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Database: PDB
Entry: 4CFX
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Original site: 4CFX 
HEADER    CELL CYCLE                              19-NOV-13   4CFX              
TITLE     STRUCTURE-BASED DESIGN OF C8-SUBSTITUTED O6-CYCLOHEXYLMETHOXYGUANINE  
TITLE    2 CDK1 AND 2 INHIBITORS.                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN-DEPENDENT KINASE 2;                                 
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: CELL DIVISION PROTEIN KINASE 2, P33 PROTEIN KINASE;         
COMPND   5 EC: 2.7.11.22, 2.7.11.23;                                            
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: PHOSPHORYLATED ON RESIDUE T160;                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CYCLIN-A2;                                                 
COMPND  10 CHAIN: B, D;                                                         
COMPND  11 FRAGMENT: CDK-ACTIVATING FRAGMENT, RESIDUES 173-432;                 
COMPND  12 SYNONYM: CYCLIN-A;                                                   
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI B;                               
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 37762;                                      
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: B834;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PGEX-6P-1;                                 
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI B;                               
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 37762;                                      
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: B834;                                      
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_VECTOR: PET21D                                     
KEYWDS    CELL CYCLE, STRUCTURE-BASED DRUG DESIGN, CONFORMATIONAL RESTRAINT,    
KEYWDS   2 REVERSED BINDING MODE                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.CARBAIN,D.J.PATERSON,E.ANSCOMBE,A.CAMPBELL,C.CANO,A.ECHALIER,       
AUTHOR   2 J.ENDICOTT,B.T.GOLDING,K.HAGGERTY,I.R.HARDCASTLE,P.JEWSBURY,         
AUTHOR   3 D.R.NEWELL,M.E.M.NOBLE,C.ROCHE,L.Z.WANG,R.GRIFFIN                    
REVDAT   1   10-DEC-14 4CFX    0                                                
JRNL        AUTH   B.CARBAIN,D.J.PATERSON,E.ANSCOMBE,A.CAMPBELL-DEXTER,C.CANO,  
JRNL        AUTH 2 A.ECHALIER,J.ENDICOTT,B.T.GOLDING,K.HAGGERTY,I.R.HARDCASTLE, 
JRNL        AUTH 3 P.J.JEWSBURY,D.R.NEWELL,M.NOBLE,C.ROCHE,L.WANG,R.J.GRIFFIN   
JRNL        TITL   8-SUBSTITUTED O6-CYCLOHEXYLMETHYLGUANINE CDK2 INHIBITORS;    
JRNL        TITL 2 USING STRUCTURE-BASED INHIBITOR DESIGN TO OPTIMISE AN        
JRNL        TITL 3 ALTERNATIVE BINDING MODE.                                    
JRNL        REF    J.MED.CHEM.                   V.  57    56 2014              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   24304238                                                     
JRNL        DOI    10.1021/JM401555V                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,                      
REMARK   3                 STEINER,NICHOLLS,WINN,LONG,VAGIN                     
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.34                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.95                          
REMARK   3   NUMBER OF REFLECTIONS             : 18483                          
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) : 0.20750                         
REMARK   3   R VALUE            (WORKING SET) : 0.20418                         
REMARK   3   FREE R VALUE                     : 0.26929                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 976                             
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) : 3.500                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.591                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1351                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.75                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.222                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 73                           
REMARK   3   BIN FREE R VALUE                    : 0.239                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9190                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 78                                      
REMARK   3   SOLVENT ATOMS            : 88                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.289                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.01                                                
REMARK   3    B22 (A**2) : 0.68                                                 
REMARK   3    B33 (A**2) : -0.68                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
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): 0.687         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.567         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 79.454        
