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Database: PDB
Entry: 4CFU
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Original site: 4CFU 
HEADER    TRANSFERASE                             19-NOV-13   4CFU              
TITLE     STRUCTURE-BASED DESIGN OF C8-SUBSTITUTED O6-                          
TITLE    2 CYCLOHEXYLMETHOXYGUANINE 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;                                                            
COMPND  11 FRAGMENT: CDK-ACTIVATING FRAGMENT, RESIDUES 172-432;                 
COMPND  12 SYNONYM: CYCLIN-A;                                                   
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: CYCLIN-A2;                                                 
COMPND  16 CHAIN: D;                                                            
COMPND  17 FRAGMENT: CDK-ACTIVATING FRAGMENT, RESIDUES 172-432;                 
COMPND  18 SYNONYM: CYCLIN-A;                                                   
COMPND  19 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: 834;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: 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: 834;                                       
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PET21D;                                   
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  21 ORGANISM_COMMON: HUMAN;                                              
SOURCE  22 ORGANISM_TAXID: 9606;                                                
SOURCE  23 EXPRESSION_SYSTEM: ESCHERICHIA COLI B;                               
SOURCE  24 EXPRESSION_SYSTEM_TAXID: 37762;                                      
SOURCE  25 EXPRESSION_SYSTEM_STRAIN: 834;                                       
SOURCE  26 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  27 EXPRESSION_SYSTEM_PLASMID: PET21D                                    
KEYWDS    TRANSFERASE, 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 4CFU    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.    2.20 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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.82                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.37                          
REMARK   3   NUMBER OF REFLECTIONS             : 70608                          
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) : 0.18383                         
REMARK   3   R VALUE            (WORKING SET) : 0.18185                         
REMARK   3   FREE R VALUE                     : 0.22071                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 3750                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.200                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.256                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5116                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.91                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.254                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 279                          
REMARK   3   BIN FREE R VALUE                    : 0.296                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8890                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 80                                      
REMARK   3   SOLVENT ATOMS            : 489                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.756                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.91                                                
REMARK   3    B22 (A**2) : 0.81                                                 
REMARK   3    B33 (A**2) : 0.10                                                 
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): 0.219         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.181         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.138         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.845        
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9202 ; 0.018 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  8965 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12517 ; 1.926 ; 1.985       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 20674 ; 2.464 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1119 ; 6.282 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   402 ;40.456 ;24.005       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1617 ;16.900 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    47 ;20.703 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1413 ; 0.125 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10179 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2064 ; 0.010 ; 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):  4422 ; 0.962 ; 1.695       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4421 ; 0.960 ; 1.695       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5529 ; 1.435 ; 2.536       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4780 ; 1.232 ; 1.848       
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    -3        A   298                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.8820  26.1200 -10.1960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0339 T22:   0.0382                                     
REMARK   3      T33:   0.0405 T12:   0.0104                                     
REMARK   3      T13:   0.0255 T23:  -0.0178                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8543 L22:   0.9955                                     
REMARK   3      L33:   1.8704 L12:   0.4495                                     
REMARK   3      L13:   0.9062 L23:   0.2145                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0168 S12:   0.0549 S13:  -0.0320                       
REMARK   3      S21:  -0.1169 S22:   0.0286 S23:  -0.1340                       
REMARK   3      S31:   0.0957 S32:   0.1211 S33:  -0.0453                       
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   171        B   432                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.1850  -0.4530   3.1690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1112 T22:   0.0797                                     
