GenomeNet

Database: PDB
Entry: 3FC2
LinkDB: 3FC2
Original site: 3FC2 
HEADER    TRANSFERASE                             21-NOV-08   3FC2              
TITLE     PLK1 IN COMPLEX WITH BI6727                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PLK1;                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDIES 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;                                                     
COMPND   9 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;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: SF21                                    
KEYWDS    PROTEIN KINASE, ATP-BINDING, CELL CYCLE, CELL DIVISION, KINASE,       
KEYWDS   2 MITOSIS, NUCLEOTIDE-BINDING, NUCLEUS, PHOSPHOPROTEIN,                
KEYWDS   3 SERINE/THREONINE-PROTEIN KINASE, TRANSFERASE                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.BADER                                                               
REVDAT   3   13-JUL-11 3FC2    1       VERSN                                    
REVDAT   2   19-JAN-10 3FC2    1       REMARK                                   
REVDAT   1   12-MAY-09 3FC2    0                                                
JRNL        AUTH   D.RUDOLPH,M.STEEGMAIER,M.HOFFMANN,M.GRAUERT,A.BAUM,J.QUANT,  
JRNL        AUTH 2 C.HASLINGER,P.GARIN-CHESA,G.R.ADOLF                          
JRNL        TITL   BI 6727, A POLO-LIKE KINASE INHIBITOR WITH IMPROVED          
JRNL        TITL 2 PHARMACOKINETIC PROFILE AND BROAD ANTITUMOR ACTIVITY.        
JRNL        REF    CLIN.CANCER RES.              V.  15  3094 2009              
JRNL        REFN                   ISSN 1078-0432                               
JRNL        PMID   19383823                                                     
JRNL        DOI    10.1158/1078-0432.CCR-08-2445                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 2.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.18                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 14942                          
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) : 0.184                           
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 374                             
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) : 2.45                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.51                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1050                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2410                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 27                           
REMARK   3   BIN FREE R VALUE                    : 0.2740                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2373                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 83                                      
REMARK   3   SOLVENT ATOMS            : 74                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 42.73                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.59                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.35000                                              
REMARK   3    B22 (A**2) : 2.35000                                              
REMARK   3    B33 (A**2) : -3.52000                                             
REMARK   3    B12 (A**2) : 1.17000                                              
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): 0.342         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.233         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.183         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.676        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2512 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2379 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3379 ; 1.222 ; 2.006       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5529 ; 0.767 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   294 ; 5.862 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   110 ;34.442 ;22.455       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   450 ;15.825 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;18.317 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   368 ; 0.072 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2694 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   522 ; 0.003 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   490 ; 0.201 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2347 ; 0.189 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1200 ; 0.180 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1365 ; 0.084 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    90 ; 0.135 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     1 ; 0.031 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):     8 ; 0.083 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    38 ; 0.227 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    10 ; 0.194 ; 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):  1915 ; 1.850 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   589 ; 0.385 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2398 ; 2.353 ; 3.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1225 ; 3.779 ; 4.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   981 ; 5.285 ; 6.000       
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    37        A   104                          
REMARK   3    ORIGIN FOR THE GROUP (A):  48.5880 -18.7960  19.9080              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0099 T22:   0.2366                                     
REMARK   3      T33:   0.0562 T12:   0.0065                                     
REMARK   3      T13:  -0.0209 T23:   0.0765                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4448 L22:   0.7330                                     
REMARK   3      L33:   6.1771 L12:  -0.1798                                     
REMARK   3      L13:  -1.4854 L23:  -1.3792                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0443 S12:  -0.1322 S13:   0.0714                       
REMARK   3      S21:   0.0591 S22:  -0.2011 S23:  -0.2136                       
REMARK   3      S31:   0.0773 S32:   1.2351 S33:   0.2453                       
