HEADER TRANSFERASE 04-OCT-10 3P37
TITLE POLO-LIKE KINASE I POLO-BOX DOMAIN IN COMPLEX WITH FDPPLHSPTA
TITLE 2 PHOSPHOPEPTIDE FROM PBIP1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PLK1;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: POLO-BOX DOMAIN;
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 MOL_ID: 2;
COMPND 10 MOLECULE: PHOSPHOPEPTIDE;
COMPND 11 CHAIN: E, D, F;
COMPND 12 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_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 OTHER_DETAILS: CHEMICALLY SYNTHESIZED
KEYWDS PHOSPHOPROTEIN BINDING DOMAIN, PLK1, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.SLEDZ,M.HYVONEN,C.ABELL
REVDAT 1 27-APR-11 3P37 0
JRNL AUTH P.SLEDZ,C.J.STUBBS,S.LANG,Y.Q.YANG,G.J.MCKENZIE,
JRNL AUTH 2 A.R.VENKITARAMAN,M.HYVONEN,C.ABELL
JRNL TITL FROM CRYSTAL PACKING TO MOLECULAR RECOGNITION: PREDICTION
JRNL TITL 2 AND DISCOVERY OF A BINDING SITE ON THE SURFACE OF POLO-LIKE
JRNL TITL 3 KINASE 1
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 50 4003 2011
JRNL REFN ISSN 1433-7851
JRNL PMID 21472932
JRNL DOI 10.1002/ANIE.201008019
REMARK 2
REMARK 2 RESOLUTION. 2.38 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.38
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 62.02
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 24149
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) : 0.235
REMARK 3 R VALUE (WORKING SET) : 0.232
REMARK 3 FREE R VALUE : 0.288
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1296
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) : 2.38
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.45
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1718
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.01
REMARK 3 BIN R VALUE (WORKING SET) : 0.2830
REMARK 3 BIN FREE R VALUE SET COUNT : 97
REMARK 3 BIN FREE R VALUE : 0.3440
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5435
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 116
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.89
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.83000
REMARK 3 B22 (A**2) : 1.03000
REMARK 3 B33 (A**2) : -0.39000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.49000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 1.004
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.337
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.277
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.427
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.925
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.890
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5596 ; 0.007 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7597 ; 1.061 ; 1.978
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 688 ; 5.232 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 241 ;31.945 ;22.988
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 913 ;17.171 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 40 ;16.495 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 856 ; 0.070 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4185 ; 0.003 ; 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): 3466 ; 0.551 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5557 ; 1.003 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2130 ; 0.732 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2038 ; 1.201 ; 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 : 3
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 372 A 590
REMARK 3 ORIGIN FOR THE GROUP (A): 8.5370 1.0490 17.1700
REMARK 3 T TENSOR
REMARK 3 T11: 0.0284 T22: 0.1808
REMARK 3 T33: 0.1262 T12: -0.0139
REMARK 3 T13: 0.0479 T23: -0.0279
REMARK 3 L TENSOR
REMARK 3 L11: 1.5760 L22: 2.9242
REMARK 3 L33: 4.0662 L12: -0.5672
REMARK 3 L13: 0.9485 L23: -2.0760
REMARK 3 S TENSOR
REMARK 3 S11: -0.0944 S12: 0.0264 S13: 0.0529
REMARK 3 S21: -0.0307 S22: -0.0544 S23: -0.0803
REMARK 3 S31: 0.0678 S32: 0.0905 S33: 0.1489
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 : B 373 B 590
REMARK 3 ORIGIN FOR THE GROUP (A): 37.5870 1.7590 -2.5590
REMARK 3 T TENSOR
REMARK 3 T11: 0.0625 T22: 0.2569
REMARK 3 T33: 0.1185 T12: 0.0008
REMARK 3 T13: 0.0470 T23: -0.0327
REMARK 3 L TENSOR
REMARK 3 L11: 3.3503 L22: 4.4734
REMARK 3 L33: 2.9012 L12: 0.8160
REMARK 3 L13: 0.3306 L23: -1.3445
REMARK 3 S TENSOR
REMARK 3 S11: -0.0055 S12: -0.1249 S13: -0.1176
REMARK 3 S21: -0.1676 S22: -0.1342 S23: 0.2831
REMARK 3 S31: 0.0534 S32: -0.0041 S33: 0.1398
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 : C 373 C 590
REMARK 3 ORIGIN FOR THE GROUP (A): 39.3050 0.0340 37.9270
REMARK 3 T TENSOR
REMARK 3 T11: 0.0608 T22: 0.3038
REMARK 3 T33: 0.1035 T12: 0.0316
REMARK 3 T13: 0.0431 T23: -0.0184
REMARK 3 L TENSOR
REMARK 3 L11: 3.8785 L22: 4.0689
REMARK 3 L33: 2.9841 L12: 0.6993
REMARK 3 L13: -0.2737 L23: -0.9003
REMARK 3 S TENSOR
REMARK 3 S11: -0.2038 S12: -0.1796 S13: 0.1145
REMARK 3 S21: -0.0543 S22: 0.0306 S23: 0.2845
REMARK 3 S31: 0.0090 S32: 0.1315 S33: 0.1732
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: NULL
REMARK 4
REMARK 4 3P37 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-OCT-10.
