GenomeNet

Database: PDB
Entry: 2RKU
LinkDB: 2RKU
Original site: 2RKU 
HEADER    TRANSFERASE                             17-OCT-07   2RKU              
TITLE     STRUCTURE OF PLK1 IN COMPLEX WITH BI2536                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PLK1;                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: POLO-LIKE KINASE 1, PLK-1, SERINE/THREONINE-PROTEIN KINASE  
COMPND   5 13, STPK13;                                                          
COMPND   6 EC: 2.7.11.21;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 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                                        
KEYWDS    STRUCTURE OF PLK1, SELECTIVITY RESIDUES, KINASE, POLO-LIKE KINASE,    
KEYWDS   2 STRUCTURE BASED DRUG DESIGN, ATP-BINDING, NUCLEOTIDE-BINDING,        
KEYWDS   3 NUCLEUS, PHOSPHORYLATION, SERINE/THREONINE-PROTEIN KINASE,           
KEYWDS   4 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.-H.DING,M.KOTHE,D.KOHLS,S.LOW                                       
REVDAT   3   13-JUL-11 2RKU    1       VERSN                                    
REVDAT   2   24-FEB-09 2RKU    1       VERSN                                    
REVDAT   1   05-FEB-08 2RKU    0                                                
JRNL        AUTH   M.KOTHE,D.KOHLS,S.LOW,R.COLI,G.R.RENNIE,F.FERU,C.KUHN,       
JRNL        AUTH 2 Y.-H.DING                                                    
JRNL        TITL   SELECTIVITY-DETERMINING RESIDUES IN PLK1.                    
JRNL        REF    CHEM.BIOL.DRUG DES.           V.  70   540 2007              
JRNL        REFN                   ISSN 1747-0277                               
JRNL        PMID   18005335                                                     
JRNL        DOI    10.1111/J.1747-0285.2007.00594.X                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 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) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.41                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 29416                          
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) : 0.192                           
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.241                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1494                            
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) : 1.95                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.00                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1943                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.48                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2500                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 107                          
REMARK   3   BIN FREE R VALUE                    : 0.3160                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2379                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 89                                      
REMARK   3   SOLVENT ATOMS            : 285                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.01                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.37000                                              
REMARK   3    B22 (A**2) : 2.37000                                              
REMARK   3    B33 (A**2) : -3.55000                                             
REMARK   3    B12 (A**2) : 1.18000                                              
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): 0.154         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.151         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.120         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.232         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.939                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2558 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3462 ; 1.438 ; 2.014       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   303 ; 5.491 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   110 ;34.619 ;22.455       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   454 ;14.890 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;16.163 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   382 ; 0.096 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1929 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1119 ; 0.195 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1755 ; 0.314 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   265 ; 0.199 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     1 ; 0.012 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    49 ; 0.185 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    16 ; 0.222 ; 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):  1550 ; 0.845 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2446 ; 1.351 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1154 ; 2.185 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1016 ; 3.520 ; 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  : 6                                          
