HEADER TRANSFERASE 26-JAN-07 2E9O
TITLE STRUCTURE OF H-CHK1 COMPLEXED WITH AA582939
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE CHK1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 2-270;
COMPND 5 EC: 2.7.11.1;
COMPND 6 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: 562
KEYWDS PROTEIN-INHIBITOR COMPLEX, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.PARK
REVDAT 3 13-MAR-24 2E9O 1 REMARK
REVDAT 2 24-FEB-09 2E9O 1 VERSN
REVDAT 1 29-JAN-08 2E9O 0
JRNL AUTH Y.TONG,A.CLAIBORNE,K.D.STEWART,C.PARK,P.KOVAR,Z.CHEN,
JRNL AUTH 2 R.B.CREDO,W.Z.GU,S.L.GWALTNEY,R.A.JUDGE,H.ZHANG,
JRNL AUTH 3 S.H.ROSENBERG,H.L.SHAM,T.J.SOWIN,N.H.LIN
JRNL TITL DISCOVERY OF 1,4-DIHYDROINDENO[1,2-C]PYRAZOLES AS A NOVEL
JRNL TITL 2 CLASS OF POTENT AND SELECTIVE CHECKPOINT KINASE 1
JRNL TITL 3 INHIBITORS.
JRNL REF BIOORG.MED.CHEM. V. 15 2759 2007
JRNL REFN ISSN 0968-0896
JRNL PMID 17287122
JRNL DOI 10.1016/J.BMC.2007.01.012
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX 2002
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN,ACCELRYS
REMARK 3 : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,
REMARK 3 : YIP,DZAKULA)
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 17.95
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 294284.860
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 88.7
REMARK 3 NUMBER OF REFLECTIONS : 17460
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) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1722
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 19667
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.17
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 74.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1294
REMARK 3 BIN R VALUE (WORKING SET) : 0.2240
REMARK 3 BIN FREE R VALUE : 0.2750
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 147
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.023
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2185
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 336
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.34000
REMARK 3 B22 (A**2) : 4.82000
REMARK 3 B33 (A**2) : -0.49000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.97000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.11
REMARK 3 LOW RESOLUTION CUTOFF (A) : 6.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.31
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.19
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.810
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.680 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.240 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 0.730 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 1.150 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 56.94
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : A58.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : A58.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2E9O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-FEB-07.
REMARK 100 THE DEPOSITION ID IS D_1000026400.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-02
REMARK 200 TEMPERATURE (KELVIN) : 110.0
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 : 17-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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 130 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18735
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.17
REMARK 200 COMPLETENESS FOR SHELL (%) : 74.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.22900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, ISOPROPANOL, HEPES, PH 7.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298.0K
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 32.85550
REMARK 290 SMTRY3 2 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: MONOMERIC
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 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 PHE A 5 -10.24 73.61
REMARK 500 VAL A 30 -60.36 -90.78