REMARK 100 THE RCSB ID CODE IS RCSB061898.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-APR-10
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9334
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25445
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.380
REMARK 200 RESOLUTION RANGE LOW (A) : 62.020
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: PHASER
REMARK 200 STARTING MODEL: 1UMW (CHAIN A)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM MES, 30% PEG 400, PH 6.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 44.32900
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, 3
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F
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 GLY A 1
REMARK 465 PRO A 2
REMARK 465 LEU A 3
REMARK 465 GLY A 4
REMARK 465 SER A 5
REMARK 465 PRO A 6
REMARK 465 GLU A 7
REMARK 465 PHE A 8
REMARK 465 GLY B 1
REMARK 465 PRO B 2
REMARK 465 LEU B 3
REMARK 465 GLY B 4
REMARK 465 SER B 5
REMARK 465 PRO B 6
REMARK 465 GLU B 7
REMARK 465 PHE B 8
REMARK 465 ASP B 371
REMARK 465 CYS B 372
REMARK 465 GLY B 502
REMARK 465 ASP B 503
REMARK 465 GLU B 504
REMARK 465 GLY C 1
REMARK 465 PRO C 2
REMARK 465 LEU C 3
REMARK 465 GLY C 4
REMARK 465 SER C 5
REMARK 465 PRO C 6
REMARK 465 GLU C 7
REMARK 465 PHE C 8
REMARK 465 ASP C 371
REMARK 465 CYS C 372
REMARK 465 GLY C 502
REMARK 465 ASP C 503
REMARK 465 NH2 E 80
REMARK 465 NH2 F 80
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 ASP A 371 CG OD1 OD2
REMARK 470 LYS A 388 CE NZ
REMARK 470 GLU A 398 CG CD OE1 OE2
REMARK 470 LYS A 420 CD CE NZ
REMARK 470 ARG A 456 CG CD NE CZ NH1 NH2
REMARK 470 HIS A 468 CG ND1 CD2 CE1 NE2
REMARK 470 ASN A 470 CG OD1
REMARK 470 LYS A 474 CD CE NZ
REMARK 470 GLU A 501 CG CD OE1 OE2
REMARK 470 GLU A 504 CG CD OE1 OE2
REMARK 470 LEU A 505 CG CD1 CD2
REMARK 470 ARG A 512 NE CZ NH1 NH2
REMARK 470 ARG A 518 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 556 CG CD CE NZ
REMARK 470 ARG A 557 NE CZ NH1 NH2
REMARK 470 ARG A 563 NE CZ NH1 NH2
REMARK 470 LYS A 574 CG CD CE NZ
REMARK 470 ARG A 594 CG CD NE CZ NH1 NH2
REMARK 470 HIS B 373 CG ND1 CD2 CE1 NE2
REMARK 470 GLN B 379 CG CD OE1 NE2
REMARK 470 GLU B 391 CG CD OE1 OE2
REMARK 470 GLU B 398 CG CD OE1 OE2
REMARK 470 GLU B 455 CG CD OE1 OE2