REMARK   3      T33:   0.0530 T12:  -0.0173                                     
REMARK   3      T13:  -0.0488 T23:   0.0547                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3030 L22:   2.0827                                     
REMARK   3      L33:   1.9545 L12:  -0.2236                                     
REMARK   3      L13:  -0.4847 L23:   0.4662                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0140 S12:  -0.1932 S13:  -0.1124                       
REMARK   3      S21:   0.0544 S22:   0.0725 S23:  -0.0021                       
REMARK   3      S31:   0.3073 S32:   0.0063 S33:  -0.0585                       
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    -2        C   296                          
REMARK   3    ORIGIN FOR THE GROUP (A): -43.8890 -15.0520 -30.8680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2442 T22:   0.0623                                     
REMARK   3      T33:   0.0956 T12:  -0.0187                                     
REMARK   3      T13:   0.0519 T23:  -0.0425                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4743 L22:   2.3192                                     
REMARK   3      L33:   1.5196 L12:   0.5375                                     
REMARK   3      L13:   0.7257 L23:   0.2284                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0894 S12:   0.0440 S13:  -0.0515                       
REMARK   3      S21:   0.1201 S22:  -0.0853 S23:   0.1309                       
REMARK   3      S31:   0.1872 S32:  -0.0940 S33:  -0.0040                       
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   171        D   432                          
REMARK   3    ORIGIN FOR THE GROUP (A): -45.3330  17.7850 -33.3150              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1696 T22:   0.0735                                     
REMARK   3      T33:   0.2259 T12:   0.0724                                     
REMARK   3      T13:  -0.0081 T23:  -0.0592                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5327 L22:   3.1798                                     
REMARK   3      L33:   1.6462 L12:   0.3956                                     
REMARK   3      L13:  -0.3947 L23:   0.4697                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0324 S12:   0.0214 S13:   0.3234                       
REMARK   3      S21:   0.0456 S22:  -0.1154 S23:   0.7403                       
REMARK   3      S31:  -0.1765 S32:  -0.2657 S33:   0.1478                       
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 4CFU 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-59023.                                       
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               : ELETTRA                            
REMARK 200  BEAMLINE                       : 5.2R                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NCCD (SX-165)                      
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 74525                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.20                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.80                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 3.24                               
REMARK 200  R MERGE                    (I) : 0.07                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.90                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.60                               
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   (%): 56.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82                     
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       36.90300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       73.73000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       66.87200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       73.73000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.90300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       66.87200            
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: 4510 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23270 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.1 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4520 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.6 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     GLY A    -4                                                      
REMARK 465     THR A    39                                                      
REMARK 465     GLU A    40                                                      
REMARK 465     GLY C    -4                                                      
REMARK 465     PRO C    -3                                                      
REMARK 465     PRO C   222                                                      
REMARK 465     ASP C   223                                                      
REMARK 465     GLU C   224                                                      
REMARK 465     VAL C   225                                                      
REMARK 465     VAL C   226                                                      
REMARK 465     TRP C   227                                                      
REMARK 465     PRO C   228                                                      
REMARK 465     GLY C   229                                                      
REMARK 465     VAL C   230                                                      
REMARK 465     THR C   231                                                      
REMARK 465     SER C   232                                                      
REMARK 465     MET C   233                                                      
REMARK 465     PRO C   234                                                      
REMARK 465     ASP C   235                                                      
REMARK 465     TYR C   236                                                      
REMARK 465     LYS C   237                                                      
REMARK 465     PRO C   238                                                      
