HEADER TRANSFERASE 09-FEB-07 2OU7
TITLE STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN POLO-LIKE KINASE 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PLK1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN (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;
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;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: SF21;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS KINASE DOMAIN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.-H.DING,M.KOTHE,D.KOHLS,S.LOW
REVDAT 4 13-JUL-11 2OU7 1 VERSN
REVDAT 3 24-FEB-09 2OU7 1 VERSN
REVDAT 2 21-AUG-07 2OU7 1 JRNL
REVDAT 1 24-APR-07 2OU7 0
JRNL AUTH M.KOTHE,D.KOHLS,S.LOW,R.COLI,A.C.CHENG,S.L.JACQUES,
JRNL AUTH 2 T.L.JOHNSON,C.LEWIS,C.LOH,J.NONOMIYA,A.L.SHEILS,
JRNL AUTH 3 K.A.VERDRIES,T.A.WYNN,C.KUHN,Y.H.DING
JRNL TITL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN POLO-LIKE KINASE
JRNL TITL 2 1.
JRNL REF BIOCHEMISTRY V. 46 5960 2007
JRNL REFN ISSN 0006-2960
JRNL PMID 17461553
JRNL DOI 10.1021/BI602474J
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 3 NUMBER OF REFLECTIONS : 14116
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) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 757
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 751
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2970
REMARK 3 BIN FREE R VALUE SET COUNT : 49
REMARK 3 BIN FREE R VALUE : 0.3500
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2366
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 97
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.25000
REMARK 3 B22 (A**2) : 4.25000
REMARK 3 B33 (A**2) : -6.37000
REMARK 3 B12 (A**2) : 2.12000
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): 0.401
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.248
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.203
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.409
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2476 ; 0.009 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2299 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3349 ; 1.246 ; 1.995
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5348 ; 0.887 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 291 ; 6.080 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 365 ; 0.149 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2658 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 519 ; 0.004 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 526 ; 0.181 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2581 ; 0.217 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 1509 ; 0.082 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 88 ; 0.164 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.042 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 9 ; 0.171 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 44 ; 0.212 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.374 ; 0.200
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): 1459 ; 0.421 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2373 ; 0.796 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1017 ; 1.051 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 976 ; 1.823 ; 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 : BABINET MODEL WITH 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 2OU7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-FEB-07.
REMARK 100 THE RCSB ID CODE IS RCSB041590.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-FEB-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14898
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 45.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.2600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 71.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.31900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.850
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: PDB ENTRY 1MQ4 (RESIDUES 274-307 DELETED).
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN BUFFER: 50 MM HEPES, PH 7.5, 5
REMARK 280 MM TCEP. PROTEIN WAS INCUBATED ON ICE WITH 5 MM LIGAND (1:20
REMARK 280 DILUTION OF 100 MM STOCK IN H2O FOR AMPPNP OR DMSO FOR PHA-
REMARK 280 680626) FOR 0.5-1 H, FOLLOWED BY A BRIEF CENTRIFUGATION STEP AND
REMARK 280 DROP SETTING AT RT (0.5 MICROLITER PROTEIN + 0.5 MICROLITER
REMARK 280 RESERVOIR SOLUTION CONSISTING OF 500 MM MAGNESIUM ACETATE, 10 %
REMARK 280 PEG 4000 AND 0.3 MM ZINC ACETATE FOR AMPPNP, VAPOR DIFFUSION,
REMARK 280 HANGING 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 102.69667
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 51.34833
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 51.34833
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 102.69667
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 4610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -131.0 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 51.34833
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 11
REMARK 465 PRO A 12