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   105        A   151                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.5010 -14.7350   8.6120              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1357 T22:  -0.0880                                     
REMARK   3      T33:  -0.1181 T12:   0.0007                                     
REMARK   3      T13:   0.0135 T23:  -0.0068                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0044 L22:   1.4685                                     
REMARK   3      L33:   5.7275 L12:  -0.9605                                     
REMARK   3      L13:   1.4127 L23:  -0.9955                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0088 S12:  -0.0213 S13:  -0.0339                       
REMARK   3      S21:  -0.1305 S22:  -0.1827 S23:  -0.2110                       
REMARK   3      S31:   0.1982 S32:   0.6732 S33:   0.1740                       
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   152        A   249                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.5500 -11.6170  10.6470              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1404 T22:  -0.1682                                     
REMARK   3      T33:  -0.1176 T12:  -0.0204                                     
REMARK   3      T13:  -0.0403 T23:   0.0033                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0257 L22:   2.3301                                     
REMARK   3      L33:   6.2776 L12:   0.3987                                     
REMARK   3      L13:  -0.4989 L23:  -0.2542                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0344 S12:  -0.1011 S13:   0.0085                       
REMARK   3      S21:   0.0751 S22:  -0.0806 S23:   0.1536                       
REMARK   3      S31:  -0.1099 S32:  -0.4256 S33:   0.0462                       
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   250        A   330                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.7580  -3.8820   0.6290              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0199 T22:  -0.0487                                     
REMARK   3      T33:  -0.0039 T12:   0.0426                                     
REMARK   3      T13:  -0.0533 T23:   0.0244                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1523 L22:   1.2412                                     
REMARK   3      L33:   3.9346 L12:   0.1127                                     
REMARK   3      L13:   0.4156 L23:   1.4135                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0299 S12:  -0.0530 S13:   0.2151                       
REMARK   3      S21:  -0.2671 S22:  -0.0742 S23:   0.1054                       
REMARK   3      S31:  -0.4202 S32:  -0.2698 S33:   0.0444                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3FC2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-NOV-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB050404.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14942                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.09400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.58                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.56800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP,           
REMARK 280  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      102.64600            
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       51.32300            
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       51.32300            
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      102.64600            
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: 4960 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 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       51.32300            
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    11                                                      
REMARK 465     PRO A    12                                                      
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     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    LYS A  76       -1.45     74.27                                   
REMARK 500    ASP A 122     -163.46   -119.73                                   
REMARK 500    ARG A 136     -122.39     60.79                                   
REMARK 500    LYS A 146     -136.03     49.73                                   
REMARK 500    ASP A 176       42.90   -154.93                                   
REMARK 500    ASP A 194       83.29     47.79                                   
REMARK 500    PHE A 195       30.51    -92.73                                   
REMARK 500    SER A 229     -145.30   -157.12                                   
REMARK 500    GLU A 267       79.97   -102.28                                   
REMARK 500    THR A 320      -51.33   -127.21                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C SSEQI                                                      
REMARK 615     IBI A   10                                                       
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   8  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  93   NE2                                                    
REMARK 620 2 CYS A 212   SG  118.0                                              
REMARK 620 3 ACT A   7   O   112.8  93.6                                        
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 IBI A 10                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 4                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 5                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 6                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 7                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 8                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 9                   
DBREF  3FC2 A   13   345  UNP    P53350   PLK1_HUMAN      13    345             
SEQADV 3FC2 GLY A   11  UNP  P53350              EXPRESSION TAG                 
SEQADV 3FC2 PRO A   12  UNP  P53350              EXPRESSION TAG                 
SEQADV 3FC2 VAL A  210  UNP  P53350    THR   210 ENGINEERED                     
SEQRES   1 A  335  GLY PRO ALA PRO ALA ASP PRO GLY LYS ALA GLY VAL PRO          
SEQRES   2 A  335  GLY VAL ALA ALA PRO GLY ALA PRO ALA ALA ALA PRO PRO          