REMARK 465     SER C   239                                                      
REMARK 465     PHE C   240                                                      
REMARK 465     PRO C   241                                                      
REMARK 465     LYS C   242                                                      
REMARK 465     TRP C   243                                                      
REMARK 465     ALA C   244                                                      
REMARK 465     ARG C   245                                                      
REMARK 465     GLN C   246                                                      
REMARK 465     ASP C   247                                                      
REMARK 465     ARG C   297                                                      
REMARK 465     LEU C   298                                                      
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     PRO A  -3    CB   CG   CD                                        
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   NH1B ARG A    22     O    HOH A  2009              2.12            
REMARK 500   OG1  THR A    72     O    HOH A  2037              2.00            
REMARK 500   SG A CYS A   177     CE   MET A   233              1.91            
REMARK 500   O    GLN A   246     O    HOH A  2111              2.05            
REMARK 500   O    PHE A   248     O    HOH A  2130              2.18            
REMARK 500   NZ   LYS B   300     O    HOH A  2035              2.20            
REMARK 500   O    LEU B   432     O    HOH B  2131              2.19            
REMARK 500   O    HOH B  2009     O    HOH A  2097              1.73            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH C  2099     O    HOH A  2153     3444     1.84            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    GLU A  51   CD    GLU A  51   OE2     0.137                       
REMARK 500    GLU A 162   C     GLU A 162   O       0.118                       
REMARK 500    ASP A 256   CB    ASP A 256   CG      0.132                       
REMARK 500    GLU B 188   CD    GLU B 188   OE1     0.071                       
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    ARG A 217   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG A 217   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ASP A 223   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP A 247   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG B 241   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    MET B 334   CG  -  SD  -  CE  ANGL. DEV. = -16.6 DEGREES          
REMARK 500    ARG C 199   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG C 199   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    VAL D 175   N   -  CA  -  C   ANGL. DEV. = -21.4 DEGREES          
REMARK 500    ARG D 241   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG D 250   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 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    PRO A  -2       63.29    -51.24                                   
REMARK 500    SER A   0     -143.22   -154.88                                   
REMARK 500    MET A   1      -42.27    126.30                                   
REMARK 500    LEU A  96      -57.61     86.06                                   
REMARK 500    ASP A 127       41.46   -156.31                                   
REMARK 500    ASP A 145       77.88     46.96                                   
REMARK 500    GLU A 162      -78.36    -15.18                                   
REMARK 500    VAL A 164      130.01     80.99                                   
REMARK 500    SER A 181     -159.74   -141.18                                   
REMARK 500    VAL B 175       67.32     28.13                                   
REMARK 500    ASP B 284       28.99     48.06                                   
REMARK 500    PHE B 304       17.18     58.75                                   
REMARK 500    TRP B 372      108.33    -35.08                                   
REMARK 500    SER C   0     -168.41    -50.88                                   
REMARK 500    THR C  14       58.36   -105.34                                   
REMARK 500    TYR C  15      -65.43   -153.79                                   
REMARK 500    THR C  41      -94.86   -138.66                                   
REMARK 500    ASP C 127       45.10   -155.43                                   
REMARK 500    ASP C 145       77.67     45.07                                   
REMARK 500    VAL C 164      126.58     73.42                                   
REMARK 500    HIS C 295       85.08    -67.74                                   
REMARK 500    ASN D 173       -5.77    -57.71                                   
REMARK 500    GLU D 174       48.33   -146.96                                   
REMARK 500    ASP D 283     -138.58     59.91                                   
REMARK 500    TRP D 372      112.75    -32.33                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU A  162     VAL A  163                  -44.79                    
REMARK 500 GLU D  174     VAL D  175                  -40.64                    
REMARK 500 ASP D  284     THR D  285                 -149.22                    
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    ILE B 281        23.9      L          L   OUTSIDE RANGE           
REMARK 500    ILE D 281        22.9      L          L   OUTSIDE RANGE           
REMARK 500    ASN D 312        12.9      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED            
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND ARE                    
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL                 
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE          
REMARK 525 NUMBER; I=INSERTION CODE): THESE HAVE BEEN REPOSITIONED              
REMARK 525 BY APPLYING THE SYMMETRY TRANSFORMATION INDICATED.                   
REMARK 525                                                                      
REMARK 525  M RES CSSEQI     ORIGINAL COORDINATES   SYMMETRY TRANS.    DIST.    
