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Database: PDB
Entry: 2F2C
LinkDB: 2F2C
Original site: 2F2C 
HEADER    CELL CYCLE/TRANSFERASE                  16-NOV-05   2F2C              
TITLE     X-RAY STRUCTURE OF HUMAN CDK6-VCYCLINWITH THE INHIBITOR               
TITLE    2 AMINOPURVALANOL                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN HOMOLOG;                                            
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: 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    SMALL MOLECULE INHIBITOR BOUND BETWEEN N-TERMINAL AND C-TERMINAL      
KEYWDS   2 DOMAIN OF KINASE, CELL CYCLE-TRANSFERASE COMPLEX                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    U.SCHULZE-GAHMEN,H.LU                                                 
REVDAT   5   24-JAN-18 2F2C    1       AUTHOR                                   
REVDAT   4   13-JUL-11 2F2C    1       VERSN                                    
REVDAT   3   24-FEB-09 2F2C    1       VERSN                                    
REVDAT   2   04-JUL-06 2F2C    1       JRNL                                     
REVDAT   1   13-JUN-06 2F2C    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.    2.80 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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 16516                          
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) : 0.241                           
REMARK   3   R VALUE            (WORKING SET) : 0.238                           
REMARK   3   FREE R VALUE                     : 0.301                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 893                             
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) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1193                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.92                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3360                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 75                           
REMARK   3   BIN FREE R VALUE                    : 0.4330                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4022                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 37                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 73.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.26000                                              
REMARK   3    B22 (A**2) : 1.26000                                              
REMARK   3    B33 (A**2) : -1.89000                                             
REMARK   3    B12 (A**2) : 0.63000                                              
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): 2.645         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.430         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.352         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 40.424        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.919                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.885                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4135 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5632 ; 1.366 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   516 ; 5.967 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   155 ;39.205 ;24.452       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   689 ;19.410 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;23.686 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   688 ; 0.092 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3001 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1952 ; 0.242 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2869 ; 0.310 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   111 ; 0.160 ; 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):    31 ; 0.311 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     2 ; 0.201 ; 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):  2671 ; 0.420 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4219 ; 0.750 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1661 ; 1.126 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1413 ; 1.815 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 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     8        A   254                          
REMARK   3    ORIGIN FOR THE GROUP (A):  39.0180  56.9210  55.4360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0871 T22:  -0.1197                                     
REMARK   3      T33:  -0.2157 T12:  -0.2842                                     
REMARK   3      T13:  -0.1111 T23:   0.1257                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0183 L22:   3.4437                                     
REMARK   3      L33:   5.1685 L12:   0.0785                                     
REMARK   3      L13:  -1.4720 L23:   1.3204                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1437 S12:  -0.3962 S13:   0.0363                       
REMARK   3      S21:  -0.2811 S22:  -0.3423 S23:  -0.3717                       
REMARK   3      S31:  -0.1574 S32:   0.2211 S33:   0.1985                       
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     9        B   100                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.6590  28.8950  60.4500              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4387 T22:   0.1423                                     
REMARK   3      T33:   0.5223 T12:  -0.2244                                     
REMARK   3      T13:  -0.0503 T23:   0.3440                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5569 L22:   5.3557                                     
REMARK   3      L33:   5.5882 L12:  -2.0697                                     
REMARK   3      L13:  -0.2830 L23:  -0.2764                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2361 S12:  -0.3511 S13:  -1.2430                       
REMARK   3      S21:  -0.3598 S22:  -0.4861 S23:  -0.9184                       
REMARK   3      S31:   1.3079 S32:   0.8997 S33:   0.2500                       
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):  14.7040  32.9970  58.2900              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1728 T22:   0.2934                                     
REMARK   3      T33:   0.0280 T12:  -0.5464                                     
REMARK   3      T13:  -0.0721 T23:  -0.0049                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8667 L22:   4.7619                                     
REMARK   3      L33:   4.1350 L12:   2.2213                                     
REMARK   3      L13:  -0.2251 L23:  -0.9814                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1428 S12:  -0.4321 S13:  -0.5909                       
REMARK   3      S21:  -0.2184 S22:  -0.2242 S23:   0.4535                       
REMARK   3      S31:   0.9360 S32:  -1.1089 S33:   0.0814                       
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 2F2C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-DEC-05.                  
REMARK 100 THE DEPOSITION ID IS D_1000035365.                                   