SEQRES   3 A  335  ALA LYS GLU ILE PRO GLU VAL LEU VAL ASP PRO ARG SER          
SEQRES   4 A  335  ARG ARG ARG TYR VAL ARG GLY ARG PHE LEU GLY LYS GLY          
SEQRES   5 A  335  GLY PHE ALA LYS CYS PHE GLU ILE SER ASP ALA ASP THR          
SEQRES   6 A  335  LYS GLU VAL PHE ALA GLY LYS ILE VAL PRO LYS SER LEU          
SEQRES   7 A  335  LEU LEU LYS PRO HIS GLN ARG GLU LYS MET SER MET GLU          
SEQRES   8 A  335  ILE SER ILE HIS ARG SER LEU ALA HIS GLN HIS VAL VAL          
SEQRES   9 A  335  GLY PHE HIS GLY PHE PHE GLU ASP ASN ASP PHE VAL PHE          
SEQRES  10 A  335  VAL VAL LEU GLU LEU CYS ARG ARG ARG SER LEU LEU GLU          
SEQRES  11 A  335  LEU HIS LYS ARG ARG LYS ALA LEU THR GLU PRO GLU ALA          
SEQRES  12 A  335  ARG TYR TYR LEU ARG GLN ILE VAL LEU GLY CYS GLN TYR          
SEQRES  13 A  335  LEU HIS ARG ASN ARG VAL ILE HIS ARG ASP LEU LYS LEU          
SEQRES  14 A  335  GLY ASN LEU PHE LEU ASN GLU ASP LEU GLU VAL LYS ILE          
SEQRES  15 A  335  GLY ASP PHE GLY LEU ALA THR LYS VAL GLU TYR ASP GLY          
SEQRES  16 A  335  GLU ARG LYS LYS VAL LEU CYS GLY THR PRO ASN TYR ILE          
SEQRES  17 A  335  ALA PRO GLU VAL LEU SER LYS LYS GLY HIS SER PHE GLU          
SEQRES  18 A  335  VAL ASP VAL TRP SER ILE GLY CYS ILE MET TYR THR LEU          
SEQRES  19 A  335  LEU VAL GLY LYS PRO PRO PHE GLU THR SER CYS LEU LYS          
SEQRES  20 A  335  GLU THR TYR LEU ARG ILE LYS LYS ASN GLU TYR SER ILE          
SEQRES  21 A  335  PRO LYS HIS ILE ASN PRO VAL ALA ALA SER LEU ILE GLN          
SEQRES  22 A  335  LYS MET LEU GLN THR ASP PRO THR ALA ARG PRO THR ILE          
SEQRES  23 A  335  ASN GLU LEU LEU ASN ASP GLU PHE PHE THR SER GLY TYR          
SEQRES  24 A  335  ILE PRO ALA ARG LEU PRO ILE THR CYS LEU THR ILE PRO          
SEQRES  25 A  335  PRO ARG PHE SER ILE ALA PRO SER SER LEU ASP PRO SER          
SEQRES  26 A  335  ASN ARG LYS PRO LEU THR VAL LEU ASN LYS                      
HET    IBI  A  10      45                                                       
HET    EDO  A   1       4                                                       
HET    EDO  A   2       4                                                       
HET    ACT  A   3       4                                                       
HET    EDO  A   4       4                                                       
HET    PEG  A   5       7                                                       
HET    EDO  A   6       4                                                       
HET    ACT  A   7       4                                                       
HET     ZN  A   8       1                                                       
HET    GOL  A   9       6                                                       
HETNAM     IBI N-{TRANS-4-[4-(CYCLOPROPYLMETHYL)PIPERAZIN-1-                    
HETNAM   2 IBI  YL]CYCLOHEXYL}-4-{[(7R)-7-ETHYL-5-METHYL-8-(1-                  
HETNAM   3 IBI  METHYLETHYL)-6-OXO-5,6,7,8-TETRAHYDROPTERIDIN-2-                
HETNAM   4 IBI  YL]AMINO}-3-METHOXYBENZAMIDE                                    
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     ACT ACETATE ION                                                      
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM      ZN ZINC ION                                                         
HETNAM     GOL GLYCEROL                                                         
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  IBI    C34 H50 N8 O3                                                
FORMUL   3  EDO    4(C2 H6 O2)                                                  
FORMUL   5  ACT    2(C2 H3 O2 1-)                                               
FORMUL   7  PEG    C4 H10 O3                                                    
FORMUL  10   ZN    ZN 2+                                                        
FORMUL  11  GOL    C3 H8 O3                                                     
FORMUL  12  HOH   *74(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  ASN A  266  1                                  12    
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 GLU A  298  ASN A  301  5                                   4    
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  ARG A  51   N  ASP A  46           
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  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         NE2 HIS A  93                ZN    ZN A   8     1555   1555  2.03  
LINK         SG  CYS A 212                ZN    ZN A   8     1555   1555  2.20  
LINK         O   ACT A   7                ZN    ZN A   8     1555   1555  2.13  
SITE     1 AC1 16 EDO A   2  GOL A   9  ARG A  57  PHE A  58                    
SITE     2 AC1 16 LEU A  59  CYS A  67  GLU A  69  VAL A 114                    
SITE     3 AC1 16 LEU A 130  GLU A 131  CYS A 133  ARG A 134                    
SITE     4 AC1 16 ARG A 136  PHE A 183  HOH A 388  HOH A 419                    
SITE     1 AC2  2 LEU A 319  HOH A 395                                          
SITE     1 AC3  5 GOL A   9  IBI A  10  LYS A 178  GLY A 180                    
SITE     2 AC3  5 ASN A 181                                                     
SITE     1 AC4  5 PHE A  64  LYS A  82  MET A  98  GLU A 101                    
SITE     2 AC4  5 HOH A 408                                                     
SITE     1 AC5  4 HIS A 110  LEU A 162  GLN A 165  HOH A 362                    
SITE     1 AC6  5 TYR A 166  ARG A 169  ASN A 170  HOH A 358                    
SITE     2 AC6  5 HOH A 362                                                     
SITE     1 AC7  2 ASN A 216  PRO A 249                                          
SITE     1 AC8  7  ZN A   8  HIS A  93  GLN A  94  LYS A  97                    
SITE     2 AC8  7 CYS A 212  CYS A 255  LEU A 256                               
SITE     1 AC9  4 ACT A   7  HIS A  93  CYS A 212  CYS A 255                    
SITE     1 BC1  7 EDO A   2  IBI A  10  ARG A 136  GLU A 140                    
SITE     2 BC1  7 GLY A 180  PHE A 183  HOH A 418                               
CRYST1   66.616   66.616  153.969  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      0.015011  0.008667  0.000000        0.00000                         
SCALE2      0.000000  0.017334  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006495        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system