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Database: PDB
Entry: 3EOC
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HEADER    TRANSFERASE/CELL CYCLE                  26-SEP-08   3EOC              
TITLE     CDK2/CYCLINA COMPLEXED WITH A IMIDAZO TRIAZIN-2-AMINE                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELL DIVISION PROTEIN KINASE 2;                            
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: P33 PROTEIN KINASE;                                         
COMPND   5 EC: 2.7.11.22;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CYCLIN-A2;                                                 
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 FRAGMENT: PROTEOLYTIC FRAGMENT: RESIDUES 173-432;                    
COMPND  11 SYNONYM: CYCLIN-A;                                                   
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_TAXID: 9606;                                                
SOURCE   4 GENE: CDK2;                                                          
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PFASTBAC;                                 
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 GENE: CCNA2, CCN1, CCNA;                                             
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  14 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  15 EXPRESSION_SYSTEM_PLASMID: PET                                       
KEYWDS    CDK, CYCLIN, ATP-BINDING, CELL CYCLE, CELL DIVISION, KINASE, MITOSIS, 
KEYWDS   2 NUCLEOTIDE-BINDING, PHOSPHOPROTEIN, SERINE/THREONINE-PROTEIN KINASE, 
KEYWDS   3 TRANSFERASE, NUCLEUS, TRANSFERASE-CELL CYCLE COMPLEX                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.CHEUNG,K.KUNTZ,M.POBANZ,J.SALOVICH,B.WILSON,W.ANDREWS,L.SHEWCHUK,   
AUTHOR   2 A.EPPERLY,D.HASSLER,M.LEESNITZER,J.SMITH,G.SMITH,T.LANSING,R.MOOK    
REVDAT   5   25-OCT-17 3EOC    1       REMARK                                   
REVDAT   4   13-JUL-11 3EOC    1       VERSN                                    
REVDAT   3   24-FEB-09 3EOC    1       VERSN                                    
REVDAT   2   25-NOV-08 3EOC    1       JRNL                                     
REVDAT   1   04-NOV-08 3EOC    0                                                
JRNL        AUTH   M.CHEUNG,K.W.KUNTZ,M.POBANZ,J.M.SALOVICH,B.J.WILSON,         
JRNL        AUTH 2 C.W.ANDREWS,L.M.SHEWCHUK,A.H.EPPERLY,D.F.HASSLER,            
JRNL        AUTH 3 M.A.LEESNITZER,J.L.SMITH,G.K.SMITH,T.J.LANSING,R.A.MOOK      
JRNL        TITL   IMIDAZO[5,1-F][1,2,4]TRIAZIN-2-AMINES AS NOVEL INHIBITORS OF 
JRNL        TITL 2 POLO-LIKE KINASE 1.                                          
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  18  6214 2008              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   18929484                                                     
JRNL        DOI    10.1016/J.BMCL.2008.09.100                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 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) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 33305                          
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) : 0.216                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.238                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1737                            
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) : 3.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.28                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2443                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.26                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3480                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 109                          
REMARK   3   BIN FREE R VALUE                    : 0.3980                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8714                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 58                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 93.24                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.32000                                              
REMARK   3    B22 (A**2) : 2.32000                                              
REMARK   3    B33 (A**2) : -3.48000                                             
REMARK   3    B12 (A**2) : 1.16000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.400         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.340         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 47.092        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.926                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8994 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12224 ; 1.036 ; 1.987       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1096 ; 4.742 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   361 ;39.282 ;24.044       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1552 ;15.124 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    38 ;15.923 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1400 ; 0.069 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6752 ; 0.002 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4061 ; 0.184 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  6165 ; 0.301 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   201 ; 0.114 ; 0.200       
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):    44 ; 0.200 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.097 ; 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):  5656 ; 0.191 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8943 ; 0.354 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3789 ; 0.404 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3281 ; 0.696 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 4                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : B D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B    180       B     430      4                      