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.899                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.831                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9524 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  9220 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12980 ; 1.553 ; 1.984       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 21294 ; 2.431 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1169 ; 5.853 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   404 ;41.334 ;24.010       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1671 ;20.382 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    46 ;17.722 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1461 ; 0.093 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10619 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2137 ; 0.003 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4610 ; 0.190 ; 1.242       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4609 ; 0.189 ; 1.242       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5801 ; 0.333 ; 1.862       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4914 ; 0.465 ; 1.392       
REMARK   3   SIDE-CHAIN ANGLE REFINED 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 : 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     0        A   298                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.4170 -26.7230  10.3610              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0860 T22:   0.5283                                     
REMARK   3      T33:   0.0335 T12:  -0.0126                                     
REMARK   3      T13:  -0.0390 T23:   0.0210                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0053 L22:   1.2298                                     
REMARK   3      L33:   2.5363 L12:  -0.6303                                     
REMARK   3      L13:  -1.1691 L23:   0.5818                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0114 S12:  -0.2605 S13:   0.0644                       
REMARK   3      S21:   0.2380 S22:   0.0778 S23:  -0.1948                       
REMARK   3      S31:  -0.1449 S32:   0.2372 S33:  -0.0892                       
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 :   B   173        B   432                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.6760   0.1310  -2.6620              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1074 T22:   0.4835                                     
REMARK   3      T33:   0.0043 T12:   0.0088                                     
REMARK   3      T13:   0.0072 T23:   0.0032                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7066 L22:   2.6090                                     
REMARK   3      L33:   3.4343 L12:   0.3802                                     
REMARK   3      L13:  -0.1449 L23:   0.3201                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0866 S12:   0.0661 S13:   0.0208                       
REMARK   3      S21:  -0.0726 S22:   0.0722 S23:   0.0861                       
REMARK   3      S31:  -0.2988 S32:   0.0639 S33:   0.0143                       
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 :   C     0        C   298                          
REMARK   3    ORIGIN FOR THE GROUP (A): -47.5350  12.5650  33.6150              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4057 T22:   0.6780                                     
REMARK   3      T33:   0.2047 T12:   0.0422                                     
REMARK   3      T13:  -0.0256 T23:  -0.1498                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8662 L22:   1.8093                                     
REMARK   3      L33:   1.7163 L12:  -0.1670                                     
REMARK   3      L13:  -1.7165 L23:   0.2006                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0706 S12:  -0.1072 S13:   0.2394                       
REMARK   3      S21:  -0.0336 S22:  -0.1224 S23:   0.2901                       
REMARK   3      S31:  -0.2188 S32:  -0.1416 S33:   0.0518                       
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 :   D   173        D   432                          
REMARK   3    ORIGIN FOR THE GROUP (A): -44.6770 -20.8750  34.9390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4298 T22:   0.7736                                     
REMARK   3      T33:   0.2041 T12:  -0.1855                                     
REMARK   3      T13:   0.0699 T23:  -0.1063                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4219 L22:   2.5530                                     
REMARK   3      L33:   1.8447 L12:   0.1156                                     
REMARK   3      L13:   0.5884 L23:   0.0771                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1089 S12:  -0.1734 S13:  -0.3482                       
REMARK   3      S21:   0.0624 S22:  -0.1644 S23:   0.5729                       
REMARK   3      S31:   0.2800 S32:  -0.5637 S33:   0.0556                       
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          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   4                                                                      
REMARK   4 4CFX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-NOV-13.                  
