GenomeNet

Database: PDB
Entry: 3G33
LinkDB: 3G33
Original site: 3G33 
HEADER    CELL CYCLE                              01-FEB-09   3G33              
TITLE     CRYSTAL STRUCTURE OF CDK4/CYCLIN D3                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELL DIVISION PROTEIN KINASE 4;                            
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: CYCLIN-DEPENDENT KINASE 4, PSK-J3;                          
COMPND   5 EC: 2.7.11.22;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CCND3 PROTEIN;                                             
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 SYNONYM: CYCLIN D3, ISOFORM CRA_B;                                   
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CDK4;                                                          
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: CCND3, HCG_16683;                                              
SOURCE  13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    SER/THR PROTEIN KINASE, CELL CYCLE, PHOSPHORYLATION, ATP-BINDING,     
KEYWDS   2 CELL DIVISION, DISEASE MUTATION, KINASE, NUCLEOTIDE-BINDING,         
KEYWDS   3 PHOSPHOPROTEIN, PROTO-ONCOGENE, SERINE/THREONINE-PROTEIN KINASE,     
KEYWDS   4 TRANSFERASE, CYCLIN                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.TAKAKI,A.ECHALIER,N.R.BROWN,T.HUNT,J.A.ENDICOTT,M.E.M.NOBLE         
REVDAT   5   23-AUG-17 3G33    1       REMARK                                   
REVDAT   4   13-JUL-11 3G33    1       VERSN                                    
REVDAT   3   05-MAY-09 3G33    1       REMARK                                   
REVDAT   2   31-MAR-09 3G33    1       JRNL                                     
REVDAT   1   10-MAR-09 3G33    0                                                
JRNL        AUTH   T.TAKAKI,A.ECHALIER,N.R.BROWN,T.HUNT,J.A.ENDICOTT,M.E.NOBLE  
JRNL        TITL   THE STRUCTURE OF CDK4/CYCLIN D3 HAS IMPLICATIONS FOR MODELS  
JRNL        TITL 2 OF CDK ACTIVATION.                                           
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 106  4171 2009              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   19237555                                                     
JRNL        DOI    10.1073/PNAS.0809674106                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0066                                      
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) : 47.19                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 27629                          
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) : 0.283                           
REMARK   3   R VALUE            (WORKING SET) : 0.281                           
REMARK   3   FREE R VALUE                     : 0.314                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1481                            
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) : 1874                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.00                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3830                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 105                          
REMARK   3   BIN FREE R VALUE                    : 0.4030                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8158                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
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) : 105.0                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.49                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.52000                                              
REMARK   3    B22 (A**2) : 0.52000                                              
REMARK   3    B33 (A**2) : -1.04000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
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): 0.525         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.524         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 66.121        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.911                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.888                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8338 ; 0.002 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11308 ; 0.535 ; 1.980       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1033 ; 3.192 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   362 ;25.668 ;22.652       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1417 ;13.552 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    78 ;10.749 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1273 ; 0.040 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6288 ; 0.002 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5187 ; 0.086 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8358 ; 0.164 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3151 ; 0.193 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2950 ; 0.366 ; 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  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    10        A   300                          
REMARK   3    ORIGIN FOR THE GROUP (A): -36.0750 -11.7890 -57.3300              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8573 T22:   1.1888                                     
REMARK   3      T33:   0.8488 T12:  -0.0174                                     
