HEADER CELL CYCLE 22-SEP-12 4BBG
TITLE CRYSTAL STRUCTURE OF HUMAN KINESIN EG5 IN COMPLEX WITH 3-(((2-
TITLE 2 AMINOETHYL)SULFANYL)(3-ETHYLPHENYL) PHENYLMETHYL)PHENOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KINESIN-LIKE PROTEIN KIF11;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: MOTOR DOMAIN, RESIDUES 1 - 368;
COMPND 5 SYNONYM: KINESIN-LIKE PROTEIN 1, KINESIN-LIKE SPINDLE PROTEIN HKSP,
COMPND 6 KINESIN-RELATED MOTOR PROTEIN EG5, THYROID RECEPTOR-INTERACTING
COMPND 7 PROTEIN 5, TR-INTERACTING PROTEIN 5, TRIP-5;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: PLYSS
KEYWDS CELL CYCLE, MITOSIS, INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR H.Y.K.KAAN,F.KOZIELSKI
REVDAT 2 20-DEC-23 4BBG 1 REMARK LINK
REVDAT 1 15-MAY-13 4BBG 0
JRNL AUTH J.A.D.GOOD,F.WANG,O.RATH,H.Y.K.KAAN,S.K.TALAPATRA,
JRNL AUTH 2 D.PODGORSKI,S.P.MACKAY,F.KOZIELSKI
JRNL TITL OPTIMIZED S-TRITYL-L-CYSTEINE-BASED INHIBITORS OF KINESIN
JRNL TITL 2 SPINDLE PROTEIN WITH POTENT IN VIVO ANTITUMOR ACTIVITY IN
JRNL TITL 3 LUNG CANCER XENOGRAFT MODELS.
JRNL REF J.MED.CHEM. V. 56 1878 2013
JRNL REFN ISSN 0022-2623
JRNL PMID 23394180
JRNL DOI 10.1021/JM3014597
REMARK 2
REMARK 2 RESOLUTION. 2.75 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) : 2.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 16379
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) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 874
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) : 2.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.82
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1212
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2170
REMARK 3 BIN FREE R VALUE SET COUNT : 66
REMARK 3 BIN FREE R VALUE : 0.3040
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2618
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 59
REMARK 3 SOLVENT ATOMS : 93
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.85
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.372
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.265
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.183
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.799
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.916
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2730 ; 0.022 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3704 ; 2.017 ; 1.993
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 338 ; 7.190 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 118 ;36.620 ;24.237
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 487 ;19.239 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;17.796 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 434 ; 0.125 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2008 ; 0.008 ; 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): 1677 ; 1.179 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2729 ; 2.282 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1053 ; 3.186 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 973 ; 5.603 ; 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 : 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. U VALUES REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4BBG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-SEP-12.
REMARK 100 THE DEPOSITION ID IS D_1290047494.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-NOV-10
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.873
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17253
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.600
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.60
REMARK 200 R MERGE FOR SHELL (I) : 0.43000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3KEN
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22 % POLYETHYLENE GLYCOL-3350, 0.3 M
REMARK 280 AMMONIUM SULPHATE, 0.1 M MES PH 5.5 AND 0.01 M TRIMETHYLAMINE
REMARK 280 HYDROCHLORIDE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
REMARK 290 13555 X+1/2,Y+1/2,Z+1/2
REMARK 290 14555 -X,-Y+1/2,Z
REMARK 290 15555 -X+1/2,Y,-Z
REMARK 290 16555 X,-Y,-Z+1/2
REMARK 290 17555 Z+1/2,X+1/2,Y+1/2
REMARK 290 18555 Z,-X,-Y+1/2
REMARK 290 19555 -Z,-X+1/2,Y
REMARK 290 20555 -Z+1/2,X,-Y
REMARK 290 21555 Y+1/2,Z+1/2,X+1/2
REMARK 290 22555 -Y+1/2,Z,-X
REMARK 290 23555 Y,-Z,-X+1/2
REMARK 290 24555 -Y,-Z+1/2,X
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 79.09500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 79.09500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 79.09500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 79.09500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 79.09500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 79.09500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 79.09500