REMARK   3           1     D    180       D     430      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   1995 ;  0.26 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   1995 ;  0.14 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A      80      4                      
REMARK   3           1     C      1       C      80      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    A    (A):    579 ;  0.22 ;  0.50           
REMARK   3   MEDIUM THERMAL     2    A (A**2):    579 ;  0.14 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : A C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     83       A     295      4                      
REMARK   3           1     C     83       C     295      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  3    A    (A):   1677 ;  0.23 ;  0.50           
REMARK   3   MEDIUM THERMAL     3    A (A**2):   1677 ;  0.13 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : A C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A       1      1                      
REMARK   3           1     C      1       C       1      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   4    A    (A):     29 ;  0.01 ;  0.05           
REMARK   3   TIGHT THERMAL      4    A (A**2):     29 ;  2.99 ;  0.50           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A    82                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.9615  84.1165  34.1713              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0685 T22:  -0.2160                                     
REMARK   3      T33:  -0.2628 T12:   0.1099                                     
REMARK   3      T13:   0.0876 T23:  -0.0307                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1650 L22:   7.4189                                     
REMARK   3      L33:   5.2076 L12:  -0.3130                                     
REMARK   3      L13:  -2.4588 L23:   2.9225                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0977 S12:   0.5109 S13:  -0.2694                       
REMARK   3      S21:  -0.2996 S22:  -0.3395 S23:   1.0484                       
REMARK   3      S31:   0.0435 S32:  -0.7215 S33:   0.4372                       
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 :   C     1        C    82                          
REMARK   3    ORIGIN FOR THE GROUP (A): -15.2139  63.0771  51.5066              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0512 T22:  -0.0857                                     
REMARK   3      T33:   0.1742 T12:  -0.1894                                     
REMARK   3      T13:   0.4065 T23:  -0.2000                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9567 L22:   6.0087                                     
REMARK   3      L33:   8.3777 L12:   0.3642                                     
REMARK   3      L13:  -0.0362 L23:   3.8378                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4237 S12:   0.0538 S13:  -0.2369                       
REMARK   3      S21:  -0.2185 S22:  -0.3648 S23:   1.0858                       
REMARK   3      S31:  -0.1267 S32:  -0.9455 S33:   0.7886                       
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    83        A   298                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.8253  91.2717  19.6230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1327 T22:  -0.2313                                     
REMARK   3      T33:  -0.3614 T12:  -0.0049                                     
REMARK   3      T13:   0.1680 T23:   0.0022                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9700 L22:   5.0127                                     
REMARK   3      L33:   4.0562 L12:  -0.3414                                     
REMARK   3      L13:  -0.9314 L23:  -0.7403                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0677 S12:   0.1357 S13:   0.1049                       
REMARK   3      S21:  -0.5685 S22:  -0.0533 S23:  -0.5574                       
REMARK   3      S31:  -0.0786 S32:   0.1869 S33:   0.1210                       
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 :   C    83        C   296                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.5514  50.9616  75.8997              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2408 T22:  -0.1671                                     
REMARK   3      T33:   0.2048 T12:  -0.1061                                     
REMARK   3      T13:   0.3546 T23:   0.1734                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5560 L22:   3.0080                                     
REMARK   3      L33:   5.9766 L12:   0.5915                                     
REMARK   3      L13:  -1.1909 L23:  -0.3955                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0357 S12:  -0.6311 S13:  -0.8185                       
REMARK   3      S21:  -0.1983 S22:  -0.1947 S23:  -0.4210                       
REMARK   3      S31:   0.3953 S32:  -0.2319 S33:   0.2304                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   176        B   432                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.0325  56.5259  29.4574              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0340 T22:  -0.3240                                     
REMARK   3      T33:  -0.3050 T12:   0.0619                                     
REMARK   3      T13:   0.3144 T23:  -0.0482                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8373 L22:   2.7258                                     
REMARK   3      L33:   2.8969 L12:  -0.6352                                     
REMARK   3      L13:  -0.5220 L23:   0.9673                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3932 S12:   0.2447 S13:  -0.3949                       
REMARK   3      S21:   0.0878 S22:   0.0241 S23:   0.0898                       
REMARK   3      S31:   0.4303 S32:   0.0444 S33:   0.3691                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   176        D   432                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.3106  83.7157  69.4855              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3067 T22:  -0.2855                                     