REMARK 500 MET A 42 80.49 -65.12
REMARK 500 ARG A 44 -113.23 67.45
REMARK 500 ALA A 45 -82.48 -170.35
REMARK 500 ASP A 47 -121.82 -67.98
REMARK 500 PRO A 49 -32.17 -36.52
REMARK 500 ASN A 63 87.48 -157.57
REMARK 500 ILE A 100 -54.41 -120.38
REMARK 500 ASP A 130 48.09 -154.25
REMARK 500 ASP A 142 30.44 72.11
REMARK 500 ASP A 148 94.25 64.14
REMARK 500 ASN A 165 -11.73 -148.05
REMARK 500 LEU A 171 -51.10 -26.55
REMARK 500 LEU A 228 -45.94 49.61
REMARK 500 ASN A 229 162.73 -48.95
REMARK 500 PRO A 230 -25.78 -28.44
REMARK 500 LEU A 269 -78.79 65.15
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 A58 A 1001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2AYP RELATED DB: PDB
REMARK 900 RELATED ID: 2FGA RELATED DB: PDB
REMARK 900 RELATED ID: 2GHG RELATED DB: PDB
REMARK 900 RELATED ID: 2E9N RELATED DB: PDB
REMARK 900 RELATED ID: 2E9P RELATED DB: PDB
REMARK 900 RELATED ID: 2E9U RELATED DB: PDB
REMARK 900 RELATED ID: 2E9V RELATED DB: PDB
DBREF 2E9O A 2 270 UNP O14757 CHK1_HUMAN 2 270
SEQRES 1 A 269 ALA VAL PRO PHE VAL GLU ASP TRP ASP LEU VAL GLN THR
SEQRES 2 A 269 LEU GLY GLU GLY ALA TYR GLY GLU VAL GLN LEU ALA VAL
SEQRES 3 A 269 ASN ARG VAL THR GLU GLU ALA VAL ALA VAL LYS ILE VAL
SEQRES 4 A 269 ASP MET LYS ARG ALA VAL ASP CYS PRO GLU ASN ILE LYS
SEQRES 5 A 269 LYS GLU ILE CYS ILE ASN LYS MET LEU ASN HIS GLU ASN
SEQRES 6 A 269 VAL VAL LYS PHE TYR GLY HIS ARG ARG GLU GLY ASN ILE
SEQRES 7 A 269 GLN TYR LEU PHE LEU GLU TYR CYS SER GLY GLY GLU LEU
SEQRES 8 A 269 PHE ASP ARG ILE GLU PRO ASP ILE GLY MET PRO GLU PRO
SEQRES 9 A 269 ASP ALA GLN ARG PHE PHE HIS GLN LEU MET ALA GLY VAL
SEQRES 10 A 269 VAL TYR LEU HIS GLY ILE GLY ILE THR HIS ARG ASP ILE
SEQRES 11 A 269 LYS PRO GLU ASN LEU LEU LEU ASP GLU ARG ASP ASN LEU
SEQRES 12 A 269 LYS ILE SER ASP PHE GLY LEU ALA THR VAL PHE ARG TYR
SEQRES 13 A 269 ASN ASN ARG GLU ARG LEU LEU ASN LYS MET CYS GLY THR
SEQRES 14 A 269 LEU PRO TYR VAL ALA PRO GLU LEU LEU LYS ARG ARG GLU
SEQRES 15 A 269 PHE HIS ALA GLU PRO VAL ASP VAL TRP SER CYS GLY ILE
SEQRES 16 A 269 VAL LEU THR ALA MET LEU ALA GLY GLU LEU PRO TRP ASP
SEQRES 17 A 269 GLN PRO SER ASP SER CYS GLN GLU TYR SER ASP TRP LYS
SEQRES 18 A 269 GLU LYS LYS THR TYR LEU ASN PRO TRP LYS LYS ILE ASP
SEQRES 19 A 269 SER ALA PRO LEU ALA LEU LEU HIS LYS ILE LEU VAL GLU
SEQRES 20 A 269 ASN PRO SER ALA ARG ILE THR ILE PRO ASP ILE LYS LYS
SEQRES 21 A 269 ASP ARG TRP TYR ASN LYS PRO LEU LYS
HET A58 A1001 30
HETNAM A58 4-(6-{[(4-METHYLCYCLOHEXYL)AMINO]METHYL}-1,4-
HETNAM 2 A58 DIHYDROINDENO[1,2-C]PYRAZOL-3-YL)BENZOIC ACID
FORMUL 2 A58 C25 H27 N3 O2
FORMUL 3 HOH *336(H2 O)
HELIX 1 1 ASP A 47 LYS A 60 1 14
HELIX 2 2 PHE A 93 ILE A 96 5 4
HELIX 3 3 PRO A 103 ILE A 124 1 22
HELIX 4 4 LYS A 132 GLU A 134 5 3
HELIX 5 5 PRO A 176 ARG A 181 1 6
HELIX 6 6 HIS A 185 GLY A 204 1 20
HELIX 7 7 CYS A 215 GLU A 223 1 9
HELIX 8 8 ASN A 229 ILE A 234 5 6
HELIX 9 9 ASP A 235 LEU A 246 1 12
HELIX 10 10 THR A 255 LYS A 260 1 6
SHEET 1 A 5 TRP A 9 GLY A 18 0
SHEET 2 A 5 GLY A 21 ASN A 28 -1 O LEU A 25 N GLN A 13
SHEET 3 A 5 ALA A 34 ASP A 41 -1 O VAL A 37 N GLN A 24
SHEET 4 A 5 ILE A 79 GLU A 85 -1 O LEU A 84 N ALA A 36
SHEET 5 A 5 PHE A 70 GLU A 76 -1 N ARG A 74 O TYR A 81
SHEET 1 B 3 GLY A 90 GLU A 91 0
SHEET 2 B 3 LEU A 136 LEU A 138 -1 O LEU A 138 N GLY A 90
SHEET 3 B 3 LEU A 144 ILE A 146 -1 O LYS A 145 N LEU A 137
SHEET 1 C 2 ILE A 126 THR A 127 0
SHEET 2 C 2 THR A 153 VAL A 154 -1 O THR A 153 N THR A 127
SHEET 1 D 2 ARG A 156 TYR A 157 0
SHEET 2 D 2 ARG A 160 GLU A 161 -1 O ARG A 160 N TYR A 157
SITE 1 AC1 14 GLN A 13 THR A 14 LEU A 15 ALA A 36
SITE 2 AC1 14 LYS A 38 LEU A 84 GLU A 85 TYR A 86
SITE 3 AC1 14 CYS A 87 LEU A 137 ASP A 148 HOH A1067
SITE 4 AC1 14 HOH A1104 HOH A1115
CRYST1 44.940 65.711 57.773 90.00 94.20 90.00 P 1 21 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 0.022252 0.000000 0.001636 0.00000
SCALE2 0.000000 0.015218 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017356 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
