3O6W 0
JRNL AUTH E.B.KUETTNER,K.KETTNER,A.KEIM,D.I.SVERGUN,D.VOLKE,D.SINGER,
JRNL AUTH 2 R.HOFFMANN,E.C.MULLER,A.OTTO,T.M.KRIEGEL,N.STRATER
JRNL TITL CRYSTAL STRUCTURE OF HEXOKINASE KLHXK1 OF KLUYVEROMYCES
JRNL TITL 2 LACTIS: A MOLECULAR BASIS FOR UNDERSTANDING THE CONTROL OF
JRNL TITL 3 YEAST HEXOKINASE FUNCTIONS VIA COVALENT MODIFICATION AND
JRNL TITL 4 OLIGOMERIZATION.
JRNL REF J.BIOL.CHEM. V. 285 41019 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20943665
JRNL DOI 10.1074/JBC.M110.185850
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.B.KUETTNER,T.M.KRIEGEL,A.KEIM,M.NAUMANN,N.STRATER
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION STUDIES OF
REMARK 1 TITL 2 HEXOKINASE KLHXK1 FROM KLUYVEROMYCES LACTIS
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.F V. 63 430 2007
REMARK 1 REFN ESSN 1744-3091
REMARK 1 PMID 17565189
REMARK 2
REMARK 2 RESOLUTION. 1.48 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.48
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.12
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 170225
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) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.184
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1723
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) : 1.48
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.52
REMARK 3 REFLECTION IN BIN (WORKING SET) : 12500
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.2640
REMARK 3 BIN FREE R VALUE SET COUNT : 129
REMARK 3 BIN FREE R VALUE : 0.2980
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7269
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 45
REMARK 3 SOLVENT ATOMS : 630
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.74
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.42000
REMARK 3 B22 (A**2) : 1.08000
REMARK 3 B33 (A**2) : -0.95000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.67000
REMARK 3 B23 (A**2) : 0.00000
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): 0.059
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.043
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.597
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.970
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7513 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10168 ; 1.409 ; 1.981
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 933 ; 5.540 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 333 ;35.274 ;25.315
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1341 ;11.524 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;18.247 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1136 ; 0.095 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5603 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 4633 ; 1.272 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7510 ; 2.120 ; 4.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2880 ; 3.548 ; 6.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2655 ; 5.859 ; 9.000
