HEADER TRANSFERASE 09-MAR-06 2CGV
TITLE IDENTIFICATION OF CHEMICALLY DIVERSE CHK1 INHIBITORS BY RECEPTOR-
TITLE 2 BASED VIRTUAL SCREENING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE CHK1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL KINASE DOMAIN, RESIDUES 1-289;
COMPND 5 SYNONYM: CHK1 KINASE;
COMPND 6 EC: 2.7.1.37;
COMPND 7 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: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1/CHK1 1-289 C8H
KEYWDS TRANSFERASE, DOCKING, DRUG DESIGN, ONCOLOGY, VIRTUAL SCREENING, ATP-
KEYWDS 2 BINDING, CELL CYCLE, DNA DAMAGE, DNA REPAIR, KINASE, NUCLEAR
KEYWDS 3 PROTEIN, NUCLEOTIDE-BINDING, PHOSPHORYLATION, POLYMORPHISM,
KEYWDS 4 SERINE/THREONINE-PROTEIN KINASE, UBL CONJUGATION
EXPDTA X-RAY DIFFRACTION
AUTHOR N.FOLOPPE,L.M.FISHER,R.HOWES,A.POTTER,A.G.S.ROBERTSON,A.E.SURGENOR
REVDAT 4 13-DEC-23 2CGV 1 REMARK
REVDAT 3 24-FEB-09 2CGV 1 VERSN
REVDAT 2 31-MAY-06 2CGV 1 JRNL
REVDAT 1 05-APR-06 2CGV 0
JRNL AUTH N.FOLOPPE,L.M.FISHER,R.HOWES,A.POTTER,A.G.S.ROBERTSON,
JRNL AUTH 2 A.E.SURGENOR
JRNL TITL IDENTIFICATION OF CHEMICALLY DIVERSE CHK1 INHIBITORS BY
JRNL TITL 2 RECEPTOR-BASED VIRTUAL SCREENING.
JRNL REF BIOORG.MED.CHEM. V. 14 4792 2006
JRNL REFN ISSN 0968-0896
JRNL PMID 16574416
JRNL DOI 10.1016/J.BMC.2006.03.021
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.09
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 82.7
REMARK 3 NUMBER OF REFLECTIONS : 7633
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) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 379
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 280
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2280
REMARK 3 BIN FREE R VALUE SET COUNT : 11
REMARK 3 BIN FREE R VALUE : 0.2990
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2134
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 19
REMARK 3 SOLVENT ATOMS : 161
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.47
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.47000
REMARK 3 B22 (A**2) : -0.47000
REMARK 3 B33 (A**2) : 3.96000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.04000
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): 0.397
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.252
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.006
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.941
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.872
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2204 ; 0.031 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2984 ; 2.728 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 262 ; 8.549 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 391 ;21.767 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;19.466 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 320 ; 0.173 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1672 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1051 ; 0.259 ; 0.200
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): 142 ; 0.208 ; 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): 42 ; 0.330 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 13 ; 1.341 ; 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): 1317 ; 1.460 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2129 ; 2.671 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 887 ; 3.888 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 855 ; 6.027 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 2CGV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-MAR-06.
