HEADER TRANSFERASE/TRANSFERASE INHIBITOR 18-AUG-11 3THB
TITLE STRUCTURE OF PLK1 KINASE DOMAIN IN COMPLEX WITH A BENZOLACTAM-DERIVED
TITLE 2 INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PLK1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 13-345;
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
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: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS KINASE DOMAIN, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.D.SINTCHAK
REVDAT 4 13-SEP-23 3THB 1 COMPND REMARK SEQADV HETNAM
REVDAT 3 08-NOV-17 3THB 1 REMARK
REVDAT 2 25-JAN-12 3THB 1 JRNL
REVDAT 1 23-NOV-11 3THB 0
JRNL AUTH M.O.DUFFEY,T.J.VOS,R.ADAMS,J.ALLEY,J.ANTHONY,C.BARRETT,
JRNL AUTH 2 I.BHARATHAN,D.BOWMAN,N.J.BUMP,R.CHAU,C.CULLIS,D.L.DRISCOLL,
JRNL AUTH 3 A.ELDER,N.FORSYTH,J.FRAZER,J.GUO,L.GUO,M.L.HYER,D.JANOWICK,
JRNL AUTH 4 B.KULKARNI,S.J.LAI,K.LASKY,G.LI,J.LI,D.LIAO,J.LITTLE,B.PENG,
JRNL AUTH 5 M.G.QIAN,D.J.REYNOLDS,M.REZAEI,M.P.SCOTT,T.B.SELLS,V.SHINDE,
JRNL AUTH 6 Q.J.SHI,M.D.SINTCHAK,F.SOUCY,K.T.SPROTT,S.G.STROUD,M.NESTOR,
JRNL AUTH 7 I.VISIERS,G.WEATHERHEAD,Y.YE,N.D'AMORE
JRNL TITL DISCOVERY OF A POTENT AND ORALLY BIOAVAILABLE
JRNL TITL 2 BENZOLACTAM-DERIVED INHIBITOR OF POLO-LIKE KINASE 1
JRNL TITL 3 (MLN0905).
JRNL REF J.MED.CHEM. V. 55 197 2012
JRNL REFN ISSN 0022-2623
JRNL PMID 22070629
JRNL DOI 10.1021/JM2011172
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0110
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.6
REMARK 3 NUMBER OF REFLECTIONS : 11950
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) : 0.253
REMARK 3 R VALUE (WORKING SET) : 0.250
REMARK 3 FREE R VALUE : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1317
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.57
REMARK 3 REFLECTION IN BIN (WORKING SET) : 442
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 47.37
REMARK 3 BIN R VALUE (WORKING SET) : 0.3780
REMARK 3 BIN FREE R VALUE SET COUNT : 54
REMARK 3 BIN FREE R VALUE : 0.4070
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2242
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 85.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.57000
REMARK 3 B22 (A**2) : 5.57000
REMARK 3 B33 (A**2) : -8.36000
REMARK 3 B12 (A**2) : 2.79000
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): 0.599
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.335
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.321
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 34.000
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.936
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2329 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3160 ; 1.394 ; 1.988
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 286 ; 6.124 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 98 ;34.006 ;22.959