REMARK 470 LEU B 463 CG CD1 CD2
REMARK 470 HIS B 468 CG ND1 CD2 CE1 NE2
REMARK 470 ASN B 470 CG OD1
REMARK 470 GLU B 501 CG CD OE1 OE2
REMARK 470 ARG B 518 NE CZ NH1 NH2
REMARK 470 GLU B 555 CG CD OE1 OE2
REMARK 470 GLU B 569 CG CD OE1 OE2
REMARK 470 LYS B 574 CG CD CE NZ
REMARK 470 HIS C 373 CG ND1 CD2 CE1 NE2
REMARK 470 GLN C 379 CG CD OE1 NE2
REMARK 470 LYS C 388 CG CD CE NZ
REMARK 470 ASP C 449 CG OD1 OD2
REMARK 470 LEU C 463 CG CD1 CD2
REMARK 470 HIS C 468 CG ND1 CD2 CE1 NE2
REMARK 470 ASN C 470 CG OD1
REMARK 470 MET C 473 CG SD CE
REMARK 470 LYS C 474 CG CD CE NZ
REMARK 470 LYS C 480 CG CD CE NZ
REMARK 470 GLU C 501 CG CD OE1 OE2
REMARK 470 GLU C 504 CG CD OE1 OE2
REMARK 470 LEU C 505 CG CD1 CD2
REMARK 470 ARG C 507 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 516 NE CZ NH1 NH2
REMARK 470 ARG C 518 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 556 CD CE NZ
REMARK 470 LYS C 574 CG CD CE NZ
REMARK 470 LYS C 589 CE NZ
REMARK 470 ARG C 594 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 GLU A 391 49.94 -88.78
REMARK 500 LYS A 420 -53.49 -123.54
REMARK 500 ASN A 430 5.02 85.30
REMARK 500 ASP A 449 -43.04 -138.43
REMARK 500 LEU A 463 -159.99 -151.61
REMARK 500 LYS B 388 74.35 50.76
REMARK 500 SER B 418 -9.51 -58.43
REMARK 500 LYS B 420 -55.10 -136.88
REMARK 500 ASP B 449 -47.30 -141.07
REMARK 500 HIS B 468 71.62 54.74
REMARK 500 LYS C 388 72.46 49.84
REMARK 500 GLU C 391 48.39 -92.93
REMARK 500 ARG C 396 72.46 -111.61
REMARK 500 TYR C 421 -49.76 -133.37
REMARK 500 SER C 439 18.84 57.99
REMARK 500 ASP C 449 -44.09 -130.11
REMARK 500 SER E 77 -178.13 -66.47
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 GOL A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3P2W RELATED DB: PDB
REMARK 900 RELATED ID: 3P2Z RELATED DB: PDB
REMARK 900 RELATED ID: 3P34 RELATED DB: PDB
REMARK 900 RELATED ID: 3P35 RELATED DB: PDB
REMARK 900 RELATED ID: 3P36 RELATED DB: PDB
DBREF 3P37 A 371 594 UNP P53350 PLK1_HUMAN 371 594
DBREF 3P37 B 371 594 UNP P53350 PLK1_HUMAN 371 594
DBREF 3P37 C 371 594 UNP P53350 PLK1_HUMAN 371 594
DBREF 3P37 E 70 80 PDB 3P37 3P37 70 80
DBREF 3P37 D 70 80 PDB 3P37 3P37 70 80
DBREF 3P37 F 70 80 PDB 3P37 3P37 70 80
SEQADV 3P37 GLY A 1 UNP P53350 EXPRESSION TAG
SEQADV 3P37 PRO A 2 UNP P53350 EXPRESSION TAG