REMARK 100 THE DEPOSITION ID IS D_1290028098.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97920
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10278
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
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 (%) : 79.9
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 36.0
REMARK 200 DATA REDUNDANCY IN SHELL : 0.80
REMARK 200 R MERGE FOR SHELL (I) : 0.29000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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 1IA8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.50
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 32.84050
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 400
REMARK 400 COMPOUND
REMARK 400 REQUIRED FOR CHECKPOINT MEDIATED CELL CYCLE ARREST IN
REMARK 400 RESPONSE TO DNA DAMAGE OR THE PRESENCE OF UNREPLICATED DNA
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 VAL A 3
REMARK 465 PRO A 4
REMARK 465 PHE A 5
REMARK 465 ALA A 45
REMARK 465 VAL A 46
REMARK 465 ASP A 47
REMARK 465 ALA A 273
REMARK 465 LYS A 274
REMARK 465 ARG A 275
REMARK 465 PRO A 276
REMARK 465 ARG A 277
REMARK 465 VAL A 278
REMARK 465 THR A 279
REMARK 465 SER A 280
REMARK 465 GLY A 281
REMARK 465 GLY A 282
REMARK 465 VAL A 283
REMARK 465 SER A 284
REMARK 465 GLU A 285
REMARK 465 SER A 286
REMARK 465 PRO A 287
REMARK 465 SER A 288
REMARK 465 GLY A 289
REMARK 465 HIS A 290
REMARK 465 HIS A 291
REMARK 465 HIS A 292
REMARK 465 HIS A 293
REMARK 465 HIS A 294
REMARK 465 HIS A 295
REMARK 465 HIS A 296
REMARK 465 HIS A 297
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 LYS A 43 CG CD CE NZ
REMARK 470 ARG A 44 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 51 CG OD1 ND2
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 2006 O HOH A 2014 0.58
REMARK 500 O HOH A 2125 O HOH A 2126 0.65
REMARK 500 O HOH A 2036 O HOH A 2037 0.70
REMARK 500 O HOH A 2018 O HOH A 2057 0.73
REMARK 500 O HOH A 2001 O HOH A 2002 0.74
REMARK 500 O HOH A 2020 O HOH A 2021 1.33
REMARK 500 OG1 THR A 31 O HOH A 2015 1.97
REMARK 500 NZ LYS A 232 O HOH A 2135 2.11
REMARK 500 OD1 ASN A 135 N 3B3 A 1273 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ASP A 8 CB ASP A 8 CG 0.137
REMARK 500 PHE A 111 CE1 PHE A 111 CZ 0.146
REMARK 500 TYR A 173 CE1 TYR A 173 CZ 0.084
REMARK 500 VAL A 189 CB VAL A 189 CG2 -0.129
REMARK 500 TRP A 221 CZ3 TRP A 221 CH2 -0.096
REMARK 500 TRP A 264 CE3 TRP A 264 CZ3 0.135
REMARK 500
REMARK 500 REMARK: NULL
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 8 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP A 10 CB - CG - OD2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 LEU A 25 CB - CG - CD2 ANGL. DEV. = 11.2 DEGREES
REMARK 500 CYS A 57 CA - CB - SG ANGL. DEV. = -12.4 DEGREES
REMARK 500 ARG A 95 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG A 109 CG - CD - NE ANGL. DEV. = -13.4 DEGREES
REMARK 500 ARG A 129 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ASP A 148 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 LEU A 178 CA - CB - CG ANGL. DEV. = 23.5 DEGREES
REMARK 500 ASP A 213 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 LEU A 242 CB - CG - CD1 ANGL. DEV. = 12.2 DEGREES
REMARK 500 ASP A 262 CB - CG - OD2 ANGL. DEV. = 12.4 DEGREES
REMARK 500 ARG A 263 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 7 74.13 -170.21
