HEADER TRANSFERASE/TRANSFERASE INHIBITOR 01-OCT-12 4HCO
TITLE HUMAN PLK1-PBD IN COMPLEX WITH THYMOQUINONE AT THE PHOPHOPEPTIDE
TITLE 2 BINDING SITE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PLK1;
COMPND 3 CHAIN: B, A;
COMPND 4 FRAGMENT: UNP RESIDUES 367-603;
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;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21
KEYWDS KINASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.YIN,P.H.REHSE
REVDAT 2 06-MAR-13 4HCO 1 JRNL
REVDAT 1 10-OCT-12 4HCO 0
SPRSDE 10-OCT-12 4HCO 4H70
JRNL AUTH Z.YIN,Y.SONG,P.H.REHSE
JRNL TITL THYMOQUINONE BLOCKS PSER/PTHR RECOGNITION BY PLK1 POLO-BOX
JRNL TITL 2 DOMAIN AS A PHOSPHATE MIMIC
JRNL REF ACS CHEM.BIOL. V. 8 303 2013
JRNL REFN ISSN 1554-8929
JRNL PMID 23135290
JRNL DOI 10.1021/CB3004379
REMARK 2
REMARK 2 RESOLUTION. 2.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0110
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.07
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 3 NUMBER OF REFLECTIONS : 10576
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) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 531
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) : 2.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.82
REMARK 3 REFLECTION IN BIN (WORKING SET) : 754
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.25
REMARK 3 BIN R VALUE (WORKING SET) : 0.2860
REMARK 3 BIN FREE R VALUE SET COUNT : 33
REMARK 3 BIN FREE R VALUE : 0.4350
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3519
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 103
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.54
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.11000
REMARK 3 B22 (A**2) : 0.04000
REMARK 3 B33 (A**2) : 0.07000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.04000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.469
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.375
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.386
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.897
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.797
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3609 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4881 ; 1.126 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 436 ; 5.742 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 164 ;29.402 ;22.988
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 628 ;16.758 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 29 ;20.312 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 543 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2699 ; 0.004 ; 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): 2187 ; 0.374 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3515 ; 0.711 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1422 ; 0.896 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1366 ; 1.511 ; 4.500
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 : NULL