REMARK 525                    X       Y       Z                                 
REMARK 525    HOH H 416   -21.853  44.427  -3.483    004      555      2.43     
REMARK 525    HOH H 383   -21.649  35.468   2.156    004      555      2.66     
REMARK 525    HOH H 244   -43.337  28.529 -17.118    004      555      4.05     
REMARK 525    HOH H 477   -24.885  27.407 -13.586    004      555      2.77     
REMARK 525    HOH H 392    15.912  24.531   5.110    004      455      2.94     
REMARK 525    HOH H 474   -53.392 -25.207 -52.821    003      454      3.28     
REMARK 525    HOH H 461     5.088  50.579   3.009    004      455      2.95     
REMARK 525    HOH H 319     5.331  49.216   5.390    004      455      2.88     
REMARK 525    HOH H 131   -15.753   4.417 -46.537    002      455      3.50     
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1300  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG A 274   O                                                      
REMARK 620 2 HOH A2143   O    74.2                                              
REMARK 620 3 PRO A 271   O   104.4 109.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D1433  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE D 206   O                                                      
REMARK 620 2 MET D 200   O   104.6                                              
REMARK 620 3 HOH D2021   O    94.8  87.1                                        
REMARK 620 4 HOH D2024   O    80.3 175.1  93.0                                  
REMARK 620 5 GLN D 203   O    91.4  90.1 173.7  89.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2WC A1299                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2WC C1297                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A1300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG D1433                 
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: 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 900 RELATED ID: 4CFX   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. SEQUENCE OF CHAINS B AND D              
REMARK 999 UNCONFIRMED                                                          
DBREF  4CFU A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  4CFU B  172   432  UNP    P20248   CCNA2_HUMAN    172    432             
DBREF  4CFU C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  4CFU D  173   432  UNP    P20248   CCNA2_HUMAN    173    432             
SEQADV 4CFU GLY A   -4  UNP  P24941              EXPRESSION TAG                 
SEQADV 4CFU PRO A   -3  UNP  P24941              EXPRESSION TAG                 
SEQADV 4CFU PRO A   -2  UNP  P24941              EXPRESSION TAG                 
SEQADV 4CFU GLY A   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 4CFU SER A    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 4CFU GLY B  171  UNP  P20248              EXPRESSION TAG                 
SEQADV 4CFU ALA B  303  UNP  P20248    THR   303 CONFLICT                       
SEQADV 4CFU ILE B  311  UNP  P20248    VAL   311 CONFLICT                       
SEQADV 4CFU ALA B  357  UNP  P20248    GLY   357 CONFLICT                       
SEQADV 4CFU VAL B  377  UNP  P20248    ILE   377 CONFLICT                       
SEQADV 4CFU GLN B  378  UNP  P20248    ARG   378 CONFLICT                       
SEQADV 4CFU THR B  386  UNP  P20248    SER   386 CONFLICT                       
SEQADV 4CFU LEU B  392  UNP  P20248    MET   392 CONFLICT                       
SEQADV 4CFU ARG B  400  UNP  P20248    LYS   400 CONFLICT                       
SEQADV 4CFU GLY C   -4  UNP  P24941              EXPRESSION TAG                 
SEQADV 4CFU PRO C   -3  UNP  P24941              EXPRESSION TAG                 
SEQADV 4CFU PRO C   -2  UNP  P24941              EXPRESSION TAG                 
SEQADV 4CFU GLY C   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 4CFU SER C    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 4CFU ASN D  171  UNP  P20248              EXPRESSION TAG                 
SEQADV 4CFU GLU D  172  UNP  P20248              EXPRESSION TAG                 
SEQADV 4CFU ALA D  303  UNP  P20248    THR   303 CONFLICT                       
SEQADV 4CFU ILE D  311  UNP  P20248    VAL   311 CONFLICT                       