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 : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 76
REMARK 3 RESIDUE RANGE : A 210 A 456
REMARK 3 ORIGIN FOR THE GROUP (A): 6.1899 5.3667 17.8310
REMARK 3 T TENSOR
REMARK 3 T11: 0.0198 T22: 0.0021
REMARK 3 T33: 0.0535 T12: 0.0008
REMARK 3 T13: 0.0098 T23: -0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 0.6001 L22: 0.7259
REMARK 3 L33: 2.1071 L12: 0.0983
REMARK 3 L13: 0.2875 L23: 0.2821
REMARK 3 S TENSOR
REMARK 3 S11: 0.0438 S12: -0.0134 S13: -0.0210
REMARK 3 S21: 0.0044 S22: -0.0207 S23: -0.0043
REMARK 3 S31: -0.0339 S32: -0.0294 S33: -0.0231
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 77 A 209
REMARK 3 RESIDUE RANGE : A 457 A 485
REMARK 3 ORIGIN FOR THE GROUP (A): 19.0435 -11.3529 -4.6582
REMARK 3 T TENSOR
REMARK 3 T11: 0.0764 T22: 0.0738
REMARK 3 T33: 0.0776 T12: 0.0065
REMARK 3 T13: -0.0053 T23: -0.0430
REMARK 3 L TENSOR
REMARK 3 L11: 2.1569 L22: 1.6028
REMARK 3 L33: 1.5464 L12: 0.0621
REMARK 3 L13: 0.0844 L23: -0.0027
REMARK 3 S TENSOR
REMARK 3 S11: 0.0366 S12: -0.0193 S13: -0.1784
REMARK 3 S21: 0.0923 S22: -0.0278 S23: -0.1913
REMARK 3 S31: 0.0997 S32: 0.1640 S33: -0.0088
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 76
REMARK 3 RESIDUE RANGE : B 210 B 456
REMARK 3 ORIGIN FOR THE GROUP (A): 18.3094 -15.5909 -58.4430
REMARK 3 T TENSOR
REMARK 3 T11: 0.0616 T22: 0.0582
REMARK 3 T33: 0.0685 T12: 0.0037
REMARK 3 T13: -0.0109 T23: -0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 1.0914 L22: 1.0276
REMARK 3 L33: 2.4654 L12: 0.1223
REMARK 3 L13: 0.0094 L23: 0.0401
REMARK 3 S TENSOR
REMARK 3 S11: 0.0145 S12: 0.0954 S13: 0.0262
REMARK 3 S21: -0.2454 S22: 0.0037 S23: 0.0810
REMARK 3 S31: 0.0150 S32: 0.1134 S33: -0.0182
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 77 B 209
REMARK 3 RESIDUE RANGE : B 457 B 485
REMARK 3 ORIGIN FOR THE GROUP (A): 0.9439 -10.8974 -33.4426
REMARK 3 T TENSOR
REMARK 3 T11: 0.0279 T22: 0.0643
REMARK 3 T33: 0.0373 T12: -0.0260
REMARK 3 T13: 0.0033 T23: 0.0005
REMARK 3 L TENSOR
REMARK 3 L11: 2.4136 L22: 1.6986
REMARK 3 L33: 0.9790 L12: 0.2250
REMARK 3 L13: -0.2630 L23: 0.0475
REMARK 3 S TENSOR
REMARK 3 S11: -0.0127 S12: 0.0763 S13: 0.1481
REMARK 3 S21: -0.0924 S22: 0.0865 S23: 0.1507
REMARK 3 S31: -0.0410 S32: -0.0120 S33: -0.0738
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. FULL B FACTORS AND ANISO RECORDS WERE COMPUTED BY
REMARK 3 CCP4 PROGRAMM TLSANL
REMARK 4
REMARK 4 3O6W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-AUG-10.
REMARK 100 THE DEPOSITION ID IS D_1000060740.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUL-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : SI-111 CRYSTAL
REMARK 200 OPTICS : 1ST MIRROR: SILICON, ACTIVE
REMARK 200 SURFACE 50 NM RH-COATED; 2ND
REMARK 200 MIRROR: GLAS, ACTIVE SURFACE 50
REMARK 200 NM RH-COATED
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 171952
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.480
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.03100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.48