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 4HCO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-OCT-12.
REMARK 100 THE RCSB ID CODE IS RCSB075299.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-MAY-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
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 FR-E SUPERBRIGHT
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 : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11125
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750
REMARK 200 RESOLUTION RANGE LOW (A) : 51.070
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.6
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : 0.15400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.38700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
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: 1UMW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4M SODIUM POTASSIUM TARTRATE, 50MM
REMARK 280 MES PH 6.5, 100MM HEPES PH 6.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
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 51.07500
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: 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 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: 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 SER B 364
REMARK 465 ASN B 365
REMARK 465 ALA B 366
REMARK 465 GLY B 367
REMARK 465 GLU B 368
REMARK 465 VAL B 369
REMARK 465 VAL B 370
REMARK 465 GLU B 501
REMARK 465 GLY B 502
REMARK 465 ASP B 503
REMARK 465 GLU B 504
REMARK 465 SER B 595
REMARK 465 ALA B 596
REMARK 465 SER B 597
REMARK 465 ASN B 598
REMARK 465 ARG B 599
REMARK 465 LEU B 600
REMARK 465 LYS B 601
REMARK 465 ALA B 602
REMARK 465 SER B 603
REMARK 465 SER A 364
REMARK 465 ASN A 365
REMARK 465 ALA A 366
REMARK 465 GLY A 367
REMARK 465 GLU A 368
REMARK 465 VAL A 369
REMARK 465 VAL A 370
REMARK 465 ASP A 371
REMARK 465 CYS A 372
REMARK 465 GLU A 504
REMARK 465 ARG A 594
REMARK 465 SER A 595
REMARK 465 ALA A 596
REMARK 465 SER A 597
REMARK 465 ASN A 598
REMARK 465 ARG A 599
REMARK 465 LEU A 600
REMARK 465 LYS A 601
REMARK 465 ALA A 602
REMARK 465 SER A 603
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 LYS B 474 CG CD CE NZ
REMARK 470 ARG B 507 CD NE CZ NH1 NH2
REMARK 470 ARG B 518 CB CG CD NE CZ NH1 NH2
REMARK 470 GLN B 536 CB CG CD OE1 NE2
REMARK 470 LYS B 574 CG CD CE NZ
REMARK 470 ARG B 594 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 379 CG CD OE1 NE2
REMARK 470 HIS A 468 CB CG ND1 CD2 CE1 NE2
REMARK 470 ILE A 497 CG1 CD1
REMARK 470 ASP A 503 CG OD1 OD2
REMARK 470 GLN A 536 CB CG CD OE1 NE2
REMARK 470 GLU A 555 CG CD OE1 OE2
REMARK 470 ARG A 584 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 LYS B 388 59.33 39.85
REMARK 500 TYR B 417 40.91 -102.40
REMARK 500 ASN B 430 -7.42 82.80
REMARK 500 SER B 439 -4.71 64.02
REMARK 500 ASP B 449 -45.80 -131.22
REMARK 500 THR B 517 -162.82 -112.90
REMARK 500 PRO A 403 0.04 -65.93
REMARK 500 LYS A 420 -56.30 -147.55
REMARK 500 ASN A 430 -8.57 78.48