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    37        A    50                          
REMARK   3    ORIGIN FOR THE GROUP (A): -40.2378  -1.8107   3.8106              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3212 T22:   0.1678                                     
REMARK   3      T33:  -0.2158 T12:  -0.1087                                     
REMARK   3      T13:   0.2629 T23:   0.1141                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  13.6610 L22:  13.0700                                     
REMARK   3      L33:  11.8916 L12:  -2.0564                                     
REMARK   3      L13:   6.1372 L23:   1.6663                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.7459 S12:  -1.0295 S13:  -0.9041                       
REMARK   3      S21:  -0.1702 S22:   0.7168 S23:   0.1412                       
REMARK   3      S31:   0.0820 S32:  -1.6849 S33:   1.0291                       
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 :   A    51        A   100                          
REMARK   3    ORIGIN FOR THE GROUP (A): -41.9653   7.7123   6.7972              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1207 T22:  -0.2169                                     
REMARK   3      T33:  -0.1699 T12:  -0.0590                                     
REMARK   3      T13:   0.0537 T23:  -0.0445                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1398 L22:   2.5081                                     
REMARK   3      L33:   6.1352 L12:   0.6483                                     
REMARK   3      L13:  -1.6425 L23:  -0.3816                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1077 S12:   0.1684 S13:  -0.1163                       
REMARK   3      S21:  -0.0765 S22:  -0.1325 S23:   0.1774                       
REMARK   3      S31:   0.7831 S32:  -0.2912 S33:   0.2402                       
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 :   A   151        A   200                          
REMARK   3    ORIGIN FOR THE GROUP (A): -35.2718  23.5720  19.3793              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2739 T22:  -0.1477                                     
REMARK   3      T33:  -0.1498 T12:   0.0325                                     
REMARK   3      T13:  -0.0217 T23:  -0.0297                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4487 L22:   1.7511                                     
REMARK   3      L33:   5.6065 L12:  -0.0316                                     
REMARK   3      L13:  -0.4016 L23:   0.3936                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1138 S12:  -0.0585 S13:  -0.0282                       
REMARK   3      S21:   0.1607 S22:   0.0579 S23:  -0.1354                       
REMARK   3      S31:   0.0641 S32:   0.2433 S33:   0.0559                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   201        A   250                          
REMARK   3    ORIGIN FOR THE GROUP (A): -37.5824  34.3778  10.9320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1896 T22:  -0.2040                                     
REMARK   3      T33:  -0.1323 T12:  -0.0112                                     
REMARK   3      T13:  -0.0289 T23:  -0.0139                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9048 L22:   0.9809                                     
REMARK   3      L33:   6.4368 L12:  -0.5113                                     
REMARK   3      L13:  -1.6760 L23:   0.4792                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0899 S12:   0.1762 S13:   0.3805                       
REMARK   3      S21:  -0.1045 S22:   0.0733 S23:  -0.1101                       
REMARK   3      S31:  -0.7222 S32:   0.0713 S33:   0.0165                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   251        A   294                          
REMARK   3    ORIGIN FOR THE GROUP (A): -42.0269  40.7659  18.4090              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1276 T22:  -0.3127                                     
REMARK   3      T33:  -0.1448 T12:   0.0167                                     
REMARK   3      T13:  -0.0609 T23:  -0.0595                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5222 L22:   2.1400                                     
REMARK   3      L33:   6.1711 L12:  -0.0667                                     
REMARK   3      L13:   1.7478 L23:  -0.0639                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3677 S12:  -0.2599 S13:   0.6680                       
REMARK   3      S21:  -0.0206 S22:   0.2258 S23:  -0.1992                       
REMARK   3      S31:  -0.9117 S32:  -0.3115 S33:   0.1419                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   501        A   507                          
REMARK   3    ORIGIN FOR THE GROUP (A): -40.4911  25.8842  37.3979              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1500 T22:  -0.0682                                     
REMARK   3      T33:  -0.2162 T12:   0.0589                                     