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.52
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.49100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
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: PDB ENTRY 3O08
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1MICROL RESERVOIR + 1MICROL PROTEIN,
REMARK 280 RESERVOIR: 2.4M DI-AMMONIA PHOSPHATE, 0.1M CHES PH 9.6, PROTEIN:
REMARK 280 10MG/ML KLHXK1, 10MM TRIS PH 7.4, 1MM EDTA, 1MM DTT, 0.5MM PMSF,
REMARK 280 1MM XYLOSE, 1MM ATP, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 292K
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 46.79500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 VAL A 2
REMARK 465 ARG A 3
REMARK 465 LEU A 4
REMARK 465 GLY A 5
REMARK 465 PRO A 6
REMARK 465 LYS A 7
REMARK 465 LYS A 8
REMARK 465 PRO A 9
REMARK 465 PRO A 10
REMARK 465 ALA A 11
REMARK 465 ARG A 12
REMARK 465 LYS A 13
REMARK 465 GLY A 14
REMARK 465 SER A 15
REMARK 465 MET A 16
REMARK 465 ALA A 17
REMARK 465 ASP A 18
REMARK 465 MET B 1
REMARK 465 VAL B 2
REMARK 465 ARG B 3
REMARK 465 LEU B 4
REMARK 465 GLY B 5
REMARK 465 PRO B 6
REMARK 465 LYS B 7
REMARK 465 LYS B 8
REMARK 465 PRO B 9
REMARK 465 PRO B 10
REMARK 465 ALA B 11
REMARK 465 ARG B 12
REMARK 465 LYS B 13
REMARK 465 GLY B 14
REMARK 465 SER B 15
REMARK 465 MET B 16
REMARK 465 ALA B 17
REMARK 465 ASP B 18
REMARK 465 VAL B 19
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 LEU B 92 CA - CB - CG ANGL. DEV. = 19.4 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 ASN A 102 57.82 -140.22
REMARK 500 SER A 157 52.11 -90.62
REMARK 500 ASN A 166 54.30 -91.19
REMARK 500 ASP A 178 69.22 -157.03
REMARK 500 VAL A 278 -33.06 -139.62
REMARK 500 SER B 157 49.74 -91.21
REMARK 500 ASN B 166 54.79 -90.90
REMARK 500 ASP B 178 69.65 -152.20
REMARK 500 ASP B 241 -162.21 -100.24
REMARK 500 VAL B 278 -30.86 -138.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 486
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 487
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 488
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 486
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 487
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 488
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 489
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 490
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3O08 RELATED DB: PDB
REMARK 900 CRYSTAL FORM I OF KLHXK1 (DIMER)
REMARK 900 RELATED ID: 3O1B RELATED DB: PDB
REMARK 900 CRYSTAL FORM II OF KLHXK1 (DIMER)
REMARK 900 RELATED ID: 3O1W RELATED DB: PDB
REMARK 900 CRYSTAL FORM III OF KLHXK1 (DIMER)
REMARK 900 RELATED ID: 3O4W RELATED DB: PDB
REMARK 900 CRYSTAL FORM IV OF KLHXK1 (DIMER)
REMARK 900 RELATED ID: 3O5B RELATED DB: PDB
REMARK 900 CRYSTAL FORM VII OF KLHXK1 (DIMER) WITH GLUCOSE BOUND
REMARK 900 RELATED ID: 3O80 RELATED DB: PDB
REMARK 900 CRYSTAL FORM IX OF KLHXK1 (MONOMER)
REMARK 900 RELATED ID: 3O8M RELATED DB: PDB
REMARK 900 CRYSTAL FORM XI OF KLHXK1 (MONONER) WITH GLUCOSE BOUND