REMARK 500 SER A 439 -7.17 78.00
REMARK 500 ASP A 449 -34.82 -135.67
REMARK 500 LEU A 463 -169.45 -164.51
REMARK 500 ASP A 537 11.83 -143.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 819 DISTANCE = 7.05 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMW A 702
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4H5X RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, DIFFERENT LIGAND
REMARK 900 RELATED ID: 4H71 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, DIFFERENT LIGAND
DBREF 4HCO B 367 603 UNP P53350 PLK1_HUMAN 367 603
DBREF 4HCO A 367 603 UNP P53350 PLK1_HUMAN 367 603
SEQADV 4HCO SER B 364 UNP P53350 EXPRESSION TAG
SEQADV 4HCO ASN B 365 UNP P53350 EXPRESSION TAG
SEQADV 4HCO ALA B 366 UNP P53350 EXPRESSION TAG
SEQADV 4HCO SER A 364 UNP P53350 EXPRESSION TAG
SEQADV 4HCO ASN A 365 UNP P53350 EXPRESSION TAG
SEQADV 4HCO ALA A 366 UNP P53350 EXPRESSION TAG
SEQRES 1 B 240 SER ASN ALA GLY GLU VAL VAL ASP CYS HIS LEU SER ASP
SEQRES 2 B 240 MET LEU GLN GLN LEU HIS SER VAL ASN ALA SER LYS PRO
SEQRES 3 B 240 SER GLU ARG GLY LEU VAL ARG GLN GLU GLU ALA GLU ASP
SEQRES 4 B 240 PRO ALA CYS ILE PRO ILE PHE TRP VAL SER LYS TRP VAL
SEQRES 5 B 240 ASP TYR SER ASP LYS TYR GLY LEU GLY TYR GLN LEU CYS
SEQRES 6 B 240 ASP ASN SER VAL GLY VAL LEU PHE ASN ASP SER THR ARG
SEQRES 7 B 240 LEU ILE LEU TYR ASN ASP GLY ASP SER LEU GLN TYR ILE
SEQRES 8 B 240 GLU ARG ASP GLY THR GLU SER TYR LEU THR VAL SER SER
SEQRES 9 B 240 HIS PRO ASN SER LEU MET LYS LYS ILE THR LEU LEU LYS
SEQRES 10 B 240 TYR PHE ARG ASN TYR MET SER GLU HIS LEU LEU LYS ALA
SEQRES 11 B 240 GLY ALA ASN ILE THR PRO ARG GLU GLY ASP GLU LEU ALA
SEQRES 12 B 240 ARG LEU PRO TYR LEU ARG THR TRP PHE ARG THR ARG SER
SEQRES 13 B 240 ALA ILE ILE LEU HIS LEU SER ASN GLY SER VAL GLN ILE
SEQRES 14 B 240 ASN PHE PHE GLN ASP HIS THR LYS LEU ILE LEU CYS PRO
SEQRES 15 B 240 LEU MET ALA ALA VAL THR TYR ILE ASP GLU LYS ARG ASP
SEQRES 16 B 240 PHE ARG THR TYR ARG LEU SER LEU LEU GLU GLU TYR GLY
SEQRES 17 B 240 CYS CYS LYS GLU LEU ALA SER ARG LEU ARG TYR ALA ARG
SEQRES 18 B 240 THR MET VAL ASP LYS LEU LEU SER SER ARG SER ALA SER
SEQRES 19 B 240 ASN ARG LEU LYS ALA SER
SEQRES 1 A 240 SER ASN ALA GLY GLU VAL VAL ASP CYS HIS LEU SER ASP
SEQRES 2 A 240 MET LEU GLN GLN LEU HIS SER VAL ASN ALA SER LYS PRO
SEQRES 3 A 240 SER GLU ARG GLY LEU VAL ARG GLN GLU GLU ALA GLU ASP
SEQRES 4 A 240 PRO ALA CYS ILE PRO ILE PHE TRP VAL SER LYS TRP VAL
SEQRES 5 A 240 ASP TYR SER ASP LYS TYR GLY LEU GLY TYR GLN LEU CYS
SEQRES 6 A 240 ASP ASN SER VAL GLY VAL LEU PHE ASN ASP SER THR ARG
SEQRES 7 A 240 LEU ILE LEU TYR ASN ASP GLY ASP SER LEU GLN TYR ILE
SEQRES 8 A 240 GLU ARG ASP GLY THR GLU SER TYR LEU THR VAL SER SER
SEQRES 9 A 240 HIS PRO ASN SER LEU MET LYS LYS ILE THR LEU LEU LYS
SEQRES 10 A 240 TYR PHE ARG ASN TYR MET SER GLU HIS LEU LEU LYS ALA
SEQRES 11 A 240 GLY ALA ASN ILE THR PRO ARG GLU GLY ASP GLU LEU ALA
SEQRES 12 A 240 ARG LEU PRO TYR LEU ARG THR TRP PHE ARG THR ARG SER