SEQADV 4CFU ALA D  357  UNP  P20248    GLY   357 CONFLICT                       
SEQADV 4CFU VAL D  377  UNP  P20248    ILE   377 CONFLICT                       
SEQADV 4CFU GLN D  378  UNP  P20248    ARG   378 CONFLICT                       
SEQADV 4CFU THR D  386  UNP  P20248    SER   386 CONFLICT                       
SEQADV 4CFU LEU D  392  UNP  P20248    MET   392 CONFLICT                       
SEQADV 4CFU ARG D  400  UNP  P20248    LYS   400 CONFLICT                       
SEQRES   1 A  303  GLY PRO PRO 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 PRO 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  262  GLY VAL ASN GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS          
SEQRES   2 B  262  THR TYR LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS          
SEQRES   3 B  262  VAL GLY TYR MET LYS LYS GLN PRO ASP ILE THR ASN SER          
SEQRES   4 B  262  MET ARG ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY          
SEQRES   5 B  262  GLU GLU TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA          
SEQRES   6 B  262  VAL ASN TYR ILE ASP ARG PHE LEU SER SER MET SER VAL          
SEQRES   7 B  262  LEU ARG GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET          
SEQRES   8 B  262  LEU LEU ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU          
SEQRES   9 B  262  VAL ALA GLU PHE VAL TYR ILE THR ASP ASP THR TYR THR          
SEQRES  10 B  262  LYS LYS GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS          
SEQRES  11 B  262  VAL LEU ALA PHE ASP LEU ALA ALA PRO THR ILE ASN GLN          
SEQRES  12 B  262  PHE LEU THR GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN          
SEQRES  13 B  262  CYS LYS VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU          
SEQRES  14 B  262  SER LEU ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO          
SEQRES  15 B  262  SER VAL ILE ALA ALA ALA ALA PHE HIS LEU ALA LEU TYR          
SEQRES  16 B  262  THR VAL THR GLY GLN SER TRP PRO GLU SER LEU VAL GLN          
SEQRES  17 B  262  LYS THR GLY TYR THR LEU GLU THR LEU LYS PRO CYS LEU          
SEQRES  18 B  262  LEU ASP LEU HIS GLN THR TYR LEU ARG ALA PRO GLN HIS          
SEQRES  19 B  262  ALA GLN GLN SER ILE ARG GLU LYS TYR LYS ASN SER LYS          
SEQRES  20 B  262  TYR HIS GLY VAL SER LEU LEU ASN PRO PRO GLU THR LEU          
SEQRES  21 B  262  ASN LEU                                                      
SEQRES   1 D  262  ASN GLU ASN GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS          
SEQRES   2 D  262  THR TYR LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS          
SEQRES   3 D  262  VAL GLY TYR MET LYS LYS GLN PRO ASP ILE THR ASN SER          
SEQRES   4 D  262  MET ARG ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY          
SEQRES   5 D  262  GLU GLU TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA          
SEQRES   6 D  262  VAL ASN TYR ILE ASP ARG PHE LEU SER SER MET SER VAL          
SEQRES   7 D  262  LEU ARG GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET          
SEQRES   8 D  262  LEU LEU ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU          
SEQRES   9 D  262  VAL ALA GLU PHE VAL TYR ILE THR ASP ASP THR TYR THR          
SEQRES  10 D  262  LYS LYS GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS          
SEQRES  11 D  262  VAL LEU ALA PHE ASP LEU ALA ALA PRO THR ILE ASN GLN          
SEQRES  12 D  262  PHE LEU THR GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN          
SEQRES  13 D  262  CYS LYS VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU          
SEQRES  14 D  262  SER LEU ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO          
SEQRES  15 D  262  SER VAL ILE ALA ALA ALA ALA PHE HIS LEU ALA LEU TYR          
SEQRES  16 D  262  THR VAL THR GLY GLN SER TRP PRO GLU SER LEU VAL GLN          
SEQRES  17 D  262  LYS THR GLY TYR THR LEU GLU THR LEU LYS PRO CYS LEU          
SEQRES  18 D  262  LEU ASP LEU HIS GLN THR TYR LEU ARG ALA PRO GLN HIS          
SEQRES  19 D  262  ALA GLN GLN SER ILE ARG GLU LYS TYR LYS ASN SER LYS          
SEQRES  20 D  262  TYR HIS GLY VAL SER LEU LEU ASN PRO PRO GLU THR LEU          
SEQRES  21 D  262  ASN LEU                                                      
MODRES 4CFU TPO A  160  THR  PHOSPHOTHREONINE                                   