SEQADV 3P37 LEU A 3 UNP P53350 EXPRESSION TAG
SEQADV 3P37 GLY A 4 UNP P53350 EXPRESSION TAG
SEQADV 3P37 SER A 5 UNP P53350 EXPRESSION TAG
SEQADV 3P37 PRO A 6 UNP P53350 EXPRESSION TAG
SEQADV 3P37 GLU A 7 UNP P53350 EXPRESSION TAG
SEQADV 3P37 PHE A 8 UNP P53350 EXPRESSION TAG
SEQADV 3P37 GLY B 1 UNP P53350 EXPRESSION TAG
SEQADV 3P37 PRO B 2 UNP P53350 EXPRESSION TAG
SEQADV 3P37 LEU B 3 UNP P53350 EXPRESSION TAG
SEQADV 3P37 GLY B 4 UNP P53350 EXPRESSION TAG
SEQADV 3P37 SER B 5 UNP P53350 EXPRESSION TAG
SEQADV 3P37 PRO B 6 UNP P53350 EXPRESSION TAG
SEQADV 3P37 GLU B 7 UNP P53350 EXPRESSION TAG
SEQADV 3P37 PHE B 8 UNP P53350 EXPRESSION TAG
SEQADV 3P37 GLY C 1 UNP P53350 EXPRESSION TAG
SEQADV 3P37 PRO C 2 UNP P53350 EXPRESSION TAG
SEQADV 3P37 LEU C 3 UNP P53350 EXPRESSION TAG
SEQADV 3P37 GLY C 4 UNP P53350 EXPRESSION TAG
SEQADV 3P37 SER C 5 UNP P53350 EXPRESSION TAG
SEQADV 3P37 PRO C 6 UNP P53350 EXPRESSION TAG
SEQADV 3P37 GLU C 7 UNP P53350 EXPRESSION TAG
SEQADV 3P37 PHE C 8 UNP P53350 EXPRESSION TAG
SEQRES 1 A 232 GLY PRO LEU GLY SER PRO GLU PHE ASP CYS HIS LEU SER
SEQRES 2 A 232 ASP MET LEU GLN GLN LEU HIS SER VAL ASN ALA SER LYS
SEQRES 3 A 232 PRO SER GLU ARG GLY LEU VAL ARG GLN GLU GLU ALA GLU
SEQRES 4 A 232 ASP PRO ALA CYS ILE PRO ILE PHE TRP VAL SER LYS TRP
SEQRES 5 A 232 VAL ASP TYR SER ASP LYS TYR GLY LEU GLY TYR GLN LEU
SEQRES 6 A 232 CYS ASP ASN SER VAL GLY VAL LEU PHE ASN ASP SER THR
SEQRES 7 A 232 ARG LEU ILE LEU TYR ASN ASP GLY ASP SER LEU GLN TYR
SEQRES 8 A 232 ILE GLU ARG ASP GLY THR GLU SER TYR LEU THR VAL SER
SEQRES 9 A 232 SER HIS PRO ASN SER LEU MET LYS LYS ILE THR LEU LEU
SEQRES 10 A 232 LYS TYR PHE ARG ASN TYR MET SER GLU HIS LEU LEU LYS
SEQRES 11 A 232 ALA GLY ALA ASN ILE THR PRO ARG GLU GLY ASP GLU LEU
SEQRES 12 A 232 ALA ARG LEU PRO TYR LEU ARG THR TRP PHE ARG THR ARG
SEQRES 13 A 232 SER ALA ILE ILE LEU HIS LEU SER ASN GLY SER VAL GLN
SEQRES 14 A 232 ILE ASN PHE PHE GLN ASP HIS THR LYS LEU ILE LEU CYS
SEQRES 15 A 232 PRO LEU MET ALA ALA VAL THR TYR ILE ASP GLU LYS ARG
SEQRES 16 A 232 ASP PHE ARG THR TYR ARG LEU SER LEU LEU GLU GLU TYR
SEQRES 17 A 232 GLY CYS CYS LYS GLU LEU ALA SER ARG LEU ARG TYR ALA
SEQRES 18 A 232 ARG THR MET VAL ASP LYS LEU LEU SER SER ARG
SEQRES 1 B 232 GLY PRO LEU GLY SER PRO GLU PHE ASP CYS HIS LEU SER