DBREF 3O6W A 1 485 UNP P33284 HXK_KLULA 1 485
DBREF 3O6W B 1 485 UNP P33284 HXK_KLULA 1 485
SEQRES 1 A 485 MET VAL ARG LEU GLY PRO LYS LYS PRO PRO ALA ARG LYS
SEQRES 2 A 485 GLY SER MET ALA ASP VAL PRO ALA ASN LEU MET GLU GLN
SEQRES 3 A 485 ILE HIS GLY LEU GLU THR LEU PHE THR VAL SER SER GLU
SEQRES 4 A 485 LYS MET ARG SER ILE VAL LYS HIS PHE ILE SER GLU LEU
SEQRES 5 A 485 ASP LYS GLY LEU SER LYS LYS GLY GLY ASN ILE PRO MET
SEQRES 6 A 485 ILE PRO GLY TRP VAL VAL GLU TYR PRO THR GLY LYS GLU
SEQRES 7 A 485 THR GLY ASP PHE LEU ALA LEU ASP LEU GLY GLY THR ASN
SEQRES 8 A 485 LEU ARG VAL VAL LEU VAL LYS LEU GLY GLY ASN HIS ASP
SEQRES 9 A 485 PHE ASP THR THR GLN ASN LYS TYR ARG LEU PRO ASP HIS
SEQRES 10 A 485 LEU ARG THR GLY THR SER GLU GLN LEU TRP SER PHE ILE
SEQRES 11 A 485 ALA LYS CYS LEU LYS GLU PHE VAL ASP GLU TRP TYR PRO
SEQRES 12 A 485 ASP GLY VAL SER GLU PRO LEU PRO LEU GLY PHE THR PHE
SEQRES 13 A 485 SER TYR PRO ALA SER GLN LYS LYS ILE ASN SER GLY VAL
SEQRES 14 A 485 LEU GLN ARG TRP THR LYS GLY PHE ASP ILE GLU GLY VAL
SEQRES 15 A 485 GLU GLY HIS ASP VAL VAL PRO MET LEU GLN GLU GLN ILE
SEQRES 16 A 485 GLU LYS LEU ASN ILE PRO ILE ASN VAL VAL ALA LEU ILE
SEQRES 17 A 485 ASN ASP THR THR GLY THR LEU VAL ALA SER LEU TYR THR
SEQRES 18 A 485 ASP PRO GLN THR LYS MET GLY ILE ILE ILE GLY THR GLY
SEQRES 19 A 485 VAL ASN GLY ALA TYR TYR ASP VAL VAL SER GLY ILE GLU
SEQRES 20 A 485 LYS LEU GLU GLY LEU LEU PRO GLU ASP ILE GLY PRO ASP
SEQRES 21 A 485 SER PRO MET ALA ILE ASN CYS GLU TYR GLY SER PHE ASP
SEQRES 22 A 485 ASN GLU HIS LEU VAL LEU PRO ARG THR LYS TYR ASP VAL
SEQRES 23 A 485 ILE ILE ASP GLU GLU SER PRO ARG PRO GLY GLN GLN ALA
SEQRES 24 A 485 PHE GLU LYS MET THR SER GLY TYR TYR LEU GLY GLU ILE
SEQRES 25 A 485 MET ARG LEU VAL LEU LEU ASP LEU TYR ASP SER GLY PHE
SEQRES 26 A 485 ILE PHE LYS ASP GLN ASP ILE SER LYS LEU LYS GLU ALA
SEQRES 27 A 485 TYR VAL MET ASP THR SER TYR PRO SER LYS ILE GLU ASP
SEQRES 28 A 485 ASP PRO PHE GLU ASN LEU GLU ASP THR ASP ASP LEU PHE
SEQRES 29 A 485 LYS THR ASN LEU ASN ILE GLU THR THR VAL VAL GLU ARG
SEQRES 30 A 485 LYS LEU ILE ARG LYS LEU ALA GLU LEU VAL GLY THR ARG
SEQRES 31 A 485 ALA ALA ARG LEU THR VAL CYS GLY VAL SER ALA ILE CYS
SEQRES 32 A 485 ASP LYS ARG GLY TYR LYS THR ALA HIS ILE ALA ALA ASP
SEQRES 33 A 485 GLY SER VAL PHE ASN ARG TYR PRO GLY TYR LYS GLU LYS
SEQRES 34 A 485 ALA ALA GLN ALA LEU LYS ASP ILE TYR ASN TRP ASP VAL
SEQRES 35 A 485 GLU LYS MET GLU ASP HIS PRO ILE GLN LEU VAL ALA ALA
SEQRES 36 A 485 GLU ASP GLY SER GLY VAL GLY ALA ALA ILE ILE ALA CYS
SEQRES 37 A 485 LEU THR GLN LYS ARG LEU ALA ALA GLY LYS SER VAL GLY
SEQRES 38 A 485 ILE LYS GLY GLU
SEQRES 1 B 485 MET VAL ARG LEU GLY PRO LYS LYS PRO PRO ALA ARG LYS
SEQRES 2 B 485 GLY SER MET ALA ASP VAL PRO ALA ASN LEU MET GLU GLN
SEQRES 3 B 485 ILE HIS GLY LEU GLU THR LEU PHE THR VAL SER SER GLU
SEQRES 4 B 485 LYS MET ARG SER ILE VAL LYS HIS PHE ILE SER GLU LEU
SEQRES 5 B 485 ASP LYS GLY LEU SER LYS LYS GLY GLY ASN ILE PRO MET