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 79.09500
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 79.09500
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 79.09500
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 79.09500
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 79.09500
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 79.09500
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 79.09500
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 79.09500
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 79.09500
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 79.09500
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 79.09500
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 79.09500
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 79.09500
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 79.09500
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 79.09500
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 79.09500
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 79.09500
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 79.09500
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 79.09500
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 79.09500
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 79.09500
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 79.09500
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 79.09500
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 79.09500
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 79.09500
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 79.09500
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 79.09500
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 79.09500
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 79.09500
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 45230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -174.1 KCAL/MOL
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 BIOMT1 2 0.000000 -1.000000 0.000000 79.09500
REMARK 350 BIOMT2 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT3 2 1.000000 0.000000 0.000000 -79.09500
REMARK 350 BIOMT1 3 0.000000 0.000000 1.000000 79.09500
REMARK 350 BIOMT2 3 -1.000000 0.000000 0.000000 79.09500
REMARK 350 BIOMT3 3 0.000000 -1.000000 0.000000 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 ALA A 2
REMARK 465 SER A 3
REMARK 465 GLN A 4
REMARK 465 PRO A 5
REMARK 465 ASN A 6
REMARK 465 SER A 7
REMARK 465 SER A 8
REMARK 465 ALA A 9
REMARK 465 LYS A 10
REMARK 465 LYS A 11
REMARK 465 LYS A 12
REMARK 465 GLU A 13
REMARK 465 GLU A 14
REMARK 465 LYS A 15
REMARK 465 GLY A 16
REMARK 465 GLY A 273
REMARK 465 ARG A 274
REMARK 465 SER A 275
REMARK 465 GLY A 276
REMARK 465 ALA A 277
REMARK 465 VAL A 278
REMARK 465 ASP A 279
REMARK 465 LYS A 280
REMARK 465 ARG A 281
REMARK 465 ALA A 282
REMARK 465 ARG A 283
REMARK 465 GLU A 284
REMARK 465 ALA A 285
REMARK 465 GLY A 286
REMARK 465 GLN A 367
REMARK 465 LYS A 368
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 123 CG CD OE1 OE2
REMARK 470 GLU A 129 CG CD OE1 OE2
REMARK 470 LYS A 191 CG CD CE NZ
REMARK 470 GLN A 212 CG CD OE1 NE2
REMARK 470 ARG A 234 CZ NH1 NH2
REMARK 470 ILE A 272 CG1 CG2 CD1
REMARK 470 GLU A 344 OE1 OE2
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 ASP A 170 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ARG A 221 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG A 221 NE - CZ - NH2 ANGL. DEV. = -3.9 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 122 -143.33 48.42
REMARK 500 GLU A 124 -71.38 55.09
REMARK 500 LEU A 132 0.11 -68.88
REMARK 500 ASP A 149 -11.95 -46.37
REMARK 500 THR A 152 128.00 33.78
REMARK 500 ARG A 189 67.67 -103.44
REMARK 500 ASN A 190 91.77 148.67
REMARK 500 LYS A 362 76.92 -117.05
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 MG A 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 112 OG1
REMARK 620 2 ADP A 600 O3B 93.3
REMARK 620 3 HOH A2033 O 76.9 93.7
REMARK 620 4 HOH A2034 O 87.4 87.6 164.3
REMARK 620 5 HOH A2035 O 95.1 171.4 86.5 94.6
REMARK 620 6 HOH A2092 O 177.6 88.2 101.1 94.5 83.4
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1368
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE V02 A 1370
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1II6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MITOTIC KINESIN EG5 IN COMPLEXWITH MG-ADP.