REMARK 100 THE PDBE ID CODE IS EBI-59026.                                       
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               : DIAMOND                            
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8726                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11358                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.95                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.35                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 2.68                               
REMARK 200  R MERGE                    (I) : 0.11                               
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) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1H1S                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM AMMONIUM ACETATE, 10%              
REMARK 280  PEG-3350, 15 MM NACL, 100 MM HEPES, PH = 7.4, 10% DMSO              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
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 -1.000000  0.000000  0.000000       37.33000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       74.51500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       68.28000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       74.51500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.33000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       68.28000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24400 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.1 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3860 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.5 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 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    -4                                                      
REMARK 465     PRO A    -3                                                      
REMARK 465     LEU A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     GLY C    -4                                                      
REMARK 465     PRO C    -3                                                      
REMARK 465     LEU C    -2                                                      
REMARK 465     GLY C    -1                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HIS A    71     O    HOH A  2017              2.14            
REMARK 500   O    THR B   282     OG1  THR B   285              2.04            
REMARK 500   O    LEU C    96     NH2  ARG C   199              2.10            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
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   ATM2   ATM3                                     
REMARK 500    VAL A 164   N   -  CA  -  C   ANGL. DEV. = -16.2 DEGREES          
REMARK 500    LEU A 298   CA  -  CB  -  CG  ANGL. DEV. =  13.9 DEGREES          
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    TYR A  15       23.62    -70.49                                   
REMARK 500    ASP A  38       45.74    -91.62                                   
REMARK 500    THR A  39      -67.60    -96.19                                   
REMARK 500    THR A  41       42.84    -78.26                                   
REMARK 500    GLU A  42       40.51    -99.48                                   
REMARK 500    GLU A  73     -141.30     54.06                                   
REMARK 500    ASP A 127       47.61   -159.85                                   
REMARK 500    ASP A 145       77.85     56.34                                   
REMARK 500    ARG A 199       10.26     55.74                                   
REMARK 500    TRP A 227       85.00   -152.11                                   
REMARK 500    LEU A 296     -151.94   -118.91                                   
REMARK 500    PRO B 176       57.22   -144.77                                   
REMARK 500    LYS B 226       54.40     39.49                                   
REMARK 500    ILE B 281        5.92    -68.29                                   
REMARK 500    ASP B 283       31.64     74.00                                   
REMARK 500    GLU C  12      -73.10   -141.73                                   
REMARK 500    THR C  14      -10.74     76.14                                   
REMARK 500    THR C  39      -64.11    -93.30                                   
REMARK 500    GLU C  40       41.84   -140.47                                   
REMARK 500    ASP C 127       41.39   -155.92                                   
REMARK 500    LYS C 129      149.94   -175.65                                   
REMARK 500    ASP C 145       71.60     55.48                                   
REMARK 500    VAL C 164     -170.45     64.39                                   
REMARK 500    ARG C 199        3.08     87.90                                   
REMARK 500    PRO C 204       42.43    -69.73                                   
REMARK 500    ARG C 297       78.20     38.57                                   
REMARK 500    PRO D 176       38.30    -86.94                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    VAL A 163        45.5      L          L   OUTSIDE RANGE           
REMARK 500    VAL A 164        45.1      L          L   OUTSIDE RANGE           
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 G6T A1299                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G6T C1299                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4CFM   RELATED DB: PDB                                   
REMARK 900  STRUCTURE-BASED DESIGN OF C8-SUBSTITUTED O6-                        
REMARK 900  CYCLOHEXYLMETHOXYGUANINE CDK1 AND 2 INHIBITORS.                     
REMARK 900 RELATED ID: 4CFN   RELATED DB: PDB                                   
REMARK 900  STRUCTURE-BASED DESIGN OF C8-SUBSTITUTED O6-                        
REMARK 900  CYCLOHEXYLMETHOXYGUANINE CDK1 AND 2 INHIBITORS.                     
REMARK 900 RELATED ID: 4CFU   RELATED DB: PDB                                   
REMARK 900  STRUCTURE-BASED DESIGN OF C8-SUBSTITUTED O6-                        
REMARK 900  CYCLOHEXYLMETHOXYGUANINE CDK1 AND 2 INHIBITORS.                     
REMARK 900 RELATED ID: 4CFV   RELATED DB: PDB                                   
REMARK 900  STRUCTURE-BASED DESIGN OF C8-SUBSTITUTED O6-                        
REMARK 900  CYCLOHEXYLMETHOXYGUANINE CDK1 AND 2 INHIBITORS.                     
REMARK 900 RELATED ID: 4CFW   RELATED DB: PDB                                   
REMARK 900  STRUCTURE-BASED DESIGN OF C8-SUBSTITUTED O6-                        
REMARK 900  CYCLOHEXYLMETHOXYGUANINE CDK1 AND 2 INHIBITORS.                     