REMARK   3      T13:   0.1633 T23:   0.2822                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8369 L22:   6.9305                                     
REMARK   3      L33:   3.2763 L12:  -1.3441                                     
REMARK   3      L13:  -0.1460 L23:  -0.6397                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3881 S12:   0.7594 S13:   1.3832                       
REMARK   3      S21:  -0.8861 S22:  -0.1450 S23:  -0.3146                       
REMARK   3      S31:  -1.0026 S32:  -0.1431 S33:  -0.2431                       
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    23        B   254                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.5150 -34.0510 -36.0310              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0176 T22:   0.8555                                     
REMARK   3      T33:   0.5252 T12:   0.0231                                     
REMARK   3      T13:   0.0072 T23:   0.0492                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.1367 L22:   4.4302                                     
REMARK   3      L33:   7.7190 L12:   0.4989                                     
REMARK   3      L13:  -2.2395 L23:  -2.7664                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1136 S12:  -0.8110 S13:   0.3792                       
REMARK   3      S21:   0.2510 S22:   0.0400 S23:  -0.1256                       
REMARK   3      S31:  -0.0790 S32:   0.3434 S33:   0.0735                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    10        C   300                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.3460 -48.4840 -65.0100              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4651 T22:   1.0576                                     
REMARK   3      T33:   0.8480 T12:  -0.0334                                     
REMARK   3      T13:   0.0641 T23:   0.1192                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2557 L22:   5.8803                                     
REMARK   3      L33:   5.6216 L12:   0.9590                                     
REMARK   3      L13:   0.3839 L23:   2.2541                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0746 S12:   0.6060 S13:  -1.1003                       
REMARK   3      S21:  -0.7416 S22:   0.2123 S23:  -0.1372                       
REMARK   3      S31:   0.5124 S32:   0.1497 S33:  -0.1378                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    23        D   254                          
REMARK   3    ORIGIN FOR THE GROUP (A): -20.2490 -37.7210 -36.8100              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0502 T22:   0.7822                                     
REMARK   3      T33:   0.4456 T12:   0.0011                                     
REMARK   3      T13:   0.0567 T23:   0.1236                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.9099 L22:   3.5887                                     
REMARK   3      L33:   9.6925 L12:  -0.0866                                     
REMARK   3      L13:   1.0079 L23:   0.7657                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0502 S12:  -0.4965 S13:  -0.1712                       
REMARK   3      S21:  -0.0493 S22:  -0.0770 S23:   0.0567                       
REMARK   3      S31:   0.4448 S32:   0.1352 S33:   0.0269                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3G33 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-FEB-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000051361.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-NOV-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97650                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM Q315R                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29147                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 57.830                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : 0.03900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.8000                            
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) : 3.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.50700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, 15% PEG 3,350, 10%          
REMARK 280  TACSIMATE, PH 6.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE       
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       70.64850            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       70.64850            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       71.76500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       70.64850            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       70.64850            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       71.76500            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       70.64850            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       70.64850            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       71.76500            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       70.64850            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       70.64850            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       71.76500            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7170 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 47220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     MET A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     THR A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     HIS A   301                                                      
