HEADER TRANSFERASE 17-OCT-11 4A4L
TITLE CRYSTAL STRUCTURE OF POLO-LIKE KINASE 1 IN COMPLEX WITH A 5-(2-AMINO-
TITLE 2 PYRIMIDIN-4-YL)-1H-PYRROLE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PLK1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN, RESIDUES 36-345;
COMPND 5 SYNONYM: POLO-LIKE KINASE 1, PLK-1, SERINE/THREONINE-PROTEIN KINASE
COMPND 6 13, STPK13, PLK1_HUMAN;
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 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.A.BERTRAND,R.T.BOSSI
REVDAT 4 03-APR-19 4A4L 1 SOURCE
REVDAT 3 06-FEB-19 4A4L 1 REMARK
REVDAT 2 30-JAN-19 4A4L 1 REMARK
REVDAT 1 11-JAN-12 4A4L 0
JRNL AUTH M.CARUSO,B.VALSASINA,D.BALLINARI,J.A.BERTRAND,M.G.BRASCA,
JRNL AUTH 2 M.CALDARELLI,P.CAPPELLA,F.FIORENTINI,L.M.GIANELLINI,
JRNL AUTH 3 A.SCOLARO,I.BERIA
JRNL TITL 5-(2-AMINO-PYRIMIDIN-4-YL)-1H-PYRROLE AND
JRNL TITL 2 2-(2-AMINO-PYRIMIDIN-4-YL)-1,5,6,7-TETRAHYDRO-PYRROLO[3,
JRNL TITL 3 2-C]PYRIDIN-4-ONE DERIVATIVES AS NEW CLASSES OF SELECTIVE
JRNL TITL 4 AND ORALLY AVAILABLE POLO-LIKE KINASE 1 INHIBITORS.
JRNL REF BIOORG.MED.CHEM.LETT. V. 22 96 2012
JRNL REFN ISSN 0960-894X
JRNL PMID 22154349
JRNL DOI 10.1016/J.BMCL.2011.11.065
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX 2005
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN,ACCELRYS
REMARK 3 : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,
REMARK 3 : YIP,DZAKULA)
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.84
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1698701.390
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.1
REMARK 3 NUMBER OF REFLECTIONS : 16307
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) : 0.224
REMARK 3 R VALUE (WORKING SET) : 0.222
REMARK 3 FREE R VALUE : 0.274
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 808
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.010
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.2710
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.2690
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.313
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 808
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : 0.0110
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 16307
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.50
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 75.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2008
REMARK 3 BIN R VALUE (WORKING SET) : 0.3250
REMARK 3 BIN FREE R VALUE : 0.3620
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 99
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.036
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2353
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 45
REMARK 3 SOLVENT ATOMS : 53
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 9.57000
REMARK 3 B22 (A**2) : 9.57000
REMARK 3 B33 (A**2) : -19.13000
REMARK 3 B12 (A**2) : 7.10000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.39
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.40
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.41
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.860
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.390 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.310 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.270 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.400 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.39
REMARK 3 BSOL : 47.75
REMARK 3
REMARK 3 NCS MODEL : NONE
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : 939.PAR
REMARK 3 PARAMETER FILE 5 : TAR.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : 939.TOP
REMARK 3 TOPOLOGY FILE 5 : TAR.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4A4L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-OCT-11.