SEQRES 6 B 485 ILE PRO GLY TRP VAL VAL GLU TYR PRO THR GLY LYS GLU
SEQRES 7 B 485 THR GLY ASP PHE LEU ALA LEU ASP LEU GLY GLY THR ASN
SEQRES 8 B 485 LEU ARG VAL VAL LEU VAL LYS LEU GLY GLY ASN HIS ASP
SEQRES 9 B 485 PHE ASP THR THR GLN ASN LYS TYR ARG LEU PRO ASP HIS
SEQRES 10 B 485 LEU ARG THR GLY THR SER GLU GLN LEU TRP SER PHE ILE
SEQRES 11 B 485 ALA LYS CYS LEU LYS GLU PHE VAL ASP GLU TRP TYR PRO
SEQRES 12 B 485 ASP GLY VAL SER GLU PRO LEU PRO LEU GLY PHE THR PHE
SEQRES 13 B 485 SER TYR PRO ALA SER GLN LYS LYS ILE ASN SER GLY VAL
SEQRES 14 B 485 LEU GLN ARG TRP THR LYS GLY PHE ASP ILE GLU GLY VAL
SEQRES 15 B 485 GLU GLY HIS ASP VAL VAL PRO MET LEU GLN GLU GLN ILE
SEQRES 16 B 485 GLU LYS LEU ASN ILE PRO ILE ASN VAL VAL ALA LEU ILE
SEQRES 17 B 485 ASN ASP THR THR GLY THR LEU VAL ALA SER LEU TYR THR
SEQRES 18 B 485 ASP PRO GLN THR LYS MET GLY ILE ILE ILE GLY THR GLY
SEQRES 19 B 485 VAL ASN GLY ALA TYR TYR ASP VAL VAL SER GLY ILE GLU
SEQRES 20 B 485 LYS LEU GLU GLY LEU LEU PRO GLU ASP ILE GLY PRO ASP
SEQRES 21 B 485 SER PRO MET ALA ILE ASN CYS GLU TYR GLY SER PHE ASP
SEQRES 22 B 485 ASN GLU HIS LEU VAL LEU PRO ARG THR LYS TYR ASP VAL
SEQRES 23 B 485 ILE ILE ASP GLU GLU SER PRO ARG PRO GLY GLN GLN ALA
SEQRES 24 B 485 PHE GLU LYS MET THR SER GLY TYR TYR LEU GLY GLU ILE
SEQRES 25 B 485 MET ARG LEU VAL LEU LEU ASP LEU TYR ASP SER GLY PHE
SEQRES 26 B 485 ILE PHE LYS ASP GLN ASP ILE SER LYS LEU LYS GLU ALA
SEQRES 27 B 485 TYR VAL MET ASP THR SER TYR PRO SER LYS ILE GLU ASP
SEQRES 28 B 485 ASP PRO PHE GLU ASN LEU GLU ASP THR ASP ASP LEU PHE
SEQRES 29 B 485 LYS THR ASN LEU ASN ILE GLU THR THR VAL VAL GLU ARG
SEQRES 30 B 485 LYS LEU ILE ARG LYS LEU ALA GLU LEU VAL GLY THR ARG
SEQRES 31 B 485 ALA ALA ARG LEU THR VAL CYS GLY VAL SER ALA ILE CYS
SEQRES 32 B 485 ASP LYS ARG GLY TYR LYS THR ALA HIS ILE ALA ALA ASP
SEQRES 33 B 485 GLY SER VAL PHE ASN ARG TYR PRO GLY TYR LYS GLU LYS
SEQRES 34 B 485 ALA ALA GLN ALA LEU LYS ASP ILE TYR ASN TRP ASP VAL
SEQRES 35 B 485 GLU LYS MET GLU ASP HIS PRO ILE GLN LEU VAL ALA ALA
SEQRES 36 B 485 GLU ASP GLY SER GLY VAL GLY ALA ALA ILE ILE ALA CYS
SEQRES 37 B 485 LEU THR GLN LYS ARG LEU ALA ALA GLY LYS SER VAL GLY
SEQRES 38 B 485 ILE LYS GLY GLU
HET GOL A 486 6
HET GOL A 487 6
HET PO4 A 488 5
HET GOL B 486 6
HET GOL B 487 6
HET GOL B 488 6
HET PO4 B 489 5
HET PO4 B 490 5
HETNAM GOL GLYCEROL
HETNAM PO4 PHOSPHATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 5(C3 H8 O3)
FORMUL 5 PO4 3(O4 P 3-)
FORMUL 11 HOH *630(H2 O)
HELIX 1 1 PRO A 20 THR A 35 1 16
HELIX 2 2 SER A 37 SER A 57 1 21
HELIX 3 3 PRO A 115 GLY A 121 5 7
HELIX 4 4 THR A 122 TYR A 142 1 21
HELIX 5 5 ASP A 186 LEU A 198 1 13
HELIX 6 6 ASN A 209 ASP A 222 1 14
HELIX 7 7 SER A 244 GLU A 250 5 7
HELIX 8 8 GLU A 268 PHE A 272 5 5
HELIX 9 9 THR A 282 SER A 292 1 11
HELIX 10 10 GLN A 298 SER A 305 1 8
HELIX 11 11 TYR A 308 SER A 323 1 16
HELIX 12 12 ILE A 332 GLU A 337 5 6
HELIX 13 13 THR A 343 ASP A 352 1 10
HELIX 14 14 LEU A 357 ASN A 369 1 13
HELIX 15 15 THR A 373 GLY A 407 1 35
HELIX 16 16 GLY A 417 TYR A 423 1 7
