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Entry: 3KB7
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HEADER    TRANSFERASE                             20-OCT-09   3KB7              
TITLE     CRYSTAL STRUCTURE OF POLO-LIKE KINASE 1 IN COMPLEX WITH A             
TITLE    2 PYRAZOLOQUINAZOLINE INHIBITOR                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PLK1;                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: KINASE DOMAIN;                                             
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;                                                          
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: H5;                                     
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    PROTEIN KINASE, ATP-BINDING, CELL CYCLE, CELL DIVISION, KINASE,       
KEYWDS   2 MITOSIS, NUCLEOTIDE-BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM,  
KEYWDS   3 SERINE/THREONINE-PROTEIN KINASE, TRANSFERASE                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.T.BOSSI,J.A.BERTRAND                                                
REVDAT   1   19-MAY-10 3KB7    0                                                
JRNL        AUTH   I.BERIA,D.BALLINARI,J.A.BERTRAND,D.BORGHI,R.T.BOSSI,         
JRNL        AUTH 2 M.G.BRASCA,P.CAPPELLA,M.CARUSO,W.CECCARELLI,A.CIAVOLELLA,    
JRNL        AUTH 3 C.CRISTIANI,V.CROCI,A.DE PONTI,G.FACHIN,R.D.FERGUSON,        
JRNL        AUTH 4 J.LANSEN,J.K.MOLL,E.PESENTI,H.POSTERI,R.PEREGO,M.ROCCHETTI,  
JRNL        AUTH 5 P.STORICI,D.VOLPI,B.VALSASINA                                
JRNL        TITL   IDENTIFICATION OF 4,5-DIHYDRO-1H-PYRAZOLO[4,3-H]QUINAZOLINE  
JRNL        TITL 2 DERIVATIVES AS A NEW CLASS OF ORALLY AND SELECTIVE           
JRNL        TITL 3 POLO-LIKE KINASE 1 INHIBITORS                                
JRNL        REF    J.MED.CHEM.                   V.  53  3532 2010              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   20397705                                                     
JRNL        DOI    10.1021/JM901713N                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 58.32                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 14616                          
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) : 0.212                           
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.303                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 736                             
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) : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 980                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2680                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 57                           
REMARK   3   BIN FREE R VALUE                    : 0.3790                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2353                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 44                                      
REMARK   3   SOLVENT ATOMS            : 75                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.81                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.70000                                              
REMARK   3    B22 (A**2) : 1.70000                                              
REMARK   3    B33 (A**2) : -2.55000                                             
REMARK   3    B12 (A**2) : 0.85000                                              
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): 0.416         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.326         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.136         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.905         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.929                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.839                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2451 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3307 ; 1.657 ; 2.004       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   287 ; 6.363 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   108 ;33.736 ;22.500       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   441 ;17.444 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;17.489 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   362 ; 0.118 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1828 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1137 ; 0.234 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1647 ; 0.320 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   125 ; 0.165 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     2 ; 0.092 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    34 ; 0.254 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     4 ; 0.113 ; 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):  1491 ; 0.678 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2351 ; 1.173 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1079 ; 1.812 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   956 ; 2.771 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3KB7 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-OCT-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB055774.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-MAY-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-3                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.071568                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14659                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 58.328                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : 0.12100                            