REMARK   3      T33:  -0.1473 T12:  -0.0607                                     
REMARK   3      T13:   0.2128 T23:   0.0314                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5886 L22:   2.5252                                     
REMARK   3      L33:   4.7218 L12:  -0.4286                                     
REMARK   3      L13:   1.0918 L23:   0.6752                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2375 S12:  -0.2779 S13:  -0.3482                       
REMARK   3      S21:   0.0971 S22:  -0.0872 S23:  -0.3690                       
REMARK   3      S31:   0.0154 S32:   0.0419 S33:   0.3247                       
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3EOC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-OCT-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000049571.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-JAN-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 6.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU300                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54178                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33305                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.61000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1FVV                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.04                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M SODIUM ACETATE, 100 MM SODIUM      
REMARK 280  CACODYLATE PH 6.7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE       
REMARK 280  277K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62 2 2                         
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   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z+2/3                                            
REMARK 290       6555   X-Y,X,Z+1/3                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+2/3                                            
REMARK 290      11555   -X+Y,Y,-Z                                               
REMARK 290      12555   X,X-Y,-Z+1/3                                            
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      142.45800            
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       71.22900            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      142.45800            
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       71.22900            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      142.45800            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       71.22900            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      142.45800            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       71.22900            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2810 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23590 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.9 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2870 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23240 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.8 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP A    38                                                      
REMARK 465     THR A    39                                                      
REMARK 465     GLU A    40                                                      
REMARK 465     ASN B   173                                                      
REMARK 465     GLU B   174                                                      
REMARK 465     VAL B   175                                                      
REMARK 465     ASP C    38                                                      
REMARK 465     THR C    39                                                      
REMARK 465     GLU C    40                                                      
REMARK 465     ARG C   297                                                      
REMARK 465     LEU C   298                                                      
REMARK 465     ASN D   173                                                      
REMARK 465     GLU D   174                                                      
REMARK 465     VAL D   175                                                      
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     GLN A   5    CG   CD   OE1  NE2                                  
REMARK 470     GLU A  12    CG   CD   OE1  OE2                                  
REMARK 470     TYR A  15    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG A  36    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A  74    CG   OD1  ND2                                       
REMARK 470     ARG A 157    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR A 159    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     HIS A 161    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A 162    CG   CD   OE1  OE2                                  
REMARK 470     VAL A 163    CG1  CG2                                            
REMARK 470     ARG A 200    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 298    CG   CD1  CD2                                       
REMARK 470     ASP B 177    CG   OD1  OD2                                       
REMARK 470     TYR B 178    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     TYR B 271    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN B 323    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 378    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C   2    CG   CD   OE1  OE2                                  
REMARK 470     GLU C  12    CG   CD   OE1  OE2                                  
REMARK 470     TYR C  15    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG C  36    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS C  71    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU C  73    CG   CD   OE1  OE2                                  
REMARK 470     TYR C 159    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     HIS C 161    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU C 162    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 200    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS C 295    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP D 177    CG   OD1  OD2                                       
