HEADER TRANSFERASE/TRANSFERASE INHIBITOR 24-JUL-14 4QYH
TITLE CHK1 KINASE DOMAIN IN COMPLEX WITH DIAZACARBAZOLE GNE-783
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE CHK1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: KINASE DOMAIN, UNP RESIDUES 1-289;
COMPND 5 SYNONYM: CHK1 CHECKPOINT HOMOLOG, CELL CYCLE CHECKPOINT KINASE,
COMPND 6 CHECKPOINT KINASE-1;
COMPND 7 EC: 2.7.11.1;
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 GENE: CHEK1, CHK1;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS PROTEIN KINASE, PHOSPHOTRANSFER CATALYST, TRANSFERASE-TRANSFERASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.WIESMANN,P.WU
REVDAT 2 28-FEB-24 4QYH 1 REMARK SEQADV
REVDAT 1 17-DEC-14 4QYH 0
JRNL AUTH L.GAZZARD,B.APPLETON,K.CHAPMAN,H.CHEN,K.CLARK,J.DROBNICK,
JRNL AUTH 2 S.GOODACRE,J.HALLADAY,J.LYSSIKATOS,S.SCHMIDT,S.SIDERIS,
JRNL AUTH 3 C.WIESMANN,K.WILLIAMS,P.WU,I.YEN,S.MALEK
JRNL TITL DISCOVERY OF THE 1,7-DIAZACARBAZOLE CLASS OF INHIBITORS OF
JRNL TITL 2 CHECKPOINT KINASE 1.
JRNL REF BIOORG.MED.CHEM.LETT. V. 24 5704 2014
JRNL REFN ISSN 0960-894X
JRNL PMID 25453805
JRNL DOI 10.1016/J.BMCL.2014.10.063
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 50152
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) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2689
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 25
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.94
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2872
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.87
REMARK 3 BIN R VALUE (WORKING SET) : 0.2720
REMARK 3 BIN FREE R VALUE SET COUNT : 161
REMARK 3 BIN FREE R VALUE : 0.3180
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4288
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 56
REMARK 3 SOLVENT ATOMS : 300
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.89000
REMARK 3 B22 (A**2) : 0.18000
REMARK 3 B33 (A**2) : 0.74000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.17000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.147
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.139
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.099
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.368
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4454 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 4044 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6034 ; 1.441 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9434 ; 0.812 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 524 ; 5.513 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 212 ;36.827 ;24.340
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 790 ;14.266 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;16.389 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 642 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4856 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 880 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 839 ; 0.194 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4030 ; 0.174 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2118 ; 0.174 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2447 ; 0.081 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 272 ; 0.142 ; 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): 26 ; 0.173 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 117 ; 0.216 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 23 ; 0.184 ; 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): 3449 ; 3.508 ; 2.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1062 ; 0.648 ; 2.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4264 ; 4.059 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2268 ; 3.189 ; 2.500