REMARK 465     LYS A   302                                                      
REMARK 465     ASP A   303                                                      
REMARK 465     GLU A   304                                                      
REMARK 465     GLY A   305                                                      
REMARK 465     ASN A   306                                                      
REMARK 465     PRO A   307                                                      
REMARK 465     GLU A   308                                                      
REMARK 465     MET B   -13                                                      
REMARK 465     ASP B   -12                                                      
REMARK 465     TYR B   -11                                                      
REMARK 465     LYS B   -10                                                      
REMARK 465     ASP B    -9                                                      
REMARK 465     ASP B    -8                                                      
REMARK 465     ASP B    -7                                                      
REMARK 465     ASP B    -6                                                      
REMARK 465     LYS B    -5                                                      
REMARK 465     SER B    -4                                                      
REMARK 465     PRO B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     LEU B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     CYS B     5                                                      
REMARK 465     CYS B     6                                                      
REMARK 465     GLU B     7                                                      
REMARK 465     GLY B     8                                                      
REMARK 465     THR B     9                                                      
REMARK 465     ARG B    10                                                      
REMARK 465     HIS B    11                                                      
REMARK 465     ALA B    12                                                      
REMARK 465     PRO B    13                                                      
REMARK 465     ARG B    14                                                      
REMARK 465     ALA B    15                                                      
REMARK 465     GLY B    16                                                      
REMARK 465     PRO B    17                                                      
REMARK 465     ASP B    18                                                      
REMARK 465     PRO B    19                                                      
REMARK 465     ARG B    20                                                      
REMARK 465     LEU B    21                                                      
REMARK 465     LEU B    22                                                      
REMARK 465     ALA B   217                                                      
REMARK 465     CYS B   218                                                      
REMARK 465     SER B   219                                                      
REMARK 465     LEU B   255                                                      
REMARK 465     ARG B   256                                                      
REMARK 465     GLU B   257                                                      
REMARK 465     ALA B   258                                                      
REMARK 465     ALA B   259                                                      
REMARK 465     GLN B   260                                                      
REMARK 465     THR B   261                                                      
REMARK 465     SER B   262                                                      
REMARK 465     SER B   263                                                      
REMARK 465     SER B   264                                                      
REMARK 465     PRO B   265                                                      
REMARK 465     ALA B   266                                                      
REMARK 465     PRO B   267                                                      
REMARK 465     LYS B   268                                                      
REMARK 465     ALA B   269                                                      
REMARK 465     PRO B   270                                                      
REMARK 465     ARG B   271                                                      
REMARK 465     GLY B   272                                                      
REMARK 465     SER B   273                                                      
REMARK 465     SER B   274                                                      
REMARK 465     SER B   275                                                      
REMARK 465     GLN B   276                                                      
REMARK 465     GLY B   277                                                      
REMARK 465     PRO B   278                                                      
REMARK 465     SER B   279                                                      
REMARK 465     GLN B   280                                                      