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 384 ;17.075 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;19.622 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 353 ; 0.096 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1762 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 1433 ; 1.463 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2307 ; 2.730 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 896 ; 4.051 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 853 ; 6.282 ; 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 : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 42 A 82
REMARK 3 ORIGIN FOR THE GROUP (A): -52.2691 18.9564 14.9651
REMARK 3 T TENSOR
REMARK 3 T11: 0.1953 T22: 1.6203
REMARK 3 T33: 0.0750 T12: 0.2963
REMARK 3 T13: -0.0787 T23: -0.3417
REMARK 3 L TENSOR
REMARK 3 L11: 1.7517 L22: 9.8233
REMARK 3 L33: 5.7236 L12: -1.4263
REMARK 3 L13: 0.1285 L23: 2.5740
REMARK 3 S TENSOR
REMARK 3 S11: -0.6348 S12: -0.1061 S13: -0.1357
REMARK 3 S21: -0.4539 S22: 0.0837 S23: -0.5003
REMARK 3 S31: -0.1569 S32: -2.9690 S33: 0.5511
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 83 A 154
REMARK 3 ORIGIN FOR THE GROUP (A): -40.1187 15.2292 14.1512
REMARK 3 T TENSOR
REMARK 3 T11: 0.6235 T22: 0.5951
REMARK 3 T33: 0.3542 T12: 0.1342
REMARK 3 T13: -0.0438 T23: -0.0229
REMARK 3 L TENSOR
REMARK 3 L11: 0.7754 L22: 0.7565
REMARK 3 L33: 6.8976 L12: -0.0270
REMARK 3 L13: -0.4508 L23: 1.5585
REMARK 3 S TENSOR
REMARK 3 S11: -0.0551 S12: -0.1380 S13: -0.0793
REMARK 3 S21: -0.2294 S22: -0.1291 S23: 0.0035
REMARK 3 S31: -0.5058 S32: -0.8047 S33: 0.1841
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 155 A 251
REMARK 3 ORIGIN FOR THE GROUP (A): -27.2985 11.6416 11.0584
REMARK 3 T TENSOR
REMARK 3 T11: 0.6507 T22: 0.5339
REMARK 3 T33: 0.4654 T12: -0.0787
REMARK 3 T13: 0.0000 T23: 0.0070
REMARK 3 L TENSOR
REMARK 3 L11: 0.3525 L22: 0.5478
REMARK 3 L33: 3.8411 L12: -0.0176
REMARK 3 L13: -0.5329 L23: 0.2381
REMARK 3 S TENSOR
REMARK 3 S11: -0.0479 S12: -0.1216 S13: -0.1642
REMARK 3 S21: -0.0240 S22: 0.0200 S23: 0.0735
REMARK 3 S31: -0.4435 S32: 0.3894 S33: 0.0279
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 252 A 328
REMARK 3 ORIGIN FOR THE GROUP (A): -23.9052 4.7329 0.4834
REMARK 3 T TENSOR
REMARK 3 T11: 0.5024 T22: 0.4935
REMARK 3 T33: 0.4149 T12: -0.0228
REMARK 3 T13: 0.0812 T23: 0.0144
REMARK 3 L TENSOR
REMARK 3 L11: 1.2896 L22: 1.6054
REMARK 3 L33: 5.6217 L12: 0.4908
REMARK 3 L13: -0.0804 L23: -0.2952
REMARK 3 S TENSOR
REMARK 3 S11: -0.1337 S12: 0.0139 S13: -0.1254
REMARK 3 S21: -0.4729 S22: -0.0377 S23: -0.3194
REMARK 3 S31: 0.2379 S32: 0.6573 S33: 0.1714
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 3THB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-AUG-11.