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1770 ; 4.442 ; 5.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 6
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 401 B 604
REMARK 3 RESIDUE RANGE : A 401 A 496
REMARK 3 RESIDUE RANGE : B 301 B 301
REMARK 3 RESIDUE RANGE : A 301 A 301
REMARK 3 RESIDUE RANGE : B 3 B 273
REMARK 3 RESIDUE RANGE : A 3 A 273
REMARK 3 ORIGIN FOR THE GROUP (A): -2.3622 -3.1905 29.0968
REMARK 3 T TENSOR
REMARK 3 T11: -0.0329 T22: -0.0249
REMARK 3 T33: -0.0168 T12: 0.0097
REMARK 3 T13: 0.0024 T23: -0.0411
REMARK 3 L TENSOR
REMARK 3 L11: 0.1645 L22: 0.2187
REMARK 3 L33: 0.9075 L12: 0.0847
REMARK 3 L13: -0.1650 L23: -0.4454
REMARK 3 S TENSOR
REMARK 3 S11: -0.0262 S12: 0.0680 S13: -0.0765
REMARK 3 S21: -0.0181 S22: -0.0080 S23: -0.0191
REMARK 3 S31: 0.0806 S32: 0.0150 S33: 0.0342
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 4QYH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1000086672.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-DEC-07
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9770
REMARK 200 MONOCHROMATOR : SI (220)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52841
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% ISOPROPANOL, 12% PEG 8000, PH 7.4,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 32.98100
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 ARG A 44
REMARK 465 ALA A 45
REMARK 465 VAL A 46
REMARK 465 ASP A 47
REMARK 465 CYS A 48
REMARK 465 PRO A 49
REMARK 465 GLU A 50
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 GLY 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 465 HIS A 298
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 ARG B 44
REMARK 465 ALA B 45
REMARK 465 VAL B 46
REMARK 465 ASP B 47
REMARK 465 CYS B 48
REMARK 465 PRO B 49
REMARK 465 GLU B 50
REMARK 465 LYS B 274
REMARK 465 ARG B 275
REMARK 465 PRO B 276
REMARK 465 ARG B 277
REMARK 465 VAL B 278
REMARK 465 THR B 279
REMARK 465 SER B 280
REMARK 465 GLY B 281
REMARK 465 GLY B 282
REMARK 465 VAL B 283
REMARK 465 SER B 284
REMARK 465 GLU B 285
REMARK 465 SER B 286
REMARK 465 PRO B 287
REMARK 465 SER B 288
REMARK 465 GLY B 289
REMARK 465 GLY B 290
REMARK 465 HIS B 291
REMARK 465 HIS B 292
REMARK 465 HIS B 293
REMARK 465 HIS B 294
REMARK 465 HIS B 295
REMARK 465 HIS B 296
REMARK 465 HIS B 297
REMARK 465 HIS B 298
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 B 190 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 17 114.80 -161.89
REMARK 500 ARG A 29 -73.50 -81.13
REMARK 500 TYR A 71 -60.23 -106.52
REMARK 500 ARG A 74 124.56 -176.83
REMARK 500 ASP A 99 -1.48 69.41
REMARK 500 ASP A 130 46.52 -153.10
REMARK 500 ASP A 148 81.93 70.22
REMARK 500 LYS A 224 30.95 71.48
REMARK 500 PHE B 5 -1.19 76.10
REMARK 500 ASP B 99 -0.81 66.90
REMARK 500 ILE B 100 -52.16 -120.23
REMARK 500 ASP B 130 47.17 -151.77
REMARK 500 ASP B 148 85.49 67.51
REMARK 500 LEU B 269 -34.37 -139.70
