HEADER TRANSFERASE 25-OCT-06 2NO9
TITLE THE STRUCTURE OF DEOXYCYTIDINE KINASE COMPLEXED WITH TROXACITABINE AND
TITLE 2 ADP.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEOXYCYTIDINE KINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DCK;
COMPND 5 EC: 2.7.1.74;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: DCK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET14B
KEYWDS DCK, TROXACITABINE, HUMAN DEOXYCYTIDINE KINASE, L-DC, ENANTIOMER,
KEYWDS 2 ANTICANCER, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.SABINI,A.LAVIE
REVDAT 5 30-AUG-23 2NO9 1 REMARK
REVDAT 4 20-OCT-21 2NO9 1 SEQADV
REVDAT 3 03-FEB-21 2NO9 1 JRNL REMARK
REVDAT 2 24-FEB-09 2NO9 1 VERSN
REVDAT 1 13-FEB-07 2NO9 0
JRNL AUTH E.SABINI,S.HAZRA,M.KONRAD,S.K.BURLEY,A.LAVIE
JRNL TITL STRUCTURAL BASIS FOR ACTIVATION OF THE THERAPEUTIC
JRNL TITL 2 L-NUCLEOSIDE ANALOGS 3TC AND TROXACITABINE BY HUMAN
JRNL TITL 3 DEOXYCYTIDINE KINASE.
JRNL REF NUCLEIC ACIDS RES. V. 35 186 2007
JRNL REFN ISSN 0305-1048
JRNL PMID 17158155
JRNL DOI 10.1093/NAR/GKL1038
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 27466
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) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3070
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) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.21
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2005
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2160
REMARK 3 BIN FREE R VALUE SET COUNT : 235
REMARK 3 BIN FREE R VALUE : 0.3090
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3850
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 84
REMARK 3 SOLVENT ATOMS : 79
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.23000
REMARK 3 B22 (A**2) : -0.70000
REMARK 3 B33 (A**2) : 0.47000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.258
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.217
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.146
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.467
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.914
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4033 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5483 ; 1.718 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 466 ; 6.092 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 202 ;39.473 ;24.455
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 681 ;17.245 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;18.746 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 590 ; 0.112 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3067 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1722 ; 0.209 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2761 ; 0.314 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 219 ; 0.174 ; 0.200
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): 62 ; 0.291 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.251 ; 0.200
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): 2402 ; 1.077 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3770 ; 1.793 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1923 ; 2.608 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1713 ; 3.851 ; 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
REMARK 4
REMARK 4 2NO9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-OCT-06.
REMARK 100 THE DEPOSITION ID IS D_1000040104.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-NOV-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK MONOCHROMATOR
REMARK 200 HIGH-RESOLUTION DOUBLE-CRYSTAL
REMARK 200 SI (111) SAGITTAL FOCUSING,
REMARK 200 ROSENBAUM-ROCK VERTICAL
