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Database: PDB
Entry: 2EUF
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Original site: 2EUF 
HEADER    CELL CYCLE/TRANSFERASE                  28-OCT-05   2EUF              
TITLE     X-RAY STRUCTURE OF HUMAN CDK6-VCYCLIN IN COMPLEX WITH THE INHIBITOR   
TITLE    2 PD0332991                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: VIRAL CYCLIN;                                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: V-CYCLIN;                                                   
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: CELL DIVISION PROTEIN KINASE 6;                            
COMPND   8 CHAIN: B;                                                            
COMPND   9 FRAGMENT: FRAGMENT 1-308;                                            
COMPND  10 SYNONYM: CDK6, SERINE/THREONINE-PROTEIN KINASE PLSTIRE;              
COMPND  11 EC: 2.7.1.37;                                                        
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HERPESVIRUS SAIMIRI (STRAIN 11);                
SOURCE   3 ORGANISM_TAXID: 10383;                                               
SOURCE   4 STRAIN: 11;                                                          
SOURCE   5 GENE: 72, ECLF2;                                                     
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: CDK6;                                                          
SOURCE  14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  15 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    INHIBITOR COMPLEX OF HUMAN CYCLIN-DEPENDENT KINASE 6, CELL CYCLE-     
KEYWDS   2 TRANSFERASE COMPLEX                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    U.SCHULZE-GAHMEN,H.LU                                                 
REVDAT   3   13-JUL-11 2EUF    1       VERSN                                    
REVDAT   2   24-FEB-09 2EUF    1       VERSN                                    
REVDAT   1   04-JUL-06 2EUF    0                                                
JRNL        AUTH   H.LU,U.SCHULZE-GAHMEN                                        
JRNL        TITL   TOWARD UNDERSTANDING THE STRUCTURAL BASIS OF                 
JRNL        TITL 2 CYCLIN-DEPENDENT KINASE 6 SPECIFIC INHIBITION.               
JRNL        REF    J.MED.CHEM.                   V.  49  3826 2006              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   16789739                                                     
JRNL        DOI    10.1021/JM0600388                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0003                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 12886                          
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) : 0.233                           
REMARK   3   R VALUE            (WORKING SET) : 0.229                           
REMARK   3   FREE R VALUE                     : 0.306                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 675                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.08                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 619                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 63.41                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3270                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 24                           
REMARK   3   BIN FREE R VALUE                    : 0.3620                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4041                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 42                                      
REMARK   3   SOLVENT ATOMS            : 1                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 53.29                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.47000                                              
REMARK   3    B22 (A**2) : 2.47000                                              
REMARK   3    B33 (A**2) : -3.71000                                             
REMARK   3    B12 (A**2) : 1.24000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.537         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.428         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 51.630        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.933                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.859                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4163 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5672 ; 1.429 ; 1.974       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   522 ; 6.005 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   157 ;37.622 ;24.522       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   696 ;20.253 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;22.765 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   686 ; 0.107 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3047 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2169 ; 0.247 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2920 ; 0.318 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   148 ; 0.138 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    25 ; 0.174 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     2 ; 0.112 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2686 ; 0.406 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4246 ; 0.729 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1688 ; 0.939 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1426 ; 1.541 ; 4.500       
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  : 3                                          