REMARK 465     THR B   281                                                      
REMARK 465     SER B   282                                                      
REMARK 465     THR B   283                                                      
REMARK 465     PRO B   284                                                      
REMARK 465     THR B   285                                                      
REMARK 465     ASP B   286                                                      
REMARK 465     VAL B   287                                                      
REMARK 465     THR B   288                                                      
REMARK 465     ALA B   289                                                      
REMARK 465     ILE B   290                                                      
REMARK 465     HIS B   291                                                      
REMARK 465     LEU B   292                                                      
REMARK 465     GLY C     1                                                      
REMARK 465     PRO C     2                                                      
REMARK 465     LEU C     3                                                      
REMARK 465     GLY C     4                                                      
REMARK 465     SER C     5                                                      
REMARK 465     MET C     6                                                      
REMARK 465     ALA C     7                                                      
REMARK 465     THR C     8                                                      
REMARK 465     SER C     9                                                      
REMARK 465     HIS C   301                                                      
REMARK 465     LYS C   302                                                      
REMARK 465     ASP C   303                                                      
REMARK 465     GLU C   304                                                      
REMARK 465     GLY C   305                                                      
REMARK 465     ASN C   306                                                      
REMARK 465     PRO C   307                                                      
REMARK 465     GLU C   308                                                      
REMARK 465     MET D   -13                                                      
REMARK 465     ASP D   -12                                                      
REMARK 465     TYR D   -11                                                      
REMARK 465     LYS D   -10                                                      
REMARK 465     ASP D    -9                                                      
REMARK 465     ASP D    -8                                                      
REMARK 465     ASP D    -7                                                      
REMARK 465     ASP D    -6                                                      
REMARK 465     LYS D    -5                                                      
REMARK 465     SER D    -4                                                      
REMARK 465     PRO D    -3                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     SER D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLU D     2                                                      
REMARK 465     LEU D     3                                                      
REMARK 465     LEU D     4                                                      
REMARK 465     CYS D     5                                                      
REMARK 465     CYS D     6                                                      
REMARK 465     GLU D     7                                                      
REMARK 465     GLY D     8                                                      
REMARK 465     THR D     9                                                      
REMARK 465     ARG D    10                                                      
REMARK 465     HIS D    11                                                      
REMARK 465     ALA D    12                                                      
REMARK 465     PRO D    13                                                      
REMARK 465     ARG D    14                                                      
REMARK 465     ALA D    15                                                      
REMARK 465     GLY D    16                                                      
REMARK 465     PRO D    17                                                      
REMARK 465     ASP D    18                                                      
REMARK 465     PRO D    19                                                      
REMARK 465     ARG D    20                                                      
REMARK 465     LEU D    21                                                      
REMARK 465     LEU D    22                                                      
REMARK 465     ALA D   217                                                      
REMARK 465     CYS D   218                                                      
REMARK 465     SER D   219                                                      
REMARK 465     MET D   220                                                      
REMARK 465     LEU D   255                                                      
