HEADER TRANSFERASE/TRANSFERASE INHIBITOR 07-FEB-13 4J52
TITLE CRYSTAL STRUCTURE OF PLK1 IN COMPLEX WITH A PYRIMIDODIAZEPINONE
TITLE 2 INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PLK1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN (UNP RESIDUES 38-330);
COMPND 5 SYNONYM: POLO-LIKE KINASE 1, PLK-1, SERINE/THREONINE-PROTEIN KINASE
COMPND 6 13, STPK13;
COMPND 7 EC: 2.7.11.21;
COMPND 8 ENGINEERED: YES;
COMPND 9 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: PLK1, PLK;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS PROTEIN SERINE/THREONINE KINASE, MITOSIS, ONCOGENESIS, REGULATION OF
KEYWDS 2 CELL CYCLE, KINASE DOMAIN, ATP BINDING, NUCLEAR, TRANSFERASE-
KEYWDS 3 TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.J.HOSFIELD,R.J.SKENE
REVDAT 4 28-FEB-24 4J52 1 REMARK SEQADV LINK
REVDAT 3 15-NOV-17 4J52 1 REMARK
REVDAT 2 05-JUN-13 4J52 1 JRNL
REVDAT 1 29-MAY-13 4J52 0
JRNL AUTH Z.NIE,V.FEHER,S.NATALA,C.MCBRIDE,A.KIRYANOV,B.JONES,B.LAM,
JRNL AUTH 2 Y.LIU,S.KALDOR,J.STAFFORD,K.HIKAMI,N.UCHIYAMA,T.KAWAMOTO,
JRNL AUTH 3 Y.HIKICHI,S.MATSUMOTO,N.AMANO,L.ZHANG,D.HOSFIELD,R.SKENE,
JRNL AUTH 4 H.ZOU,X.CAO,T.ICHIKAWA
JRNL TITL DISCOVERY OF TAK-960: AN ORALLY AVAILABLE SMALL MOLECULE
JRNL TITL 2 INHIBITOR OF POLO-LIKE KINASE 1 (PLK1).
JRNL REF BIOORG.MED.CHEM.LETT. V. 23 3662 2013
JRNL REFN ISSN 0960-894X
JRNL PMID 23664874
JRNL DOI 10.1016/J.BMCL.2013.02.083
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.16
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.4
REMARK 3 NUMBER OF REFLECTIONS : 16160
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 812
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 688
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 55.37
REMARK 3 BIN R VALUE (WORKING SET) : 0.2710
REMARK 3 BIN FREE R VALUE SET COUNT : 39
REMARK 3 BIN FREE R VALUE : 0.3290
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2374
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 45
REMARK 3 SOLVENT ATOMS : 122
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.28000
REMARK 3 B22 (A**2) : 3.28000
REMARK 3 B33 (A**2) : -4.92000
REMARK 3 B12 (A**2) : 1.64000
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): 0.334
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.240
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.194
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.693
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2483 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2421 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3353 ; 1.183 ; 2.001
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5575 ; 0.696 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 292 ; 5.812 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 110 ;33.162 ;22.273
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 452 ;15.573 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;13.487 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 365 ; 0.063 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2703 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 566 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 38 A 330
REMARK 3 RESIDUE RANGE : A 400 A 402
REMARK 3 RESIDUE RANGE : A 501 A 622
REMARK 3 ORIGIN FOR THE GROUP (A): 39.7769 -23.1138 -15.7788
REMARK 3 T TENSOR
REMARK 3 T11: 0.1058 T22: 0.0631
REMARK 3 T33: 0.0117 T12: 0.0357
REMARK 3 T13: 0.0045 T23: 0.0241
REMARK 3 L TENSOR
REMARK 3 L11: 1.6012 L22: 1.3613
REMARK 3 L33: 4.7259 L12: 0.3069
REMARK 3 L13: -0.8577 L23: -0.4254
REMARK 3 S TENSOR
REMARK 3 S11: 0.0433 S12: -0.0415 S13: -0.0296
REMARK 3 S21: 0.1354 S22: -0.1794 S23: -0.0767
REMARK 3 S31: 0.0231 S32: 0.2124 S33: 0.1361
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 4J52 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-FEB-13.