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 N-TERMINAL 3C PROTEASE SITE                                          
DBREF  4CFX A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  4CFX B  173   432  UNP    P20248   CCNA2_HUMAN    173    432             
DBREF  4CFX C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  4CFX D  173   432  UNP    P20248   CCNA2_HUMAN    173    432             
SEQADV 4CFX GLY A   -4  UNP  P24941              EXPRESSION TAG                 
SEQADV 4CFX PRO A   -3  UNP  P24941              EXPRESSION TAG                 
SEQADV 4CFX LEU A   -2  UNP  P24941              EXPRESSION TAG                 
SEQADV 4CFX GLY A   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 4CFX SER A    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 4CFX GLY C   -4  UNP  P24941              EXPRESSION TAG                 
SEQADV 4CFX PRO C   -3  UNP  P24941              EXPRESSION TAG                 
SEQADV 4CFX LEU C   -2  UNP  P24941              EXPRESSION TAG                 
SEQADV 4CFX GLY C   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 4CFX SER C    0  UNP  P24941              EXPRESSION TAG                 
SEQRES   1 A  303  GLY PRO LEU GLY SER MET GLU ASN PHE GLN LYS VAL GLU          
SEQRES   2 A  303  LYS ILE GLY GLU GLY THR TYR GLY VAL VAL TYR LYS ALA          
SEQRES   3 A  303  ARG ASN LYS LEU THR GLY GLU VAL VAL ALA LEU LYS LYS          
SEQRES   4 A  303  ILE ARG LEU ASP THR GLU THR GLU GLY VAL PRO SER THR          
SEQRES   5 A  303  ALA ILE ARG GLU ILE SER LEU LEU LYS GLU LEU ASN HIS          
SEQRES   6 A  303  PRO ASN ILE VAL LYS LEU LEU ASP VAL ILE HIS THR GLU          
SEQRES   7 A  303  ASN LYS LEU TYR LEU VAL PHE GLU PHE LEU HIS GLN ASP          
SEQRES   8 A  303  LEU LYS LYS PHE MET ASP ALA SER ALA LEU THR GLY ILE          
SEQRES   9 A  303  PRO LEU PRO LEU ILE LYS SER TYR LEU PHE GLN LEU LEU          
SEQRES  10 A  303  GLN GLY LEU ALA PHE CYS HIS SER HIS ARG VAL LEU HIS          
SEQRES  11 A  303  ARG ASP LEU LYS PRO GLN ASN LEU LEU ILE ASN THR GLU          
SEQRES  12 A  303  GLY ALA ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA          
SEQRES  13 A  303  PHE GLY VAL PRO VAL ARG THR TYR TPO HIS GLU VAL VAL          
SEQRES  14 A  303  THR LEU TRP TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS          
SEQRES  15 A  303  LYS TYR TYR SER THR ALA VAL ASP ILE TRP SER LEU GLY          
SEQRES  16 A  303  CYS ILE PHE ALA GLU MET VAL THR ARG ARG ALA LEU PHE          
SEQRES  17 A  303  PRO GLY ASP SER GLU ILE ASP GLN LEU PHE ARG ILE PHE          
SEQRES  18 A  303  ARG THR LEU GLY THR PRO ASP GLU VAL VAL TRP PRO GLY          
SEQRES  19 A  303  VAL THR SER MET PRO ASP TYR LYS PRO SER PHE PRO LYS          
SEQRES  20 A  303  TRP ALA ARG GLN ASP PHE SER LYS VAL VAL PRO PRO LEU          
SEQRES  21 A  303  ASP GLU ASP GLY ARG SER LEU LEU SER GLN MET LEU HIS          
SEQRES  22 A  303  TYR ASP PRO ASN LYS ARG ILE SER ALA LYS ALA ALA LEU          
SEQRES  23 A  303  ALA HIS PRO PHE PHE GLN ASP VAL THR LYS PRO VAL PRO          
SEQRES  24 A  303  HIS LEU ARG LEU                                              
SEQRES   1 C  303  GLY PRO LEU GLY SER MET GLU ASN PHE GLN LYS VAL GLU          
SEQRES   2 C  303  LYS ILE GLY GLU GLY THR TYR GLY VAL VAL TYR LYS ALA          
SEQRES   3 C  303  ARG ASN LYS LEU THR GLY GLU VAL VAL ALA LEU LYS LYS          
SEQRES   4 C  303  ILE ARG LEU ASP THR GLU THR GLU GLY VAL PRO SER THR          
SEQRES   5 C  303  ALA ILE ARG GLU ILE SER LEU LEU LYS GLU LEU ASN HIS          
SEQRES   6 C  303  PRO ASN ILE VAL LYS LEU LEU ASP VAL ILE HIS THR GLU          
SEQRES   7 C  303  ASN LYS LEU TYR LEU VAL PHE GLU PHE LEU HIS GLN ASP          