REMARK 465     ARG D   256                                                      
REMARK 465     GLU D   257                                                      
REMARK 465     ALA D   258                                                      
REMARK 465     ALA D   259                                                      
REMARK 465     GLN D   260                                                      
REMARK 465     THR D   261                                                      
REMARK 465     SER D   262                                                      
REMARK 465     SER D   263                                                      
REMARK 465     SER D   264                                                      
REMARK 465     PRO D   265                                                      
REMARK 465     ALA D   266                                                      
REMARK 465     PRO D   267                                                      
REMARK 465     LYS D   268                                                      
REMARK 465     ALA D   269                                                      
REMARK 465     PRO D   270                                                      
REMARK 465     ARG D   271                                                      
REMARK 465     GLY D   272                                                      
REMARK 465     SER D   273                                                      
REMARK 465     SER D   274                                                      
REMARK 465     SER D   275                                                      
REMARK 465     GLN D   276                                                      
REMARK 465     GLY D   277                                                      
REMARK 465     PRO D   278                                                      
REMARK 465     SER D   279                                                      
REMARK 465     GLN D   280                                                      
REMARK 465     THR D   281                                                      
REMARK 465     SER D   282                                                      
REMARK 465     THR D   283                                                      
REMARK 465     PRO D   284                                                      
REMARK 465     THR D   285                                                      
REMARK 465     ASP D   286                                                      
REMARK 465     VAL D   287                                                      
REMARK 465     THR D   288                                                      
REMARK 465     ALA D   289                                                      
REMARK 465     ILE D   290                                                      
REMARK 465     HIS D   291                                                      
REMARK 465     LEU D   292                                                      
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     ARG A  90    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 125    CD1  CD2                                            
REMARK 470     PRO A 239    CG   CD                                             
REMARK 470     GLU A 240    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 241    CG   OD1  OD2                                       
REMARK 470     THR B  94    CG2                                                 
REMARK 470     THR B 116    CG2                                                 
REMARK 470     THR B 117    CG2                                                 
REMARK 470     THR B 120    CG2                                                 
REMARK 470     ARG C  90    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU C 125    CD1  CD2                                            
REMARK 470     PRO C 239    CG   CD                                             
REMARK 470     GLU C 240    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 241    CG   OD1  OD2                                       
REMARK 470     THR D  94    CG2                                                 
REMARK 470     THR D 116    CG2                                                 
REMARK 470     THR D 117    CG2                                                 
REMARK 470     THR D 120    CG2                                                 
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   CG1  VAL B    48     CD1  ILE B    52              1.51            
REMARK 500   CG1  VAL D    48     CD1  ILE D    52              1.51            
REMARK 500   CB   VAL B    48     CD1  ILE B    52              1.74            
REMARK 500   CB   VAL D    48     CD1  ILE D    52              1.75            
REMARK 500   CG1  VAL D    48     CG1  ILE D    52              1.89            
REMARK 500   CG1  VAL B    48     CG1  ILE B    52              1.89            
REMARK 500   CB   GLU C   189     OG   SER C   194              1.98            
REMARK 500   O    HIS C   143     OD1  ASP C   201              2.11            
REMARK 500   O    HIS A   143     OD1  ASP A   201              2.12            
REMARK 500   OE1  GLU B   141     CG   LEU C    54              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CG2  VAL C    19     CG2  VAL C    19     8554     1.50            
REMARK 500   NH1  ARG A   257     CB   ALA C   175     7554     2.10            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A  31       -5.84    -57.08                                   