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     9        A   254                          
REMARK   3    ORIGIN FOR THE GROUP (A):  39.3200  56.2600  55.1230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0417 T22:  -0.0500                                     
REMARK   3      T33:  -0.0806 T12:  -0.2162                                     
REMARK   3      T13:  -0.0929 T23:   0.1516                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7284 L22:   3.4102                                     
REMARK   3      L33:   5.9060 L12:   0.2756                                     
REMARK   3      L13:  -1.9384 L23:   1.2215                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0753 S12:  -0.4649 S13:   0.0451                       
REMARK   3      S21:  -0.2249 S22:  -0.3943 S23:  -0.4119                       
REMARK   3      S31:  -0.0463 S32:   0.2212 S33:   0.3189                       
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    10        B   100                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.5020  28.3780  59.5000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7844 T22:   0.1784                                     
REMARK   3      T33:   0.5583 T12:  -0.1308                                     
REMARK   3      T13:   0.0820 T23:   0.2768                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5788 L22:   5.8647                                     
REMARK   3      L33:   5.9654 L12:  -0.7385                                     
REMARK   3      L13:  -1.6028 L23:  -0.7814                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0628 S12:   0.0089 S13:  -1.2990                       
REMARK   3      S21:  -0.4112 S22:  -0.3283 S23:  -1.2060                       
REMARK   3      S31:   1.7825 S32:   0.4628 S33:   0.2655                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   101        B   305                          
REMARK   3    RESIDUE RANGE :   B   401        B   401                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.5060  32.3950  57.3900              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3924 T22:   0.4703                                     
REMARK   3      T33:   0.1852 T12:  -0.5414                                     
REMARK   3      T13:   0.0407 T23:  -0.0953                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3991 L22:   4.4705                                     
REMARK   3      L33:   4.3399 L12:   1.3487                                     
REMARK   3      L13:   0.4920 L23:  -1.0985                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1534 S12:  -0.1850 S13:  -0.5827                       
REMARK   3      S21:  -0.1730 S22:  -0.2110 S23:   0.7007                       
REMARK   3      S31:   1.1155 S32:  -1.0566 S33:   0.0576                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2EUF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-NOV-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB035105.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-MAY-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (TRUNCATE)                    
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13633                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 63.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM TRIS/HCL PH 8.0, 0.1 M             
REMARK 280  CAACETATE, 10% PEG3350, 10 MM DTT, VAPOR DIFFUSION, SITTING DROP,   
REMARK 280  TEMPERATURE 295K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      297.91733            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      148.95867            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      223.43800            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       74.47933            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      372.39667            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      297.91733            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      148.95867            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       74.47933            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      223.43800            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      372.39667            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5780 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22060 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     ASN A     6                                                      
REMARK 465     ARG A     7                                                      
REMARK 465     CYS A   124                                                      
REMARK 465     ASP A   125                                                      
REMARK 465     CYS A   126                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     LYS B     3                                                      
REMARK 465     ASP B     4                                                      
REMARK 465     GLY B     5                                                      
REMARK 465     LEU B     6                                                      
REMARK 465     CYS B     7                                                      
REMARK 465     ARG B     8                                                      
REMARK 465     ALA B     9                                                      
REMARK 465     ARG B   245                                                      
REMARK 465     ASP B   246                                                      
REMARK 465     VAL B   247                                                      