REMARK 100 THE DEPOSITION ID IS D_1000077605.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-AUG-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : SI(220)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16203
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.4
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.35
REMARK 200 COMPLETENESS FOR SHELL (%) : 55.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.20800
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.95 MM SUCCINIC ACID, 1.7% PEG2000
REMARK 280 MME, 0.4 MM ZINC ACETATE, 100 MM HEPES, PH 7.0, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 101.66000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 50.83000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 50.83000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 101.66000
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 LYS A 61 78.53 -114.06
REMARK 500 ASP A 122 -166.82 -121.23
REMARK 500 ARG A 136 -136.57 63.96
REMARK 500 LYS A 146 -125.22 50.97
REMARK 500 ARG A 175 -8.70 78.14
REMARK 500 ASP A 194 88.41 57.10
REMARK 500 TYR A 217 78.61 -107.16
REMARK 500 SER A 229 -140.85 -138.38
REMARK 500 LEU A 286 58.55 -103.31
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 93 NE2
REMARK 620 2 CYS A 212 SG 99.6
REMARK 620 3 HOH A 578 O 90.0 87.4
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1J3 A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4J53 RELATED DB: PDB
DBREF 4J52 A 38 330 UNP P53350 PLK1_HUMAN 38 330
SEQADV 4J52 VAL A 210 UNP P53350 THR 210 ENGINEERED MUTATION
SEQRES 1 A 293 LYS GLU ILE PRO GLU VAL LEU VAL ASP PRO ARG SER ARG
SEQRES 2 A 293 ARG ARG TYR VAL ARG GLY ARG PHE LEU GLY LYS GLY GLY
SEQRES 3 A 293 PHE ALA LYS CYS PHE GLU ILE SER ASP ALA ASP THR LYS
SEQRES 4 A 293 GLU VAL PHE ALA GLY LYS ILE VAL PRO LYS SER LEU LEU
SEQRES 5 A 293 LEU LYS PRO HIS GLN ARG GLU LYS MET SER MET GLU ILE
SEQRES 6 A 293 SER ILE HIS ARG SER LEU ALA HIS GLN HIS VAL VAL GLY
SEQRES 7 A 293 PHE HIS GLY PHE PHE GLU ASP ASN ASP PHE VAL PHE VAL
SEQRES 8 A 293 VAL LEU GLU LEU CYS ARG ARG ARG SER LEU LEU GLU LEU
SEQRES 9 A 293 HIS LYS ARG ARG LYS ALA LEU THR GLU PRO GLU ALA ARG
SEQRES 10 A 293 TYR TYR LEU ARG GLN ILE VAL LEU GLY CYS GLN TYR LEU
SEQRES 11 A 293 HIS ARG ASN ARG VAL ILE HIS ARG ASP LEU LYS LEU GLY
SEQRES 12 A 293 ASN LEU PHE LEU ASN GLU ASP LEU GLU VAL LYS ILE GLY
SEQRES 13 A 293 ASP PHE GLY LEU ALA THR LYS VAL GLU TYR ASP GLY GLU
SEQRES 14 A 293 ARG LYS LYS VAL LEU CYS GLY THR PRO ASN TYR ILE ALA
SEQRES 15 A 293 PRO GLU VAL LEU SER LYS LYS GLY HIS SER PHE GLU VAL
SEQRES 16 A 293 ASP VAL TRP SER ILE GLY CYS ILE MET TYR THR LEU LEU