REMARK 500 ASP A 8 -45.33 70.93
REMARK 500 GLU A 17 74.76 -67.83
REMARK 500 GLU A 32 -0.51 88.34
REMARK 500 GLU A 76 52.74 25.14
REMARK 500 ILE A 79 97.95 -69.07
REMARK 500 ASP A 99 -7.26 72.26
REMARK 500 ARG A 129 -5.53 89.53
REMARK 500 ASP A 130 50.46 -146.54
REMARK 500 ASP A 139 -167.42 -78.34
REMARK 500 ASP A 142 30.30 73.33
REMARK 500 ASP A 148 97.35 68.93
REMARK 500 SER A 214 16.00 -67.94
REMARK 500 ILE A 234 -64.37 -97.87
REMARK 500 ASP A 235 138.71 114.78
REMARK 500 LEU A 269 -34.07 -139.54
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU A 228 ASN A 229 -137.97
REMARK 500 ASN A 229 PRO A 230 147.73
REMARK 500 ASP A 235 SER A 236 -144.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2012 DISTANCE = 6.74 ANGSTROMS
REMARK 525 HOH A2020 DISTANCE = 7.30 ANGSTROMS
REMARK 525 HOH A2021 DISTANCE = 6.99 ANGSTROMS
REMARK 525 HOH A2051 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH A2061 DISTANCE = 6.82 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3B3 A1273
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IA8 RELATED DB: PDB
REMARK 900 THE 1.7 A CRYSTAL STRUCTURE OF HUMAN CELL CYCLE CHECKPOINTKINASE
REMARK 900 CHK1
REMARK 900 RELATED ID: 1NVQ RELATED DB: PDB
REMARK 900 THE COMPLEX STRUCTURE OF CHECKPOINT KINASE CHK1/UCN-01
REMARK 900 RELATED ID: 1NVR RELATED DB: PDB
REMARK 900 THE COMPLEX STRUCTURE OF CHECKPOINT KINASECHK1 /STAUROSPORINE
REMARK 900 RELATED ID: 1NVS RELATED DB: PDB
REMARK 900 THE COMPLEX STRUCTURE OF CHECKPOINT KINASE CHK1/SB218078
REMARK 900 RELATED ID: 2BR1 RELATED DB: PDB
REMARK 900 STRUCTURE-BASED DESIGN OF NOVEL CHK1 INHIBITORS: INSIGHTS INTO
REMARK 900 HYDROGEN BONDING AND PROTEIN-LIGAND AFFINITY
REMARK 900 RELATED ID: 2BRB RELATED DB: PDB
REMARK 900 STRUCTURE-BASED DESIGN OF NOVEL CHK1 INHIBITORS: INSIGHTS INTO
REMARK 900 HYDROGEN BONDING AND PROTEIN-LIGAND AFFINITY
REMARK 900 RELATED ID: 2BRG RELATED DB: PDB
REMARK 900 STRUCTURE-BASED DESIGN OF NOVEL CHK1 INHIBITORS: INSIGHTS INTO
REMARK 900 HYDROGEN BONDING AND PROTEIN-LIGAND AFFINITY
REMARK 900 RELATED ID: 2BRH RELATED DB: PDB
REMARK 900 STRUCTURE-BASED DESIGN OF NOVEL CHK1 INHIBITORS: INSIGHTS INTO
REMARK 900 HYDROGEN BONDING AND PROTEIN-LIGAND AFFINITY
REMARK 900 RELATED ID: 2BRM RELATED DB: PDB
REMARK 900 STRUCTURE-BASED DESIGN OF NOVEL CHK1 INHIBITORS: INSIGHTS INTO
REMARK 900 HYDROGEN BONDING AND PROTEIN-LIGAND AFFINITY
REMARK 900 RELATED ID: 2BRN RELATED DB: PDB
REMARK 900 STRUCTURE-BASED DESIGN OF NOVEL CHK1 INHIBITORS: INSIGHTS INTO
REMARK 900 HYDROGEN BONDING AND PROTEIN-LIGAND AFFINITY
REMARK 900 RELATED ID: 2BRO RELATED DB: PDB
REMARK 900 STRUCTURE-BASED DESIGN OF NOVEL CHK1 INHIBITORS: INSIGHTS INTO
REMARK 900 HYDROGEN BONDING AND PROTEIN-LIGAND AFFINITY
REMARK 900 RELATED ID: 2C3J RELATED DB: PDB
REMARK 900 IDENTIFICATION OF A BURIED POCKET FOR POTENT AND SELECTIVE
REMARK 900 INHIBITION OF CHK1: PREDICTION AND VERIFICATION
REMARK 900 RELATED ID: 2C3K RELATED DB: PDB
REMARK 900 IDENTIFICATION OF A BURIED POCKET FOR POTENT AND SELECTIVE
REMARK 900 INHIBITION OF CHK1: PREDICTION AND VERIFICATION
REMARK 900 RELATED ID: 2C3L RELATED DB: PDB
REMARK 900 IDENTIFICATION OF A BURIED POCKET FOR POTENT AND SELECTIVE
REMARK 900 INHIBITION OF CHK1: PREDICTION AND VERIFICATION
REMARK 900 RELATED ID: 2CGU RELATED DB: PDB
REMARK 900 IDENTIFICATION OF CHEMICALLY DIVERSE CHK1 INHIBITORS BY RECEPTOR-
REMARK 900 BASED VIRTUAL SCREENING