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 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 508 O HOH A 583 5555 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 176 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 38 91.72 66.13
REMARK 500 LYS A 76 -3.24 68.04
REMARK 500 ASP A 122 -157.96 -114.76
REMARK 500 ARG A 135 32.85 -98.06
REMARK 500 ARG A 136 -145.59 59.16
REMARK 500 LYS A 146 -149.69 53.89
REMARK 500 ALA A 147 117.98 -36.52
REMARK 500 ARG A 175 -6.25 79.22
REMARK 500 ASP A 176 49.08 -141.78
REMARK 500 ASP A 194 83.89 64.03
REMARK 500 PHE A 195 31.27 -94.43
REMARK 500 SER A 229 -139.56 -146.81
REMARK 500 LEU A 286 49.43 -94.07
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 MG A 504 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ANP A 500 O2A
REMARK 620 2 ANP A 500 O3' 72.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 212 SG
REMARK 620 2 ACT A 502 O 106.3
REMARK 620 3 HIS A 93 NE2 120.8 105.3
REMARK 620 4 CYS A 255 SG 122.1 113.0 87.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 505 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 101 OE1
REMARK 620 2 ASP A 194 OD1 89.1
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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 500
DBREF 2OU7 A 13 345 UNP P53350 PLK1_HUMAN 13 345
SEQADV 2OU7 GLY A 11 UNP P53350 CLONING ARTIFACT
SEQADV 2OU7 PRO A 12 UNP P53350 CLONING ARTIFACT
SEQADV 2OU7 VAL A 210 UNP P53350 THR 210 ENGINEERED
SEQRES 1 A 335 GLY PRO ALA PRO ALA ASP PRO GLY LYS ALA GLY VAL PRO
SEQRES 2 A 335 GLY VAL ALA ALA PRO GLY ALA PRO ALA ALA ALA PRO PRO
SEQRES 3 A 335 ALA LYS GLU ILE PRO GLU VAL LEU VAL ASP PRO ARG SER
SEQRES 4 A 335 ARG ARG ARG TYR VAL ARG GLY ARG PHE LEU GLY LYS GLY
SEQRES 5 A 335 GLY PHE ALA LYS CYS PHE GLU ILE SER ASP ALA ASP THR
SEQRES 6 A 335 LYS GLU VAL PHE ALA GLY LYS ILE VAL PRO LYS SER LEU
SEQRES 7 A 335 LEU LEU LYS PRO HIS GLN ARG GLU LYS MET SER MET GLU
SEQRES 8 A 335 ILE SER ILE HIS ARG SER LEU ALA HIS GLN HIS VAL VAL
SEQRES 9 A 335 GLY PHE HIS GLY PHE PHE GLU ASP ASN ASP PHE VAL PHE
SEQRES 10 A 335 VAL VAL LEU GLU LEU CYS ARG ARG ARG SER LEU LEU GLU
SEQRES 11 A 335 LEU HIS LYS ARG ARG LYS ALA LEU THR GLU PRO GLU ALA
SEQRES 12 A 335 ARG TYR TYR LEU ARG GLN ILE VAL LEU GLY CYS GLN TYR
SEQRES 13 A 335 LEU HIS ARG ASN ARG VAL ILE HIS ARG ASP LEU LYS LEU
SEQRES 14 A 335 GLY ASN LEU PHE LEU ASN GLU ASP LEU GLU VAL LYS ILE
SEQRES 15 A 335 GLY ASP PHE GLY LEU ALA THR LYS VAL GLU TYR ASP GLY
SEQRES 16 A 335 GLU ARG LYS LYS VAL LEU CYS GLY THR PRO ASN TYR ILE
SEQRES 17 A 335 ALA PRO GLU VAL LEU SER LYS LYS GLY HIS SER PHE GLU
SEQRES 18 A 335 VAL ASP VAL TRP SER ILE GLY CYS ILE MET TYR THR LEU
SEQRES 19 A 335 LEU VAL GLY LYS PRO PRO PHE GLU THR SER CYS LEU LYS
SEQRES 20 A 335 GLU THR TYR LEU ARG ILE LYS LYS ASN GLU TYR SER ILE
SEQRES 21 A 335 PRO LYS HIS ILE ASN PRO VAL ALA ALA SER LEU ILE GLN
SEQRES 22 A 335 LYS MET LEU GLN THR ASP PRO THR ALA ARG PRO THR ILE
SEQRES 23 A 335 ASN GLU LEU LEU ASN ASP GLU PHE PHE THR SER GLY TYR
SEQRES 24 A 335 ILE PRO ALA ARG LEU PRO ILE THR CYS LEU THR ILE PRO
SEQRES 25 A 335 PRO ARG PHE SER ILE ALA PRO SER SER LEU ASP PRO SER
SEQRES 26 A 335 ASN ARG LYS PRO LEU THR VAL LEU ASN LYS
HET ZN A 501 1
HET ACT A 502 4
HET ACT A 503 4
HET MG A 504 1
HET MG A 505 1
HET ANP A 500 44
HETNAM ZN ZINC ION
HETNAM ACT ACETATE ION
HETNAM MG MAGNESIUM ION
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
FORMUL 2 ZN ZN 2+
FORMUL 3 ACT 2(C2 H3 O2 1-)
FORMUL 5 MG 2(MG 2+)
FORMUL 7 ANP C10 H17 N6 O12 P3
FORMUL 8 HOH *97(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 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 ASP A 289 ARG A 293 5 5
HELIX 11 11 GLU A 298 ASN A 301 5 4
HELIX 12 12 ASP A 302 SER A 307 1 6
HELIX 13 13 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 62 -1 O TYR A 53 N LEU A 44
SHEET 3 A 6 ALA A 65 ASP A 72 -1 O SER A 71 N VAL A 54
SHEET 4 A 6 VAL A 78 PRO A 85 -1 O ILE A 83 N LYS A 66
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 O2ABANP A 500 MG MG A 504 1555 1555 1.95
LINK ZN ZN A 501 SG CYS A 212 1555 1555 2.12
LINK ZN ZN A 501 O ACT A 502 1555 1555 2.03
LINK ZN ZN A 501 NE2 HIS A 93 1555 1555 2.24
LINK MG MG A 504 O3' ANP A 500 1555 1555 3.10
LINK MG MG A 505 OE1 GLU A 101 1555 1555 2.91
LINK MG MG A 505 OD1 ASP A 194 1555 1555 2.56
LINK ZN ZN A 501 SG CYS A 255 1555 5555 2.38
SITE 1 AC1 4 HIS A 93 CYS A 212 CYS A 255 ACT A 502
SITE 1 AC2 6 HIS A 93 GLN A 94 CYS A 212 CYS A 255
SITE 2 AC2 6 LEU A 256 ZN A 501
SITE 1 AC3 6 LYS A 178 LEU A 179 GLY A 180 ASN A 216
SITE 2 AC3 6 TYR A 217 HOH A 561
SITE 1 AC4 2 GLY A 62 ANP A 500
SITE 1 AC5 4 LYS A 82 GLU A 101 ASP A 194 ANP A 500
SITE 1 AC6 17 GLY A 62 GLY A 63 ALA A 80 LYS A 82
SITE 2 AC6 17 GLU A 131 CYS A 133 LYS A 178 GLY A 180
SITE 3 AC6 17 ASN A 181 PHE A 183 ASP A 194 GLY A 196
SITE 4 AC6 17 LEU A 197 MG A 504 MG A 505 HOH A 542
SITE 5 AC6 17 HOH A 600
CRYST1 65.958 65.958 154.045 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 0.015161 0.008753 0.000000 0.00000
SCALE2 0.000000 0.017507 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006492 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