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                             : 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                       : 5.0.1                              
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 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (TRUNCATE)                    
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17833                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.780                              
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     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.78                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.88                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 1.0                                
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   (%): 52.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM TRIS/HCL PH 8.0, 0.1 M CAOAC,      
REMARK 280  13% PEG 3350, 10 MM DTT, 0.1M SULFOBETAINE, 1MM INHIBITOR, VAPOR    
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
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      299.53133            
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      149.76567            
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      224.64850            
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       74.88283            
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      374.41417            
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      299.53133            
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      149.76567            
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       74.88283            
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      224.64850            
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      374.41417            
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: 5570 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22630 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     VAL B    16                                                      
REMARK 465     GLU B    21                                                      
REMARK 465     GLY B    22                                                      
REMARK 465     ALA B    23                                                      
REMARK 465     TYR B    24                                                      
REMARK 465     ARG B    87                                                      
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     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 211    CG   OD1  ND2                                       
REMARK 470     THR A 212    OG1  CG2                                            
REMARK 470     ASN A 213    CG   OD1  ND2                                       
REMARK 470     ARG A 215    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 221    CG   CD1  CD2                                       
REMARK 470     GLU B  14    CG   CD   OE1  OE2                                  
REMARK 470     CYS B  15    SG                                                  
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     LYS B  34    CG   CD   CE   NZ                                   
REMARK 470     ASN B  35    CG   OD1  ND2                                       
REMARK 470     ARG B  38    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE B  39    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG B  44    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     THR B  88    OG1  CG2                                            
REMARK 470     ARG B  90    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  91    CG   CD   OE1  OE2                                  
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     ASP B 110    CG   OD1  OD2                                       
REMARK 470     LYS B 111    CD   CE   NZ                                        
REMARK 470     LYS B 216    CG   CD   CE   NZ                                   
REMARK 470     GLN B 252    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 260    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 271    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 274    CG   CD   CE   NZ                                   
REMARK 470     GLN B 301    CG   CD   OE1  NE2                                  
REMARK 470     ASP B 302    CG   OD1  OD2                                       
REMARK 470     ARG B 305    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU B 114   CD    GLU B 114   OE1     0.146                       
REMARK 500    GLU B 114   CD    GLU B 114   OE2     0.188                       
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  20   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    LEU A  34   CA  -  CB  -  CG  ANGL. DEV. =  15.0 DEGREES          
REMARK 500    ASP A  50   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP A 223   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP B 124   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP B 201   CB  -  CG  -  OD2 ANGL. DEV. =   7.3 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    LEU A  32        4.74    -65.15                                   
REMARK 500    GLU A  46      -94.48    -97.25                                   
REMARK 500    VAL A  47      137.39    -35.43                                   
REMARK 500    SER A 117       15.80    -61.99                                   
REMARK 500    THR A 120      -77.50    -65.26                                   
REMARK 500    TYR A 121      -33.95    -39.68                                   
REMARK 500    LEU A 122       61.25   -100.98                                   
REMARK 500    LEU A 185       -9.97    -56.31                                   
REMARK 500    GLU A 208      -73.59    -64.15                                   
REMARK 500    ASP A 210       63.58     75.02                                   
REMARK 500    THR A 212       96.75     49.89                                   
REMARK 500    ASN A 213       55.53     35.00                                   
REMARK 500    THR A 218      -63.41    -26.94                                   
REMARK 500    CYS A 219       -4.91    -58.35                                   
REMARK 500    ASN A 229       40.47     78.42                                   
REMARK 500    ASP A 250      106.71   -166.63                                   
REMARK 500    GLN B  12       -2.76     54.64                                   
REMARK 500    ASN B  35     -175.92    -68.07                                   
REMARK 500    ARG B  38     -147.76    -73.71                                   