REMARK 100 THE DEPOSITION ID IS D_1290050004.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-MAY-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.931
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 : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16356
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 57.350
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 200 DATA REDUNDANCY : 2.300
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 78.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.44000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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: INTERNAL STRUCTURE WITH AMP-PNP
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2 M NA/K TARTRATE, 25 MM ZN ACETATE,
REMARK 280 0.10 M MES PH 6.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 277 K
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 102.69000
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 51.34500
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 51.34500
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 102.69000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -85.6 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 115.34592
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 51.34500
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 GLY A 35
REMARK 465 PRO A 36
REMARK 465 ALA A 37
REMARK 465 LYS A 38
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 PRO A 329 CA C O CB CG CD
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 ARG A 50 -14.90 59.85
REMARK 500 ASP A 72 6.37 -64.61
REMARK 500 ALA A 73 -32.57 56.32
REMARK 500 ASP A 122 -141.76 -90.72
REMARK 500 ARG A 136 -131.46 56.55
REMARK 500 LYS A 146 -137.73 47.50
REMARK 500 ARG A 175 -4.51 81.34
REMARK 500 ASP A 176 42.27 -143.42
REMARK 500 ASP A 194 82.87 58.67
REMARK 500 PHE A 195 34.14 -91.40
REMARK 500 ASN A 216 -82.61 -60.53
REMARK 500 SER A 224 80.58 -69.37
REMARK 500 LYS A 225 76.62 -63.41
REMARK 500 SER A 229 -150.08 -147.72
REMARK 500 THR A 320 -22.12 -140.89
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 LYS A 61 GLY A 62 130.22
REMARK 500 GLU A 121 ASP A 122 149.35
REMARK 500 ASN A 123 ASP A 124 138.75
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 A1329 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 255 SG
REMARK 620 2 HIS A 93 NE2 110.6
REMARK 620 3 CYS A 212 SG 125.5 111.0
REMARK 620 4 TLA A1330 O41 148.0 83.6 70.0
REMARK 620 5 TLA A1330 O4 94.5 106.4 105.8 53.5
REMARK 620 N 1 2 3 4
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 1329
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TLA A 1330
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 939 A 1331
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1UMW RELATED DB: PDB
REMARK 900 STRUCTURE OF A HUMAN PLK1 POLO-BOX DOMAIN/ PHOSPHOPEPTIDE COMPLEX
REMARK 900 RELATED ID: 2V5Q RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF WILD-TYPE PLK-1 KINASE DOMAIN IN COMPLEX WITH
REMARK 900 A SELECTIVE DARPIN
REMARK 900 RELATED ID: 1Q4K RELATED DB: PDB
REMARK 900 THE POLO-BOX DOMAIN OF PLK1 IN COMPLEX WITH A PHOSPHO-PEPTIDE
REMARK 900 RELATED ID: 4A4O RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF POLO-LIKE KINASE 1 IN COMPLEX WITH A 2-(2-
REMARK 900 AMINO-PYRIMIDIN-4-YL)-1,5,6,7- TETRAHYDRO-PYRROLOPYRIDIN-4-ONE
REMARK 900 INHIBITOR
REMARK 900 RELATED ID: 2YAC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF POLO-LIKE KINASE 1 IN COMPLEX WITH NMS-P937
REMARK 900 RELATED ID: 1Q4O RELATED DB: PDB
REMARK 900 THE STRUCTURE OF THE POLO BOX DOMAIN OF HUMAN PLK1
DBREF 4A4L A 36 345 UNP P53350 PLK1_HUMAN 36 345
SEQADV 4A4L GLY A 35 UNP P53350 EXPRESSION TAG