REMARK 200 OPTICS : MIRRORS
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 : 30536
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
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 (%) : 99.7
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.51100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1P5Z
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR CONTAINING 0.95-1.5M
REMARK 280 TRISODIUM CITRATE DIHYDRATE AND 100MM HEPES, PH 7.5., VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 77.67000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 77.67000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 26.42500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 67.23000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 26.42500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 67.23000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 77.67000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 26.42500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 67.23000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 77.67000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 26.42500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 67.23000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: 5000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 134.46000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 155.34000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 26.42500
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 -67.23000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 26.42500
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 201.69000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 155.34000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 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 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 134.46000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 155.34000
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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 THR A 3
REMARK 465 PRO A 4
REMARK 465 PRO A 5
REMARK 465 LYS A 6
REMARK 465 ARG A 7
REMARK 465 SER A 8
REMARK 465 SER A 9
REMARK 465 PRO A 10
REMARK 465 SER A 11
REMARK 465 PHE A 12
REMARK 465 SER A 13
REMARK 465 ALA A 14
REMARK 465 SER A 15
REMARK 465 SER A 16
REMARK 465 GLU A 17
REMARK 465 GLY A 18
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 THR B 3
REMARK 465 PRO B 4
REMARK 465 PRO B 5
REMARK 465 LYS B 6
REMARK 465 ARG B 7
REMARK 465 SER B 8
REMARK 465 SER B 9
REMARK 465 PRO B 10
REMARK 465 SER B 11
REMARK 465 PHE B 12
REMARK 465 SER B 13
REMARK 465 ALA B 14
REMARK 465 SER B 15
REMARK 465 SER B 16
REMARK 465 GLU B 17
REMARK 465 GLY B 18
REMARK 465 THR B 19
REMARK 465 SER B 63
REMARK 465 THR B 64
REMARK 465 GLN B 65
REMARK 465 ASP B 66
REMARK 465 GLU B 67
REMARK 465 PHE B 68
REMARK 465 GLU B 69
REMARK 465 GLU B 70
REMARK 465 LEU B 71
REMARK 465 THR B 72
REMARK 465 MET B 73
REMARK 465 SER B 74
REMARK 465 GLN B 75
REMARK 465 LYS B 76
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 THR A 19 OG1 CG2
REMARK 470 GLN A 43 CG CD OE1 NE2
REMARK 470 GLU A 46 CG CD OE1 OE2
REMARK 470 LYS A 117 CG CD CE NZ
REMARK 470 ASP A 118 CG OD1 OD2
REMARK 470 GLU A 120 CG CD OE1 OE2
REMARK 470 LYS A 121 CG CD CE NZ
REMARK 470 SER A 146 OG
REMARK 470 GLN A 168 CG CD OE1 NE2
REMARK 470 TYR A 190 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN A 229 CG CD OE1 NE2
REMARK 470 GLU A 251 CG CD OE1 OE2
REMARK 470 SER B 45 OG
REMARK 470 SER B 59 OG
REMARK 470 LYS B 117 CG CD CE NZ
REMARK 470 ASP B 118 CG OD1 OD2
REMARK 470 LYS B 121 CG CD CE NZ
REMARK 470 GLN B 168 CG CD OE1 NE2
