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Database: PDB
Entry: 4CFM
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Original site: 4CFM 
HEADER    CELL CYCLE                              18-NOV-13   4CFM              
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, D;                                                         
COMPND  11 FRAGMENT: CDK-ACTIVATING FRAGMENT, RESIDUES 175-432;                 
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, CYCLIN DEPENDENT KINASES, STRUCTURE-BASED DRUG DESIGN,    
KEYWDS   2 CONFORMATIONAL RESTRAINT, 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 4CFM    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.    2.85 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) : 2.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 22.34                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.95                          
REMARK   3   NUMBER OF REFLECTIONS             : 32029                          
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) : 0.21916                         
REMARK   3   R VALUE            (WORKING SET) : 0.21711                         
REMARK   3   FREE R VALUE                     : 0.25806                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1671                            
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) : 2.850                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.923                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1153                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 47.21                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.337                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 58                           
REMARK   3   BIN FREE R VALUE                    : 0.387                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8747                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 72                                      
REMARK   3   SOLVENT ATOMS            : 10                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 58.092                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.46                                                 
REMARK   3    B22 (A**2) : 2.75                                                 
REMARK   3    B33 (A**2) : -4.21                                                
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): 0.401         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.362         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 44.014        
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.915                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.878                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9045 ; 0.015 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  8802 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12288 ; 1.834 ; 1.984       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 20295 ; 2.443 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1089 ; 6.586 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   387 ;40.730 ;23.928       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1583 ;20.847 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    43 ;16.228 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1387 ; 0.106 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9959 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2026 ; 0.005 ; 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):  4359 ; 0.228 ; 0.739       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4358 ; 0.228 ; 0.739       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5447 ; 0.391 ; 1.109       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4686 ; 0.353 ; 0.845       
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   296                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.7560 -26.3170  10.0880              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1009 T22:   0.0410                                     
REMARK   3      T33:   0.5984 T12:  -0.0229                                     
REMARK   3      T13:  -0.0667 T23:  -0.0244                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1027 L22:   1.7303                                     
REMARK   3      L33:   1.9834 L12:  -0.5676                                     
REMARK   3      L13:  -1.0947 L23:   0.3162                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0443 S12:  -0.1932 S13:  -0.0511                       
REMARK   3      S21:   0.2456 S22:   0.0269 S23:  -0.1918                       
REMARK   3      S31:  -0.1221 S32:   0.2760 S33:  -0.0712                       
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   175        B   432                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.7730   0.2440  -2.6690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1947 T22:   0.0225                                     
REMARK   3      T33:   0.5121 T12:  -0.0065                                     
REMARK   3      T13:   0.0471 T23:   0.0208                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1955 L22:   2.7222                                     
REMARK   3      L33:   3.2385 L12:   0.5415                                     
REMARK   3      L13:   0.8552 L23:   0.2371                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0985 S12:   0.2143 S13:   0.1731                       
REMARK   3      S21:  -0.1753 S22:   0.0998 S23:   0.0566                       
REMARK   3      S31:  -0.3704 S32:   0.1088 S33:  -0.0013                       
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   296                          
REMARK   3    ORIGIN FOR THE GROUP (A): -44.5900  13.0790  32.1580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5710 T22:   0.7644                                     
REMARK   3      T33:   0.6614 T12:   0.2575                                     
REMARK   3      T13:  -0.0531 T23:  -0.2883                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0307 L22:   2.3163                                     
REMARK   3      L33:   2.7546 L12:  -0.1381                                     
REMARK   3      L13:   0.5625 L23:   0.1279                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1976 S12:  -1.0300 S13:   0.4853                       
REMARK   3      S21:  -0.0619 S22:  -0.0181 S23:   0.1994                       
REMARK   3      S31:  -0.5424 S32:  -1.1904 S33:   0.2158                       
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   175        D   432                          
REMARK   3    ORIGIN FOR THE GROUP (A): -44.7550 -19.6520  35.0210              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5699 T22:   0.8472                                     
REMARK   3      T33:   0.7133 T12:  -0.4903                                     
REMARK   3      T13:  -0.0884 T23:   0.1059                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0757 L22:   3.3743                                     
REMARK   3      L33:   2.4146 L12:  -0.4670                                     
REMARK   3      L13:   0.5009 L23:  -0.5096                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1707 S12:  -0.6048 S13:  -0.5683                       
REMARK   3      S21:  -0.2863 S22:   0.1543 S23:   0.7070                       
REMARK   3      S31:   0.6282 S32:  -1.3442 S33:  -0.3250                       
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 4CFM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-NOV-13.                  