SEQRES 1 A 311 GLY PRO ALA LYS GLU ILE PRO GLU VAL LEU VAL ASP PRO
SEQRES 2 A 311 ARG SER ARG ARG ARG TYR VAL ARG GLY ARG PHE LEU GLY
SEQRES 3 A 311 LYS GLY GLY PHE ALA LYS CYS PHE GLU ILE SER ASP ALA
SEQRES 4 A 311 ASP THR LYS GLU VAL PHE ALA GLY LYS ILE VAL PRO LYS
SEQRES 5 A 311 SER LEU LEU LEU LYS PRO HIS GLN ARG GLU LYS MET SER
SEQRES 6 A 311 MET GLU ILE SER ILE HIS ARG SER LEU ALA HIS GLN HIS
SEQRES 7 A 311 VAL VAL GLY PHE HIS GLY PHE PHE GLU ASP ASN ASP PHE
SEQRES 8 A 311 VAL PHE VAL VAL LEU GLU LEU CYS ARG ARG ARG SER LEU
SEQRES 9 A 311 LEU GLU LEU HIS LYS ARG ARG LYS ALA LEU THR GLU PRO
SEQRES 10 A 311 GLU ALA ARG TYR TYR LEU ARG GLN ILE VAL LEU GLY CYS
SEQRES 11 A 311 GLN TYR LEU HIS ARG ASN ARG VAL ILE HIS ARG ASP LEU
SEQRES 12 A 311 LYS LEU GLY ASN LEU PHE LEU ASN GLU ASP LEU GLU VAL
SEQRES 13 A 311 LYS ILE GLY ASP PHE GLY LEU ALA THR LYS VAL GLU TYR
SEQRES 14 A 311 ASP GLY GLU ARG LYS LYS THR LEU CYS GLY THR PRO ASN
SEQRES 15 A 311 TYR ILE ALA PRO GLU VAL LEU SER LYS LYS GLY HIS SER
SEQRES 16 A 311 PHE GLU VAL ASP VAL TRP SER ILE GLY CYS ILE MET TYR
SEQRES 17 A 311 THR LEU LEU VAL GLY LYS PRO PRO PHE GLU THR SER CYS
SEQRES 18 A 311 LEU LYS GLU THR TYR LEU ARG ILE LYS LYS ASN GLU TYR
SEQRES 19 A 311 SER ILE PRO LYS HIS ILE ASN PRO VAL ALA ALA SER LEU
SEQRES 20 A 311 ILE GLN LYS MET LEU GLN THR ASP PRO THR ALA ARG PRO
SEQRES 21 A 311 THR ILE ASN GLU LEU LEU ASN ASP GLU PHE PHE THR SER
SEQRES 22 A 311 GLY TYR ILE PRO ALA ARG LEU PRO ILE THR CYS LEU THR
SEQRES 23 A 311 ILE PRO PRO ARG PHE SER ILE ALA PRO SER SER LEU ASP
SEQRES 24 A 311 PRO SER ASN ARG LYS PRO LEU THR VAL LEU ASN LYS
HET ZN A1329 1
HET TLA A1330 10
HET 939 A1331 34
HETNAM ZN ZINC ION
HETNAM TLA L(+)-TARTARIC ACID
HETNAM 939 1-METHYL-5-(2-{[5-(4-METHYLPIPERAZIN-1-YL)-2-
HETNAM 2 939 (TRIFLUOROMETHOXY)PHENYL]AMINO}PYRIMIDIN-4-YL)-1H-
HETNAM 3 939 PYRROLE-3-CARBOXAMIDE
FORMUL 2 ZN ZN 2+
FORMUL 3 TLA C4 H6 O6
FORMUL 4 939 C22 H24 F3 N7 O2
FORMUL 5 HOH *53(H2 O)
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 ALA A 219 SER A 224 1 6
HELIX 6 6 PHE A 230 GLY A 247 1 18
HELIX 7 7 CYS A 255 LYS A 265 1 11
HELIX 8 8 ASN A 275 LEU A 286 1 12
HELIX 9 9 ASP A 289 ARG A 293 5 5
HELIX 10 10 THR A 295 LEU A 300 1 6
HELIX 11 11 ASP A 302 SER A 307 1 6
HELIX 12 12 PRO A 315 THR A 320 5 6
SHEET 1 AA 6 VAL A 43 VAL A 45 0
SHEET 2 AA 6 ARG A 52 LYS A 61 -1 O TYR A 53 N LEU A 44
SHEET 3 AA 6 LYS A 66 SER A 71 -1 O CYS A 67 N LEU A 59
SHEET 4 AA 6 VAL A 78 PRO A 85 -1 O PHE A 79 N ILE A 70
SHEET 5 AA 6 PHE A 125 GLU A 131 -1 O VAL A 126 N VAL A 84
SHEET 6 AA 6 PHE A 116 GLU A 121 -1 N HIS A 117 O VAL A 129
SHEET 1 AB 2 VAL A 172 ILE A 173 0
SHEET 2 AB 2 THR A 199 LYS A 200 -1 O THR A 199 N ILE A 173
SHEET 1 AC 2 LEU A 182 LEU A 184 0
SHEET 2 AC 2 VAL A 190 ILE A 192 -1 O LYS A 191 N PHE A 183
LINK ZN ZN A1329 SG CYS A 255 1555 5675 2.33
LINK ZN ZN A1329 NE2 HIS A 93 1555 1555 2.15
LINK ZN ZN A1329 SG CYS A 212 1555 1555 2.36
LINK ZN ZN A1329 O41 TLA A1330 1555 1555 2.65
LINK ZN ZN A1329 O4 TLA A1330 1555 1555 2.06
SITE 1 AC1 4 HIS A 93 CYS A 212 CYS A 255 TLA A1330
SITE 1 AC2 8 LYS A 91 HIS A 93 GLN A 94 LYS A 97
SITE 2 AC2 8 CYS A 212 CYS A 255 LEU A 256 ZN A1329
SITE 1 AC3 16 ARG A 57 LEU A 59 CYS A 67 ALA A 80
SITE 2 AC3 16 LYS A 82 GLU A 131 LEU A 132 CYS A 133
SITE 3 AC3 16 ARG A 134 ARG A 136 SER A 137 GLU A 140
SITE 4 AC3 16 GLY A 180 PHE A 183 ASP A 194 HOH A2035
CRYST1 66.595 66.595 154.035 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 0.015016 0.008670 0.000000 0.00000
SCALE2 0.000000 0.017339 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006492 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