SEQRES   8 C  303  LEU LYS LYS PHE MET ASP ALA SER ALA LEU THR GLY ILE          
SEQRES   9 C  303  PRO LEU PRO LEU ILE LYS SER TYR LEU PHE GLN LEU LEU          
SEQRES  10 C  303  GLN GLY LEU ALA PHE CYS HIS SER HIS ARG VAL LEU HIS          
SEQRES  11 C  303  ARG ASP LEU LYS PRO GLN ASN LEU LEU ILE ASN THR GLU          
SEQRES  12 C  303  GLY ALA ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA          
SEQRES  13 C  303  PHE GLY VAL PRO VAL ARG THR TYR TPO HIS GLU VAL VAL          
SEQRES  14 C  303  THR LEU TRP TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS          
SEQRES  15 C  303  LYS TYR TYR SER THR ALA VAL ASP ILE TRP SER LEU GLY          
SEQRES  16 C  303  CYS ILE PHE ALA GLU MET VAL THR ARG ARG ALA LEU PHE          
SEQRES  17 C  303  PRO GLY ASP SER GLU ILE ASP GLN LEU PHE ARG ILE PHE          
SEQRES  18 C  303  ARG THR LEU GLY THR PRO ASP GLU VAL VAL TRP PRO GLY          
SEQRES  19 C  303  VAL THR SER MET PRO ASP TYR LYS PRO SER PHE PRO LYS          
SEQRES  20 C  303  TRP ALA ARG GLN ASP PHE SER LYS VAL VAL PRO PRO LEU          
SEQRES  21 C  303  ASP GLU ASP GLY ARG SER LEU LEU SER GLN MET LEU HIS          
SEQRES  22 C  303  TYR ASP PRO ASN LYS ARG ILE SER ALA LYS ALA ALA LEU          
SEQRES  23 C  303  ALA HIS PRO PHE PHE GLN ASP VAL THR LYS PRO VAL PRO          
SEQRES  24 C  303  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 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          
MODRES 4CFX TPO A  160  THR  PHOSPHOTHREONINE                                   
MODRES 4CFX TPO C  160  THR  PHOSPHOTHREONINE                                   
HET    TPO  A 160      11                                                       
HET    TPO  C 160      11                                                       
HET    G6T  A1299      28                                                       
HET    G6T  C1299      28                                                       
HETNAM     G6T 3-[2-AMINO-6-(CYCLOHEXYLMETHOXY)-7H-PURIN-8-                     
HETNAM   2 G6T  YL]BENZENESULFONAMIDE                                           
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   3  G6T    2(C18 H22 N6 O3 S)                                           
FORMUL   4  TPO    2(C4 H10 N O6 P)                                             
FORMUL   5  HOH   *88(H2 O)                                                     
HELIX    1   1 PRO A   45  LEU A   58  1                                  14    
HELIX    2   2 LEU A   87  SER A   94  1                                   8    
HELIX    3   3 PRO A  100  SER A  120  1                                  21    
HELIX    4   4 LYS A  129  GLN A  131  5                                   3    
HELIX    5   5 THR A  165  ARG A  169  5                                   5    
HELIX    6   6 ALA A  170  LEU A  175  1                                   6    
HELIX    7   7 THR A  182  ARG A  199  1                                  18    
HELIX    8   8 SER A  207  GLY A  220  1                                  14    
HELIX    9   9 GLY A  229  MET A  233  5                                   5    
HELIX   10  10 ASP A  247  VAL A  252  1                                   6    
HELIX   11  11 ASP A  256  LEU A  267  1                                  12    
HELIX   12  12 SER A  276  LEU A  281  1                                   6    
HELIX   13  13 ALA A  282  GLN A  287  5                                   6    
HELIX   14  14 TYR B  178  CYS B  193  1                                  16    
HELIX   15  15 GLY B  198  GLN B  203  1                                   6    
HELIX   16  16 THR B  207  TYR B  225  1                                  19    
