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Database: PDB
Entry: 3THB
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Original site: 3THB 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       18-AUG-11   3THB              
TITLE     STRUCTURE OF PLK1 KINASE DOMAIN IN COMPLEX WITH A BENZOLACTAM-DERIVED 
TITLE    2 INHIBITOR                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PLK1;                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 13-345;                                       
COMPND   5 SYNONYM: POLO-LIKE KINASE 1, PLK-1, SERINE/THREONINE-PROTEIN KINASE  
COMPND   6 13, STPK13;                                                          
COMPND   7 EC: 2.7.11.21;                                                       
COMPND   8 ENGINEERED: YES                                                      
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                                         
KEYWDS    KINASE DOMAIN, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.D.SINTCHAK                                                          
REVDAT   2   25-JAN-12 3THB    1       JRNL                                     
REVDAT   1   23-NOV-11 3THB    0                                                
JRNL        AUTH   M.O.DUFFEY,T.J.VOS,R.ADAMS,J.ALLEY,J.ANTHONY,C.BARRETT,      
JRNL        AUTH 2 I.BHARATHAN,D.BOWMAN,N.J.BUMP,R.CHAU,C.CULLIS,D.L.DRISCOLL,  
JRNL        AUTH 3 A.ELDER,N.FORSYTH,J.FRAZER,J.GUO,L.GUO,M.L.HYER,D.JANOWICK,  
JRNL        AUTH 4 B.KULKARNI,S.J.LAI,K.LASKY,G.LI,J.LI,D.LIAO,J.LITTLE,B.PENG, 
JRNL        AUTH 5 M.G.QIAN,D.J.REYNOLDS,M.REZAEI,M.P.SCOTT,T.B.SELLS,V.SHINDE, 
JRNL        AUTH 6 Q.J.SHI,M.D.SINTCHAK,F.SOUCY,K.T.SPROTT,S.G.STROUD,M.NESTOR, 
JRNL        AUTH 7 I.VISIERS,G.WEATHERHEAD,Y.YE,N.D'AMORE                       
JRNL        TITL   DISCOVERY OF A POTENT AND ORALLY BIOAVAILABLE                
JRNL        TITL 2 BENZOLACTAM-DERIVED INHIBITOR OF POLO-LIKE KINASE 1          
JRNL        TITL 3 (MLN0905).                                                   
JRNL        REF    J.MED.CHEM.                   V.  55   197 2012              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   22070629                                                     
JRNL        DOI    10.1021/JM2011172                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0110                                      
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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 11950                          
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) : 0.253                           
REMARK   3   R VALUE            (WORKING SET) : 0.250                           
REMARK   3   FREE R VALUE                     : 0.286                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1317                            
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) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.57                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 442                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 47.37                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3780                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 54                           
REMARK   3   BIN FREE R VALUE                    : 0.4070                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2242                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 32                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 85.71                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.57000                                              
REMARK   3    B22 (A**2) : 5.57000                                              
REMARK   3    B33 (A**2) : -8.36000                                             
REMARK   3    B12 (A**2) : 2.79000                                              
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): 0.599         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.335         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.321         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 34.000        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.936                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2329 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3160 ; 1.394 ; 1.988       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   286 ; 6.124 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    98 ;34.006 ;22.959       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   384 ;17.075 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;19.622 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   353 ; 0.096 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1762 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1433 ; 1.463 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2307 ; 2.730 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   896 ; 4.051 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   853 ; 6.282 ; 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  : 4                                          
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    42        A    82                          
REMARK   3    ORIGIN FOR THE GROUP (A): -52.2691  18.9564  14.9651              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1953 T22:   1.6203                                     