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 3DX A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3DX B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4QYE RELATED DB: PDB
REMARK 900 RELATED ID: 4QYF RELATED DB: PDB
REMARK 900 RELATED ID: 4QYG RELATED DB: PDB
DBREF 4QYH A 1 289 UNP O14757 CHK1_HUMAN 1 289
DBREF 4QYH B 1 289 UNP O14757 CHK1_HUMAN 1 289
SEQADV 4QYH GLY A 290 UNP O14757 EXPRESSION TAG
SEQADV 4QYH HIS A 291 UNP O14757 EXPRESSION TAG
SEQADV 4QYH HIS A 292 UNP O14757 EXPRESSION TAG
SEQADV 4QYH HIS A 293 UNP O14757 EXPRESSION TAG
SEQADV 4QYH HIS A 294 UNP O14757 EXPRESSION TAG
SEQADV 4QYH HIS A 295 UNP O14757 EXPRESSION TAG
SEQADV 4QYH HIS A 296 UNP O14757 EXPRESSION TAG
SEQADV 4QYH HIS A 297 UNP O14757 EXPRESSION TAG
SEQADV 4QYH HIS A 298 UNP O14757 EXPRESSION TAG
SEQADV 4QYH GLY B 290 UNP O14757 EXPRESSION TAG
SEQADV 4QYH HIS B 291 UNP O14757 EXPRESSION TAG
SEQADV 4QYH HIS B 292 UNP O14757 EXPRESSION TAG
SEQADV 4QYH HIS B 293 UNP O14757 EXPRESSION TAG
SEQADV 4QYH HIS B 294 UNP O14757 EXPRESSION TAG
SEQADV 4QYH HIS B 295 UNP O14757 EXPRESSION TAG
SEQADV 4QYH HIS B 296 UNP O14757 EXPRESSION TAG
SEQADV 4QYH HIS B 297 UNP O14757 EXPRESSION TAG
SEQADV 4QYH HIS B 298 UNP O14757 EXPRESSION TAG
SEQRES 1 A 298 MET ALA VAL PRO PHE VAL GLU ASP TRP ASP LEU VAL GLN
SEQRES 2 A 298 THR LEU GLY GLU GLY ALA TYR GLY GLU VAL GLN LEU ALA
SEQRES 3 A 298 VAL ASN ARG VAL THR GLU GLU ALA VAL ALA VAL LYS ILE
SEQRES 4 A 298 VAL ASP MET LYS ARG ALA VAL ASP CYS PRO GLU ASN ILE
SEQRES 5 A 298 LYS LYS GLU ILE CYS ILE ASN LYS MET LEU ASN HIS GLU
SEQRES 6 A 298 ASN VAL VAL LYS PHE TYR GLY HIS ARG ARG GLU GLY ASN
SEQRES 7 A 298 ILE GLN TYR LEU PHE LEU GLU TYR CYS SER GLY GLY GLU
SEQRES 8 A 298 LEU PHE ASP ARG ILE GLU PRO ASP ILE GLY MET PRO GLU
SEQRES 9 A 298 PRO ASP ALA GLN ARG PHE PHE HIS GLN LEU MET ALA GLY
SEQRES 10 A 298 VAL VAL TYR LEU HIS GLY ILE GLY ILE THR HIS ARG ASP
SEQRES 11 A 298 ILE LYS PRO GLU ASN LEU LEU LEU ASP GLU ARG ASP ASN
SEQRES 12 A 298 LEU LYS ILE SER ASP PHE GLY LEU ALA THR VAL PHE ARG
SEQRES 13 A 298 TYR ASN ASN ARG GLU ARG LEU LEU ASN LYS MET CYS GLY
SEQRES 14 A 298 THR LEU PRO TYR VAL ALA PRO GLU LEU LEU LYS ARG ARG
SEQRES 15 A 298 GLU PHE HIS ALA GLU PRO VAL ASP VAL TRP SER CYS GLY
SEQRES 16 A 298 ILE VAL LEU THR ALA MET LEU ALA GLY GLU LEU PRO TRP
SEQRES 17 A 298 ASP GLN PRO SER ASP SER CYS GLN GLU TYR SER ASP TRP
SEQRES 18 A 298 LYS GLU LYS LYS THR TYR LEU ASN PRO TRP LYS LYS ILE
SEQRES 19 A 298 ASP SER ALA PRO LEU ALA LEU LEU HIS LYS ILE LEU VAL
SEQRES 20 A 298 GLU ASN PRO SER ALA ARG ILE THR ILE PRO ASP ILE LYS
SEQRES 21 A 298 LYS ASP ARG TRP TYR ASN LYS PRO LEU LYS LYS GLY ALA
SEQRES 22 A 298 LYS ARG PRO ARG VAL THR SER GLY GLY VAL SER GLU SER
SEQRES 23 A 298 PRO SER GLY GLY HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 B 298 MET ALA VAL PRO PHE VAL GLU ASP TRP ASP LEU VAL GLN
SEQRES 2 B 298 THR LEU GLY GLU GLY ALA TYR GLY GLU VAL GLN LEU ALA
SEQRES 3 B 298 VAL ASN ARG VAL THR GLU GLU ALA VAL ALA VAL LYS ILE
SEQRES 4 B 298 VAL ASP MET LYS ARG ALA VAL ASP CYS PRO GLU ASN ILE
SEQRES 5 B 298 LYS LYS GLU ILE CYS ILE ASN LYS MET LEU ASN HIS GLU
SEQRES 6 B 298 ASN VAL VAL LYS PHE TYR GLY HIS ARG ARG GLU GLY ASN
SEQRES 7 B 298 ILE GLN TYR LEU PHE LEU GLU TYR CYS SER GLY GLY GLU
SEQRES 8 B 298 LEU PHE ASP ARG ILE GLU PRO ASP ILE GLY MET PRO GLU