REMARK 470 LYS B 222 CG CD CE NZ
REMARK 470 LYS B 243 CG CD CE NZ
REMARK 470 GLU B 247 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 310 O HOH A 337 2.15
REMARK 500 O SER A 45 O HOH A 345 2.17
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 PRO A 54 44.83 -75.32
REMARK 500 ARG A 128 174.45 64.05
REMARK 500 ILE A 136 -69.12 -107.64
REMARK 500 ASN A 224 2.14 -69.93
REMARK 500 PRO B 54 48.80 -77.44
REMARK 500 LYS B 115 143.57 172.91
REMARK 500 LEU B 116 -125.28 64.85
REMARK 500 LYS B 117 -28.81 50.92
REMARK 500 GLU B 120 -71.99 -50.66
REMARK 500 ARG B 128 -179.43 67.17
REMARK 500 ILE B 136 -68.15 -107.48
REMARK 500 GLN B 165 -88.40 -80.97
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 ADP A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LTT A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LTT B 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1P5Z RELATED DB: PDB
REMARK 900 WILD TYPE HUMAN DEOXYCYTIDINE KINASE IN COMPLEX WITH CYTARABINE AND
REMARK 900 ADP-MG
REMARK 900 RELATED ID: 1P60 RELATED DB: PDB
REMARK 900 WILD TYPE HUMAN DEOXYCYTIDINE KINASE IN COMPLEX WITH DEOXYCYTIDINE
REMARK 900 AND ADP
REMARK 900 RELATED ID: 1P61 RELATED DB: PDB
REMARK 900 WILD TYPE HUMAN DEOXYCYTIDINE KINASE IN COMPLEX WITH DEOXYCYTIDINE
REMARK 900 AND ADP
REMARK 900 RELATED ID: 1P62 RELATED DB: PDB
REMARK 900 WILD TYPE HUMAN DEOXYCYTIDINE KINASE IN COMPLEX WITH GEMCITABINE
REMARK 900 AND ADP-MG
REMARK 900 RELATED ID: 2A2Z RELATED DB: PDB
REMARK 900 INSERT-DELETION MUTANT OF HUMAN DEOXYCYTIDINE KINASE IN COMPLEX
REMARK 900 WITH DEOXYCYTIDINE AND UDP
REMARK 900 RELATED ID: 2A30 RELATED DB: PDB
REMARK 900 INSERT-DELETION MUTANT OF HUMAN DEOXYCYTIDINE KINASE IN COMPLEX
REMARK 900 WITH DEOXYCYTIDINE
REMARK 900 RELATED ID: 2NO0 RELATED DB: PDB
REMARK 900 RELATED ID: 2NO1 RELATED DB: PDB
REMARK 900 RELATED ID: 1NO6 RELATED DB: PDB
REMARK 900 RELATED ID: 2NO7 RELATED DB: PDB
REMARK 900 RELATED ID: 2NOA RELATED DB: PDB
DBREF 2NO9 A 1 260 UNP P27707 DCK_HUMAN 1 260
DBREF 2NO9 B 1 260 UNP P27707 DCK_HUMAN 1 260
SEQADV 2NO9 MET A -19 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 GLY A -18 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 SER A -17 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 SER A -16 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 HIS A -15 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 HIS A -14 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 HIS A -13 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 HIS A -12 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 HIS A -11 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 HIS A -10 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 SER A -9 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 SER A -8 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 GLY A -7 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 LEU A -6 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 VAL A -5 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 PRO A -4 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 ARG A -3 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 GLY A -2 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 SER A -1 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 HIS A 0 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 SER A 9 UNP P27707 CYS 9 ENGINEERED MUTATION
SEQADV 2NO9 SER A 45 UNP P27707 CYS 45 ENGINEERED MUTATION
SEQADV 2NO9 SER A 59 UNP P27707 CYS 59 ENGINEERED MUTATION
SEQADV 2NO9 SER A 146 UNP P27707 CYS 146 ENGINEERED MUTATION