REMARK   3      T13:  -0.0095 T23:  -0.0304                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0836 L22:   1.7111                                     
REMARK   3      L33:   5.3953 L12:   1.3720                                     
REMARK   3      L13:   0.7399 L23:  -0.1778                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0100 S12:  -0.5493 S13:  -0.1186                       
REMARK   3      S21:   0.5604 S22:  -0.0010 S23:  -0.0022                       
REMARK   3      S31:   0.2500 S32:  -0.3905 S33:   0.0110                       
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2RKU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JAN-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB044981.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
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   : 29527                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : 0.06900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.50500                            
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: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.82                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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      102.74000            
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       51.37000            
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       51.37000            
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      102.74000            
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                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4670 ANGSTROM**2                          
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 -0.500000  0.866025  0.000000      -99.88950            
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000       57.67123            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
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   O    HOH A   732     O    HOH A   733              1.97            
REMARK 500   O    HOH A   513     O    HOH A   787              1.99            
REMARK 500   OD2  ASP A   176     O    HOH A   513              2.03            
REMARK 500   O    HOH A   687     O    HOH A   761              2.10            
REMARK 500   O    HOH A   675     O    HOH A   752              2.12            
REMARK 500   O    HOH A   508     O    HOH A   697              2.18            
REMARK 500   O    HOH A   510     O    HOH A   700              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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   OG   SER A    99     O    ILE A   327     2564     2.09            
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    GLU A  42   CG    GLU A  42   CD      0.117                       
REMARK 500    GLU A  42   CD    GLU A  42   OE1     0.105                       
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      117.61     54.24                                   
REMARK 500    ASP A 122     -161.58   -121.70                                   
REMARK 500    ARG A 136     -125.32     60.55                                   
REMARK 500    LYS A 146     -134.80     55.34                                   
REMARK 500    ARG A 175       -2.57     75.93                                   
REMARK 500    ASP A 176       37.18   -141.48                                   
REMARK 500    ASP A 194       79.11     54.06                                   
REMARK 500    SER A 229     -148.69   -150.19                                   
REMARK 500    LEU A 286       30.33    -94.95                                   
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                              ZN A 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  93   NE2                                                    
REMARK 620 2 CYS A 212   SG  118.1                                              
REMARK 620 3 TLA A 502   O1  101.9 109.6                                        
REMARK 620 N                    1     2                                         
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 R78 A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TLA A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TLA A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRT A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRT A 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAR A 503                 
DBREF  2RKU A   37   330  UNP    P53350   PLK1_HUMAN      37    330             
SEQADV 2RKU VAL A  210  UNP  P53350    THR   210 ENGINEERED                     
SEQRES   1 A  294  ALA LYS GLU ILE PRO GLU VAL LEU VAL ASP PRO ARG SER          
SEQRES   2 A  294  ARG ARG ARG TYR VAL ARG GLY ARG PHE LEU GLY LYS GLY          
SEQRES   3 A  294  GLY PHE ALA LYS CYS PHE GLU ILE SER ASP ALA ASP THR          
SEQRES   4 A  294  LYS GLU VAL PHE ALA GLY LYS ILE VAL PRO LYS SER LEU          
SEQRES   5 A  294  LEU LEU LYS PRO HIS GLN ARG GLU LYS MET SER MET GLU          
SEQRES   6 A  294  ILE SER ILE HIS ARG SER LEU ALA HIS GLN HIS VAL VAL          