HELIX   17  17 GLN B  228  SER B  244  1                                  17    
HELIX   18  18 LEU B  249  GLY B  251  5                                   3    
HELIX   19  19 LYS B  252  GLU B  269  1                                  18    
HELIX   20  20 GLU B  274  ILE B  281  1                                   8    
HELIX   21  21 THR B  287  LEU B  302  1                                  16    
HELIX   22  22 THR B  310  PHE B  319  1                                  10    
HELIX   23  23 LEU B  320  GLN B  322  5                                   3    
HELIX   24  24 ASN B  326  LEU B  341  1                                  16    
HELIX   25  25 ASP B  343  LEU B  348  1                                   6    
HELIX   26  26 LEU B  351  THR B  368  1                                  18    
HELIX   27  27 PRO B  373  GLY B  381  1                                   9    
HELIX   28  28 THR B  383  ALA B  401  1                                  19    
HELIX   29  29 PRO B  402  HIS B  404  5                                   3    
HELIX   30  30 GLN B  407  TYR B  413  1                                   7    
HELIX   31  31 LYS B  414  HIS B  419  5                                   6    
HELIX   32  32 GLY B  420  LEU B  424  5                                   5    
HELIX   33  33 PRO C   45  LEU C   58  1                                  14    
HELIX   34  34 LEU C   87  SER C   94  1                                   8    
HELIX   35  35 PRO C  100  HIS C  121  1                                  22    
HELIX   36  36 LYS C  129  GLN C  131  5                                   3    
HELIX   37  37 ASP C  145  ALA C  149  5                                   5    
HELIX   38  38 THR C  165  ARG C  169  5                                   5    
HELIX   39  39 ALA C  170  LEU C  175  1                                   6    
HELIX   40  40 THR C  182  ARG C  199  1                                  18    
HELIX   41  41 SER C  207  GLY C  220  1                                  14    
HELIX   42  42 GLY C  229  MET C  233  5                                   5    
HELIX   43  43 ASP C  247  VAL C  252  1                                   6    
HELIX   44  44 ASP C  256  LEU C  267  1                                  12    
HELIX   45  45 SER C  276  ALA C  282  1                                   7    
HELIX   46  46 HIS C  283  GLN C  287  5                                   5    
HELIX   47  47 TYR D  178  CYS D  193  1                                  16    
HELIX   48  48 GLY D  198  GLN D  203  1                                   6    
HELIX   49  49 THR D  207  TYR D  225  1                                  19    
HELIX   50  50 GLN D  228  MET D  246  1                                  19    
HELIX   51  51 LEU D  249  GLU D  269  1                                  21    
HELIX   52  52 GLU D  274  ILE D  281  1                                   8    
HELIX   53  53 THR D  287  LEU D  302  1                                  16    
HELIX   54  54 THR D  310  PHE D  319  1                                  10    
HELIX   55  55 LEU D  320  GLN D  322  5                                   3    
HELIX   56  56 ASN D  326  ASP D  343  1                                  18    
HELIX   57  57 ASP D  343  LEU D  348  1                                   6    
HELIX   58  58 LEU D  351  THR D  368  1                                  18    
HELIX   59  59 PRO D  373  GLY D  381  1                                   9    
HELIX   60  60 THR D  383  LYS D  400  1                                  18    
HELIX   61  61 ALA D  401  HIS D  404  5                                   4    
HELIX   62  62 GLN D  407  TYR D  413  1                                   7    