REMARK   3      T33:   0.0750 T12:   0.2963                                     
REMARK   3      T13:  -0.0787 T23:  -0.3417                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7517 L22:   9.8233                                     
REMARK   3      L33:   5.7236 L12:  -1.4263                                     
REMARK   3      L13:   0.1285 L23:   2.5740                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6348 S12:  -0.1061 S13:  -0.1357                       
REMARK   3      S21:  -0.4539 S22:   0.0837 S23:  -0.5003                       
REMARK   3      S31:  -0.1569 S32:  -2.9690 S33:   0.5511                       
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    83        A   154                          
REMARK   3    ORIGIN FOR THE GROUP (A): -40.1187  15.2292  14.1512              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6235 T22:   0.5951                                     
REMARK   3      T33:   0.3542 T12:   0.1342                                     
REMARK   3      T13:  -0.0438 T23:  -0.0229                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7754 L22:   0.7565                                     
REMARK   3      L33:   6.8976 L12:  -0.0270                                     
REMARK   3      L13:  -0.4508 L23:   1.5585                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0551 S12:  -0.1380 S13:  -0.0793                       
REMARK   3      S21:  -0.2294 S22:  -0.1291 S23:   0.0035                       
REMARK   3      S31:  -0.5058 S32:  -0.8047 S33:   0.1841                       
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   155        A   251                          
REMARK   3    ORIGIN FOR THE GROUP (A): -27.2985  11.6416  11.0584              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6507 T22:   0.5339                                     
REMARK   3      T33:   0.4654 T12:  -0.0787                                     
REMARK   3      T13:   0.0000 T23:   0.0070                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3525 L22:   0.5478                                     
REMARK   3      L33:   3.8411 L12:  -0.0176                                     
REMARK   3      L13:  -0.5329 L23:   0.2381                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0479 S12:  -0.1216 S13:  -0.1642                       
REMARK   3      S21:  -0.0240 S22:   0.0200 S23:   0.0735                       
REMARK   3      S31:  -0.4435 S32:   0.3894 S33:   0.0279                       
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   252        A   328                          
REMARK   3    ORIGIN FOR THE GROUP (A): -23.9052   4.7329   0.4834              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5024 T22:   0.4935                                     
REMARK   3      T33:   0.4149 T12:  -0.0228                                     
REMARK   3      T13:   0.0812 T23:   0.0144                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2896 L22:   1.6054                                     
REMARK   3      L33:   5.6217 L12:   0.4908                                     
REMARK   3      L13:  -0.0804 L23:  -0.2952                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1337 S12:   0.0139 S13:  -0.1254                       
REMARK   3      S21:  -0.4729 S22:  -0.0377 S23:  -0.3194                       
REMARK   3      S31:   0.2379 S32:   0.6573 S33:   0.1714                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3THB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-AUG-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB067477.                                      
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                       : 31-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97989                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-225                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13436                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
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     (%) : 90.6                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : 0.08400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 50.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39600                            
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: NULL                                                  
REMARK 200 STARTING MODEL: 2OWB                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73                     
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      103.12267            
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       51.56133            
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       51.56133            
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      103.12267            
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: 1230 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27310 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -91.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       51.56133            
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     ALA A    13                                                      
REMARK 465     PRO A    14                                                      
REMARK 465     ALA A    15                                                      