SEQRES 9 B 298 PRO ASP ALA GLN ARG PHE PHE HIS GLN LEU MET ALA GLY
SEQRES 10 B 298 VAL VAL TYR LEU HIS GLY ILE GLY ILE THR HIS ARG ASP
SEQRES 11 B 298 ILE LYS PRO GLU ASN LEU LEU LEU ASP GLU ARG ASP ASN
SEQRES 12 B 298 LEU LYS ILE SER ASP PHE GLY LEU ALA THR VAL PHE ARG
SEQRES 13 B 298 TYR ASN ASN ARG GLU ARG LEU LEU ASN LYS MET CYS GLY
SEQRES 14 B 298 THR LEU PRO TYR VAL ALA PRO GLU LEU LEU LYS ARG ARG
SEQRES 15 B 298 GLU PHE HIS ALA GLU PRO VAL ASP VAL TRP SER CYS GLY
SEQRES 16 B 298 ILE VAL LEU THR ALA MET LEU ALA GLY GLU LEU PRO TRP
SEQRES 17 B 298 ASP GLN PRO SER ASP SER CYS GLN GLU TYR SER ASP TRP
SEQRES 18 B 298 LYS GLU LYS LYS THR TYR LEU ASN PRO TRP LYS LYS ILE
SEQRES 19 B 298 ASP SER ALA PRO LEU ALA LEU LEU HIS LYS ILE LEU VAL
SEQRES 20 B 298 GLU ASN PRO SER ALA ARG ILE THR ILE PRO ASP ILE LYS
SEQRES 21 B 298 LYS ASP ARG TRP TYR ASN LYS PRO LEU LYS LYS GLY ALA
SEQRES 22 B 298 LYS ARG PRO ARG VAL THR SER GLY GLY VAL SER GLU SER
SEQRES 23 B 298 PRO SER GLY GLY HIS HIS HIS HIS HIS HIS HIS HIS
HET 3DX A 301 28
HET 3DX B 301 28
HETNAM 3DX 3-[4-(4-METHYLPIPERAZIN-1-YL)PHENYL]-9H-PYRROLO[2,3-
HETNAM 2 3DX B:5,4-C']DIPYRIDINE-6-CARBONITRILE
FORMUL 3 3DX 2(C22 H20 N6)
FORMUL 5 HOH *300(H2 O)
HELIX 1 1 ILE A 52 LEU A 62 1 11
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 ALA A 175 ARG A 181 1 7
HELIX 5 5 HIS A 185 GLY A 204 1 20
HELIX 6 6 CYS A 215 GLU A 223 1 9
HELIX 7 7 PRO A 230 ILE A 234 5 5
HELIX 8 8 ASP A 235 LEU A 246 1 12
HELIX 9 9 THR A 255 LYS A 260 1 6
HELIX 10 10 ILE B 52 MET B 61 1 10
HELIX 11 11 PHE B 93 ILE B 96 5 4
HELIX 12 12 PRO B 103 ILE B 124 1 22
HELIX 13 13 THR B 170 VAL B 174 5 5
HELIX 14 14 ALA B 175 LYS B 180 5 6
HELIX 15 15 HIS B 185 GLY B 204 1 20
HELIX 16 16 CYS B 215 GLU B 223 1 9
HELIX 17 17 PRO B 230 ILE B 234 5 5
HELIX 18 18 ASP B 235 LEU B 246 1 12
HELIX 19 19 THR B 255 LYS B 260 1 6
SHEET 1 A 5 ASP A 10 GLU A 17 0
SHEET 2 A 5 GLY A 21 VAL A 27 -1 O LEU A 25 N VAL A 12
SHEET 3 A 5 ALA A 34 ASP A 41 -1 O VAL A 35 N ALA A 26
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 GLY A 72 O PHE A 83
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
SHEET 1 E 5 TRP B 9 GLY B 16 0
SHEET 2 E 5 VAL B 23 ASN B 28 -1 O VAL B 23 N LEU B 15
SHEET 3 E 5 ALA B 34 ASP B 41 -1 O VAL B 35 N ALA B 26
SHEET 4 E 5 ILE B 79 GLU B 85 -1 O LEU B 84 N ALA B 36
SHEET 5 E 5 PHE B 70 GLU B 76 -1 N ARG B 74 O TYR B 81
SHEET 1 F 3 GLY B 90 GLU B 91 0
SHEET 2 F 3 LEU B 136 LEU B 138 -1 O LEU B 138 N GLY B 90
SHEET 3 F 3 LEU B 144 ILE B 146 -1 O LYS B 145 N LEU B 137
SHEET 1 G 2 ILE B 126 THR B 127 0
SHEET 2 G 2 THR B 153 VAL B 154 -1 O THR B 153 N THR B 127
SHEET 1 H 2 ARG B 156 TYR B 157 0
SHEET 2 H 2 ARG B 160 GLU B 161 -1 O ARG B 160 N TYR B 157
CISPEP 1 ASN A 229 PRO A 230 0 2.35
CISPEP 2 ASN B 229 PRO B 230 0 1.72
SITE 1 AC1 10 LEU A 15 ALA A 36 VAL A 68 LEU A 84
SITE 2 AC1 10 GLU A 85 TYR A 86 CYS A 87 LEU A 137
SITE 3 AC1 10 ASP A 148 HOH A 457
SITE 1 AC2 11 LEU B 15 ALA B 36 LYS B 38 VAL B 68
SITE 2 AC2 11 GLU B 85 TYR B 86 CYS B 87 LEU B 137
SITE 3 AC2 11 ASP B 148 HOH B 420 HOH B 421
CRYST1 45.078 65.962 115.682 90.00 94.49 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.022184 0.000000 0.001743 0.00000
SCALE2 0.000000 0.015160 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008671 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