REMARK 900 RELATED ID: 1Q0B RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOTOR PROTEIN KSP IN COMPLEX WITHADP AND
REMARK 900 MONASTROL
REMARK 900 RELATED ID: 1X88 RELATED DB: PDB
REMARK 900 HUMAN EG5 MOTOR DOMAIN BOUND TO MG-ADP AND MONASTROL
REMARK 900 RELATED ID: 1YRS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF KSP IN COMPLEX WITH INHIBITOR 1
REMARK 900 RELATED ID: 2FKY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF KSP IN COMPLEX WITH INHIBITOR 13
REMARK 900 RELATED ID: 2FL2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF KSP IN COMPLEX WITH INHIBITOR 19
REMARK 900 RELATED ID: 2FL6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF KSP IN COMPLEX WITH INHIBITOR 6
REMARK 900 RELATED ID: 2G1Q RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF KSP IN COMPLEX WITH INHIBITOR 9H
REMARK 900 RELATED ID: 2GM1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MITOTIC KINESIN EG5 IN COMPLEXWITH MG-ADP
REMARK 900 AND N-(3-AMINOPROPYL)-N-((3- BENZYL-5-CHLORO-4-OXO-3,4-
REMARK 900 DIHYDROPYRROLO[2,1-F][ 1,2,4]TRIAZIN-2-YL)(CYCLOPROPYL)METHYL)-4-
REMARK 900 METHYLBENZAMIDE
REMARK 900 RELATED ID: 2UYI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF KSP IN COMPLEX WITH ADP AND THIOPHENE
REMARK 900 CONTAINING INHIBITOR 33
REMARK 900 RELATED ID: 2UYM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF KSP IN COMPLEX WITH ADP AND THIOPHENE
REMARK 900 CONTAINING INHIBITOR 37
REMARK 900 RELATED ID: 2WOG RELATED DB: PDB
REMARK 900 INTERMEDIATE AND FINAL STATES OF HUMAN KINESIN EG5 IN COMPLEX WITH
REMARK 900 S-TRITYL-L-CYSTEINE
REMARK 900 RELATED ID: 2X2R RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN KINESIN EG5 IN COMPLEX WITH (R)-2-AMINO-
REMARK 900 3-((4-CHLOROPHENYL)DIPHENYLMETHYLTHIO) PROPANOIC ACID
REMARK 900 RELATED ID: 2X7C RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN KINESIN EG5 IN COMPLEX WITH (S)-ENASTRON
REMARK 900 RELATED ID: 2X7D RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN KINESIN EG5 IN COMPLEX WITH (S)-
REMARK 900 DIMETHYLENASTRON
REMARK 900 RELATED ID: 2X7E RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN KINESIN EG5 IN COMPLEX WITH (R)-
REMARK 900 FLUORASTROL
REMARK 900 RELATED ID: 2XAE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN KINESIN EG5 IN COMPLEX WITH (R)-2-AMINO-
REMARK 900 3-((S)-2-METHYL-1,1-DIPHENYLBUTYLTHIO )PROPANOIC ACID
REMARK 900 RELATED ID: 4A1Z RELATED DB: PDB
REMARK 900 EG5-1
REMARK 900 RELATED ID: 4A28 RELATED DB: PDB
REMARK 900 EG5-2
REMARK 900 RELATED ID: 4A50 RELATED DB: PDB
REMARK 900 EG5-INHIBITOR COMPLEX
REMARK 900 RELATED ID: 4A51 RELATED DB: PDB
REMARK 900 EG5-INHIBITOR COMPLEX
REMARK 900 RELATED ID: 4A5Y RELATED DB: PDB
REMARK 900 INTERMEDIATE STATE OF HUMAN KINESIN EG5 IN COMPLEX WITH ISPINESIB
REMARK 900 RELATED ID: 4AP0 RELATED DB: PDB
REMARK 900 THE MITOTIC KINESIN EG5 IN COMPLEX WITH MG-ADP AND ISPINESIB
REMARK 900 RELATED ID: 4AQV RELATED DB: PDB
REMARK 900 MODEL OF HUMAN KINESIN-5 MOTOR DOMAIN (3HQD) AND MAMMALIAN TUBULIN
REMARK 900 HETERODIMER (1JFF) DOCKED INTO THE 9. 7-ANGSTROM CRYO-EM MAP OF
REMARK 900 MICROTUBULE-BOUND KINESIN- 5 MOTOR DOMAIN IN THE AMPPPNP STATE.
REMARK 900 RELATED ID: 4AQW RELATED DB: PDB
REMARK 900 MODEL OF HUMAN KINESIN-5 MOTOR DOMAIN (1II6, 3HQD) AND MAMMALIAN
REMARK 900 TUBULIN HETERODIMER (1JFF) DOCKED INTO THE 9.5-ANGSTROM CRYO-EM MAP
REMARK 900 OF MICROTUBULE-BOUND KINESIN-5 MOTOR DOMAIN IN THE RIGOR STATE.