REMARK 100 THE DEPOSITION ID IS D_1000067477.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 31-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97989
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13436
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.6
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.08400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 50.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.39600
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: NULL
REMARK 200 STARTING MODEL: 2OWB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 103.12267
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 51.56133
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 51.56133
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 103.12267
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -91.0 KCAL/MOL
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 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 51.56133
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 ALA A 13
REMARK 465 PRO A 14
REMARK 465 ALA A 15
REMARK 465 ASP A 16
REMARK 465 PRO A 17
REMARK 465 GLY A 18
REMARK 465 LYS A 19
REMARK 465 ALA A 20
REMARK 465 GLY A 21
REMARK 465 VAL A 22
REMARK 465 PRO A 23
REMARK 465 GLY A 24
REMARK 465 VAL A 25
REMARK 465 ALA A 26
REMARK 465 ALA A 27
REMARK 465 PRO A 28
REMARK 465 GLY A 29
REMARK 465 ALA A 30
REMARK 465 PRO A 31
REMARK 465 ALA A 32
REMARK 465 ALA A 33
REMARK 465 ALA A 34
REMARK 465 PRO A 35
REMARK 465 PRO A 36
REMARK 465 ALA A 37
REMARK 465 LYS A 38
REMARK 465 GLU A 39
REMARK 465 ILE A 40
REMARK 465 PRO A 41
REMARK 465 PRO A 329
REMARK 465 SER A 330
REMARK 465 SER A 331
REMARK 465 LEU A 332
REMARK 465 ASP A 333
REMARK 465 PRO A 334
REMARK 465 SER A 335
REMARK 465 ASN A 336
REMARK 465 ARG A 337
REMARK 465 LYS A 338
REMARK 465 PRO A 339
REMARK 465 LEU A 340
REMARK 465 THR A 341
REMARK 465 VAL A 342
REMARK 465 LEU A 343
REMARK 465 ASN A 344
REMARK 465 LYS A 345
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 GLU A 42 CG CD OE1 OE2
REMARK 470 VAL A 43 CG1 CG2
REMARK 470 LEU A 44 CG CD1 CD2
REMARK 470 ARG A 48 CG CD NE CZ NH1 NH2
REMARK 470 SER A 49 OG
REMARK 470 ARG A 50 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 51 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 74 CG OD1 OD2
REMARK 470 LYS A 76 CG CD CE NZ
REMARK 470 ILE A 83 CG1 CG2 CD1
REMARK 470 ARG A 134 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 169 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 171 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 209 CG CD CE NZ
REMARK 470 LYS A 225 CG CD CE NZ
REMARK 470 LYS A 264 CG CD CE NZ
REMARK 470 LYS A 265 CG CD CE NZ
REMARK 470 GLU A 267 CG CD OE1 OE2
REMARK 470 LYS A 272 CG CD CE NZ
REMARK 470 ARG A 324 CG CD NE CZ NH1 NH2
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 ASP A 122 -159.82 -120.81
REMARK 500 ARG A 136 -134.56 62.36
REMARK 500 LYS A 146 -133.68 45.06
REMARK 500 ARG A 175 -10.07 73.84
REMARK 500 ASP A 194 75.45 55.15
REMARK 500 SER A 229 -140.21 -142.32
REMARK 500 GLU A 231 -7.29 -58.44
REMARK 500 GLU A 303 -37.82 -31.58
REMARK 500 THR A 317 -42.66 -27.75