SEQADV 2NO9 MET B -19 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 GLY B -18 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 SER B -17 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 SER B -16 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 HIS B -15 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 HIS B -14 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 HIS B -13 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 HIS B -12 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 HIS B -11 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 HIS B -10 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 SER B -9 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 SER B -8 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 GLY B -7 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 LEU B -6 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 VAL B -5 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 PRO B -4 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 ARG B -3 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 GLY B -2 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 SER B -1 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 HIS B 0 UNP P27707 CLONING ARTIFACT
SEQADV 2NO9 SER B 9 UNP P27707 CYS 9 ENGINEERED MUTATION
SEQADV 2NO9 SER B 45 UNP P27707 CYS 45 ENGINEERED MUTATION
SEQADV 2NO9 SER B 59 UNP P27707 CYS 59 ENGINEERED MUTATION
SEQADV 2NO9 SER B 146 UNP P27707 CYS 146 ENGINEERED MUTATION
SEQRES 1 A 280 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 280 LEU VAL PRO ARG GLY SER HIS MET ALA THR PRO PRO LYS
SEQRES 3 A 280 ARG SER SER PRO SER PHE SER ALA SER SER GLU GLY THR
SEQRES 4 A 280 ARG ILE LYS LYS ILE SER ILE GLU GLY ASN ILE ALA ALA
SEQRES 5 A 280 GLY LYS SER THR PHE VAL ASN ILE LEU LYS GLN LEU SER
SEQRES 6 A 280 GLU ASP TRP GLU VAL VAL PRO GLU PRO VAL ALA ARG TRP
SEQRES 7 A 280 SER ASN VAL GLN SER THR GLN ASP GLU PHE GLU GLU LEU
SEQRES 8 A 280 THR MET SER GLN LYS ASN GLY GLY ASN VAL LEU GLN MET
SEQRES 9 A 280 MET TYR GLU LYS PRO GLU ARG TRP SER PHE THR PHE GLN
SEQRES 10 A 280 THR TYR ALA CYS LEU SER ARG ILE ARG ALA GLN LEU ALA
SEQRES 11 A 280 SER LEU ASN GLY LYS LEU LYS ASP ALA GLU LYS PRO VAL
SEQRES 12 A 280 LEU PHE PHE GLU ARG SER VAL TYR SER ASP ARG TYR ILE
SEQRES 13 A 280 PHE ALA SER ASN LEU TYR GLU SER GLU SER MET ASN GLU
SEQRES 14 A 280 THR GLU TRP THR ILE TYR GLN ASP TRP HIS ASP TRP MET
SEQRES 15 A 280 ASN ASN GLN PHE GLY GLN SER LEU GLU LEU ASP GLY ILE
SEQRES 16 A 280 ILE TYR LEU GLN ALA THR PRO GLU THR CYS LEU HIS ARG
SEQRES 17 A 280 ILE TYR LEU ARG GLY ARG ASN GLU GLU GLN GLY ILE PRO
SEQRES 18 A 280 LEU GLU TYR LEU GLU LYS LEU HIS TYR LYS HIS GLU SER
SEQRES 19 A 280 TRP LEU LEU HIS ARG THR LEU LYS THR ASN PHE ASP TYR
SEQRES 20 A 280 LEU GLN GLU VAL PRO ILE LEU THR LEU ASP VAL ASN GLU
SEQRES 21 A 280 ASP PHE LYS ASP LYS TYR GLU SER LEU VAL GLU LYS VAL
SEQRES 22 A 280 LYS GLU PHE LEU SER THR LEU
SEQRES 1 B 280 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 280 LEU VAL PRO ARG GLY SER HIS MET ALA THR PRO PRO LYS
SEQRES 3 B 280 ARG SER SER PRO SER PHE SER ALA SER SER GLU GLY THR
SEQRES 4 B 280 ARG ILE LYS LYS ILE SER ILE GLU GLY ASN ILE ALA ALA
SEQRES 5 B 280 GLY LYS SER THR PHE VAL ASN ILE LEU LYS GLN LEU SER
SEQRES 6 B 280 GLU ASP TRP GLU VAL VAL PRO GLU PRO VAL ALA ARG TRP
SEQRES 7 B 280 SER ASN VAL GLN SER THR GLN ASP GLU PHE GLU GLU LEU
SEQRES 8 B 280 THR MET SER GLN LYS ASN GLY GLY ASN VAL LEU GLN MET
SEQRES 9 B 280 MET TYR GLU LYS PRO GLU ARG TRP SER PHE THR PHE GLN
SEQRES 10 B 280 THR TYR ALA CYS LEU SER ARG ILE ARG ALA GLN LEU ALA
SEQRES 11 B 280 SER LEU ASN GLY LYS LEU LYS ASP ALA GLU LYS PRO VAL