HELIX   63  63 GLY D  420  LEU D  424  5                                   5    
SHEET    1  AA 5 PHE A   4  GLY A  13  0                                        
SHEET    2  AA 5 GLY A  16  ASN A  23 -1  O  GLY A  16   N  GLY A  13           
SHEET    3  AA 5 VAL A  29  ARG A  36 -1  O  VAL A  30   N  ALA A  21           
SHEET    4  AA 5 LYS A  75  GLU A  81 -1  O  LEU A  76   N  ILE A  35           
SHEET    5  AA 5 LEU A  66  ILE A  70 -1  N  LEU A  67   O  VAL A  79           
SHEET    1  AB 3 GLN A  85  ASP A  86  0                                        
SHEET    2  AB 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
SHEET    3  AB 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
SHEET    1  AC 2 VAL A 123  LEU A 124  0                                        
SHEET    2  AC 2 ARG A 150  ALA A 151 -1  O  ARG A 150   N  LEU A 124           
SHEET    1  CA 5 PHE C   4  GLY C  11  0                                        
SHEET    2  CA 5 VAL C  17  ASN C  23 -1  O  VAL C  18   N  ILE C  10           
SHEET    3  CA 5 VAL C  29  ARG C  36 -1  O  VAL C  30   N  ALA C  21           
SHEET    4  CA 5 LYS C  75  GLU C  81 -1  O  LEU C  76   N  ILE C  35           
SHEET    5  CA 5 LEU C  66  HIS C  71 -1  N  LEU C  67   O  VAL C  79           
SHEET    1  CB 3 GLN C  85  ASP C  86  0                                        
SHEET    2  CB 3 LEU C 133  ILE C 135 -1  O  ILE C 135   N  GLN C  85           
SHEET    3  CB 3 ILE C 141  LEU C 143 -1  O  LYS C 142   N  LEU C 134           
SHEET    1  CC 2 VAL C 123  LEU C 124  0                                        
SHEET    2  CC 2 ARG C 150  ALA C 151 -1  O  ARG C 150   N  LEU C 124           
LINK         C   TYR A 159                 N   TPO A 160     1555   1555  1.34  
LINK         C   TPO A 160                 N   HIS A 161     1555   1555  1.33  
LINK         C   TYR C 159                 N   TPO C 160     1555   1555  1.34  
LINK         C   TPO C 160                 N   HIS C 161     1555   1555  1.32  
CISPEP   1 VAL A  154    PRO A  155          0        -3.73                     
CISPEP   2 VAL A  163    VAL A  164          0        12.59                     
CISPEP   3 VAL B  175    PRO B  176          0       -21.12                     
CISPEP   4 GLN B  323    PRO B  324          0       -14.92                     
CISPEP   5 ASP B  345    PRO B  346          0         2.51                     
CISPEP   6 VAL C  154    PRO C  155          0        -4.03                     
CISPEP   7 LEU C  296    ARG C  297          0         5.88                     
CISPEP   8 GLN D  323    PRO D  324          0       -16.88                     
CISPEP   9 ASP D  345    PRO D  346          0         0.63                     
SITE     1 AC1 12 ILE A  10  ALA A  31  PHE A  80  GLU A  81                    
SITE     2 AC1 12 LEU A  83  HIS A  84  ASP A  86  LYS A  89                    
SITE     3 AC1 12 GLN A 131  ASN A 132  LEU A 134  ASP A 145                    
SITE     1 AC2 13 ILE C  10  GLU C  12  ALA C  31  PHE C  80                    
SITE     2 AC2 13 GLU C  81  LEU C  83  HIS C  84  ASP C  86                    
SITE     3 AC2 13 LYS C  89  GLN C 131  ASN C 132  LEU C 134                    
SITE     4 AC2 13 ASP C 145                                                     
CRYST1   74.660  136.560  149.030  90.00  90.00  90.00 P 21 21 21    8          
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      0.013394  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007323  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006710        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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