HEADER TRANSFERASE 18-JAN-08 3BZI
TITLE MOLECULAR AND STRUCTURAL BASIS OF POLO-LIKE KINASE 1
TITLE 2 SUBSTRATE RECOGNITION: IMPLICATIONS IN CENTROSOMAL
TITLE 3 LOCALIZATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PLK1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: POLO BOX DOMAIN;
COMPND 5 SYNONYM: POLO-LIKE KINASE 1, PLK-1, SERINE/THREONINE-
COMPND 6 PROTEIN KINASE 13, STPK13;
COMPND 7 EC: 2.7.11.21;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: 9 MER PEPTIDE FROM M-PHASE INDUCER PHOSPHATASE 3;
COMPND 11 CHAIN: E;
COMPND 12 SYNONYM: 9 MER PEPTIDE FROM DUAL SPECIFICITY PHOSPHATASE
COMPND 13 CDC25C;
COMPND 14 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;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-ROSETTA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-6-1P;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: SYNTHETIC PEPTIDE
KEYWDS KINASE, CELL CYCLE, LOCALIZATION, ATP-BINDING, NUCLEOTIDE-
KEYWDS 2 BINDING, NUCLEUS, PHOSPHOPROTEIN, SERINE/THREONINE-PROTEIN
KEYWDS 3 KINASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.GARCIA-ALVAREZ,G.DE CARCER,S.IBANEZ,E.BRAGADO-NILSSON,
AUTHOR 2 G.MONTOYA
REVDAT 2 24-FEB-09 3BZI 1 VERSN
REVDAT 1 05-FEB-08 3BZI 0
SPRSDE 05-FEB-08 3BZI 2OJS
JRNL AUTH B.GARCIA-ALVAREZ,G.DE CARCER,S.IBANEZ,
JRNL AUTH 2 E.BRAGADO-NILSSON,G.MONTOYA
JRNL TITL MOLECULAR AND STRUCTURAL BASIS OF POLO-LIKE KINASE
JRNL TITL 2 1 SUBSTRATE RECOGNITION: IMPLICATIONS IN
JRNL TITL 3 CENTROSOMAL LOCALIZATION.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 104 3107 2007
JRNL REFN ISSN 0027-8424
JRNL PMID 17307877
JRNL DOI 10.1073/PNAS.0609131104
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.84
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.8
REMARK 3 NUMBER OF REFLECTIONS : 12144
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) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 627
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 844
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.09
REMARK 3 BIN R VALUE (WORKING SET) : 0.2030
REMARK 3 BIN FREE R VALUE SET COUNT : 40
REMARK 3 BIN FREE R VALUE : 0.2760
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1865
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 175
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.74
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
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): 0.275
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.222
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.138
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.194
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1905 ; 0.022 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2576 ; 1.959 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 228 ; 6.625 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 90 ;33.112 ;23.222
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 339 ;16.939 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;16.975 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 286 ; 0.133 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1423 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 843 ; 0.225 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1309 ; 0.308 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 140 ; 0.192 ; 0.200
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): 35 ; 0.202 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 16 ; 0.185 ; 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): 1181 ; 1.209 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1850 ; 2.046 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 829 ; 3.195 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 726 ; 4.737 ; 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 : 1.20
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 3BZI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-JAN-08.