REMARK 465     ASP A    16                                                      
REMARK 465     PRO A    17                                                      
REMARK 465     GLY A    18                                                      
REMARK 465     LYS A    19                                                      
REMARK 465     ALA A    20                                                      
REMARK 465     GLY A    21                                                      
REMARK 465     VAL A    22                                                      
REMARK 465     PRO A    23                                                      
REMARK 465     GLY A    24                                                      
REMARK 465     VAL A    25                                                      
REMARK 465     ALA A    26                                                      
REMARK 465     ALA A    27                                                      
REMARK 465     PRO A    28                                                      
REMARK 465     GLY A    29                                                      
REMARK 465     ALA A    30                                                      
REMARK 465     PRO A    31                                                      
REMARK 465     ALA A    32                                                      
REMARK 465     ALA A    33                                                      
REMARK 465     ALA A    34                                                      
REMARK 465     PRO A    35                                                      
REMARK 465     PRO A    36                                                      
REMARK 465     ALA A    37                                                      
REMARK 465     LYS A    38                                                      
REMARK 465     GLU A    39                                                      
REMARK 465     ILE A    40                                                      
REMARK 465     PRO A    41                                                      
REMARK 465     PRO A   329                                                      
REMARK 465     SER A   330                                                      
REMARK 465     SER A   331                                                      
REMARK 465     LEU A   332                                                      
REMARK 465     ASP A   333                                                      
REMARK 465     PRO A   334                                                      
REMARK 465     SER A   335                                                      
REMARK 465     ASN A   336                                                      
REMARK 465     ARG A   337                                                      
REMARK 465     LYS A   338                                                      
REMARK 465     PRO A   339                                                      
REMARK 465     LEU A   340                                                      
REMARK 465     THR A   341                                                      
REMARK 465     VAL A   342                                                      
REMARK 465     LEU A   343                                                      
REMARK 465     ASN A   344                                                      
REMARK 465     LYS A   345                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  42    CG   CD   OE1  OE2                                  
REMARK 470     VAL A  43    CG1  CG2                                            
REMARK 470     LEU A  44    CG   CD1  CD2                                       
REMARK 470     ARG A  48    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A  49    OG                                                  
REMARK 470     ARG A  50    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A  51    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A  74    CG   OD1  OD2                                       
REMARK 470     LYS A  76    CG   CD   CE   NZ                                   
REMARK 470     ILE A  83    CG1  CG2  CD1                                       
REMARK 470     ARG A 134    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 169    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 171    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 209    CG   CD   CE   NZ                                   
REMARK 470     LYS A 225    CG   CD   CE   NZ                                   
REMARK 470     LYS A 264    CG   CD   CE   NZ                                   
REMARK 470     LYS A 265    CG   CD   CE   NZ                                   
REMARK 470     GLU A 267    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 272    CG   CD   CE   NZ                                   
REMARK 470     ARG A 324    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 122     -159.82   -120.81                                   
REMARK 500    ARG A 136     -134.56     62.36                                   
REMARK 500    LYS A 146     -133.68     45.06                                   
REMARK 500    ARG A 175      -10.07     73.84                                   
REMARK 500    ASP A 194       75.45     55.15                                   
REMARK 500    SER A 229     -140.21   -142.32                                   
REMARK 500    GLU A 231       -7.29    -58.44                                   