REMARK 500    GLU B  51      -98.06   -133.54                                   
REMARK 500    GLU B  72       41.92     28.12                                   
REMARK 500    THR B  84      -14.08     78.29                                   
REMARK 500    VAL B  85      129.46    -39.49                                   
REMARK 500    PRO B 113     -169.00    -52.12                                   
REMARK 500    GLU B 114     -144.58    -63.11                                   
REMARK 500    PRO B 115       22.68    -11.47                                   
REMARK 500    ARG B 144       47.09   -106.02                                   
REMARK 500    ASP B 145       34.90   -163.10                                   
REMARK 500    SER B 156       34.81    -81.48                                   
REMARK 500    ASP B 163       92.44     48.55                                   
REMARK 500    PHE B 172      132.40    -36.53                                   
REMARK 500    SER B 178       39.60    -89.86                                   
REMARK 500    VAL B 181      144.60     71.15                                   
REMARK 500    ALA B 197     -147.98   -147.24                                   
REMARK 500    VAL B 234      -66.37    -95.26                                   
REMARK 500    ALA B 253     -137.93    -87.48                                   
REMARK 500    GLN B 260      101.51     61.72                                   
REMARK 500    ASP B 268       -4.28     91.99                                   
REMARK 500    LEU B 281       49.00   -100.17                                   
REMARK 500    PRO B 298      -11.88    -43.11                                   
REMARK 500    ASP B 302       21.76    -79.53                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU B  114     PRO B  115                 -132.55                    
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 SO4 B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AP9 B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 403                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2EUF   RELATED DB: PDB                                   
DBREF  2F2C A    1   254  UNP    Q01043   CGH2_SHV21       1    254             
DBREF  2F2C 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    SO4  B 402       5                                                       
HET    AP9  B 401      28                                                       
HET    DMS  B 403       4                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     AP9 (2S)-2-({6-[(3-AMINO-5-CHLOROPHENYL)AMINO]-9-ISOPROPYL-          
HETNAM   2 AP9  9H-PURIN-2-YL}AMINO)-3-METHYLBUTAN-1-OL                         
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETSYN     AP9 AMINOPURVALANOL                                                  
FORMUL   3  SO4    O4 S 2-                                                      
FORMUL   4  AP9    C19 H26 CL N7 O                                              
FORMUL   5  DMS    C2 H6 O S                                                    
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  LEU A   84  1                                  14    
HELIX    5   5 THR A   93  THR A  110  1                                  18    
HELIX    6   6 THR A  115  THR A  120  1                                   6    
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  ALA A  191  5                                   6    
HELIX   13  13 SER A  194  THR A  209  1                                  16    
HELIX   14  14 TRP A  217  ASN A  229  1                                  13    
HELIX   15  15 SER A  231  LEU A  248  1                                  18    
HELIX   16  16 ASP A  250  LEU A  254  5                                   5    
HELIX   17  17 PRO B   55  GLU B   69  1                                  15    
HELIX   18  18 THR B   70  GLU B   72  5                                   3    
HELIX   19  19 LEU B  105  VAL B  112  1                                   8    
HELIX   20  20 PRO B  118  SER B  138  1                                  21    
HELIX   21  21 LYS B  147  GLN B  149  5                                   3    
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  215  1                                  18    
HELIX   25  25 SER B  223  GLY B  236  1                                  14    
HELIX   26  26 GLY B  239  TRP B  243  5                                   5    
HELIX   27  27 PRO B  261  PHE B  265  5                                   5    
HELIX   28  28 ASP B  270  LEU B  281  1                                  12    
HELIX   29  29 ASN B  284  ARG B  288  5                                   5    
HELIX   30  30 SER B  290  LEU B  295  1                                   6    
SHEET    1   A 5 TYR B  13  GLU B  14  0                                        
SHEET    2   A 5 LYS B  26  ASP B  32 -1  O  ARG B  31   N  GLU B  14           
SHEET    3   A 5 VAL B  40  VAL B  45 -1  O  VAL B  40   N  ALA B  30           
SHEET    4   A 5 LEU B  94  GLU B  99 -1  O  PHE B  98   N  ALA B  41           
SHEET    5   A 5 LEU B  79  VAL B  82 -1  N  PHE B  80   O  VAL B  97           
SHEET    1   B 3 GLN B 103  ASP B 104  0                                        
SHEET    2   B 3 ILE B 151  VAL B 153 -1  O  VAL B 153   N  GLN B 103           
SHEET    3   B 3 ILE B 159  LEU B 161 -1  O  LYS B 160   N  LEU B 152           
SHEET    1   C 2 VAL B 141  VAL B 142  0                                        
SHEET    2   C 2 ARG B 168  ILE B 169 -1  O  ARG B 168   N  VAL B 142           
SITE     1 AC1  9 VAL A 111  ARG B  60  ARG B 144  ARG B 168                    
SITE     2 AC1  9 MET B 174  ALA B 175  LEU B 176  THR B 177                    
SITE     3 AC1  9 TYR B 196                                                     
SITE     1 AC2 14 ILE B  19  GLY B  20  VAL B  27  ALA B  41                    
SITE     2 AC2 14 VAL B  77  PHE B  98  GLU B  99  VAL B 101                    
SITE     3 AC2 14 ASP B 102  GLN B 103  ASP B 104  THR B 107                    
SITE     4 AC2 14 GLN B 149  LEU B 152                                          
SITE     1 AC3  5 LEU B  65  LEU B  68  GLU B  69  HIS B  73                    
SITE     2 AC3  5 VAL B  77                                                     
CRYST1   71.517   71.517  449.297  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      0.013983  0.008073  0.000000        0.00000                         
SCALE2      0.000000  0.016146  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002226        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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