HEADER TRANSFERASE 03-JUL-09 2WMU
TITLE CRYSTAL STRUCTURE OF CHECKPOINT KINASE 1 (CHK1) IN COMPLEX WITH
TITLE 2 INHIBITORS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE CHK1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN, RESIDUES 1-289;
COMPND 5 SYNONYM: CHECKPOINT KINASE 1;
COMPND 6 EC: 2.7.11.1;
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
KEYWDS SERINE/THREONINE-PROTEIN KINASE, POLYMORPHISM, PHOSPHOPROTEIN, UBL
KEYWDS 2 CONJUGATION, ISOPEPTIDE BOND, CHECKPOINT KINASE, NUCLEOTIDE-BINDING,
KEYWDS 3 SERINE/THREONINE KINASE, DNA DAMAGE, DNA REPAIR, ATP-BINDING,
KEYWDS 4 TRANSFERASE, CHK1, KINASE, NUCLEUS, CYTOPLASM, CELL CYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.P.MATTHEWS,S.KLAIR,S.BURNS,K.BOXALL,M.CHERRY,M.FISHER,I.M.WESTWOOD,
AUTHOR 2 M.I.WALTON,T.MCHARDY,K.-M.J.CHEUNG,R.VAN MONTFORT,D.WILLIAMS,
AUTHOR 3 G.W.AHERNE,M.D.GARRETT,J.READER,I.COLLINS
REVDAT 4 13-DEC-23 2WMU 1 REMARK
REVDAT 3 28-JUN-17 2WMU 1 REMARK
REVDAT 2 12-OCT-11 2WMU 1 JRNL REMARK FORMUL VERSN
REVDAT 1 28-JUL-09 2WMU 0
JRNL AUTH T.P.MATTHEWS,S.KLAIR,S.BURNS,K.BOXALL,M.CHERRY,M.FISHER,
JRNL AUTH 2 I.M.WESTWOOD,M.I.WALTON,T.MCHARDY,K.-M.J.CHEUNG,
JRNL AUTH 3 R.VAN MONTFORT,D.WILLIAMS,G.W.AHERNE,M.D.GARRETT,J.READER,
JRNL AUTH 4 I.COLLINS
JRNL TITL IDENTIFICATION OF INHIBITORS OF CHECKPOINT KINASE 1 THROUGH
JRNL TITL 2 TEMPLATE SCREENING.
JRNL REF J.MED.CHEM. V. 52 4810 2009
JRNL REFN ISSN 0022-2623
JRNL PMID 19572549
JRNL DOI 10.1021/JM900314J
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.79
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.160
REMARK 3 COMPLETENESS FOR RANGE (%) : 70.9
REMARK 3 NUMBER OF REFLECTIONS : 13149
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.232
REMARK 3 R VALUE (WORKING SET) : 0.231
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 623
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 24.7899 - 4.1227 0.70 3046 171 0.2074 0.2333
REMARK 3 2 4.1227 - 3.2747 0.70 3106 155 0.1892 0.2026
REMARK 3 3 3.2747 - 2.8614 0.72 3167 155 0.2439 0.3089
REMARK 3 4 2.8614 - 2.6001 0.72 3207 142 0.2761 0.3077
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.42
REMARK 3 B_SOL : 50.82
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.370
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.240
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.63
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.14
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -11.05610
REMARK 3 B22 (A**2) : -2.85290
REMARK 3 B33 (A**2) : -0.83420
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.17770
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 2062
REMARK 3 ANGLE : 1.158 2795
REMARK 3 CHIRALITY : 0.078 304
REMARK 3 PLANARITY : 0.010 357
REMARK 3 DIHEDRAL : 17.910 764
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 9:53)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5233 -3.5115 -0.2499
REMARK 3 T TENSOR
REMARK 3 T11: 0.5946 T22: 0.5049
REMARK 3 T33: 0.3278 T12: -0.0065
REMARK 3 T13: -0.0697 T23: -0.0629
REMARK 3 L TENSOR
REMARK 3 L11: 0.9132 L22: 0.5674
REMARK 3 L33: -0.0141 L12: -0.1253
REMARK 3 L13: 1.0464 L23: 0.3599
REMARK 3 S TENSOR
REMARK 3 S11: 0.0001 S12: 0.6405 S13: -0.2781
REMARK 3 S21: -0.1899 S22: 0.1826 S23: 0.0710
REMARK 3 S31: -0.1037 S32: 0.0345 S33: -0.2476
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 54:270)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.4101 3.4376 24.5273
REMARK 3 T TENSOR
REMARK 3 T11: 0.1633 T22: 0.1449
REMARK 3 T33: 0.1352 T12: 0.0031
REMARK 3 T13: 0.0113 T23: -0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 1.6697 L22: 0.8064
REMARK 3 L33: -0.0452 L12: -0.1934
REMARK 3 L13: -0.1550 L23: 0.0227
REMARK 3 S TENSOR
REMARK 3 S11: -0.0123 S12: -0.0495 S13: -0.0392
REMARK 3 S21: -0.0182 S22: -0.0289 S23: 0.0190
REMARK 3 S31: -0.0348 S32: -0.0120 S33: 0.0472
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2WMU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-JUL-09.