MODRES 4CFU TPO C  160  THR  PHOSPHOTHREONINE                                   
HET    TPO  A 160      11                                                       
HET    TPO  C 160      11                                                       
HET    2WC  A1299      28                                                       
HET    2WC  C1297      28                                                       
HET     MG  A1300       1                                                       
HET     MG  D1433       1                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     2WC 3-[2-AZANYL-6-(CYCLOHEXYLMETHOXY)-7H-PURIN-8-                    
HETNAM   2 2WC  YL]-2-METHYL-BENZOIC ACID                                       
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   5  TPO    2(C4 H10 N O6 P)                                             
FORMUL   6  2WC    2(C20 H23 N5 O3)                                             
FORMUL   7   MG    2(MG 2+)                                                     
FORMUL   8  HOH   *489(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  HIS A  121  1                                  22    
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  256  LEU A  267  1                                  12    
HELIX   11  11 SER A  276  LEU A  281  1                                   6    
HELIX   12  12 ALA A  282  VAL A  289  5                                   8    
HELIX   13  13 GLY B  171  VAL B  175  5                                   5    
HELIX   14  14 TYR B  178  CYS B  193  1                                  16    
HELIX   15  15 GLY B  198  GLN B  203  5                                   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  THR B  282  1                                   9    
HELIX   21  21 THR B  287  LEU B  302  1                                  16    
HELIX   22  22 THR B  310  LEU B  320  1                                  11    
HELIX   23  23 ASN B  326  ASP B  343  1                                  18    
HELIX   24  24 ASP B  343  LEU B  348  1                                   6    
HELIX   25  25 LEU B  351  GLY B  369  1                                  19    
HELIX   26  26 PRO B  373  GLY B  381  1                                   9    
HELIX   27  27 THR B  383  ALA B  401  1                                  19    
HELIX   28  28 PRO B  402  HIS B  404  5                                   3    
HELIX   29  29 GLN B  407  TYR B  413  1                                   7    
HELIX   30  30 LYS B  414  HIS B  419  5                                   6    
HELIX   31  31 GLY B  420  LEU B  424  5                                   5    
HELIX   32  32 PRO C   45  LEU C   58  1                                  14    
HELIX   33  33 LEU C   87  SER C   94  1                                   8    
HELIX   34  34 PRO C  100  HIS C  121  1                                  22    
HELIX   35  35 LYS C  129  GLN C  131  5                                   3    
HELIX   36  36 ASP C  145  ALA C  149  5                                   5    
HELIX   37  37 THR C  165  ARG C  169  5                                   5    
HELIX   38  38 ALA C  170  LEU C  175  1                                   6    
HELIX   39  39 THR C  182  ARG C  199  1                                  18    
HELIX   40  40 SER C  207  GLY C  220  1                                  14    
HELIX   41  41 ASP C  256  LEU C  267  1                                  12    
HELIX   42  42 SER C  276  ALA C  282  1                                   7    
HELIX   43  43 HIS C  283  GLN C  287  5                                   5    
HELIX   44  44 ASN D  171  VAL D  175  5                                   5    
HELIX   45  45 TYR D  178  CYS D  193  1                                  16    
HELIX   46  46 TYR D  199  GLN D  203  5                                   5    
HELIX   47  47 THR D  207  TYR D  225  1                                  19    
HELIX   48  48 GLN D  228  SER D  244  1                                  17    
HELIX   49  49 LEU D  249  GLY D  251  5                                   3    
HELIX   50  50 LYS D  252  GLU D  269  1                                  18    
HELIX   51  51 GLU D  274  THR D  282  1                                   9    