REMARK 200  R SYM                      (I) : 0.12100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.3000                            
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) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58300                            
REMARK 200  R SYM FOR SHELL            (I) : 0.58300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: IN-HOUSE AVAILABLE PLK1 CRYSTAL STRUCTURE            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2M NA/K TARTRATE, 25MM ZN ACETATE,     
REMARK 280  0.1M MES, PH 6.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      102.73933            
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       51.36967            
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       51.36967            
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      102.73933            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28270 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -86.0 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 -0.500000  0.866025  0.000000      101.02800            
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000      -58.32854            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 387  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    35                                                      
REMARK 465     PRO A    36                                                      
REMARK 465     ALA A    37                                                      
REMARK 465     LYS A    38                                                      
REMARK 465     PRO A   329                                                      
REMARK 465     SER A   330                                                      
REMARK 465     SER A   331                                                      
REMARK 465     LEU A   332                                                      
REMARK 465     ASP A   333                                                      
REMARK 465     PRO A   334                                                      
REMARK 465     SER A   335                                                      
REMARK 465     ASN A   336                                                      
REMARK 465     ARG A   337                                                      
REMARK 465     LYS A   338                                                      
REMARK 465     PRO A   339                                                      
REMARK 465     LEU A   340                                                      
REMARK 465     THR A   341                                                      
REMARK 465     VAL A   342                                                      
REMARK 465     LEU A   343                                                      
REMARK 465     ASN A   344                                                      
REMARK 465     LYS A   345                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A  48      -39.87     98.69                                   
REMARK 500    ARG A  50       -9.13     74.01                                   
REMARK 500    LEU A  59      -61.56    -94.26                                   
REMARK 500    ASP A  74      -74.58    -99.59                                   
REMARK 500    LYS A  76       -5.22     74.37                                   
REMARK 500    ASP A 122     -157.12   -119.38                                   
REMARK 500    ARG A 136     -128.85     62.65                                   
REMARK 500    LYS A 146     -145.51     54.49                                   
REMARK 500    ARG A 175       -3.76     69.06                                   
REMARK 500    ASP A 194       88.77     62.15                                   
REMARK 500    TYR A 217       62.12   -101.53                                   
REMARK 500    SER A 229     -154.85   -145.66                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    NMM A 324        -22.31                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    NMM A 324        19.4      L          L   OUTSIDE RANGE           
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 346  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  93   NE2                                                    
REMARK 620 2 CYS A 212   SG  111.7                                              
REMARK 620 3 TLA A 400   O1  120.5  86.6                                        
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 071 A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 346                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TLA A 400                 