REMARK 900 RELATED ID: 2CGW RELATED DB: PDB
REMARK 900 IDENTIFICATION OF CHEMICALLY DIVERSE CHK1 INHIBITORS BY RECEPTOR-
REMARK 900 BASED VIRTUAL SCREENING
REMARK 900 RELATED ID: 2CGX RELATED DB: PDB
REMARK 900 IDENTIFICATION OF CHEMICALLY DIVERSE CHK1 INHIBITORS BY RECEPTOR-
REMARK 900 BASED VIRTUAL SCREENING
DBREF 2CGV A 1 289 UNP O14757 CHK1_HUMAN 1 289
DBREF 2CGV A 290 297 PDB 2CGV 2CGV 290 297
SEQRES 1 A 297 MET ALA VAL PRO PHE VAL GLU ASP TRP ASP LEU VAL GLN
SEQRES 2 A 297 THR LEU GLY GLU GLY ALA TYR GLY GLU VAL GLN LEU ALA
SEQRES 3 A 297 VAL ASN ARG VAL THR GLU GLU ALA VAL ALA VAL LYS ILE
SEQRES 4 A 297 VAL ASP MET LYS ARG ALA VAL ASP CYS PRO GLU ASN ILE
SEQRES 5 A 297 LYS LYS GLU ILE CYS ILE ASN LYS MET LEU ASN HIS GLU
SEQRES 6 A 297 ASN VAL VAL LYS PHE TYR GLY HIS ARG ARG GLU GLY ASN
SEQRES 7 A 297 ILE GLN TYR LEU PHE LEU GLU TYR CYS SER GLY GLY GLU
SEQRES 8 A 297 LEU PHE ASP ARG ILE GLU PRO ASP ILE GLY MET PRO GLU
SEQRES 9 A 297 PRO ASP ALA GLN ARG PHE PHE HIS GLN LEU MET ALA GLY
SEQRES 10 A 297 VAL VAL TYR LEU HIS GLY ILE GLY ILE THR HIS ARG ASP
SEQRES 11 A 297 ILE LYS PRO GLU ASN LEU LEU LEU ASP GLU ARG ASP ASN
SEQRES 12 A 297 LEU LYS ILE SER ASP PHE GLY LEU ALA THR VAL PHE ARG
SEQRES 13 A 297 TYR ASN ASN ARG GLU ARG LEU LEU ASN LYS MET CYS GLY
SEQRES 14 A 297 THR LEU PRO TYR VAL ALA PRO GLU LEU LEU LYS ARG ARG
SEQRES 15 A 297 GLU PHE HIS ALA GLU PRO VAL ASP VAL TRP SER CYS GLY
SEQRES 16 A 297 ILE VAL LEU THR ALA MET LEU ALA GLY GLU LEU PRO TRP
SEQRES 17 A 297 ASP GLN PRO SER ASP SER CYS GLN GLU TYR SER ASP TRP
SEQRES 18 A 297 LYS GLU LYS LYS THR TYR LEU ASN PRO TRP LYS LYS ILE
SEQRES 19 A 297 ASP SER ALA PRO LEU ALA LEU LEU HIS LYS ILE LEU VAL
SEQRES 20 A 297 GLU ASN PRO SER ALA ARG ILE THR ILE PRO ASP ILE LYS
SEQRES 21 A 297 LYS ASP ARG TRP TYR ASN LYS PRO LEU LYS LYS GLY ALA
SEQRES 22 A 297 LYS ARG PRO ARG VAL THR SER GLY GLY VAL SER GLU SER
SEQRES 23 A 297 PRO SER GLY HIS HIS HIS HIS HIS HIS HIS HIS
HET 3B3 A1273 19
HETNAM 3B3 (2S)-1-AMINO-3-[(5-NITROQUINOLIN-8-YL)AMINO]PROPAN-2-OL
FORMUL 2 3B3 C12 H14 N4 O3
FORMUL 3 HOH *161(H2 O)
HELIX 1 1 PRO A 49 LEU A 62 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 THR A 170 VAL A 174 5 5
HELIX 6 6 ALA A 175 ARG A 181 1 7
HELIX 7 7 HIS A 185 GLY A 204 1 20
HELIX 8 8 CYS A 215 GLU A 223 1 9
HELIX 9 9 PRO A 230 ILE A 234 5 5
HELIX 10 10 ASP A 235 LEU A 246 1 12
HELIX 11 11 THR A 255 LYS A 260 1 6
SHEET 1 AA 5 ASP A 10 THR A 14 0
SHEET 2 AA 5 GLY A 21 VAL A 27 -1 O LEU A 25 N VAL A 12
SHEET 3 AA 5 ALA A 34 ASP A 41 -1 O VAL A 35 N ALA A 26
SHEET 4 AA 5 ILE A 79 LEU A 84 -1 O GLN A 80 N VAL A 40
SHEET 5 AA 5 PHE A 70 ARG A 74 -1 N TYR A 71 O PHE A 83
SHEET 1 AB 3 GLY A 90 GLU A 91 0
SHEET 2 AB 3 LEU A 136 LEU A 138 -1 N LEU A 138 O GLY A 90
SHEET 3 AB 3 LEU A 144 ILE A 146 -1 O LYS A 145 N LEU A 137
SHEET 1 AC 2 ILE A 126 THR A 127 0
SHEET 2 AC 2 THR A 153 VAL A 154 -1 O THR A 153 N THR A 127
SHEET 1 AD 2 ARG A 156 TYR A 157 0
SHEET 2 AD 2 ARG A 160 GLU A 161 -1 O ARG A 160 N TYR A 157
SITE 1 AC1 10 LEU A 15 VAL A 23 TYR A 86 CYS A 87
SITE 2 AC1 10 GLU A 91 GLU A 134 ASN A 135 LEU A 137
SITE 3 AC1 10 SER A 147 ASP A 148
CRYST1 44.945 65.681 54.867 90.00 102.65 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 0.022249 0.000000 0.004994 0.00000
SCALE2 0.000000 0.015225 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018679 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