REMARK 465     ALA B   248                                                      
REMARK 465     LEU B   249                                                      
REMARK 465     PRO B   250                                                      
REMARK 465     ARG B   251                                                      
REMARK 465     GLN B   252                                                      
REMARK 465     ALA B   253                                                      
REMARK 465     PHE B   254                                                      
REMARK 465     HIS B   255                                                      
REMARK 465     SER B   256                                                      
REMARK 465     LYS B   257                                                      
REMARK 465     SER B   258                                                      
REMARK 465     CYS B   306                                                      
REMARK 465     LYS B   307                                                      
REMARK 465     GLU B   308                                                      
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     GLU A  42    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  92    CG   CD   CE   NZ                                   
REMARK 470     SER A 123    OG                                                  
REMARK 470     ASP A 210    CG   OD1  OD2                                       
REMARK 470     ASN A 213    CG   OD1                                            
REMARK 470     ARG A 215    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 221    CG   CD1  CD2                                       
REMARK 470     ASP B  10    CG   OD1  OD2                                       
REMARK 470     GLN B  11    CG   CD   OE1  NE2                                  
REMARK 470     GLN B  12    CG   CD   OE1  NE2                                  
REMARK 470     GLU B  14    CG   CD   OE1  OE2                                  
REMARK 470     CYS B  15    SG                                                  
REMARK 470     VAL B  16    CG1  CG2                                            
REMARK 470     GLU B  21    CG   CD   OE1  OE2                                  
REMARK 470     TYR B  24    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS B  26    CG   CD   CE   NZ                                   
REMARK 470     LYS B  29    CG   CD   CE   NZ                                   
REMARK 470     ARG B  31    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B  32    CG   OD1  OD2                                       
REMARK 470     LEU B  33    CG   CD1  CD2                                       
REMARK 470     ASN B  35    CG   OD1                                            
REMARK 470     ARG B  38    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B  40    CG1  CG2                                            
REMARK 470     ARG B  44    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  46    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  51    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  78    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     CYS B  83    SG                                                  
REMARK 470     ARG B  87    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR B  88    OG1  CG2                                            
REMARK 470     ARG B  90    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR B  92    OG1  CG2                                            
REMARK 470     LYS B  93    CG   CD   CE   NZ                                   
REMARK 470     THR B  95    OG1  CG2                                            
REMARK 470     LYS B 111    CG   CD   CE   NZ                                   
REMARK 470     LEU B 183    CG   CD1  CD2                                       
REMARK 470     GLN B 260    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 304    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 305    CG   CD   NE   CZ   NH1  NH2                        
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    LEU A   119     O    LEU A   122              2.17            
REMARK 500   CB   ALA B    23     O    HOH B   403              2.19            
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    ASP A  50   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP A  81   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP B 110   CB  -  CG  -  OD2 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ASP B 124   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP B 134   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 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    PHE A  37       94.28    -57.69                                   
REMARK 500    ILE A  43      -17.97    -46.18                                   
REMARK 500    GLU A  46      -65.49   -155.53                                   
REMARK 500    LEU A  84       33.67    -86.86                                   
REMARK 500    LYS A  92       21.72    -76.84                                   
REMARK 500    THR A  93      -11.62   -141.02                                   
REMARK 500    GLU A 136      -65.66    -94.20                                   
REMARK 500    TRP A 145        0.86     59.74                                   
REMARK 500    GLU A 148      177.76    -59.42                                   
REMARK 500    ASP A 210      101.54     72.97                                   
REMARK 500    CYS A 214     -151.37    -95.85                                   
REMARK 500    THR A 218      -56.02    -18.33                                   
REMARK 500    ASN A 229       38.26     80.80                                   