REMARK 500    GLU A 303      -37.82    -31.58                                   
REMARK 500    THR A 317      -42.66    -27.75                                   
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 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  93   NE2                                                    
REMARK 620 2 CYS A 212   SG  105.0                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3TA A 1                   
DBREF  3THB A   13   345  UNP    P53350   PLK1_HUMAN      13    345             
SEQADV 3THB VAL A  210  UNP  P53350    THR   210 ENGINEERED MUTATION            
SEQRES   1 A  333  ALA PRO ALA ASP PRO GLY LYS ALA GLY VAL PRO GLY VAL          
SEQRES   2 A  333  ALA ALA PRO GLY ALA PRO ALA ALA ALA PRO PRO ALA LYS          
SEQRES   3 A  333  GLU ILE PRO GLU VAL LEU VAL ASP PRO ARG SER ARG ARG          
SEQRES   4 A  333  ARG TYR VAL ARG GLY ARG PHE LEU GLY LYS GLY GLY PHE          
SEQRES   5 A  333  ALA LYS CYS PHE GLU ILE SER ASP ALA ASP THR LYS GLU          
SEQRES   6 A  333  VAL PHE ALA GLY LYS ILE VAL PRO LYS SER LEU LEU LEU          
SEQRES   7 A  333  LYS PRO HIS GLN ARG GLU LYS MET SER MET GLU ILE SER          
SEQRES   8 A  333  ILE HIS ARG SER LEU ALA HIS GLN HIS VAL VAL GLY PHE          
SEQRES   9 A  333  HIS GLY PHE PHE GLU ASP ASN ASP PHE VAL PHE VAL VAL          
SEQRES  10 A  333  LEU GLU LEU CYS ARG ARG ARG SER LEU LEU GLU LEU HIS          
SEQRES  11 A  333  LYS ARG ARG LYS ALA LEU THR GLU PRO GLU ALA ARG TYR          
SEQRES  12 A  333  TYR LEU ARG GLN ILE VAL LEU GLY CYS GLN TYR LEU HIS          
SEQRES  13 A  333  ARG ASN ARG VAL ILE HIS ARG ASP LEU LYS LEU GLY ASN          
SEQRES  14 A  333  LEU PHE LEU ASN GLU ASP LEU GLU VAL LYS ILE GLY ASP          
SEQRES  15 A  333  PHE GLY LEU ALA THR LYS VAL GLU TYR ASP GLY GLU ARG          
SEQRES  16 A  333  LYS LYS VAL LEU CYS GLY THR PRO ASN TYR ILE ALA PRO          
SEQRES  17 A  333  GLU VAL LEU SER LYS LYS GLY HIS SER PHE GLU VAL ASP          
SEQRES  18 A  333  VAL TRP SER ILE GLY CYS ILE MET TYR THR LEU LEU VAL          
SEQRES  19 A  333  GLY LYS PRO PRO PHE GLU THR SER CYS LEU LYS GLU THR          
SEQRES  20 A  333  TYR LEU ARG ILE LYS LYS ASN GLU TYR SER ILE PRO LYS          
SEQRES  21 A  333  HIS ILE ASN PRO VAL ALA ALA SER LEU ILE GLN LYS MET          
SEQRES  22 A  333  LEU GLN THR ASP PRO THR ALA ARG PRO THR ILE ASN GLU          
SEQRES  23 A  333  LEU LEU ASN ASP GLU PHE PHE THR SER GLY TYR ILE PRO          
SEQRES  24 A  333  ALA ARG LEU PRO ILE THR CYS LEU THR ILE PRO PRO ARG          
SEQRES  25 A  333  PHE SER ILE ALA PRO SER SER LEU ASP PRO SER ASN ARG          
SEQRES  26 A  333  LYS PRO LEU THR VAL LEU ASN LYS                              
HET     ZN  A 502       1                                                       
HET    3TA  A   1      31                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     3TA 9-CHLORO-2-({5-[3-(DIMETHYLAMINO)PROPYL]-2-                      
HETNAM   2 3TA  METHYLPYRIDIN-3-YL}AMINO)-5,7-DIHYDRO-6H-PYRIMIDO[5,4-          
HETNAM   3 3TA  D][1]BENZAZEPINE-6-THIONE                                       
HETSYN     3TA MLN0905                                                          
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  3TA    C23 H25 CL N6 S                                              
HELIX    1   1 SER A   87  LEU A   89  5                                   3    
HELIX    2   2 LYS A   91  SER A  107  1                                  17    
HELIX    3   3 SER A  137  LYS A  146  1                                  10    
HELIX    4   4 THR A  149  ASN A  170  1                                  22    
HELIX    5   5 LYS A  178  GLY A  180  5                                   3    
HELIX    6   6 ALA A  219  SER A  224  1                                   6    
HELIX    7   7 PHE A  230  GLY A  247  1                                  18    
HELIX    8   8 CYS A  255  ASN A  266  1                                  12    
HELIX    9   9 ASN A  275  LEU A  286  1                                  12    
HELIX   10  10 GLU A  298  ASN A  301  5                                   4    
HELIX   11  11 ASP A  302  SER A  307  1                                   6    
HELIX   12  12 PRO A  315  THR A  320  5                                   6    
SHEET    1   A 6 VAL A  43  VAL A  45  0                                        
SHEET    2   A 6 ARG A  52  GLY A  62 -1  O  TYR A  53   N  LEU A  44           
SHEET    3   A 6 ALA A  65  ASP A  72 -1  O  CYS A  67   N  GLY A  60           
SHEET    4   A 6 VAL A  78  PRO A  85 -1  O  PHE A  79   N  ILE A  70           
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 502     1555   1555  2.04  
LINK         SG  CYS A 212                ZN    ZN A 502     1555   1555  2.40  
SITE     1 AC1  3 HIS A  93  CYS A 212  CYS A 255                               
SITE     1 AC2 12 LEU A  59  GLY A  60  LYS A  61  ALA A  80                    
SITE     2 AC2 12 GLU A 131  LEU A 132  CYS A 133  ARG A 136                    
SITE     3 AC2 12 GLU A 140  GLY A 180  PHE A 183  ASP A 194                    
CRYST1   67.668   67.668  154.684  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      0.014778  0.008532  0.000000        0.00000                         
SCALE2      0.000000  0.017064  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006465        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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