SEQRES 2 B 232 ASP MET LEU GLN GLN LEU HIS SER VAL ASN ALA SER LYS
SEQRES 3 B 232 PRO SER GLU ARG GLY LEU VAL ARG GLN GLU GLU ALA GLU
SEQRES 4 B 232 ASP PRO ALA CYS ILE PRO ILE PHE TRP VAL SER LYS TRP
SEQRES 5 B 232 VAL ASP TYR SER ASP LYS TYR GLY LEU GLY TYR GLN LEU
SEQRES 6 B 232 CYS ASP ASN SER VAL GLY VAL LEU PHE ASN ASP SER THR
SEQRES 7 B 232 ARG LEU ILE LEU TYR ASN ASP GLY ASP SER LEU GLN TYR
SEQRES 8 B 232 ILE GLU ARG ASP GLY THR GLU SER TYR LEU THR VAL SER
SEQRES 9 B 232 SER HIS PRO ASN SER LEU MET LYS LYS ILE THR LEU LEU
SEQRES 10 B 232 LYS TYR PHE ARG ASN TYR MET SER GLU HIS LEU LEU LYS
SEQRES 11 B 232 ALA GLY ALA ASN ILE THR PRO ARG GLU GLY ASP GLU LEU
SEQRES 12 B 232 ALA ARG LEU PRO TYR LEU ARG THR TRP PHE ARG THR ARG
SEQRES 13 B 232 SER ALA ILE ILE LEU HIS LEU SER ASN GLY SER VAL GLN
SEQRES 14 B 232 ILE ASN PHE PHE GLN ASP HIS THR LYS LEU ILE LEU CYS
SEQRES 15 B 232 PRO LEU MET ALA ALA VAL THR TYR ILE ASP GLU LYS ARG
SEQRES 16 B 232 ASP PHE ARG THR TYR ARG LEU SER LEU LEU GLU GLU TYR
SEQRES 17 B 232 GLY CYS CYS LYS GLU LEU ALA SER ARG LEU ARG TYR ALA
SEQRES 18 B 232 ARG THR MET VAL ASP LYS LEU LEU SER SER ARG
SEQRES 1 C 232 GLY PRO LEU GLY SER PRO GLU PHE ASP CYS HIS LEU SER
SEQRES 2 C 232 ASP MET LEU GLN GLN LEU HIS SER VAL ASN ALA SER LYS
SEQRES 3 C 232 PRO SER GLU ARG GLY LEU VAL ARG GLN GLU GLU ALA GLU
SEQRES 4 C 232 ASP PRO ALA CYS ILE PRO ILE PHE TRP VAL SER LYS TRP
SEQRES 5 C 232 VAL ASP TYR SER ASP LYS TYR GLY LEU GLY TYR GLN LEU
SEQRES 6 C 232 CYS ASP ASN SER VAL GLY VAL LEU PHE ASN ASP SER THR
SEQRES 7 C 232 ARG LEU ILE LEU TYR ASN ASP GLY ASP SER LEU GLN TYR
SEQRES 8 C 232 ILE GLU ARG ASP GLY THR GLU SER TYR LEU THR VAL SER
SEQRES 9 C 232 SER HIS PRO ASN SER LEU MET LYS LYS ILE THR LEU LEU
SEQRES 10 C 232 LYS TYR PHE ARG ASN TYR MET SER GLU HIS LEU LEU LYS
SEQRES 11 C 232 ALA GLY ALA ASN ILE THR PRO ARG GLU GLY ASP GLU LEU
SEQRES 12 C 232 ALA ARG LEU PRO TYR LEU ARG THR TRP PHE ARG THR ARG
SEQRES 13 C 232 SER ALA ILE ILE LEU HIS LEU SER ASN GLY SER VAL GLN
SEQRES 14 C 232 ILE ASN PHE PHE GLN ASP HIS THR LYS LEU ILE LEU CYS
SEQRES 15 C 232 PRO LEU MET ALA ALA VAL THR TYR ILE ASP GLU LYS ARG
SEQRES 16 C 232 ASP PHE ARG THR TYR ARG LEU SER LEU LEU GLU GLU TYR
SEQRES 17 C 232 GLY CYS CYS LYS GLU LEU ALA SER ARG LEU ARG TYR ALA