REMARK 100 THE PDBE ID CODE IS EBI-58957.                                       
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               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (QUANTUM 4)                    
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33733                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.85                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 22.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY                : 3.21                               
REMARK 200  R MERGE                    (I) : 0.12                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.10                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 64.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.45                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.50                               
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   (%): 57.94                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       37.05500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       74.68500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       67.72150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       74.68500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.05500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       67.72150            
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: 4060 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23370 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.6 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: 4130 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22530 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.2 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     PRO A    -3                                                      
REMARK 465     LEU A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     ARG A   297                                                      
REMARK 465     LEU A   298                                                      
REMARK 465     GLY C    -4                                                      
REMARK 465     PRO C    -3                                                      
REMARK 465     LEU C    -2                                                      
REMARK 465     GLY C    -1                                                      
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     PHE C   248                                                      
REMARK 465     SER C   249                                                      
REMARK 465     LYS C   250                                                      
REMARK 465     VAL C   251                                                      
REMARK 465     VAL C   252                                                      
REMARK 465     ARG C   297                                                      
REMARK 465     LEU C   298                                                      
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    GLU A    81     N2   4QE A  1297              2.13            
REMARK 500   CD2B HIS C    84     CD1  LEU C   296              2.09            
REMARK 500   O    ALA C    95     NH1  ARG C   199              2.14            
REMARK 500   OH   TYR D   347     OG1  THR D   397              2.18            
REMARK 500   O    HOH C  2004     O    HOH C  2005              2.02            
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    ASP A  38      -43.53   -135.74                                   
REMARK 500    THR A  39      172.67     77.97                                   
REMARK 500    GLU A  40      -17.01     63.08                                   
REMARK 500    THR A  41     -113.32   -120.47                                   
REMARK 500    ASP A 127       55.15   -156.74                                   
REMARK 500    ASP A 145       75.94     51.50                                   
REMARK 500    GLU A 162       85.07    -59.70                                   
REMARK 500    VAL A 164      137.41     73.77                                   
REMARK 500    SER A 181     -152.89   -151.04                                   
REMARK 500    ARG A 199       -9.63     67.45                                   
REMARK 500    THR A 290     -165.11   -128.69                                   
REMARK 500    PRO B 176      -14.80    -40.98                                   
REMARK 500    THR B 282       42.34    -93.69                                   
REMARK 500    ASP B 283       57.59     13.02                                   
REMARK 500    PHE B 304       13.04     58.33                                   
REMARK 500    TRP B 372      110.70    -29.63                                   
REMARK 500    ASP C  38      -24.22   -150.77                                   
REMARK 500    THR C  39      175.49     87.92                                   
REMARK 500    GLU C  40      -19.54     67.00                                   
REMARK 500    THR C  41     -105.65   -125.43                                   
REMARK 500    ASP C 127       48.21   -164.17                                   
REMARK 500    ASP C 145       76.15     51.13                                   
REMARK 500    GLU C 162       81.01    -64.94                                   
REMARK 500    VAL C 164      140.32     71.18                                   
REMARK 500    SER C 181     -151.06   -156.71                                   
REMARK 500    ARG C 199      -19.42     73.25                                   
REMARK 500    LYS D 226       51.02     37.06                                   
REMARK 500    ASP D 283       54.19     34.55                                   
REMARK 500    ASP D 284       13.29     58.47                                   
REMARK 500    TRP D 372      108.40    -22.57                                   
REMARK 500    PRO D 402      -39.15    -37.96                                   
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 ASP A   38     THR A   39                 -149.25                    
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    ASP C  38        22.8      L          L   OUTSIDE RANGE           