REMARK 100 THE DEPOSITION ID IS D_1290040259.
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
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8005
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 24.790
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.1
REMARK 200 DATA REDUNDANCY : 2.300
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.8000
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) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.47000
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: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2HY0
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: DL-MALIC ACID/PEG3350
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 32.80500
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: 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 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 VAL A 6
REMARK 465 GLU A 7
REMARK 465 ASP A 8
REMARK 465 GLU A 17
REMARK 465 GLY A 18
REMARK 465 ALA A 19
REMARK 465 TYR A 20
REMARK 465 GLY A 21
REMARK 465 MET A 42
REMARK 465 LYS A 43
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 GLY A 77
REMARK 465 ASN A 78
REMARK 465 LYS A 271
REMARK 465 GLY A 272
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 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 GLN A 24 CG CD OE1 NE2
REMARK 470 LYS A 60 CG CD CE NZ
REMARK 470 ARG A 74 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 75 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 76 CG CD OE1 OE2
REMARK 470 ILE A 79 CG1 CG2 CD1
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 OD1 ASP A 142 O HOH A 2019 1.99
REMARK 500 OD1 ASN A 59 O HOH A 2005 2.14
REMARK 500 OE1 GLU A 140 O HOH A 2018 2.18
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 32 4.39 83.93
REMARK 500 ARG A 129 -8.04 80.18
REMARK 500 ARG A 129 -9.80 81.01
REMARK 500 ASP A 142 7.72 82.70
REMARK 500 ASP A 148 98.24 73.48
REMARK 500 ASN A 159 17.56 55.35
REMARK 500 LEU A 246 58.31 -90.48
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 ZYU A 1271
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2CGX RELATED DB: PDB
REMARK 900 IDENTIFICATION OF CHEMICALLY DIVERSE CHK1 INHIBITORS BY RECEPTOR-
REMARK 900 BASED VIRTUAL SCREENING
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: 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: 2CGV RELATED DB: PDB
REMARK 900 IDENTIFICATION OF CHEMICALLY DIVERSE CHK1 INHIBITORS BY RECEPTOR-
REMARK 900 BASED VIRTUAL SCREENING
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: 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: 1NVR RELATED DB: PDB
REMARK 900 THE COMPLEX STRUCTURE OF CHECKPOINT KINASECHK1 /STAUROSPORINE
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: 1ZLT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHK1 COMPLEXED WITH A HYMENALDISINEANALOG
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: 2AYP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHK1 WITH AN INDOL INHIBITOR
REMARK 900 RELATED ID: 1ZYS RELATED DB: PDB
REMARK 900 CO-CRYSTAL STRUCTURE OF CHECKPOINT KINASE CHK1 WITH APYRROLO-
REMARK 900 PYRIDINE INHIBITOR
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: 1IA8 RELATED DB: PDB
REMARK 900 THE 1.7 A CRYSTAL STRUCTURE OF HUMAN CELL CYCLE CHECKPOINTKINASE
REMARK 900 CHK1
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: 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: 1NVS RELATED DB: PDB
REMARK 900 THE COMPLEX STRUCTURE OF CHECKPOINT KINASE CHK1/SB218078
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: 1NVQ RELATED DB: PDB
REMARK 900 THE COMPLEX STRUCTURE OF CHECKPOINT KINASE CHK1/UCN-01
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: 2WMT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHECKPOINT KINASE 1 (CHK1) IN COMPLEX WITH