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 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 93 NE2
REMARK 620 2 CYS A 212 SG 105.0
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3TA A 1
DBREF 3THB A 13 345 UNP P53350 PLK1_HUMAN 13 345
SEQADV 3THB VAL A 210 UNP P53350 THR 210 ENGINEERED MUTATION
SEQRES 1 A 333 ALA PRO ALA ASP PRO GLY LYS ALA GLY VAL PRO GLY VAL
SEQRES 2 A 333 ALA ALA PRO GLY ALA PRO ALA ALA ALA PRO PRO ALA LYS
SEQRES 3 A 333 GLU ILE PRO GLU VAL LEU VAL ASP PRO ARG SER ARG ARG
SEQRES 4 A 333 ARG TYR VAL ARG GLY ARG PHE LEU GLY LYS GLY GLY PHE
SEQRES 5 A 333 ALA LYS CYS PHE GLU ILE SER ASP ALA ASP THR LYS GLU
SEQRES 6 A 333 VAL PHE ALA GLY LYS ILE VAL PRO LYS SER LEU LEU LEU
SEQRES 7 A 333 LYS PRO HIS GLN ARG GLU LYS MET SER MET GLU ILE SER
SEQRES 8 A 333 ILE HIS ARG SER LEU ALA HIS GLN HIS VAL VAL GLY PHE
SEQRES 9 A 333 HIS GLY PHE PHE GLU ASP ASN ASP PHE VAL PHE VAL VAL
SEQRES 10 A 333 LEU GLU LEU CYS ARG ARG ARG SER LEU LEU GLU LEU HIS
SEQRES 11 A 333 LYS ARG ARG LYS ALA LEU THR GLU PRO GLU ALA ARG TYR
SEQRES 12 A 333 TYR LEU ARG GLN ILE VAL LEU GLY CYS GLN TYR LEU HIS
SEQRES 13 A 333 ARG ASN ARG VAL ILE HIS ARG ASP LEU LYS LEU GLY ASN
SEQRES 14 A 333 LEU PHE LEU ASN GLU ASP LEU GLU VAL LYS ILE GLY ASP
SEQRES 15 A 333 PHE GLY LEU ALA THR LYS VAL GLU TYR ASP GLY GLU ARG
SEQRES 16 A 333 LYS LYS VAL LEU CYS GLY THR PRO ASN TYR ILE ALA PRO
SEQRES 17 A 333 GLU VAL LEU SER LYS LYS GLY HIS SER PHE GLU VAL ASP
SEQRES 18 A 333 VAL TRP SER ILE GLY CYS ILE MET TYR THR LEU LEU VAL
SEQRES 19 A 333 GLY LYS PRO PRO PHE GLU THR SER CYS LEU LYS GLU THR
SEQRES 20 A 333 TYR LEU ARG ILE LYS LYS ASN GLU TYR SER ILE PRO LYS
SEQRES 21 A 333 HIS ILE ASN PRO VAL ALA ALA SER LEU ILE GLN LYS MET
SEQRES 22 A 333 LEU GLN THR ASP PRO THR ALA ARG PRO THR ILE ASN GLU
SEQRES 23 A 333 LEU LEU ASN ASP GLU PHE PHE THR SER GLY TYR ILE PRO
SEQRES 24 A 333 ALA ARG LEU PRO ILE THR CYS LEU THR ILE PRO PRO ARG
SEQRES 25 A 333 PHE SER ILE ALA PRO SER SER LEU ASP PRO SER ASN ARG
SEQRES 26 A 333 LYS PRO LEU THR VAL LEU ASN LYS
HET ZN A 502 1
HET 3TA A 1 31
HETNAM ZN ZINC ION
HETNAM 3TA 9-CHLORO-2-({5-[3-(DIMETHYLAMINO)PROPYL]-2-
HETNAM 2 3TA METHYLPYRIDIN-3-YL}AMINO)-5,7-DIHYDRO-6H-PYRIMIDO[5,4-
HETNAM 3 3TA D][1]BENZAZEPINE-6-THI ONE
HETSYN 3TA MLN0905
FORMUL 2 ZN ZN 2+
FORMUL 3 3TA C23 H25 CL N6 S
HELIX 1 1 SER A 87 LEU A 89 5 3
HELIX 2 2 LYS A 91 SER A 107 1 17
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 VAL A 45 0
SHEET 2 A 6 ARG A 52 GLY A 62 -1 O TYR A 53 N LEU A 44
SHEET 3 A 6 ALA A 65 ASP A 72 -1 O CYS A 67 N GLY A 60
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 GLU A 131 -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 502 1555 1555 2.04
LINK SG CYS A 212 ZN ZN A 502 1555 1555 2.40
SITE 1 AC1 3 HIS A 93 CYS A 212 CYS A 255
SITE 1 AC2 12 LEU A 59 GLY A 60 LYS A 61 ALA A 80
SITE 2 AC2 12 GLU A 131 LEU A 132 CYS A 133 ARG A 136
SITE 3 AC2 12 GLU A 140 GLY A 180 PHE A 183 ASP A 194
CRYST1 67.668 67.668 154.684 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 0.014778 0.008532 0.000000 0.00000
SCALE2 0.000000 0.017064 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006465 0.00000
(ATOM LINES ARE NOT SHOWN.)
END