SEQRES 18 C 232 ARG THR MET VAL ASP LYS LEU LEU SER SER ARG
SEQRES 1 E 11 ACE PHE ASP PRO PRO LEU HIS SER TPO ALA NH2
SEQRES 1 D 11 ACE PHE ASP PRO PRO LEU HIS SER TPO ALA NH2
SEQRES 1 F 11 ACE PHE ASP PRO PRO LEU HIS SER TPO ALA NH2
MODRES 3P37 TPO E 78 THR PHOSPHOTHREONINE
MODRES 3P37 TPO D 78 THR PHOSPHOTHREONINE
MODRES 3P37 TPO F 78 THR PHOSPHOTHREONINE
HET ACE E 70 3
HET TPO E 78 11
HET ACE D 70 3
HET TPO D 78 11
HET NH2 D 80 1
HET ACE F 70 3
HET TPO F 78 11
HET GOL A 3 6
HET GOL A 5 6
HET GOL B 2 6
HET GOL C 1 6
HETNAM ACE ACETYL GROUP
HETNAM TPO PHOSPHOTHREONINE
HETNAM NH2 AMINO GROUP
HETNAM GOL GLYCEROL
HETSYN TPO PHOSPHONOTHREONINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 4 ACE 3(C2 H4 O)
FORMUL 4 TPO 3(C4 H10 N O6 P)
FORMUL 5 NH2 H2 N
FORMUL 7 GOL 4(C3 H8 O3)
FORMUL 11 HOH *116(H2 O)
HELIX 1 1 ASP A 371 SER A 387 1 17
HELIX 2 2 ARG A 396 GLU A 401 5 6
HELIX 3 3 ASP A 402 ILE A 406 5 5
HELIX 4 4 SER A 466 HIS A 468 5 3
HELIX 5 5 PRO A 469 SER A 471 5 3
HELIX 6 6 LEU A 472 LEU A 490 1 19
HELIX 7 7 LEU A 564 GLY A 571 1 8
HELIX 8 8 CYS A 573 SER A 593 1 21
HELIX 9 9 HIS B 373 SER B 387 1 15
HELIX 10 10 ARG B 396 GLU B 401 5 6
HELIX 11 11 ASP B 402 ILE B 406 5 5
HELIX 12 12 LEU B 472 LEU B 490 1 19
HELIX 13 13 LEU B 564 GLY B 571 1 8
HELIX 14 14 CYS B 573 SER B 593 1 21
HELIX 15 15 HIS C 373 SER C 387 1 15
HELIX 16 16 ARG C 396 GLU C 401 5 6
HELIX 17 17 ASP C 402 ILE C 406 5 5
HELIX 18 18 PRO C 469 SER C 471 5 3
HELIX 19 19 LEU C 472 LEU C 490 1 19
HELIX 20 20 LEU C 564 GLY C 571 1 8
HELIX 21 21 CYS C 573 SER C 593 1 21
SHEET 1 A 7 GLU A 460 THR A 464 0
SHEET 2 A 7 SER A 450 ILE A 454 -1 N LEU A 451 O LEU A 463
SHEET 3 A 7 ARG A 441 LEU A 444 -1 N ARG A 441 O ILE A 454
SHEET 4 A 7 VAL A 432 PHE A 436 -1 N VAL A 432 O LEU A 444
SHEET 5 A 7 GLY A 422 LEU A 427 -1 N LEU A 423 O LEU A 435
SHEET 6 A 7 VAL A 411 ASP A 416 -1 N VAL A 415 O GLY A 424
SHEET 7 A 7 LEU E 75 HIS E 76 -1 O LEU E 75 N ASP A 416
SHEET 1 B 6 LEU A 511 ARG A 516 0
SHEET 2 B 6 ALA A 520 LEU A 525 -1 O ILE A 522 N PHE A 515
SHEET 3 B 6 VAL A 530 PHE A 534 -1 O GLN A 531 N LEU A 523
SHEET 4 B 6 LYS A 540 CYS A 544 -1 O LEU A 543 N VAL A 530
SHEET 5 B 6 ALA A 549 ILE A 553 -1 O THR A 551 N ILE A 542