REMARK 500    ASP A 250      102.71   -165.61                                   
REMARK 500    VAL B  16     -101.71   -107.54                                   
REMARK 500    ILE B  19       36.71    -76.49                                   
REMARK 500    ASN B  35     -148.75    -69.31                                   
REMARK 500    ARG B  38     -167.00    -74.89                                   
REMARK 500    THR B  49       43.08    -65.65                                   
REMARK 500    GLU B  51       70.23    176.75                                   
REMARK 500    THR B  84      113.62     47.20                                   
REMARK 500    ARG B 144       32.90    -86.95                                   
REMARK 500    ASP B 145       42.46   -144.58                                   
REMARK 500    ASP B 163       92.34     38.68                                   
REMARK 500    PHE B 172      139.88    -37.33                                   
REMARK 500    GLN B 173       13.38     58.02                                   
REMARK 500    VAL B 181      142.49     54.99                                   
REMARK 500    ALA B 197     -130.27   -159.07                                   
REMARK 500    PHE B 209      -55.94    -27.86                                   
REMARK 500    ARG B 215       53.97    -67.69                                   
REMARK 500    SER B 222      -36.57   -149.07                                   
REMARK 500    VAL B 234      -72.41    -86.93                                   
REMARK 500    LEU B 281       46.13   -103.05                                   
REMARK 500    PRO B 298       -7.87    -40.03                                   
REMARK 500    LEU B 303     -129.58    -60.22                                   
REMARK 500    GLU B 304      -16.73    -49.84                                   
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 CA A 255                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 309                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LQQ B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 402                 
DBREF  2EUF A    1   254  UNP    Q01043   CGH2_SHV21       1    254             
DBREF  2EUF B    1   308  UNP    Q00534   CDK6_HUMAN       1    308             
SEQRES   1 A  254  MET ALA ASP SER PRO ASN ARG LEU ASN ARG ALA LYS ILE          
SEQRES   2 A  254  ASP SER THR THR MET LYS ASP PRO ARG VAL LEU ASN ASN          
SEQRES   3 A  254  LEU LYS LEU ARG GLU LEU LEU LEU PRO LYS PHE THR SER          
SEQRES   4 A  254  LEU TRP GLU ILE GLN THR GLU VAL THR VAL ASP ASN ARG          
SEQRES   5 A  254  THR ILE LEU LEU THR TRP MET HIS LEU LEU CYS GLU SER          
SEQRES   6 A  254  PHE GLU LEU ASP LYS SER VAL PHE PRO LEU SER VAL SER          
SEQRES   7 A  254  ILE LEU ASP ARG TYR LEU CYS LYS LYS GLN GLY THR LYS          
SEQRES   8 A  254  LYS THR LEU GLN LYS ILE GLY ALA ALA CYS VAL LEU ILE          
SEQRES   9 A  254  GLY SER LYS ILE ARG THR VAL LYS PRO MET THR VAL SER          
SEQRES  10 A  254  LYS LEU THR TYR LEU SER CYS ASP CYS PHE THR ASN LEU          
SEQRES  11 A  254  GLU LEU ILE ASN GLN GLU LYS ASP ILE LEU GLU ALA LEU          
SEQRES  12 A  254  LYS TRP ASP THR GLU ALA VAL LEU ALA THR ASP PHE LEU          
SEQRES  13 A  254  ILE PRO LEU CYS ASN ALA LEU LYS ILE PRO GLU ASP LEU          
SEQRES  14 A  254  TRP PRO GLN LEU TYR GLU ALA ALA SER THR THR ILE CYS          
SEQRES  15 A  254  LYS ALA LEU ILE GLN PRO ASN ILE ALA LEU LEU SER PRO          
SEQRES  16 A  254  GLY LEU ILE CYS ALA GLY GLY LEU LEU THR THR ILE GLU          
SEQRES  17 A  254  THR ASP ASN THR ASN CYS ARG PRO TRP THR CYS TYR LEU          
SEQRES  18 A  254  GLU ASP LEU SER SER ILE LEU ASN PHE SER THR ASN THR          
SEQRES  19 A  254  VAL ARG THR VAL LYS ASP GLN VAL SER GLU ALA PHE SER          
SEQRES  20 A  254  LEU TYR ASP LEU GLU ILE LEU                                  
SEQRES   1 B  308  MET GLU LYS ASP GLY LEU CYS ARG ALA ASP GLN GLN TYR          
SEQRES   2 B  308  GLU CYS VAL ALA GLU ILE GLY GLU GLY ALA TYR GLY LYS          
SEQRES   3 B  308  VAL PHE LYS ALA ARG ASP LEU LYS ASN GLY GLY ARG PHE          
SEQRES   4 B  308  VAL ALA LEU LYS ARG VAL ARG VAL GLN THR GLY GLU GLU          
SEQRES   5 B  308  GLY MET PRO LEU SER THR ILE ARG GLU VAL ALA VAL LEU          
SEQRES   6 B  308  ARG HIS LEU GLU THR PHE GLU HIS PRO ASN VAL VAL ARG          
SEQRES   7 B  308  LEU PHE ASP VAL CYS THR VAL SER ARG THR ASP ARG GLU          
SEQRES   8 B  308  THR LYS LEU THR LEU VAL PHE GLU HIS VAL ASP GLN ASP          
SEQRES   9 B  308  LEU THR THR TYR LEU ASP LYS VAL PRO GLU PRO GLY VAL          
SEQRES  10 B  308  PRO THR GLU THR ILE LYS ASP MET MET PHE GLN LEU LEU          
SEQRES  11 B  308  ARG GLY LEU ASP PHE LEU HIS SER HIS ARG VAL VAL HIS          
SEQRES  12 B  308  ARG ASP LEU LYS PRO GLN ASN ILE LEU VAL THR SER SER          
SEQRES  13 B  308  GLY GLN ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ILE          
SEQRES  14 B  308  TYR SER PHE GLN MET ALA LEU THR SER VAL VAL VAL THR          
SEQRES  15 B  308  LEU TRP TYR ARG ALA PRO GLU VAL LEU LEU GLN SER SER          
SEQRES  16 B  308  TYR ALA THR PRO VAL ASP LEU TRP SER VAL GLY CYS ILE          
SEQRES  17 B  308  PHE ALA GLU MET PHE ARG ARG LYS PRO LEU PHE ARG GLY          
SEQRES  18 B  308  SER SER ASP VAL ASP GLN LEU GLY LYS ILE LEU ASP VAL          
SEQRES  19 B  308  ILE GLY LEU PRO GLY GLU GLU ASP TRP PRO ARG ASP VAL          
SEQRES  20 B  308  ALA LEU PRO ARG GLN ALA PHE HIS SER LYS SER ALA GLN          
SEQRES  21 B  308  PRO ILE GLU LYS PHE VAL THR ASP ILE ASP GLU LEU GLY          
SEQRES  22 B  308  LYS ASP LEU LEU LEU LYS CYS LEU THR PHE ASN PRO ALA          