REMARK 900 RELATED ID: 4AS7 RELATED DB: PDB
REMARK 900 EG5 COMPLEX 1
REMARK 900 RELATED ID: 4B7B RELATED DB: PDB
REMARK 900 EG5-3
DBREF 4BBG A 1 368 UNP P52732 KIF11_HUMAN 1 368
SEQRES 1 A 368 MET ALA SER GLN PRO ASN SER SER ALA LYS LYS LYS GLU
SEQRES 2 A 368 GLU LYS GLY LYS ASN ILE GLN VAL VAL VAL ARG CYS ARG
SEQRES 3 A 368 PRO PHE ASN LEU ALA GLU ARG LYS ALA SER ALA HIS SER
SEQRES 4 A 368 ILE VAL GLU CYS ASP PRO VAL ARG LYS GLU VAL SER VAL
SEQRES 5 A 368 ARG THR GLY GLY LEU ALA ASP LYS SER SER ARG LYS THR
SEQRES 6 A 368 TYR THR PHE ASP MET VAL PHE GLY ALA SER THR LYS GLN
SEQRES 7 A 368 ILE ASP VAL TYR ARG SER VAL VAL CYS PRO ILE LEU ASP
SEQRES 8 A 368 GLU VAL ILE MET GLY TYR ASN CYS THR ILE PHE ALA TYR
SEQRES 9 A 368 GLY GLN THR GLY THR GLY LYS THR PHE THR MET GLU GLY
SEQRES 10 A 368 GLU ARG SER PRO ASN GLU GLU TYR THR TRP GLU GLU ASP
SEQRES 11 A 368 PRO LEU ALA GLY ILE ILE PRO ARG THR LEU HIS GLN ILE
SEQRES 12 A 368 PHE GLU LYS LEU THR ASP ASN GLY THR GLU PHE SER VAL
SEQRES 13 A 368 LYS VAL SER LEU LEU GLU ILE TYR ASN GLU GLU LEU PHE
SEQRES 14 A 368 ASP LEU LEU ASN PRO SER SER ASP VAL SER GLU ARG LEU
SEQRES 15 A 368 GLN MET PHE ASP ASP PRO ARG ASN LYS ARG GLY VAL ILE
SEQRES 16 A 368 ILE LYS GLY LEU GLU GLU ILE THR VAL HIS ASN LYS ASP
SEQRES 17 A 368 GLU VAL TYR GLN ILE LEU GLU LYS GLY ALA ALA LYS ARG
SEQRES 18 A 368 THR THR ALA ALA THR LEU MET ASN ALA TYR SER SER ARG
SEQRES 19 A 368 SER HIS SER VAL PHE SER VAL THR ILE HIS MET LYS GLU
SEQRES 20 A 368 THR THR ILE ASP GLY GLU GLU LEU VAL LYS ILE GLY LYS
SEQRES 21 A 368 LEU ASN LEU VAL ASP LEU ALA GLY SER GLU ASN ILE GLY
SEQRES 22 A 368 ARG SER GLY ALA VAL ASP LYS ARG ALA ARG GLU ALA GLY
SEQRES 23 A 368 ASN ILE ASN GLN SER LEU LEU THR LEU GLY ARG VAL ILE
SEQRES 24 A 368 THR ALA LEU VAL GLU ARG THR PRO HIS VAL PRO TYR ARG
SEQRES 25 A 368 GLU SER LYS LEU THR ARG ILE LEU GLN ASP SER LEU GLY
SEQRES 26 A 368 GLY ARG THR ARG THR SER ILE ILE ALA THR ILE SER PRO
SEQRES 27 A 368 ALA SER LEU ASN LEU GLU GLU THR LEU SER THR LEU GLU
SEQRES 28 A 368 TYR ALA HIS ARG ALA LYS ASN ILE LEU ASN LYS PRO GLU
SEQRES 29 A 368 VAL ASN GLN LYS
HET ADP A 600 27
HET MG A 601 1
HET CL A1367 1
HET CL A1368 1
HET CL A1369 1
HET V02 A1370 26
HET CL A1371 1
HET CL A1372 1
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
HETNAM V02 3-[(R)-2-AZANYLETHYLSULFANYL-(3-ETHYLPHENYL)-PHENYL-
HETNAM 2 V02 METHYL]PHENOL
FORMUL 2 ADP C10 H15 N5 O10 P2
FORMUL 3 MG MG 2+
FORMUL 4 CL 5(CL 1-)
FORMUL 7 V02 C23 H25 N O S
FORMUL 10 HOH *93(H2 O)
HELIX 1 1 ASN A 29 ALA A 35 1 7
HELIX 2 2 LYS A 77 MET A 95 1 19