SHEET 6 B 6 PHE A 559 ARG A 563 -1 O TYR A 562 N VAL A 550
SHEET 1 C 7 GLU B 460 THR B 464 0
SHEET 2 C 7 SER B 450 ILE B 454 -1 N LEU B 451 O LEU B 463
SHEET 3 C 7 ARG B 441 LEU B 444 -1 N ARG B 441 O ILE B 454
SHEET 4 C 7 VAL B 432 PHE B 436 -1 N VAL B 432 O LEU B 444
SHEET 5 C 7 GLY B 422 LEU B 427 -1 N LEU B 423 O LEU B 435
SHEET 6 C 7 VAL B 411 ASP B 416 -1 N VAL B 415 O GLY B 424
SHEET 7 C 7 LEU D 75 HIS D 76 -1 O LEU D 75 N ASP B 416
SHEET 1 D 6 LEU B 511 ARG B 516 0
SHEET 2 D 6 ALA B 520 LEU B 525 -1 O ILE B 522 N PHE B 515
SHEET 3 D 6 VAL B 530 PHE B 534 -1 O GLN B 531 N LEU B 523
SHEET 4 D 6 LYS B 540 CYS B 544 -1 O LEU B 543 N VAL B 530
SHEET 5 D 6 ALA B 549 ILE B 553 -1 O ALA B 549 N CYS B 544
SHEET 6 D 6 PHE B 559 ARG B 563 -1 O TYR B 562 N VAL B 550
SHEET 1 E 7 GLU C 460 SER C 461 0
SHEET 2 E 7 LEU C 451 ILE C 454 -1 N TYR C 453 O SER C 461
SHEET 3 E 7 ARG C 441 LEU C 444 -1 N ARG C 441 O ILE C 454
SHEET 4 E 7 VAL C 432 PHE C 436 -1 N VAL C 432 O LEU C 444
SHEET 5 E 7 GLY C 422 LEU C 427 -1 N LEU C 423 O LEU C 435
SHEET 6 E 7 VAL C 411 TYR C 417 -1 N VAL C 415 O GLY C 424
SHEET 7 E 7 LEU F 75 HIS F 76 -1 O LEU F 75 N ASP C 416
SHEET 1 F 6 LEU C 511 ARG C 516 0
SHEET 2 F 6 ALA C 520 LEU C 525 -1 O ILE C 522 N PHE C 515
SHEET 3 F 6 VAL C 530 PHE C 534 -1 O GLN C 531 N LEU C 523
SHEET 4 F 6 LYS C 540 CYS C 544 -1 O LEU C 543 N VAL C 530
SHEET 5 F 6 ALA C 549 ILE C 553 -1 O ALA C 549 N CYS C 544
SHEET 6 F 6 PHE C 559 ARG C 563 -1 O TYR C 562 N VAL C 550
LINK C ACE E 70 N PHE E 71 1555 1555 1.34
LINK C SER E 77 N TPO E 78 1555 1555 1.34
LINK C TPO E 78 N ALA E 79 1555 1555 1.33
LINK C ACE D 70 N PHE D 71 1555 1555 1.33
LINK C SER D 77 N TPO D 78 1555 1555 1.33
LINK C TPO D 78 N ALA D 79 1555 1555 1.34
LINK C ALA D 79 N NH2 D 80 1555 1555 1.34
LINK C ACE F 70 N PHE F 71 1555 1555 1.34
LINK C SER F 77 N TPO F 78 1555 1555 1.33
LINK C TPO F 78 N ALA F 79 1555 1555 1.34
SITE 1 AC1 1 GLU A 455
SITE 1 AC2 2 HOH A 135 TRP A 514
SITE 1 AC3 4 HOH B 131 ASP B 376 GLN B 380 PRO B 545
CRYST1 58.969 88.658 67.590 90.00 113.48 90.00 P 1 21 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 0.016958 0.000000 0.007367 0.00000
SCALE2 0.000000 0.011279 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016131 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