SEQRES 17 A 293 VAL GLY LYS PRO PRO PHE GLU THR SER CYS LEU LYS GLU
SEQRES 18 A 293 THR TYR LEU ARG ILE LYS LYS ASN GLU TYR SER ILE PRO
SEQRES 19 A 293 LYS HIS ILE ASN PRO VAL ALA ALA SER LEU ILE GLN LYS
SEQRES 20 A 293 MET LEU GLN THR ASP PRO THR ALA ARG PRO THR ILE ASN
SEQRES 21 A 293 GLU LEU LEU ASN ASP GLU PHE PHE THR SER GLY TYR ILE
SEQRES 22 A 293 PRO ALA ARG LEU PRO ILE THR CYS LEU THR ILE PRO PRO
SEQRES 23 A 293 ARG PHE SER ILE ALA PRO SER
HET 1J3 A 400 40
HET ZN A 401 1
HET ACT A 402 4
HETNAM 1J3 4-{[(7R)-9-CYCLOPENTYL-7-ETHENYL-7-FLUORO-5-METHYL-6-
HETNAM 2 1J3 OXO-6,7,8,9-TETRAHYDRO-5H-PYRIMIDO[4,5-B][1,
HETNAM 3 1J3 4]DIAZEPIN-2-YL]AMINO}-3-METHOXY-N-(4-METHYLPIPERAZIN-
HETNAM 4 1J3 1-YL)BENZAMIDE
HETNAM ZN ZINC ION
HETNAM ACT ACETATE ION
FORMUL 2 1J3 C28 H37 F N8 O3
FORMUL 3 ZN ZN 2+
FORMUL 4 ACT C2 H3 O2 1-
FORMUL 5 HOH *122(H2 O)
HELIX 1 1 SER A 87 LEU A 89 5 3
HELIX 2 2 LYS A 91 ARG A 106 1 16
HELIX 3 3 SER A 137 LYS A 146 1 10
HELIX 4 4 THR A 149 ASN A 170 1 22
HELIX 5 5 LYS A 178 GLY A 180 5 3
HELIX 6 6 ALA A 219 SER A 224 1 6
HELIX 7 7 PHE A 230 GLY A 247 1 18
HELIX 8 8 CYS A 255 ASN A 266 1 12
HELIX 9 9 ASN A 275 LEU A 286 1 12
HELIX 10 10 GLU A 298 ASN A 301 5 4
HELIX 11 11 ASP A 302 SER A 307 1 6
HELIX 12 12 PRO A 315 THR A 320 5 6
SHEET 1 A 6 VAL A 43 ASP A 46 0
SHEET 2 A 6 ARG A 51 GLY A 60 -1 O ARG A 51 N ASP A 46
SHEET 3 A 6 LYS A 66 ASP A 72 -1 O SER A 71 N VAL A 54
SHEET 4 A 6 VAL A 78 PRO A 85 -1 O PHE A 79 N ILE A 70
SHEET 5 A 6 PHE A 125 LEU A 130 -1 O LEU A 130 N ALA A 80
SHEET 6 A 6 PHE A 116 GLU A 121 -1 N GLY A 118 O VAL A 129
SHEET 1 B 2 VAL A 172 ILE A 173 0
SHEET 2 B 2 THR A 199 LYS A 200 -1 O THR A 199 N ILE A 173
SHEET 1 C 2 LEU A 182 LEU A 184 0
SHEET 2 C 2 VAL A 190 ILE A 192 -1 O LYS A 191 N PHE A 183
LINK NE2 HIS A 93 ZN ZN A 401 1555 1555 2.28
LINK SG CYS A 212 ZN ZN A 401 1555 1555 2.15
LINK ZN ZN A 401 O HOH A 578 1555 1555 2.66
SITE 1 AC1 17 ARG A 57 PHE A 58 LEU A 59 CYS A 67
SITE 2 AC1 17 GLY A 81 LYS A 82 VAL A 114 LEU A 130
SITE 3 AC1 17 GLU A 131 LEU A 132 CYS A 133 ARG A 134
SITE 4 AC1 17 ARG A 136 PHE A 183 HOH A 505 HOH A 561
SITE 5 AC1 17 HOH A 575
SITE 1 AC2 5 HIS A 93 CYS A 212 CYS A 255 LEU A 256
SITE 2 AC2 5 HOH A 578
SITE 1 AC3 7 LYS A 178 LEU A 179 GLY A 180 ASN A 216
SITE 2 AC3 7 TYR A 217 HOH A 549 HOH A 550
CRYST1 66.873 66.873 152.490 90.00 90.00 120.00 P 32 2 1 6
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 0.014954 0.008634 0.000000 0.00000
SCALE2 0.000000 0.017267 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006558 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