REMARK 500    HIS A  32      -63.56    -97.47                                   
REMARK 500    LYS A 111       58.46   -102.73                                   
REMARK 500    ASP A 145       82.50   -152.65                                   
REMARK 500    LYS A 147      149.98   -174.09                                   
REMARK 500    PRO A 148      -17.67    -47.91                                   
REMARK 500    PHE A 164      -74.88    -95.76                                   
REMARK 500    LEU A 176        1.32    108.74                                   
REMARK 500    SER A 194      -70.85    -70.35                                   
REMARK 500    PRO A 199       -4.58    -58.53                                   
REMARK 500    ARG A 214      -38.63   -133.93                                   
REMARK 500    PRO A 217      146.66    -36.71                                   
REMARK 500    SER A 223     -161.27   -118.06                                   
REMARK 500    ASP A 246       66.51     60.88                                   
REMARK 500    LEU A 281       40.27    -96.58                                   
REMARK 500    GLN A 296       42.84   -101.30                                   
REMARK 500    PRO B  40      133.54    -37.86                                   
REMARK 500    TRP B 150       16.65     56.68                                   
REMARK 500    LEU B 161      -72.49    -46.66                                   
REMARK 500    ARG B 167       35.05    -87.15                                   
REMARK 500    PRO C  31       -5.76    -57.41                                   
REMARK 500    HIS C  32      -63.73    -97.54                                   
REMARK 500    LYS C 111       58.50   -102.78                                   
REMARK 500    ASP C 145       82.59   -152.34                                   
REMARK 500    PRO C 148      -17.62    -48.18                                   
REMARK 500    PHE C 164      -75.01    -95.59                                   
REMARK 500    GLN C 193       56.62     34.60                                   
REMARK 500    TYR C 196      161.27    -41.65                                   
REMARK 500    PRO C 199       -4.20    -58.55                                   
REMARK 500    ARG C 214      -38.73   -134.10                                   
REMARK 500    PRO C 217      146.50    -36.76                                   
REMARK 500    SER C 223     -161.13   -117.83                                   
REMARK 500    ASP C 246       66.61     60.63                                   
REMARK 500    LEU C 281       40.38    -96.63                                   
REMARK 500    GLN C 296       42.87   -101.51                                   
REMARK 500    PRO D  40      133.74    -37.37                                   
REMARK 500    TRP D 150       15.42     56.89                                   
REMARK 500    LEU D 161      -72.83    -46.50                                   
REMARK 500    ARG D 167       35.20    -87.30                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3G33 A    6   308  UNP    P11802   CDK4_HUMAN       1    303             
DBREF  3G33 B    1   292  UNP    Q6FG62   Q6FG62_HUMAN     1    292             
DBREF  3G33 C    6   308  UNP    P11802   CDK4_HUMAN       1    303             
DBREF  3G33 D    1   292  UNP    Q6FG62   Q6FG62_HUMAN     1    292             
SEQADV 3G33 GLY A    1  UNP  P11802              EXPRESSION TAG                 
SEQADV 3G33 PRO A    2  UNP  P11802              EXPRESSION TAG                 
SEQADV 3G33 LEU A    3  UNP  P11802              EXPRESSION TAG                 
SEQADV 3G33 GLY A    4  UNP  P11802              EXPRESSION TAG                 
SEQADV 3G33 SER A    5  UNP  P11802              EXPRESSION TAG                 
SEQADV 3G33 MET B  -13  UNP  Q6FG62              EXPRESSION TAG                 
SEQADV 3G33 ASP B  -12  UNP  Q6FG62              EXPRESSION TAG                 
SEQADV 3G33 TYR B  -11  UNP  Q6FG62              EXPRESSION TAG                 
SEQADV 3G33 LYS B  -10  UNP  Q6FG62              EXPRESSION TAG                 
SEQADV 3G33 ASP B   -9  UNP  Q6FG62              EXPRESSION TAG                 
SEQADV 3G33 ASP B   -8  UNP  Q6FG62              EXPRESSION TAG                 
SEQADV 3G33 ASP B   -7  UNP  Q6FG62              EXPRESSION TAG                 
SEQADV 3G33 ASP B   -6  UNP  Q6FG62              EXPRESSION TAG                 
SEQADV 3G33 LYS B   -5  UNP  Q6FG62              EXPRESSION TAG                 
SEQADV 3G33 SER B   -4  UNP  Q6FG62              EXPRESSION TAG                 
SEQADV 3G33 PRO B   -3  UNP  Q6FG62              EXPRESSION TAG                 
SEQADV 3G33 GLY B   -2  UNP  Q6FG62              EXPRESSION TAG                 
SEQADV 3G33 GLY B   -1  UNP  Q6FG62              EXPRESSION TAG                 
SEQADV 3G33 SER B    0  UNP  Q6FG62              EXPRESSION TAG                 
SEQADV 3G33 GLY C    1  UNP  P11802              EXPRESSION TAG                 
SEQADV 3G33 PRO C    2  UNP  P11802              EXPRESSION TAG                 
SEQADV 3G33 LEU C    3  UNP  P11802              EXPRESSION TAG                 
SEQADV 3G33 GLY C    4  UNP  P11802              EXPRESSION TAG                 
SEQADV 3G33 SER C    5  UNP  P11802              EXPRESSION TAG                 