SEQRES   7 A  294  GLY PHE HIS GLY PHE PHE GLU ASP ASN ASP PHE VAL PHE          
SEQRES   8 A  294  VAL VAL LEU GLU LEU CYS ARG ARG ARG SER LEU LEU GLU          
SEQRES   9 A  294  LEU HIS LYS ARG ARG LYS ALA LEU THR GLU PRO GLU ALA          
SEQRES  10 A  294  ARG TYR TYR LEU ARG GLN ILE VAL LEU GLY CYS GLN TYR          
SEQRES  11 A  294  LEU HIS ARG ASN ARG VAL ILE HIS ARG ASP LEU LYS LEU          
SEQRES  12 A  294  GLY ASN LEU PHE LEU ASN GLU ASP LEU GLU VAL LYS ILE          
SEQRES  13 A  294  GLY ASP PHE GLY LEU ALA THR LYS VAL GLU TYR ASP GLY          
SEQRES  14 A  294  GLU ARG LYS LYS VAL LEU CYS GLY THR PRO ASN TYR ILE          
SEQRES  15 A  294  ALA PRO GLU VAL LEU SER LYS LYS GLY HIS SER PHE GLU          
SEQRES  16 A  294  VAL ASP VAL TRP SER ILE GLY CYS ILE MET TYR THR LEU          
SEQRES  17 A  294  LEU VAL GLY LYS PRO PRO PHE GLU THR SER CYS LEU LYS          
SEQRES  18 A  294  GLU THR TYR LEU ARG ILE LYS LYS ASN GLU TYR SER ILE          
SEQRES  19 A  294  PRO LYS HIS ILE ASN PRO VAL ALA ALA SER LEU ILE GLN          
SEQRES  20 A  294  LYS MET LEU GLN THR ASP PRO THR ALA ARG PRO THR ILE          
SEQRES  21 A  294  ASN GLU LEU LEU ASN ASP GLU PHE PHE THR SER GLY TYR          
SEQRES  22 A  294  ILE PRO ALA ARG LEU PRO ILE THR CYS LEU THR ILE PRO          
SEQRES  23 A  294  PRO ARG PHE SER ILE ALA PRO SER                              
HET     ZN  A 501       1                                                       
HET    R78  A 500      38                                                       
HET    TLA  A 502      10                                                       
HET    TLA  A 504      10                                                       
HET    SRT  A 505      10                                                       
HET    SRT  A 507      10                                                       
HET    TAR  A 503      10                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     R78 4-{[(7R)-8-CYCLOPENTYL-7-ETHYL-5-METHYL-6-OXO-5,6,7,8-           
HETNAM   2 R78  TETRAHYDROPTERIDIN-2-YL]AMINO}-3-METHOXY-N-(1-                  
HETNAM   3 R78  METHYLPIPERIDIN-4-YL)BENZAMIDE                                  
HETNAM     TLA L(+)-TARTARIC ACID                                               
HETNAM     SRT S,R MESO-TARTARIC ACID                                           
HETNAM     TAR D(-)-TARTARIC ACID                                               
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  R78    C28 H39 N7 O3                                                
FORMUL   4  TLA    2(C4 H6 O6)                                                  
FORMUL   6  SRT    2(C4 H6 O6)                                                  
FORMUL   8  TAR    C4 H6 O6                                                     
FORMUL   9  HOH   *285(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  LYS A  265  1                                  11    
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 THR A  295  ASN A  301  5                                   7    
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  GLU A  69   N  GLY A  56           
SHEET    4   A 6 VAL A  78  PRO A  85 -1  O  GLY A  81   N  PHE A  68           
SHEET    5   A 6 PHE A 125  GLU A 131 -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         NE2 HIS A  93                ZN    ZN A 501     1555   1555  2.09  
LINK         SG  CYS A 212                ZN    ZN A 501     1555   1555  2.25  
LINK        ZN    ZN A 501                 O1  TLA A 502     1555   1555  2.01  
SITE     1 AC1  4 HIS A  93  CYS A 212  CYS A 255  TLA A 502                    
SITE     1 AC2 15 ARG A  57  PHE A  58  LEU A  59  LYS A  61                    
SITE     2 AC2 15 GLU A  69  VAL A 114  LEU A 130  GLU A 131                    
SITE     3 AC2 15 LEU A 132  CYS A 133  ARG A 136  PHE A 183                    
SITE     4 AC2 15 HOH A 527  HOH A 563  HOH A 619                               
SITE     1 AC3 11 LYS A  91  HIS A  93  LYS A  97  CYS A 212                    
SITE     2 AC3 11 SER A 254  CYS A 255  LEU A 256   ZN A 501                    
SITE     3 AC3 11 TLA A 504  HOH A 608  HOH A 677                               
SITE     1 AC4  8 PHE A  64  LYS A  91  GLN A  94  LYS A  97                    
SITE     2 AC4  8 TLA A 502  HOH A 552  HOH A 608  HOH A 733                    
SITE     1 AC5  5 ASN A 266  TYR A 268  SER A 269  ILE A 270                    
SITE     2 AC5  5 GLN A 283                                                     
SITE     1 AC6  7 ARG A 135  GLU A 140  LEU A 141  LEU A 319                    
SITE     2 AC6  7 HOH A 592  HOH A 648  HOH A 698                               
SITE     1 AC7  7 LEU A 139  LYS A 178  LEU A 179  GLY A 180                    
SITE     2 AC7  7 ASN A 216  HOH A 743  HOH A 783                               
CRYST1   66.593   66.593  154.110  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      0.015017  0.008670  0.000000        0.00000                         
SCALE2      0.000000  0.017340  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006489        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system