DBREF  3KB7 A   36   345  UNP    P53350   PLK1_HUMAN      36    345             
SEQADV 3KB7 GLY A   35  UNP  P53350              EXPRESSION TAG                 
SEQRES   1 A  311  GLY PRO ALA LYS GLU ILE PRO GLU VAL LEU VAL ASP PRO          
SEQRES   2 A  311  ARG SER ARG ARG ARG TYR VAL ARG GLY ARG PHE LEU GLY          
SEQRES   3 A  311  LYS GLY GLY PHE ALA LYS CYS PHE GLU ILE SER ASP ALA          
SEQRES   4 A  311  ASP THR LYS GLU VAL PHE ALA GLY LYS ILE VAL PRO LYS          
SEQRES   5 A  311  SER LEU LEU LEU LYS PRO HIS GLN ARG GLU LYS MET SER          
SEQRES   6 A  311  MET GLU ILE SER ILE HIS ARG SER LEU ALA HIS GLN HIS          
SEQRES   7 A  311  VAL VAL GLY PHE HIS GLY PHE PHE GLU ASP ASN ASP PHE          
SEQRES   8 A  311  VAL PHE VAL VAL LEU GLU LEU CYS ARG ARG ARG SER LEU          
SEQRES   9 A  311  LEU GLU LEU HIS LYS ARG ARG LYS ALA LEU THR GLU PRO          
SEQRES  10 A  311  GLU ALA ARG TYR TYR LEU ARG GLN ILE VAL LEU GLY CYS          
SEQRES  11 A  311  GLN TYR LEU HIS ARG ASN ARG VAL ILE HIS ARG ASP LEU          
SEQRES  12 A  311  LYS LEU GLY ASN LEU PHE LEU ASN GLU ASP LEU GLU VAL          
SEQRES  13 A  311  LYS ILE GLY ASP PHE GLY LEU ALA THR LYS VAL GLU TYR          
SEQRES  14 A  311  ASP GLY GLU ARG LYS LYS THR LEU CYS GLY THR PRO ASN          
SEQRES  15 A  311  TYR ILE ALA PRO GLU VAL LEU SER LYS LYS GLY HIS SER          
SEQRES  16 A  311  PHE GLU VAL ASP VAL TRP SER ILE GLY CYS ILE MET TYR          
SEQRES  17 A  311  THR LEU LEU VAL GLY LYS PRO PRO PHE GLU THR SER CYS          
SEQRES  18 A  311  LEU LYS GLU THR TYR LEU ARG ILE LYS LYS ASN GLU TYR          
SEQRES  19 A  311  SER ILE PRO LYS HIS ILE ASN PRO VAL ALA ALA SER LEU          
SEQRES  20 A  311  ILE GLN LYS MET LEU GLN THR ASP PRO THR ALA ARG PRO          
SEQRES  21 A  311  THR ILE ASN GLU LEU LEU ASN ASP GLU PHE PHE THR SER          
SEQRES  22 A  311  GLY TYR ILE PRO ALA ARG LEU PRO ILE THR CYS LEU THR          
SEQRES  23 A  311  ILE PRO PRO NMM PHE SER ILE ALA PRO SER SER LEU ASP          
SEQRES  24 A  311  PRO SER ASN ARG LYS PRO LEU THR VAL LEU ASN LYS              
MODRES 3KB7 NMM A  324  ARG                                                     
HET    NMM  A 324      12                                                       
HET    071  A   1      33                                                       
HET     ZN  A 346       1                                                       
HET    TLA  A 400      10                                                       
HETNAM     NMM (2S)-2-AMINO-5-[(N-METHYLCARBAMIMIDOYL)AMINO]PENTANOIC           
HETNAM   2 NMM  ACID                                                            
HETNAM     071 8-{[2-METHOXY-5-(4-METHYLPIPERAZIN-1-YL)PHENYL]AMINO}-           
HETNAM   2 071  1-METHYL-4,5-DIHYDRO-1H-PYRAZOLO[4,3-H]QUINAZOLINE-3-           
HETNAM   3 071  CARBOXAMIDE                                                     
HETNAM      ZN ZINC ION                                                         
HETNAM     TLA L(+)-TARTARIC ACID                                               
HETSYN     NMM L-NMMA                                                           
FORMUL   1  NMM    C7 H16 N4 O2                                                 
FORMUL   2  071    C23 H28 N8 O2                                                
FORMUL   3   ZN    ZN 2+                                                        
FORMUL   4  TLA    C4 H6 O6                                                     
FORMUL   5  HOH   *75(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 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  LEU A  59           
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  LEU A 130 -1  O  LEU A 130   N  ALA A  80           
SHEET    6   A 6 PHE A 116  GLU A 121 -1  N  PHE A 120   O  PHE A 127           
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         C   PRO A 323                 N   NMM A 324     1555   1555  1.32  
LINK         C   NMM A 324                 N   PHE A 325     1555   1555  1.30  
LINK         NE2 HIS A  93                ZN    ZN A 346     1555   1555  1.99  
LINK         SG  CYS A 212                ZN    ZN A 346     1555   1555  2.49  
LINK        ZN    ZN A 346                 O1  TLA A 400     1555   1555  1.91  
SITE     1 AC1 15 HOH A   3  LEU A  59  CYS A  67  ALA A  80                    
SITE     2 AC1 15 LYS A  82  LEU A 130  GLU A 131  CYS A 133                    
SITE     3 AC1 15 ARG A 134  ARG A 136  SER A 137  GLU A 140                    
SITE     4 AC1 15 GLY A 180  PHE A 183  ASP A 194                               
SITE     1 AC2  4 HIS A  93  CYS A 212  CYS A 255  TLA A 400                    
SITE     1 AC3  8 HIS A  93  GLN A  94  LYS A  97  CYS A 212                    
SITE     2 AC3  8 SER A 254  CYS A 255  LEU A 256   ZN A 346                    
CRYST1   67.352   67.352  154.109  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      0.014847  0.008572  0.000000        0.00000                         
SCALE2      0.000000  0.017144  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006489        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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