REMARK 470     TYR D 178    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS D 196    CG   CD   CE   NZ                                   
REMARK 470     SER D 247    OG                                                  
REMARK 470     ASP D 283    CG   OD1  OD2                                       
REMARK 470     ASP D 284    CG   OD1  OD2                                       
REMARK 470     ARG D 378    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    LYS C 242   CD    LYS C 242   CE      0.320                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  14      -83.78     53.88                                   
REMARK 500    THR A  72     -161.05   -127.58                                   
REMARK 500    ALA A  95      -52.60    -28.48                                   
REMARK 500    ARG A 122       36.81     39.33                                   
REMARK 500    ARG A 126       -2.90     74.20                                   
REMARK 500    ASP A 127       51.77   -148.78                                   
REMARK 500    ASP A 145       88.40     46.72                                   
REMARK 500    PHE A 152       47.16   -109.80                                   
REMARK 500    SER A 239       20.81    -77.87                                   
REMARK 500    THR A 290     -164.65   -123.44                                   
REMARK 500    CYS B 193       32.84    -79.13                                   
REMARK 500    PHE B 304        3.33     56.00                                   
REMARK 500    ALA B 307       49.71    -72.08                                   
REMARK 500    LEU B 320        6.08    -67.43                                   
REMARK 500    THR C  14      -84.41     60.00                                   
REMARK 500    THR C  72     -166.08   -103.87                                   
REMARK 500    ARG C 126       -5.56     74.56                                   
REMARK 500    ASP C 127       45.30   -141.54                                   
REMARK 500    ASP C 145       76.83     57.27                                   
REMARK 500    PHE C 146       37.28    -94.67                                   
REMARK 500    ARG C 199      -39.86     77.30                                   
REMARK 500    SER C 249        2.90    -69.67                                   
REMARK 500    ASP C 256     -169.14    -73.85                                   
REMARK 500    THR C 290     -168.27   -126.39                                   
REMARK 500    TRP D 372      107.77    -48.91                                   
REMARK 500    HIS D 419       19.75     50.22                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T2A A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T2A C 501                 
DBREF  3EOC A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  3EOC B  173   432  UNP    P20248   CCNA2_HUMAN    173    432             
DBREF  3EOC C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  3EOC D  173   432  UNP    P20248   CCNA2_HUMAN    173    432             
SEQRES   1 A  298  MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU GLY          
SEQRES   2 A  298  THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU THR          
SEQRES   3 A  298  GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP THR          
SEQRES   4 A  298  GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE          
SEQRES   5 A  298  SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL LYS          
SEQRES   6 A  298  LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR LEU          
SEQRES   7 A  298  VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE MET          
SEQRES   8 A  298  ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU ILE          
SEQRES   9 A  298  LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA PHE          
SEQRES  10 A  298  CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  11 A  298  GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS LEU          
SEQRES  12 A  298  ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO VAL          
SEQRES  13 A  298  ARG THR TYR THR HIS GLU VAL VAL THR LEU TRP TYR ARG          
SEQRES  14 A  298  ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER THR          
SEQRES  15 A  298  ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA GLU          
SEQRES  16 A  298  MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER GLU          
SEQRES  17 A  298  ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY THR          
SEQRES  18 A  298  PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET PRO          
SEQRES  19 A  298  ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN ASP          
SEQRES  20 A  298  PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY ARG          
SEQRES  21 A  298  SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN LYS          
SEQRES  22 A  298  ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE PHE          
SEQRES  23 A  298  GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU              
SEQRES   1 B  260  ASN GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR          
SEQRES   2 B  260  LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY          
SEQRES   3 B  260  TYR MET LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG          
SEQRES   4 B  260  ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU          
SEQRES   5 B  260  TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN          
SEQRES   6 B  260  TYR ILE ASP ARG PHE LEU SER SER MET SER VAL LEU ARG          
SEQRES   7 B  260  GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU          
SEQRES   8 B  260  ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA          
SEQRES   9 B  260  GLU PHE VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS          
SEQRES  10 B  260  GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU          
SEQRES  11 B  260  THR PHE ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU          