REMARK 500    ILE D 281        24.8      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 4QE A1297                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4QE C1297                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 N-TERMINAL 3C PROTEASE SITE                                          
DBREF  4CFM A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  4CFM B  175   432  UNP    P20248   CCNA2_HUMAN    175    432             
DBREF  4CFM C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  4CFM D  175   432  UNP    P20248   CCNA2_HUMAN    175    432             
SEQADV 4CFM GLY A   -4  UNP  P24941              EXPRESSION TAG                 
SEQADV 4CFM PRO A   -3  UNP  P24941              EXPRESSION TAG                 
SEQADV 4CFM LEU A   -2  UNP  P24941              EXPRESSION TAG                 
SEQADV 4CFM GLY A   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 4CFM SER A    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 4CFM GLY C   -4  UNP  P24941              EXPRESSION TAG                 
SEQADV 4CFM PRO C   -3  UNP  P24941              EXPRESSION TAG                 
SEQADV 4CFM LEU C   -2  UNP  P24941              EXPRESSION TAG                 
SEQADV 4CFM GLY C   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 4CFM 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 B  258  VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR LEU ARG          
SEQRES   2 B  258  GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR MET          
SEQRES   3 B  258  LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG ALA ILE          
SEQRES   4 B  258  LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR LYS          
SEQRES   5 B  258  LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR ILE          
SEQRES   6 B  258  ASP ARG PHE LEU SER SER MET SER VAL LEU ARG GLY LYS          
SEQRES   7 B  258  LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA SER          
SEQRES   8 B  258  LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU PHE          
SEQRES   9 B  258  VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS GLN VAL          
SEQRES  10 B  258  LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU THR PHE          
SEQRES  11 B  258  ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR GLN          
SEQRES  12 B  258  TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS VAL GLU          
SEQRES  13 B  258  SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE ASP          
SEQRES  14 B  258  ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL ILE ALA          
SEQRES  15 B  258  GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR GLY          
SEQRES  16 B  258  GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR GLY TYR          
SEQRES  17 B  258  THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP LEU HIS          
SEQRES  18 B  258  GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN SER          
SEQRES  19 B  258  ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS GLY VAL          
SEQRES  20 B  258  SER LEU LEU ASN PRO PRO GLU THR LEU ASN 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 D  258  VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR LEU ARG          
SEQRES   2 D  258  GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR MET          
SEQRES   3 D  258  LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG ALA ILE          
SEQRES   4 D  258  LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR LYS          
SEQRES   5 D  258  LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR ILE          
SEQRES   6 D  258  ASP ARG PHE LEU SER SER MET SER VAL LEU ARG GLY LYS          
SEQRES   7 D  258  LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA SER          
SEQRES   8 D  258  LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU PHE          
SEQRES   9 D  258  VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS GLN VAL          
SEQRES  10 D  258  LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU THR PHE          
SEQRES  11 D  258  ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR GLN          
SEQRES  12 D  258  TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS VAL GLU          
SEQRES  13 D  258  SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE ASP          
SEQRES  14 D  258  ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL ILE ALA          
SEQRES  15 D  258  GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR GLY          
SEQRES  16 D  258  GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR GLY TYR          
SEQRES  17 D  258  THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP LEU HIS          
SEQRES  18 D  258  GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN SER          
SEQRES  19 D  258  ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS GLY VAL          
SEQRES  20 D  258  SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU                  
MODRES 4CFM TPO A  160  THR  PHOSPHOTHREONINE                                   
MODRES 4CFM TPO C  160  THR  PHOSPHOTHREONINE                                   
HET    TPO  A 160      11                                                       
HET    TPO  C 160      11                                                       
HET    4QE  A1297      25                                                       
HET    4QE  C1297      25                                                       
HETNAM     4QE 6-(CYCLOHEXYLMETHOXY)-8-(2-METHYLPHENYL)-9H-                     
HETNAM   2 4QE  PURIN-2-AMINE                                                   
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   3  4QE    2(C19 H23 N5 O)                                              
FORMUL   4  TPO    2(C4 H10 N O6 P)                                             
FORMUL   5  HOH   *10(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 ASP A  145  ALA A  149  5                                   5    
HELIX    6   6 THR A  165  ARG A  169  5                                   5    
HELIX    7   7 ALA A  170  LEU A  175  1                                   6    
