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Database: PDB
Entry: 2OJX
LinkDB: 2OJX
Original site: 2OJX 
HEADER    TRANSFERASE                             15-JAN-07   2OJX              
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: RESIDUES 365-603;                                          
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: SYNTHETIC PEPTIDE;                                         
COMPND  11 CHAIN: E;                                                            
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_STRAIN: BL21-PLYS;                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-2;                                
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 OTHER_DETAILS: SYNTHETIC PEPTIDE                                     
KEYWDS    POLO BOX DOMAIN, KINASE, CENTROSOME, TRANSFERASE                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.GARCIA-ALVAREZ,G.DE CARCER,S.IBANEZ,E.BRAGADO-NILSSON,              
AUTHOR   2 G.MONTOYA                                                            
REVDAT   4   24-FEB-09 2OJX    1       VERSN                                    
REVDAT   3   06-NOV-07 2OJX    1       REMARK                                   
REVDAT   2   27-MAR-07 2OJX    1       JRNL                                     
REVDAT   1   13-FEB-07 2OJX    0                                                
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.    2.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5                                             
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 18.94                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 4225                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.230                           
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.270                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE SET COUNT          : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1725                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 10                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : NULL                          
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL                          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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 : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : NULL                                          
REMARK   3   ION PROBE RADIUS   : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2OJX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JAN-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB041228.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JUL-05                          
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               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 4971                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY                : 2.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.31000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1UMW                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 33.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.84                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 % PEG 10000, PH 7.5, VAPOR            
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 289K                           
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       24.58900            
REMARK 290   SMTRY3   2  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 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     ASP A   371                                                      
REMARK 465     CYS A   372                                                      
REMARK 465     HIS A   489                                                      
REMARK 465     LEU A   490                                                      
REMARK 465     LEU A   491                                                      
REMARK 465     LYS A   492                                                      
REMARK 465     ALA A   493                                                      
REMARK 465     GLY A   494                                                      
REMARK 465     ALA A   495                                                      
REMARK 465     ASN A   496                                                      
REMARK 465     ILE A   497                                                      
REMARK 465     THR A   498                                                      
REMARK 465     PRO A   499                                                      
REMARK 465     ARG A   500                                                      
REMARK 465     GLU A   501                                                      
REMARK 465     GLY A   502                                                      
REMARK 465     ASP A   503                                                      
REMARK 465     GLU A   504                                                      
REMARK 465     LEU A   505                                                      
REMARK 465     ALA A   506                                                      
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: 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    THR A 517   N   -  CA  -  C   ANGL. DEV. = -17.7 DEGREES          
REMARK 500    LEU E   2   N   -  CA  -  C   ANGL. DEV. =  18.1 DEGREES          
REMARK 500    SER E   4   N   -  CA  -  C   ANGL. DEV. =  18.1 DEGREES          
REMARK 500    PRO E   6   C   -  N   -  CA  ANGL. DEV. = -11.9 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    ARG A 396       69.03   -105.67                                   
REMARK 500    ASP A 402       95.11   -165.05                                   
REMARK 500    LYS A 420      -65.63   -106.68                                   
REMARK 500    ARG A 456      -17.65    -48.06                                   
REMARK 500    LEU A 463     -151.17   -109.57                                   
REMARK 500    PRO A 469       87.52    -26.73                                   
REMARK 500    ASN A 470      -90.01     -9.04                                   
REMARK 500    THR A 513      176.53    176.72                                   
REMARK 500    PHE A 515      141.91    165.56                                   
REMARK 500    HIS A 538       16.06     56.73                                   
REMARK 500    ARG A 557       26.75     91.03                                   
REMARK 500    GLU A 575      -65.41     93.46                                   
REMARK 500    SER A 592      -82.62    -70.52                                   
REMARK 500    LEU E   2      152.22     70.63                                   
REMARK 500    SER E   4      -22.54    -38.89                                   
REMARK 500    THR E   5      -12.93     94.68                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2OGQ   RELATED DB: PDB                                   
REMARK 900 MOLECULAR AND STRUCTURAL BASIS OF PLK1 SUBSTRATE                     
REMARK 900 RECOGNITION: IMPLICATIONS IN CENTROSOMAL LOCALIZATION                
REMARK 900 RELATED ID: 2OJS   RELATED DB: PDB                                   
REMARK 900 MOLECULAR AND STRUCTURAL BASIS OF POLO-LIKE KINASE 1                 
REMARK 900 SUBSTRATE RECOGNITION: IMPLICATIONS IN CENTROSOMAL                   
REMARK 900 LOCALIZATION                                                         
DBREF  2OJX A  365   603  UNP    P53350   PLK1_HUMAN     365    603             
DBREF  2OJX E    1     9  PDB    2OJX     2OJX             1      9             
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 THR PRO ASN GLY LEU                          
FORMUL   3  HOH   *10(H2 O)                                                     
HELIX    1   1 HIS A  373  SER A  387  1                                  15    
HELIX    2   2 ARG A  396  GLU A  401  5                                   6    
HELIX    3   3 PRO A  469  SER A  471  5                                   3    
HELIX    4   4 LEU A  472  GLU A  488  1                                  17    
HELIX    5   5 LEU A  566  GLY A  571  1                                   6    
HELIX    6   6 GLU A  575  SER A  593  1                                  19    
SHEET    1   A 6 VAL A 411  TYR A 417  0                                        
SHEET    2   A 6 GLY A 422  LEU A 427 -1  O  GLN A 426   N  LYS A 413           
SHEET    3   A 6 VAL A 432  PHE A 436 -1  O  GLY A 433   N  TYR A 425           
SHEET    4   A 6 ARG A 441  LEU A 444 -1  O  LEU A 444   N  VAL A 432           
SHEET    5   A 6 SER A 450  ILE A 454 -1  O  GLN A 452   N  ILE A 443           
SHEET    6   A 6 GLU A 460  THR A 464 -1  O  SER A 461   N  TYR A 453           
SHEET    1   B 6 LEU A 511  ARG A 516  0                                        
SHEET    2   B 6 ALA A 520  LEU A 525 -1  O  HIS A 524   N  THR A 513           
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  THR A 551   N  ILE A 542           
SHEET    6   B 6 PHE A 559  ARG A 563 -1  O  ARG A 560   N  TYR A 552           
CRYST1   40.186   49.178   56.234  90.00 109.48  90.00 P 1 21 1      2          
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      0.024884  0.000000  0.008802        0.00000                         
SCALE2      0.000000  0.020334  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018863        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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