REMARK 100 THE RCSB ID CODE IS RCSB046151.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
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 : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12144
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 36.840
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.8
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: MOLREP
REMARK 200 STARTING MODEL: 1OWL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM HEPES PH 7.5, 2M AMMONIUM
REMARK 280 FORMATE, VAPOR DIFFUSION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 19.36300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.94400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.74050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.94400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.36300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.74050
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1230 ANGSTROM**2
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 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 GLU A 365
REMARK 465 THR A 366
REMARK 465 GLY A 367
REMARK 465 GLU A 368
REMARK 465 VAL A 369
REMARK 465 VAL A 370
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 465 GLY E 8
REMARK 465 LEU E 9
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 N ASP A 371 O HOH A 706 2.02
REMARK 500 O HOH A 605 O HOH A 768 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ALA A 520 CA ALA A 520 CB 0.129
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 ARG A 441 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 LEU A 508 CA - CB - CG ANGL. DEV. = 15.9 DEGREES
REMARK 500 ASP A 554 CB - CG - OD1 ANGL. DEV. = 5.5 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 420 -50.66 -122.82
REMARK 500 ASN A 446 3.23 -63.73
REMARK 500 ASP A 449 -42.27 -146.01
REMARK 500 ASP A 503 -152.90 -105.21
REMARK 500 SER A 592 -71.10 -51.83
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 FMT A 1
DBREF 3BZI A 365 603 UNP P53350 PLK1_HUMAN 365 603
DBREF 3BZI E 1 9 UNP P30307 MPIP3_HUMAN 126 134
SEQRES 1 A 239 GLU THR GLY GLU VAL VAL ASP CYS HIS LEU SER ASP MET
SEQRES 2 A 239 LEU GLN GLN LEU HIS SER VAL ASN ALA SER LYS PRO SER
SEQRES 3 A 239 GLU ARG GLY LEU VAL ARG GLN GLU GLU ALA GLU ASP PRO
SEQRES 4 A 239 ALA CYS ILE PRO ILE PHE TRP VAL SER LYS TRP VAL ASP
SEQRES 5 A 239 TYR SER ASP LYS TYR GLY LEU GLY TYR GLN LEU CYS ASP
SEQRES 6 A 239 ASN SER VAL GLY VAL LEU PHE ASN ASP SER THR ARG LEU
SEQRES 7 A 239 ILE LEU TYR ASN ASP GLY ASP SER LEU GLN TYR ILE GLU
SEQRES 8 A 239 ARG ASP GLY THR GLU SER TYR LEU THR VAL SER SER HIS
SEQRES 9 A 239 PRO ASN SER LEU MET LYS LYS ILE THR LEU LEU LYS TYR
SEQRES 10 A 239 PHE ARG ASN TYR MET SER GLU HIS LEU LEU LYS ALA GLY
SEQRES 11 A 239 ALA ASN ILE THR PRO ARG GLU GLY ASP GLU LEU ALA ARG
SEQRES 12 A 239 LEU PRO TYR LEU ARG THR TRP PHE ARG THR ARG SER ALA
SEQRES 13 A 239 ILE ILE LEU HIS LEU SER ASN GLY SER VAL GLN ILE ASN
SEQRES 14 A 239 PHE PHE GLN ASP HIS THR LYS LEU ILE LEU CYS PRO LEU
SEQRES 15 A 239 MET ALA ALA VAL THR TYR ILE ASP GLU LYS ARG ASP PHE
SEQRES 16 A 239 ARG THR TYR ARG LEU SER LEU LEU GLU GLU TYR GLY CYS
SEQRES 17 A 239 CYS LYS GLU LEU ALA SER ARG LEU ARG TYR ALA ARG THR
SEQRES 18 A 239 MET VAL ASP LYS LEU LEU SER SER ARG SER ALA SER ASN
SEQRES 19 A 239 ARG LEU LYS ALA SER
SEQRES 1 E 9 LEU LEU CYS SER TPO PRO ASN GLY LEU
MODRES 3BZI TPO E 5 THR PHOSPHOTHREONINE
HET TPO E 5 11
HET FMT A 1 3
HETNAM TPO PHOSPHOTHREONINE
HETNAM FMT FORMIC ACID
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 2 TPO C4 H10 N O6 P
FORMUL 3 FMT C H2 O2
FORMUL 4 HOH *172(H2 O)
HELIX 1 1 ASP A 371 SER A 387 1 17
HELIX 2 2 ARG A 396 ALA A 400 5 5
HELIX 3 3 ASP A 402 ILE A 406 5 5
HELIX 4 4 PRO A 469 SER A 471 5 3
HELIX 5 5 LEU A 472 LEU A 490 1 19
HELIX 6 6 LEU A 564 GLY A 571 1 8
HELIX 7 7 CYS A 573 SER A 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 TYR A 453 O SER A 461
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 TYR A 425 O GLY A 433
SHEET 6 A 7 VAL A 411 ASP A 416 -1 N SER A 412 O GLN A 426
SHEET 7 A 7 LEU E 2 CYS E 3 -1 O LEU E 2 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 541 N ILE A 532
SHEET 5 B 6 ALA A 549 ILE A 553 -1 O ILE A 553 N LYS A 540
SHEET 6 B 6 PHE A 559 ARG A 563 -1 O TYR A 562 N VAL A 550
LINK C SER E 4 N TPO E 5 1555 1555 1.33
LINK C TPO E 5 N PRO E 6 1555 1555 1.36
SITE 1 AC1 5 TYR A 481 ALA A 506 ARG A 507 ASN A 527
SITE 2 AC1 5 HOH A 756
CRYST1 38.726 67.481 87.888 90.00 90.00 90.00 P 21 21 21 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 0.025822 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014819 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011378 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