SEQRES  12 B  260  THR GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS          
SEQRES  13 B  260  VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU          
SEQRES  14 B  260  ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL          
SEQRES  15 B  260  ILE ALA GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL          
SEQRES  16 B  260  THR GLY GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR          
SEQRES  17 B  260  GLY TYR THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP          
SEQRES  18 B  260  LEU HIS GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN          
SEQRES  19 B  260  GLN SER ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS          
SEQRES  20 B  260  GLY VAL SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU          
SEQRES   1 C  298  MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU GLY          
SEQRES   2 C  298  THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU THR          
SEQRES   3 C  298  GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP THR          
SEQRES   4 C  298  GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE          
SEQRES   5 C  298  SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL LYS          
SEQRES   6 C  298  LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR LEU          
SEQRES   7 C  298  VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE MET          
SEQRES   8 C  298  ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU ILE          
SEQRES   9 C  298  LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA PHE          
SEQRES  10 C  298  CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  11 C  298  GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS LEU          
SEQRES  12 C  298  ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO VAL          
SEQRES  13 C  298  ARG THR TYR THR HIS GLU VAL VAL THR LEU TRP TYR ARG          
SEQRES  14 C  298  ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER THR          
SEQRES  15 C  298  ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA GLU          
SEQRES  16 C  298  MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER GLU          
SEQRES  17 C  298  ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY THR          
SEQRES  18 C  298  PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET PRO          
SEQRES  19 C  298  ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN ASP          
SEQRES  20 C  298  PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY ARG          
SEQRES  21 C  298  SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN LYS          
SEQRES  22 C  298  ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE PHE          
SEQRES  23 C  298  GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU              
SEQRES   1 D  260  ASN GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR          
SEQRES   2 D  260  LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY          
SEQRES   3 D  260  TYR MET LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG          
SEQRES   4 D  260  ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU          
SEQRES   5 D  260  TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN          
SEQRES   6 D  260  TYR ILE ASP ARG PHE LEU SER SER MET SER VAL LEU ARG          
SEQRES   7 D  260  GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU          
SEQRES   8 D  260  ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA          
SEQRES   9 D  260  GLU PHE VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS          
SEQRES  10 D  260  GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU          
SEQRES  11 D  260  THR PHE ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU          
SEQRES  12 D  260  THR GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS          
SEQRES  13 D  260  VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU          
SEQRES  14 D  260  ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL          
SEQRES  15 D  260  ILE ALA GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL          
SEQRES  16 D  260  THR GLY GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR          
SEQRES  17 D  260  GLY TYR THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP          
SEQRES  18 D  260  LEU HIS GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN          
SEQRES  19 D  260  GLN SER ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS          
SEQRES  20 D  260  GLY VAL SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU          
HET    T2A  A 501      29                                                       
HET    T2A  C 501      29                                                       
HETNAM     T2A 5-METHYL-7-PHENYL-N-(3,4,5-TRIMETHOXYPHENYL)IMIDAZO[5,           
HETNAM   2 T2A  1-F][1,2,4]TRIAZIN-2-AMINE                                      
FORMUL   5  T2A    2(C21 H21 N5 O3)                                             
HELIX    1   1 PRO A   45  LYS A   56  1                                  12    
HELIX    2   2 LEU A   87  ALA A   95  1                                   9    
HELIX    3   3 PRO A  100  SER A  120  1                                  21    
HELIX    4   4 ALA A  170  LEU A  175  1                                   6    
HELIX    5   5 SER A  181  ARG A  199  1                                  19    
HELIX    6   6 SER A  207  GLY A  220  1                                  14    
HELIX    7   7 GLY A  229  MET A  233  5                                   5    
HELIX    8   8 ASP A  247  VAL A  252  1                                   6    
HELIX    9   9 ASP A  256  LEU A  267  1                                  12    
HELIX   10  10 SER A  276  ALA A  282  1                                   7    
HELIX   11  11 HIS A  283  GLN A  287  5                                   5    
HELIX   12  12 TYR B  178  CYS B  193  1                                  16    
HELIX   13  13 TYR B  199  GLN B  203  5                                   5    
HELIX   14  14 THR B  207  TYR B  225  1                                  19    
HELIX   15  15 GLN B  228  MET B  246  1                                  19    