HELIX    8   8 THR A  182  ARG A  199  1                                  18    
HELIX    9   9 SER A  207  GLY A  220  1                                  14    
HELIX   10  10 GLY A  229  MET A  233  5                                   5    
HELIX   11  11 ASP A  247  VAL A  252  1                                   6    
HELIX   12  12 ASP A  256  LEU A  267  1                                  12    
HELIX   13  13 SER A  276  LEU A  281  1                                   6    
HELIX   14  14 ALA A  282  GLN A  287  5                                   6    
HELIX   15  15 VAL B  175  ASP B  177  5                                   3    
HELIX   16  16 TYR B  178  CYS B  193  1                                  16    
HELIX   17  17 GLY B  198  GLN B  203  1                                   6    
HELIX   18  18 THR B  207  TYR B  225  1                                  19    
HELIX   19  19 GLN B  228  SER B  244  1                                  17    
HELIX   20  20 LEU B  249  GLU B  269  1                                  21    
HELIX   21  21 GLU B  274  THR B  282  1                                   9    
HELIX   22  22 THR B  287  LEU B  302  1                                  16    
HELIX   23  23 THR B  310  PHE B  319  1                                  10    
HELIX   24  24 LEU B  320  GLN B  322  5                                   3    
HELIX   25  25 ASN B  326  ASP B  343  1                                  18    
HELIX   26  26 ASP B  343  LEU B  348  1                                   6    
HELIX   27  27 LEU B  351  THR B  368  1                                  18    
HELIX   28  28 PRO B  373  GLY B  381  1                                   9    
HELIX   29  29 THR B  383  ALA B  401  1                                  19    
HELIX   30  30 PRO B  402  HIS B  404  5                                   3    
HELIX   31  31 GLN B  407  TYR B  413  1                                   7    
HELIX   32  32 LYS B  414  HIS B  419  5                                   6    
HELIX   33  33 GLY B  420  LEU B  424  5                                   5    
HELIX   34  34 PRO C   45  LEU C   58  1                                  14    
HELIX   35  35 LEU C   87  SER C   94  1                                   8    
HELIX   36  36 PRO C  100  HIS C  121  1                                  22    
HELIX   37  37 LYS C  129  GLN C  131  5                                   3    
HELIX   38  38 ASP C  145  ALA C  149  5                                   5    
HELIX   39  39 THR C  165  ARG C  169  5                                   5    
HELIX   40  40 ALA C  170  LEU C  175  1                                   6    
HELIX   41  41 THR C  182  ARG C  199  1                                  18    
HELIX   42  42 SER C  207  GLY C  220  1                                  14    
HELIX   43  43 ASP C  256  LEU C  267  1                                  12    
HELIX   44  44 SER C  276  LEU C  281  1                                   6    
HELIX   45  45 ALA C  282  GLN C  287  5                                   6    
HELIX   46  46 VAL D  175  ASP D  177  5                                   3    
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  GLY D  251  5                                   3    
HELIX   52  52 LYS D  252  GLU D  269  1                                  18    
HELIX   53  53 GLU D  274  THR D  282  1                                   9    
HELIX   54  54 THR D  287  LEU D  302  1                                  16    
HELIX   55  55 THR D  310  PHE D  319  1                                  10    
HELIX   56  56 LEU D  320  GLN D  322  5                                   3    
HELIX   57  57 ASN D  326  ASP D  343  1                                  18    
HELIX   58  58 ASP D  343  LEU D  348  1                                   6    
HELIX   59  59 LEU D  351  GLY D  369  1                                  19    
HELIX   60  60 PRO D  373  GLY D  381  1                                   9    
HELIX   61  61 THR D  383  LYS D  400  1                                  18    
HELIX   62  62 ALA D  401  HIS D  404  5                                   4    
HELIX   63  63 GLN D  407  TYR D  413  1                                   7    
HELIX   64  64 LYS D  414  HIS D  419  5                                   6    
HELIX   65  65 GLY D  420  LEU D  424  5                                   5    
SHEET    1  AA 5 PHE A   4  GLU A  12  0                                        
SHEET    2  AA 5 VAL A  17  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  GLU C  12  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  1.33  
LINK         C   TPO A 160                 N   HIS A 161     1555   1555  1.32  
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  
CISPEP   1 VAL A  154    PRO A  155          0        -7.07                     
CISPEP   2 GLN B  323    PRO B  324          0        -3.10                     
CISPEP   3 ASP B  345    PRO B  346          0         8.05                     
CISPEP   4 VAL C  154    PRO C  155          0        -2.08                     
CISPEP   5 GLN D  323    PRO D  324          0        -2.76                     
CISPEP   6 ASP D  345    PRO D  346          0         7.12                     
SITE     1 AC1 13 ILE A  10  GLY A  13  VAL A  18  ALA A  31                    
SITE     2 AC1 13 PHE A  80  GLU A  81  LEU A  83  HIS A  84                    
SITE     3 AC1 13 ASP A  86  ASN A 132  ASP A 145  HOH A2003                    
SITE     4 AC1 13 HOH A2005                                                     
SITE     1 AC2 15 ILE C  10  GLU C  12  GLY C  13  VAL C  18                    
SITE     2 AC2 15 ALA C  31  VAL C  64  PHE C  80  GLU C  81                    
SITE     3 AC2 15 LEU C  83  HIS C  84  ASP C  86  ASN C 132                    
SITE     4 AC2 15 ASP C 145  HOH C2003  HOH C2005                               
CRYST1   74.110  135.443  149.370  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      0.013493  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007383  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006695        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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