SEQRES 13 A 240 ALA ILE ILE LEU HIS LEU SER ASN GLY SER VAL GLN ILE
SEQRES 14 A 240 ASN PHE PHE GLN ASP HIS THR LYS LEU ILE LEU CYS PRO
SEQRES 15 A 240 LEU MET ALA ALA VAL THR TYR ILE ASP GLU LYS ARG ASP
SEQRES 16 A 240 PHE ARG THR TYR ARG LEU SER LEU LEU GLU GLU TYR GLY
SEQRES 17 A 240 CYS CYS LYS GLU LEU ALA SER ARG LEU ARG TYR ALA ARG
SEQRES 18 A 240 THR MET VAL ASP LYS LEU LEU SER SER ARG SER ALA SER
SEQRES 19 A 240 ASN ARG LEU LYS ALA SER
HET GOL A 701 6
HET IMW A 702 12
HETNAM GOL GLYCEROL
HETNAM IMW 2-METHYL-5-(1-METHYLETHYL)CYCLOHEXA-2,5-DIENE-1,4-DIONE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN IMW THYMOQUINONE, 2-ISOPROPYL-5-METHYLBENZO-1,4-QUINONE
FORMUL 3 GOL C3 H8 O3
FORMUL 4 IMW C10 H12 O2
FORMUL 5 HOH *103(H2 O)
HELIX 1 1 ASP B 371 ALA B 386 1 16
HELIX 2 2 LYS B 388 ARG B 392 5 5
HELIX 3 3 ARG B 396 GLU B 401 5 6
HELIX 4 4 ASP B 402 ILE B 406 5 5
HELIX 5 5 SER B 466 HIS B 468 5 3
HELIX 6 6 PRO B 469 SER B 471 5 3
HELIX 7 7 LEU B 472 LEU B 490 1 19
HELIX 8 8 LEU B 564 GLY B 571 1 8
HELIX 9 9 CYS B 573 SER B 593 1 21
HELIX 10 10 LEU A 374 SER A 387 1 14
HELIX 11 11 ARG A 396 GLU A 401 5 6
HELIX 12 12 LEU A 472 LEU A 490 1 19
HELIX 13 13 LEU A 564 GLY A 571 1 8
HELIX 14 14 CYS A 573 SER A 592 1 20
SHEET 1 A 6 VAL B 411 TYR B 417 0
SHEET 2 A 6 GLY B 422 LEU B 427 -1 O GLY B 424 N VAL B 415
SHEET 3 A 6 VAL B 432 PHE B 436 -1 O LEU B 435 N LEU B 423
SHEET 4 A 6 ARG B 441 LEU B 444 -1 O LEU B 444 N VAL B 432
SHEET 5 A 6 SER B 450 ILE B 454 -1 O ILE B 454 N ARG B 441
SHEET 6 A 6 GLU B 460 THR B 464 -1 O LEU B 463 N LEU B 451
SHEET 1 B 6 LEU B 511 ARG B 516 0
SHEET 2 B 6 ALA B 520 LEU B 525 -1 O ILE B 522 N PHE B 515
SHEET 3 B 6 VAL B 530 PHE B 534 -1 O GLN B 531 N LEU B 523
SHEET 4 B 6 LYS B 540 CYS B 544 -1 O LEU B 543 N VAL B 530
SHEET 5 B 6 ALA B 549 ILE B 553 -1 O ALA B 549 N CYS B 544
SHEET 6 B 6 PHE B 559 ARG B 563 -1 O TYR B 562 N VAL B 550
SHEET 1 C 6 VAL A 411 ASP A 416 0
SHEET 2 C 6 GLY A 422 LEU A 427 -1 O GLY A 424 N VAL A 415
SHEET 3 C 6 VAL A 432 PHE A 436 -1 O GLY A 433 N TYR A 425
SHEET 4 C 6 ARG A 441 LEU A 444 -1 O LEU A 444 N VAL A 432
SHEET 5 C 6 SER A 450 ILE A 454 -1 O ILE A 454 N ARG A 441
SHEET 6 C 6 GLU A 460 THR A 464 -1 O LEU A 463 N LEU A 451
SHEET 1 D 6 LEU A 511 ARG A 516 0
SHEET 2 D 6 ALA A 520 LEU A 525 -1 O ILE A 522 N PHE A 515
SHEET 3 D 6 VAL A 530 PHE A 534 -1 O GLN A 531 N LEU A 523
SHEET 4 D 6 LYS A 540 CYS A 544 -1 O LEU A 543 N VAL A 530
SHEET 5 D 6 ALA A 549 ILE A 553 -1 O ALA A 549 N CYS A 544
SHEET 6 D 6 PHE A 559 ARG A 563 -1 O TYR A 562 N VAL A 550
SITE 1 AC1 4 TRP A 414 GLU A 460 LEU A 490 IMW A 702
SITE 1 AC2 10 GLU A 460 LEU A 491 ALA A 493 ARG A 507
SITE 2 AC2 10 HIS A 538 LYS A 540 ARG A 557 GOL A 701
SITE 3 AC2 10 HOH A 802 HOH A 805
CRYST1 33.260 102.150 67.740 90.00 93.96 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 0.030066 0.000000 0.002081 0.00000
SCALE2 0.000000 0.009790 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014798 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