HELIX   16  16 LEU B  249  GLU B  269  1                                  21    
HELIX   17  17 GLU B  274  ILE B  281  1                                   8    
HELIX   18  18 THR B  287  THR B  303  1                                  17    
HELIX   19  19 THR B  310  LEU B  320  1                                  11    
HELIX   20  20 ASN B  326  SER B  340  1                                  15    
HELIX   21  21 ASP B  343  LEU B  348  1                                   6    
HELIX   22  22 LEU B  351  THR B  368  1                                  18    
HELIX   23  23 PRO B  373  GLY B  381  1                                   9    
HELIX   24  24 LEU B  387  ALA B  401  1                                  15    
HELIX   25  25 PRO B  402  HIS B  404  5                                   3    
HELIX   26  26 GLN B  407  LYS B  414  1                                   8    
HELIX   27  27 ASN B  415  HIS B  419  5                                   5    
HELIX   28  28 GLY B  420  LEU B  424  5                                   5    
HELIX   29  29 PRO C   45  LYS C   56  1                                  12    
HELIX   30  30 LEU C   87  ALA C   93  1                                   7    
HELIX   31  31 PRO C  100  HIS C  121  1                                  22    
HELIX   32  32 ALA C  170  LEU C  175  1                                   6    
HELIX   33  33 THR C  182  ARG C  199  1                                  18    
HELIX   34  34 SER C  207  GLY C  220  1                                  14    
HELIX   35  35 GLY C  229  MET C  233  5                                   5    
HELIX   36  36 ASP C  247  VAL C  252  1                                   6    
HELIX   37  37 ASP C  256  LEU C  267  1                                  12    
HELIX   38  38 ASP C  270  ARG C  274  5                                   5    
HELIX   39  39 SER C  276  ALA C  282  1                                   7    
HELIX   40  40 HIS C  283  GLN C  287  5                                   5    
HELIX   41  41 TYR D  178  CYS D  193  1                                  16    
HELIX   42  42 THR D  207  TYR D  225  1                                  19    
HELIX   43  43 GLN D  228  MET D  246  1                                  19    
HELIX   44  44 LEU D  249  GLU D  269  1                                  21    
HELIX   45  45 GLU D  274  ILE D  281  1                                   8    
HELIX   46  46 THR D  287  LEU D  302  1                                  16    
HELIX   47  47 THR D  310  PHE D  319  1                                  10    
HELIX   48  48 LEU D  320  GLN D  322  5                                   3    
HELIX   49  49 ASN D  326  SER D  340  1                                  15    
HELIX   50  50 ASP D  343  LEU D  348  1                                   6    
HELIX   51  51 LEU D  351  THR D  368  1                                  18    
HELIX   52  52 PRO D  373  GLY D  381  1                                   9    
HELIX   53  53 THR D  383  LYS D  400  1                                  18    
HELIX   54  54 GLN D  407  TYR D  413  1                                   7    
HELIX   55  55 LYS D  414  HIS D  419  5                                   6    
HELIX   56  56 GLY D  420  LEU D  424  5                                   5    
SHEET    1   A 5 PHE A   4  GLY A  13  0                                        
SHEET    2   A 5 GLY A  16  ASN A  23 -1  O  LYS A  20   N  GLU A   8           
SHEET    3   A 5 VAL A  29  ARG A  36 -1  O  VAL A  30   N  ALA A  21           
SHEET    4   A 5 LYS A  75  GLU A  81 -1  O  PHE A  80   N  ALA A  31           
SHEET    5   A 5 LEU A  66  HIS A  71 -1  N  ASP A  68   O  VAL A  79           
SHEET    1   B 3 GLN A  85  ASP A  86  0                                        
SHEET    2   B 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
SHEET    3   B 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
SHEET    1   C 2 VAL A 123  LEU A 124  0                                        
SHEET    2   C 2 ARG A 150  ALA A 151 -1  O  ARG A 150   N  LEU A 124           
SHEET    1   D 5 PHE C   4  GLY C  13  0                                        
SHEET    2   D 5 GLY C  16  ASN C  23 -1  O  LYS C  20   N  GLU C   8           
SHEET    3   D 5 VAL C  29  ARG C  36 -1  O  LEU C  32   N  TYR C  19           
SHEET    4   D 5 LYS C  75  GLU C  81 -1  O  PHE C  80   N  ALA C  31           
SHEET    5   D 5 LEU C  66  HIS C  71 -1  N  ASP C  68   O  VAL C  79           
SHEET    1   E 3 GLN C  85  ASP C  86  0                                        
SHEET    2   E 3 LEU C 133  ILE C 135 -1  O  ILE C 135   N  GLN C  85           
SHEET    3   E 3 ILE C 141  LEU C 143 -1  O  LYS C 142   N  LEU C 134           
SHEET    1   F 2 VAL C 123  LEU C 124  0                                        
SHEET    2   F 2 ARG C 150  ALA C 151 -1  O  ARG C 150   N  LEU C 124           
CISPEP   1 GLN B  323    PRO B  324          0        -6.36                     
CISPEP   2 ASP B  345    PRO B  346          0         4.31                     
CISPEP   3 GLN D  323    PRO D  324          0        -6.49                     
CISPEP   4 ASP D  345    PRO D  346          0         5.07                     
SITE     1 AC1 14 ILE A  10  GLY A  11  GLU A  12  VAL A  18                    
SITE     2 AC1 14 ALA A  31  PHE A  80  GLU A  81  PHE A  82                    
SITE     3 AC1 14 LEU A  83  HIS A  84  GLN A  85  ASP A  86                    
SITE     4 AC1 14 LYS A  89  LEU A 134                                          
SITE     1 AC2  9 ILE C  10  ALA C  31  VAL C  64  PHE C  80                    
SITE     2 AC2  9 GLU C  81  LEU C  83  HIS C  84  ASP C  86                    
SITE     3 AC2  9 LEU C 134                                                     
CRYST1  182.977  182.977  213.687  90.00  90.00 120.00 P 62 2 2     24          
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      0.005465  0.003155  0.000000        0.00000                         
SCALE2      0.000000  0.006311  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004680        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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