REMARK 900 INHIBITORS
REMARK 900 RELATED ID: 2WMX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHECKPOINT KINASE 1 (CHK1) IN COMPLEX WITH
REMARK 900 INHIBITORS
REMARK 900 RELATED ID: 2WMQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHECKPOINT KINASE 1 (CHK1) IN COMPLEX WITH
REMARK 900 INHIBITORS
REMARK 900 RELATED ID: 2WMV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHECKPOINT KINASE 1 (CHK1) IN COMPLEX WITH
REMARK 900 INHIBITORS
REMARK 900 RELATED ID: 2WMS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHECKPOINT KINASE 1 (CHK1) IN COMPLEX WITH
REMARK 900 INHIBITORS
REMARK 900 RELATED ID: 2WMW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHECKPOINT KINASE 1 (CHK1) IN COMPLEX WITH
REMARK 900 INHIBITORS
REMARK 900 RELATED ID: 2WMR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHECKPOINT KINASE 1 (CHK1) IN COMPLEX WITH
REMARK 900 INHIBITORS
DBREF 2WMU A 1 289 UNP O14757 CHK1_HUMAN 1 289
SEQRES 1 A 289 MET ALA VAL PRO PHE VAL GLU ASP TRP ASP LEU VAL GLN
SEQRES 2 A 289 THR LEU GLY GLU GLY ALA TYR GLY GLU VAL GLN LEU ALA
SEQRES 3 A 289 VAL ASN ARG VAL THR GLU GLU ALA VAL ALA VAL LYS ILE
SEQRES 4 A 289 VAL ASP MET LYS ARG ALA VAL ASP CYS PRO GLU ASN ILE
SEQRES 5 A 289 LYS LYS GLU ILE CYS ILE ASN LYS MET LEU ASN HIS GLU
SEQRES 6 A 289 ASN VAL VAL LYS PHE TYR GLY HIS ARG ARG GLU GLY ASN
SEQRES 7 A 289 ILE GLN TYR LEU PHE LEU GLU TYR CYS SER GLY GLY GLU
SEQRES 8 A 289 LEU PHE ASP ARG ILE GLU PRO ASP ILE GLY MET PRO GLU
SEQRES 9 A 289 PRO ASP ALA GLN ARG PHE PHE HIS GLN LEU MET ALA GLY
SEQRES 10 A 289 VAL VAL TYR LEU HIS GLY ILE GLY ILE THR HIS ARG ASP
SEQRES 11 A 289 ILE LYS PRO GLU ASN LEU LEU LEU ASP GLU ARG ASP ASN
SEQRES 12 A 289 LEU LYS ILE SER ASP PHE GLY LEU ALA THR VAL PHE ARG
SEQRES 13 A 289 TYR ASN ASN ARG GLU ARG LEU LEU ASN LYS MET CYS GLY
SEQRES 14 A 289 THR LEU PRO TYR VAL ALA PRO GLU LEU LEU LYS ARG ARG
SEQRES 15 A 289 GLU PHE HIS ALA GLU PRO VAL ASP VAL TRP SER CYS GLY
SEQRES 16 A 289 ILE VAL LEU THR ALA MET LEU ALA GLY GLU LEU PRO TRP
SEQRES 17 A 289 ASP GLN PRO SER ASP SER CYS GLN GLU TYR SER ASP TRP
SEQRES 18 A 289 LYS GLU LYS LYS THR TYR LEU ASN PRO TRP LYS LYS ILE
SEQRES 19 A 289 ASP SER ALA PRO LEU ALA LEU LEU HIS LYS ILE LEU VAL
SEQRES 20 A 289 GLU ASN PRO SER ALA ARG ILE THR ILE PRO ASP ILE LYS
SEQRES 21 A 289 LYS ASP ARG TRP TYR ASN LYS PRO LEU LYS LYS GLY ALA
SEQRES 22 A 289 LYS ARG PRO ARG VAL THR SER GLY GLY VAL SER GLU SER
SEQRES 23 A 289 PRO SER GLY
HET ZYU A1271 15
HETNAM ZYU 6-MORPHOLIN-4-YL-9H-PURINE
HETSYN ZYU 4-(9H-PURIN-6-YL)MORPHOLINE
FORMUL 2 ZYU C9 H11 N5 O
FORMUL 3 HOH *38(H2 O)
HELIX 1 1 ASN A 51 LYS A 60 1 10
HELIX 2 2 GLU A 91 ILE A 96 5 6
HELIX 3 3 PRO A 103 ALA A 116 1 14
HELIX 4 4 LYS A 132 GLU A 134 5 3
HELIX 5 5 ALA A 175 ARG A 181 1 7
HELIX 6 6 ALA A 186 CYS A 194 1 9
HELIX 7 7 ILE A 196 ALA A 203 1 8
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 261 1 7
SHEET 1 AA 5 ASP A 10 THR A 14 0
SHEET 2 AA 5 VAL A 23 VAL A 27 -1 O LEU A 25 N VAL A 12
SHEET 3 AA 5 ALA A 34 VAL A 40 -1 O VAL A 35 N ALA A 26
SHEET 4 AA 5 GLN A 80 LEU A 84 -1 O GLN A 80 N VAL A 40
SHEET 5 AA 5 ARG A 74 ARG A 75 -1 O ARG A 74 N TYR A 81
SHEET 1 AB 2 LEU A 136 LEU A 138 0
SHEET 2 AB 2 LEU A 144 ILE A 146 -1 O LYS A 145 N LEU A 137
SHEET 1 AC 2 ARG A 156 TYR A 157 0
SHEET 2 AC 2 ARG A 160 GLU A 161 -1 O ARG A 160 N TYR A 157
CISPEP 1 ASN A 229 PRO A 230 0 -2.15
SITE 1 AC1 7 LEU A 15 GLY A 16 ALA A 36 GLU A 85
SITE 2 AC1 7 CYS A 87 LEU A 137 HOH A2038
CRYST1 44.830 65.610 54.090 90.00 101.99 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 0.022306 0.000000 0.004737 0.00000
SCALE2 0.000000 0.015242 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018900 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