SEQRES  23 B  308  LYS ARG ILE SER ALA TYR SER ALA LEU SER HIS PRO TYR          
SEQRES  24 B  308  PHE GLN ASP LEU GLU ARG CYS LYS GLU                          
HET     CA  A 255       1                                                       
HET    ACT  B 309       4                                                       
HET    LQQ  B 401      33                                                       
HET    DMS  B 402       4                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     ACT ACETATE ION                                                      
HETNAM     LQQ 6-ACETYL-8-CYCLOPENTYL-5-METHYL-2-[(5-PIPERAZIN-1-               
HETNAM   2 LQQ  YLPYRIDIN-2-YL)AMINO]PYRIDO[2,3-D]PYRIMIDIN-7(8H)-ONE           
HETNAM     DMS DIMETHYL SULFOXIDE                                               
FORMUL   3   CA    CA 2+                                                        
FORMUL   4  ACT    C2 H3 O2 1-                                                  
FORMUL   5  LQQ    C24 H29 N7 O2                                                
FORMUL   6  DMS    C2 H6 O S                                                    
FORMUL   7  HOH   *(H2 O)                                                       
HELIX    1   1 ASP A   14  LYS A   19  1                                   6    
HELIX    2   2 ASP A   20  LEU A   32  1                                  13    
HELIX    3   3 THR A   48  PHE A   66  1                                  19    
HELIX    4   4 SER A   71  LYS A   87  1                                  17    
HELIX    5   5 THR A   90  THR A  110  1                                  21    
HELIX    6   6 THR A  115  LEU A  122  1                                   8    
HELIX    7   7 THR A  128  LEU A  143  1                                  16    
HELIX    8   8 LEU A  151  ASP A  154  5                                   4    
HELIX    9   9 PHE A  155  LEU A  163  1                                   9    
HELIX   10  10 PRO A  166  ASP A  168  5                                   3    
HELIX   11  11 LEU A  169  LEU A  185  1                                  17    
HELIX   12  12 ILE A  186  LEU A  193  5                                   8    
HELIX   13  13 SER A  194  THR A  209  1                                  16    
HELIX   14  14 PRO A  216  CYS A  219  5                                   4    
HELIX   15  15 TYR A  220  ASN A  229  1                                  10    
HELIX   16  16 SER A  231  LEU A  248  1                                  18    
HELIX   17  17 ASP A  250  LEU A  254  5                                   5    
HELIX   18  18 PRO B   55  GLU B   69  1                                  15    
HELIX   19  19 THR B   70  GLU B   72  5                                   3    
HELIX   20  20 LEU B  105  VAL B  112  1                                   8    
HELIX   21  21 PRO B  118  HIS B  139  1                                  22    
HELIX   22  22 THR B  182  ARG B  186  5                                   5    
HELIX   23  23 ALA B  187  LEU B  192  1                                   6    
HELIX   24  24 THR B  198  ARG B  214  1                                  17    
HELIX   25  25 SER B  223  GLY B  236  1                                  14    
HELIX   26  26 PRO B  261  PHE B  265  5                                   5    
HELIX   27  27 ASP B  270  LEU B  281  1                                  12    
HELIX   28  28 SER B  290  HIS B  297  1                                   8    
SHEET    1   A 2 ASN A   9  ARG A  10  0                                        
SHEET    2   A 2 ALA B 175  LEU B 176 -1  O  LEU B 176   N  ASN A   9           
SHEET    1   B 5 TYR B  13  CYS B  15  0                                        
SHEET    2   B 5 LYS B  26  ASP B  32 -1  O  ARG B  31   N  GLU B  14           
SHEET    3   B 5 PHE B  39  VAL B  45 -1  O  VAL B  40   N  ALA B  30           
SHEET    4   B 5 LEU B  94  GLU B  99 -1  O  LEU B  96   N  LYS B  43           
SHEET    5   B 5 LEU B  79  VAL B  82 -1  N  PHE B  80   O  VAL B  97           
SHEET    1   C 3 GLN B 103  ASP B 104  0                                        
SHEET    2   C 3 ILE B 151  VAL B 153 -1  O  VAL B 153   N  GLN B 103           
SHEET    3   C 3 ILE B 159  LEU B 161 -1  O  LYS B 160   N  LEU B 152           
SHEET    1   D 2 VAL B 141  VAL B 142  0                                        
SHEET    2   D 2 ARG B 168  ILE B 169 -1  O  ARG B 168   N  VAL B 142           
LINK        CA    CA A 255                 OG1 THR A 110     1555   1555  3.22  
CISPEP   1 GLU B  114    PRO B  115          0         0.89                     
SITE     1 AC1  2 THR A 110  LYS A 112                                          
SITE     1 AC2  8 HIS B 143  ARG B 144  ASP B 145  ASP B 163                    
SITE     2 AC2  8 PHE B 164  GLY B 165  LEU B 166  ALA B 167                    
SITE     1 AC3 12 ILE B  19  VAL B  77  PHE B  98  GLU B  99                    
SITE     2 AC3 12 VAL B 101  ASP B 102  GLN B 103  THR B 107                    
SITE     3 AC3 12 GLN B 149  LEU B 152  ALA B 162  ASP B 163                    
SITE     1 AC4  6 LEU B  68  GLU B  69  GLU B  72  HIS B  73                    
SITE     2 AC4  6 VAL B  76  VAL B  77                                          
CRYST1   71.146   71.146  446.876  90.00  90.00 120.00 P 65 2 2     12          
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      0.014056  0.008115  0.000000        0.00000                         
SCALE2      0.000000  0.016230  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002238        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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