SEQRES 12 B 280 LEU PHE PHE GLU ARG SER VAL TYR SER ASP ARG TYR ILE
SEQRES 13 B 280 PHE ALA SER ASN LEU TYR GLU SER GLU SER MET ASN GLU
SEQRES 14 B 280 THR GLU TRP THR ILE TYR GLN ASP TRP HIS ASP TRP MET
SEQRES 15 B 280 ASN ASN GLN PHE GLY GLN SER LEU GLU LEU ASP GLY ILE
SEQRES 16 B 280 ILE TYR LEU GLN ALA THR PRO GLU THR CYS LEU HIS ARG
SEQRES 17 B 280 ILE TYR LEU ARG GLY ARG ASN GLU GLU GLN GLY ILE PRO
SEQRES 18 B 280 LEU GLU TYR LEU GLU LYS LEU HIS TYR LYS HIS GLU SER
SEQRES 19 B 280 TRP LEU LEU HIS ARG THR LEU LYS THR ASN PHE ASP TYR
SEQRES 20 B 280 LEU GLN GLU VAL PRO ILE LEU THR LEU ASP VAL ASN GLU
SEQRES 21 B 280 ASP PHE LYS ASP LYS TYR GLU SER LEU VAL GLU LYS VAL
SEQRES 22 B 280 LYS GLU PHE LEU SER THR LEU
HET ADP A 301 27
HET LTT A 302 15
HET ADP B 301 27
HET LTT B 302 15
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM LTT 4-AMINO-1-[(2S,4S)-2-(HYDROXYMETHYL)-1,3-DIOXOLAN-4-
HETNAM 2 LTT YL]PYRIMIDIN-2(1H)-ONE
HETSYN LTT (-)-L-2',3'-DIDEOXY-3'-OXACYTIDINE; TROXACITABINE;
HETSYN 2 LTT TROXATYL
FORMUL 3 ADP 2(C10 H15 N5 O10 P2)
FORMUL 4 LTT 2(C8 H11 N3 O4)
FORMUL 7 HOH *79(H2 O)
HELIX 1 1 GLY A 33 LYS A 42 1 10
HELIX 2 2 GLN A 43 SER A 45 5 3
HELIX 3 3 PRO A 54 ASN A 60 1 7
HELIX 4 4 PHE A 68 THR A 72 5 5
HELIX 5 5 ASN A 80 LYS A 88 1 9
HELIX 6 6 LYS A 88 LYS A 115 1 28
HELIX 7 7 SER A 129 ILE A 136 1 8
HELIX 8 8 ILE A 136 SER A 144 1 9
HELIX 9 9 ASN A 148 GLY A 167 1 20
HELIX 10 10 THR A 181 GLY A 193 1 13
HELIX 11 11 ARG A 194 GLN A 198 5 5
HELIX 12 12 PRO A 201 LEU A 217 1 17
HELIX 13 13 PHE A 225 GLU A 230 5 6
HELIX 14 14 ASP A 241 ASP A 244 5 4
HELIX 15 15 LYS A 245 LEU A 260 1 16
HELIX 16 16 GLY B 33 LYS B 42 1 10
HELIX 17 17 GLN B 43 SER B 45 5 3
HELIX 18 18 PRO B 54 ASN B 60 1 7
HELIX 19 19 ASN B 80 LYS B 88 1 9
HELIX 20 20 LYS B 88 GLY B 114 1 27
HELIX 21 21 SER B 129 ILE B 136 1 8
HELIX 22 22 ILE B 136 SER B 144 1 9
HELIX 23 23 ASN B 148 GLY B 167 1 20
HELIX 24 24 THR B 181 GLY B 193 1 13
HELIX 25 25 ARG B 194 GLN B 198 5 5
HELIX 26 26 PRO B 201 LEU B 217 1 17
HELIX 27 27 PHE B 225 VAL B 231 5 7
HELIX 28 28 LYS B 245 LEU B 260 1 16
SHEET 1 A 5 TRP A 48 VAL A 51 0
SHEET 2 A 5 VAL A 123 GLU A 127 1 O PHE A 125 N GLU A 49
SHEET 3 A 5 LYS A 22 GLU A 27 1 N ILE A 26 O PHE A 126
SHEET 4 A 5 GLY A 174 GLN A 179 1 O ILE A 176 N SER A 25
SHEET 5 A 5 ILE A 233 ASP A 237 1 O LEU A 234 N TYR A 177
SHEET 1 B 5 TRP B 48 VAL B 51 0
SHEET 2 B 5 VAL B 123 GLU B 127 1 O PHE B 125 N GLU B 49
SHEET 3 B 5 LYS B 22 GLU B 27 1 N LYS B 22 O LEU B 124
SHEET 4 B 5 GLY B 174 GLN B 179 1 O ILE B 176 N GLU B 27
SHEET 5 B 5 ILE B 233 ASP B 237 1 O LEU B 234 N TYR B 177
SITE 1 AC1 17 ALA A 31 ALA A 32 GLY A 33 LYS A 34
SITE 2 AC1 17 SER A 35 THR A 36 ARG A 188 ARG A 192
SITE 3 AC1 17 GLU A 240 ASP A 241 PHE A 242 HOH A 314
SITE 4 AC1 17 HOH A 319 HOH A 326 HOH A 338 ASP B 241
SITE 5 AC1 17 PHE B 242
SITE 1 AC2 13 ILE A 30 GLU A 53 TRP A 58 LEU A 82
SITE 2 AC2 13 TYR A 86 PHE A 96 GLN A 97 ARG A 128
SITE 3 AC2 13 ASP A 133 PHE A 137 HOH A 308 HOH A 326
SITE 4 AC2 13 HOH A 350
SITE 1 AC3 16 ASP A 241 LYS A 243 ALA B 31 ALA B 32
SITE 2 AC3 16 GLY B 33 LYS B 34 SER B 35 THR B 36
SITE 3 AC3 16 ARG B 188 ARG B 192 GLU B 240 ASP B 241
SITE 4 AC3 16 PHE B 242 TYR B 246 HOH B 310 HOH B 329
SITE 1 AC4 9 GLU B 53 LEU B 82 TYR B 86 PHE B 96
SITE 2 AC4 9 GLN B 97 ARG B 128 ASP B 133 PHE B 137
SITE 3 AC4 9 HOH B 322
CRYST1 52.850 134.460 155.340 90.00 90.00 90.00 C 2 2 21 16
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 0.018921 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007437 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006437 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