HELIX 3 3 GLY A 110 GLU A 116 1 7
HELIX 4 4 GLY A 134 ASP A 149 1 16
HELIX 5 5 GLU A 209 MET A 228 1 20
HELIX 6 6 ALA A 230 SER A 235 1 6
HELIX 7 7 ASN A 289 GLU A 304 1 16
HELIX 8 8 PRO A 310 GLU A 313 5 4
HELIX 9 9 SER A 314 LEU A 320 1 7
HELIX 10 10 GLN A 321 LEU A 324 5 4
HELIX 11 11 ASN A 342 ALA A 356 1 15
HELIX 12 12 LYS A 357 ILE A 359 5 3
SHEET 1 AA 8 MET A 70 PHE A 72 0
SHEET 2 AA 8 GLN A 20 CYS A 25 1 O VAL A 23 N PHE A 72
SHEET 3 AA 8 ARG A 329 ILE A 336 1 O THR A 330 N GLN A 20
SHEET 4 AA 8 ASN A 98 GLY A 105 1 O ASN A 98 N ARG A 329
SHEET 5 AA 8 GLU A 254 ASP A 265 1 O LYS A 260 N CYS A 99
SHEET 6 AA 8 HIS A 236 THR A 248 -1 O SER A 237 N ASP A 265
SHEET 7 AA 8 PHE A 154 TYR A 164 -1 O SER A 155 N HIS A 244
SHEET 8 AA 8 GLU A 167 ASP A 170 -1 O GLU A 167 N TYR A 164
SHEET 1 AB 8 MET A 70 PHE A 72 0
SHEET 2 AB 8 GLN A 20 CYS A 25 1 O VAL A 23 N PHE A 72
SHEET 3 AB 8 ARG A 329 ILE A 336 1 O THR A 330 N GLN A 20
SHEET 4 AB 8 ASN A 98 GLY A 105 1 O ASN A 98 N ARG A 329
SHEET 5 AB 8 GLU A 254 ASP A 265 1 O LYS A 260 N CYS A 99
SHEET 6 AB 8 HIS A 236 THR A 248 -1 O SER A 237 N ASP A 265
SHEET 7 AB 8 PHE A 154 TYR A 164 -1 O SER A 155 N HIS A 244
SHEET 8 AB 8 ILE A 202 VAL A 204 -1 O ILE A 202 N VAL A 158
SHEET 1 AC 2 GLU A 167 ASP A 170 0
SHEET 2 AC 2 PHE A 154 TYR A 164 -1 O GLU A 162 N PHE A 169
SHEET 1 AD 3 VAL A 41 ASP A 44 0
SHEET 2 AD 3 GLU A 49 GLY A 55 -1 O GLU A 49 N ASP A 44
SHEET 3 AD 3 ASP A 59 THR A 67 -1 N ASP A 59 O GLY A 55
SHEET 1 AE 2 GLN A 183 ASP A 186 0
SHEET 2 AE 2 VAL A 194 LYS A 197 -1 O ILE A 195 N PHE A 185
LINK OG1 THR A 112 MG MG A 601 1555 1555 2.32
LINK O3B ADP A 600 MG MG A 601 1555 1555 1.99
LINK MG MG A 601 O HOH A2033 1555 1555 1.89
LINK MG MG A 601 O HOH A2034 1555 1555 1.86
LINK MG MG A 601 O HOH A2035 1555 1555 1.95
LINK MG MG A 601 O HOH A2092 1555 1555 1.98
SITE 1 AC1 16 ARG A 24 ARG A 26 PRO A 27 THR A 107
SITE 2 AC1 16 GLY A 108 THR A 109 GLY A 110 LYS A 111
SITE 3 AC1 16 THR A 112 PHE A 113 GLU A 118 MG A 601
SITE 4 AC1 16 HOH A2005 HOH A2033 HOH A2034 HOH A2092
SITE 1 AC2 6 THR A 112 ADP A 600 HOH A2033 HOH A2034
SITE 2 AC2 6 HOH A2035 HOH A2092
SITE 1 AC3 2 ILE A 79 ARG A 138
SITE 1 AC4 6 GLU A 116 GLY A 117 GLU A 118 ALA A 133
SITE 2 AC4 6 PRO A 137 ARG A 221
CRYST1 158.190 158.190 158.190 90.00 90.00 90.00 I 21 3 24
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 0.006322 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006322 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006322 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