HELIX 17 17 GLY A 425 ASN A 439 1 15
HELIX 18 18 LYS A 444 HIS A 448 5 5
HELIX 19 19 GLY A 460 ALA A 476 1 17
HELIX 20 20 PRO B 20 THR B 35 1 16
HELIX 21 21 SER B 37 SER B 57 1 21
HELIX 22 22 PRO B 115 THR B 120 5 6
HELIX 23 23 THR B 122 TYR B 142 1 21
HELIX 24 24 ASP B 186 LEU B 198 1 13
HELIX 25 25 ASN B 209 ASP B 222 1 14
HELIX 26 26 SER B 244 GLU B 250 5 7
HELIX 27 27 GLU B 268 PHE B 272 5 5
HELIX 28 28 THR B 282 GLU B 291 1 10
HELIX 29 29 GLN B 298 SER B 305 1 8
HELIX 30 30 TYR B 308 SER B 323 1 16
HELIX 31 31 ILE B 332 GLU B 337 5 6
HELIX 32 32 THR B 343 ASP B 352 1 10
HELIX 33 33 LEU B 357 ASN B 369 1 13
HELIX 34 34 THR B 373 GLY B 407 1 35
HELIX 35 35 GLY B 417 TYR B 423 1 7
HELIX 36 36 GLY B 425 ASN B 439 1 15
HELIX 37 37 LYS B 444 HIS B 448 5 5
HELIX 38 38 GLY B 460 ALA B 476 1 17
SHEET 1 A 6 ILE A 66 PRO A 67 0
SHEET 2 A 6 PRO A 262 ASN A 266 -1 O ASN A 266 N ILE A 66
SHEET 3 A 6 VAL A 235 VAL A 242 -1 N TYR A 239 O ILE A 265
SHEET 4 A 6 THR A 225 ILE A 231 -1 N ILE A 230 O ASN A 236
SHEET 5 A 6 ALA A 411 ASP A 416 1 O HIS A 412 N LYS A 226
SHEET 6 A 6 ILE A 450 ALA A 454 1 O VAL A 453 N ALA A 415
SHEET 1 B 5 PHE A 105 ARG A 113 0
SHEET 2 B 5 ASN A 91 GLY A 100 -1 N LEU A 92 O TYR A 112
SHEET 3 B 5 THR A 79 LEU A 87 -1 N PHE A 82 O VAL A 97
SHEET 4 B 5 LEU A 150 THR A 155 1 O THR A 155 N LEU A 85
SHEET 5 B 5 ILE A 202 ILE A 208 1 O ASN A 203 N LEU A 152
SHEET 1 C 2 ALA A 160 SER A 161 0
SHEET 2 C 2 VAL A 169 LEU A 170 -1 O VAL A 169 N SER A 161
SHEET 1 D 6 ILE B 66 PRO B 67 0
SHEET 2 D 6 PRO B 262 ASN B 266 -1 O ASN B 266 N ILE B 66
SHEET 3 D 6 VAL B 235 VAL B 242 -1 N TYR B 239 O ILE B 265
SHEET 4 D 6 THR B 225 ILE B 231 -1 N ILE B 230 O ASN B 236
SHEET 5 D 6 ALA B 411 ASP B 416 1 O HIS B 412 N LYS B 226
SHEET 6 D 6 ILE B 450 ALA B 454 1 O VAL B 453 N ALA B 415
SHEET 1 E 5 PHE B 105 ARG B 113 0
SHEET 2 E 5 ASN B 91 GLY B 100 -1 N LEU B 92 O TYR B 112
SHEET 3 E 5 THR B 79 LEU B 87 -1 N PHE B 82 O VAL B 97
SHEET 4 E 5 LEU B 150 THR B 155 1 O THR B 155 N LEU B 85
SHEET 5 E 5 ILE B 202 ILE B 208 1 O ALA B 206 N PHE B 154
SHEET 1 F 2 ALA B 160 SER B 161 0
SHEET 2 F 2 VAL B 169 LEU B 170 -1 O VAL B 169 N SER B 161
SITE 1 AC1 7 ASN A 209 ASP A 210 THR A 211 GLY A 234
SITE 2 AC1 7 VAL A 235 ASN A 236 HOH A 579
SITE 1 AC2 9 PHE A 156 TYR A 158 ALA A 160 GLN A 162
SITE 2 AC2 9 HOH A 537 HOH A 575 HOH A 630 HOH A 684
SITE 3 AC2 9 HOH A 828
SITE 1 AC3 4 GLY A 232 THR A 233 GLY A 417 SER A 418
SITE 1 AC4 6 ASN B 209 ASP B 210 THR B 211 GLY B 234
SITE 2 AC4 6 VAL B 235 ASN B 236
SITE 1 AC5 4 THR A 372 THR A 373 VAL A 374 ARG A 377
SITE 1 AC6 3 HIS B 185 ASP B 186 HOH B 551
SITE 1 AC7 3 THR B 233 GLY B 417 SER B 418
SITE 1 AC8 5 SER B 37 SER B 38 GLU B 39 HOH B 702
SITE 2 AC8 5 HOH B 772
CRYST1 50.540 93.590 114.290 90.00 102.42 90.00 P 1 21 1 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 0.019786 0.000000 0.004358 0.00000
SCALE2 0.000000 0.010685 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008959 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