HELIX   52  52 THR D  287  LEU D  302  1                                  16    
HELIX   53  53 THR D  310  LEU D  320  1                                  11    
HELIX   54  54 ASN D  326  ASP D  343  1                                  18    
HELIX   55  55 ASP D  343  LEU D  348  1                                   6    
HELIX   56  56 LEU D  351  GLY D  369  1                                  19    
HELIX   57  57 PRO D  373  GLY D  381  1                                   9    
HELIX   58  58 THR D  383  ALA D  401  1                                  19    
HELIX   59  59 PRO D  402  HIS D  404  5                                   3    
HELIX   60  60 GLN D  407  TYR D  413  1                                   7    
HELIX   61  61 LYS D  414  HIS D  419  5                                   6    
HELIX   62  62 GLY D  420  LEU D  424  5                                   5    
SHEET    1  AA 5 PHE A   4  GLU A  12  0                                        
SHEET    2  AA 5 GLY A  16  ASN A  23 -1  O  VAL A  18   N  ILE A  10           
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  HIS A  71 -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 GLY C  16  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  1.33  
LINK         C   TPO A 160                 N   HIS A 161     1555   1555  1.33  
LINK        MG    MG A1300                 O   ARG A 274     1555   1555  2.61  
LINK        MG    MG A1300                 O   HOH A2143     1555   1555  2.74  
LINK        MG    MG A1300                 O   PRO A 271     1555   1555  2.68  
LINK         C   TYR C 159                 N   TPO C 160     1555   1555  1.34  
LINK         C   TPO C 160                 N   HIS C 161     1555   1555  1.33  
LINK        MG    MG D1433                 O   MET D 200     1555   1555  2.56  
LINK        MG    MG D1433                 O   HOH D2021     1555   1555  2.47  
LINK        MG    MG D1433                 O   HOH D2024     1555   1555  2.44  
LINK        MG    MG D1433                 O   GLN D 203     1555   1555  2.34  
LINK        MG    MG D1433                 O   ILE D 206     1555   1555  2.52  
CISPEP   1 GLY A   -1    SER A    0          0        -2.58                     
CISPEP   2 THR A   14    TYR A   15          0        11.19                     
CISPEP   3 TYR A   15    GLY A   16          0        -0.08                     
CISPEP   4 VAL A  154    PRO A  155          0        -5.80                     
CISPEP   5 GLN B  323    PRO B  324          0       -12.09                     
CISPEP   6 ASP B  345    PRO B  346          0         6.87                     
CISPEP   7 PRO C   -2    GLY C   -1          0        -5.50                     
CISPEP   8 TYR C   15    GLY C   16          0       -11.45                     
CISPEP   9 VAL C  154    PRO C  155          0        -6.28                     
CISPEP  10 GLN D  323    PRO D  324          0        -4.13                     
CISPEP  11 ASP D  345    PRO D  346          0         5.22                     
SITE     1 AC1 15 ILE A  10  ALA A  31  VAL A  64  PHE A  80                    
SITE     2 AC1 15 GLU A  81  LEU A  83  HIS A  84  GLN A  85                    
SITE     3 AC1 15 ASP A  86  LYS A  89  GLN A 131  ASN A 132                    
SITE     4 AC1 15 LEU A 134  HOH A2007  HOH A2155                               
SITE     1 AC2 17 ILE C  10  ALA C  31  LYS C  33  VAL C  64                    
SITE     2 AC2 17 PHE C  80  GLU C  81  PHE C  82  LEU C  83                    
SITE     3 AC2 17 HIS C  84  GLN C  85  ASP C  86  LYS C  89                    
SITE     4 AC2 17 GLN C 131  ASN C 132  LEU C 134  HOH C2007                    
SITE     5 AC2 17 HOH C2112                                                     
SITE     1 AC3  4 PRO A 271  ARG A 274  HOH A2143  VAL B 172                    
SITE     1 AC4  5 MET D 200  GLN D 203  ILE D 206  HOH D2021                    
SITE     2 AC4  5 HOH D2024                                                     
CRYST1   73.806  133.744  147.460  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      0.013549  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007477  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006782        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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