SEQADV 3G33 MET D  -13  UNP  Q6FG62              EXPRESSION TAG                 
SEQADV 3G33 ASP D  -12  UNP  Q6FG62              EXPRESSION TAG                 
SEQADV 3G33 TYR D  -11  UNP  Q6FG62              EXPRESSION TAG                 
SEQADV 3G33 LYS D  -10  UNP  Q6FG62              EXPRESSION TAG                 
SEQADV 3G33 ASP D   -9  UNP  Q6FG62              EXPRESSION TAG                 
SEQADV 3G33 ASP D   -8  UNP  Q6FG62              EXPRESSION TAG                 
SEQADV 3G33 ASP D   -7  UNP  Q6FG62              EXPRESSION TAG                 
SEQADV 3G33 ASP D   -6  UNP  Q6FG62              EXPRESSION TAG                 
SEQADV 3G33 LYS D   -5  UNP  Q6FG62              EXPRESSION TAG                 
SEQADV 3G33 SER D   -4  UNP  Q6FG62              EXPRESSION TAG                 
SEQADV 3G33 PRO D   -3  UNP  Q6FG62              EXPRESSION TAG                 
SEQADV 3G33 GLY D   -2  UNP  Q6FG62              EXPRESSION TAG                 
SEQADV 3G33 GLY D   -1  UNP  Q6FG62              EXPRESSION TAG                 
SEQADV 3G33 SER D    0  UNP  Q6FG62              EXPRESSION TAG                 
SEQRES   1 A  308  GLY PRO LEU GLY SER MET ALA THR SER ARG TYR GLU PRO          
SEQRES   2 A  308  VAL ALA GLU ILE GLY VAL GLY ALA TYR GLY THR VAL TYR          
SEQRES   3 A  308  LYS ALA ARG ASP PRO HIS SER GLY HIS PHE VAL ALA LEU          
SEQRES   4 A  308  LYS SER VAL ARG VAL PRO ASN GLY GLY GLY GLY GLY GLY          
SEQRES   5 A  308  GLY LEU PRO ILE SER THR VAL ARG GLU VAL ALA LEU LEU          
SEQRES   6 A  308  ARG ARG LEU GLU ALA PHE GLU HIS PRO ASN VAL VAL ARG          
SEQRES   7 A  308  LEU MET ASP VAL CYS ALA THR SER ARG THR ASP ARG GLU          
SEQRES   8 A  308  ILE LYS VAL THR LEU VAL PHE GLU HIS VAL ASP GLN ASP          
SEQRES   9 A  308  LEU ARG THR TYR LEU ASP LYS ALA PRO PRO PRO GLY LEU          
SEQRES  10 A  308  PRO ALA GLU THR ILE LYS ASP LEU MET ARG GLN PHE LEU          
SEQRES  11 A  308  ARG GLY LEU ASP PHE LEU HIS ALA ASN CYS ILE VAL HIS          
SEQRES  12 A  308  ARG ASP LEU LYS PRO GLU ASN ILE LEU VAL THR SER GLY          
SEQRES  13 A  308  GLY THR VAL LYS LEU ALA ASP PHE GLY LEU ALA ARG ILE          
SEQRES  14 A  308  TYR SER TYR GLN MET ALA LEU THR PRO VAL VAL VAL THR          
SEQRES  15 A  308  LEU TRP TYR ARG ALA PRO GLU VAL LEU LEU GLN SER THR          
SEQRES  16 A  308  TYR ALA THR PRO VAL ASP MET TRP SER VAL GLY CYS ILE          
SEQRES  17 A  308  PHE ALA GLU MET PHE ARG ARG LYS PRO LEU PHE CYS GLY          
SEQRES  18 A  308  ASN SER GLU ALA ASP GLN LEU GLY LYS ILE PHE ASP LEU          
SEQRES  19 A  308  ILE GLY LEU PRO PRO GLU ASP ASP TRP PRO ARG ASP VAL          
SEQRES  20 A  308  SER LEU PRO ARG GLY ALA PHE PRO PRO ARG GLY PRO ARG          
SEQRES  21 A  308  PRO VAL GLN SER VAL VAL PRO GLU MET GLU GLU SER GLY          
SEQRES  22 A  308  ALA GLN LEU LEU LEU GLU MET LEU THR PHE ASN PRO HIS          
SEQRES  23 A  308  LYS ARG ILE SER ALA PHE ARG ALA LEU GLN HIS SER TYR          
SEQRES  24 A  308  LEU HIS LYS ASP GLU GLY ASN PRO GLU                          
SEQRES   1 B  306  MET ASP TYR LYS ASP ASP ASP ASP LYS SER PRO GLY GLY          
SEQRES   2 B  306  SER MET GLU LEU LEU CYS CYS GLU GLY THR ARG HIS ALA          
SEQRES   3 B  306  PRO ARG ALA GLY PRO ASP PRO ARG LEU LEU GLY ASP GLN          
SEQRES   4 B  306  ARG VAL LEU GLN SER LEU LEU ARG LEU GLU GLU ARG TYR          
SEQRES   5 B  306  VAL PRO ARG ALA SER TYR PHE GLN CYS VAL GLN ARG GLU          
SEQRES   6 B  306  ILE LYS PRO HIS MET ARG LYS MET LEU ALA TYR TRP MET          
SEQRES   7 B  306  LEU GLU VAL CYS GLU GLU GLN ARG CYS GLU GLU GLU VAL          
SEQRES   8 B  306  PHE PRO LEU ALA MET ASN TYR LEU ASP ARG TYR LEU SER          
SEQRES   9 B  306  CYS VAL PRO THR ARG LYS ALA GLN LEU GLN LEU LEU GLY          
SEQRES  10 B  306  ALA VAL CYS MET LEU LEU ALA SER LYS LEU ARG GLU THR          
SEQRES  11 B  306  THR PRO LEU THR ILE GLU LYS LEU CYS ILE TYR THR ASP          
SEQRES  12 B  306  HIS ALA VAL SER PRO ARG GLN LEU ARG ASP TRP GLU VAL          
SEQRES  13 B  306  LEU VAL LEU GLY LYS LEU LYS TRP ASP LEU ALA ALA VAL          
SEQRES  14 B  306  ILE ALA HIS ASP PHE LEU ALA PHE ILE LEU HIS ARG LEU          
SEQRES  15 B  306  SER LEU PRO ARG ASP ARG GLN ALA LEU VAL LYS LYS HIS          
SEQRES  16 B  306  ALA GLN THR PHE LEU ALA LEU CYS ALA THR ASP TYR THR          
SEQRES  17 B  306  PHE ALA MET TYR PRO PRO SER MET ILE ALA THR GLY SER          
SEQRES  18 B  306  ILE GLY ALA ALA VAL GLN GLY LEU GLY ALA CYS SER MET          
SEQRES  19 B  306  SER GLY ASP GLU LEU THR GLU LEU LEU ALA GLY ILE THR          
SEQRES  20 B  306  GLY THR GLU VAL ASP CYS LEU ARG ALA CYS GLN GLU GLN          
SEQRES  21 B  306  ILE GLU ALA ALA LEU ARG GLU SER LEU ARG GLU ALA ALA          
SEQRES  22 B  306  GLN THR SER SER SER PRO ALA PRO LYS ALA PRO ARG GLY          
SEQRES  23 B  306  SER SER SER GLN GLY PRO SER GLN THR SER THR PRO THR          
SEQRES  24 B  306  ASP VAL THR ALA ILE HIS LEU                                  
SEQRES   1 C  308  GLY PRO LEU GLY SER MET ALA THR SER ARG TYR GLU PRO          
SEQRES   2 C  308  VAL ALA GLU ILE GLY VAL GLY ALA TYR GLY THR VAL TYR          
SEQRES   3 C  308  LYS ALA ARG ASP PRO HIS SER GLY HIS PHE VAL ALA LEU          
SEQRES   4 C  308  LYS SER VAL ARG VAL PRO ASN GLY GLY GLY GLY GLY GLY          
SEQRES   5 C  308  GLY LEU PRO ILE SER THR VAL ARG GLU VAL ALA LEU LEU          
SEQRES   6 C  308  ARG ARG LEU GLU ALA PHE GLU HIS PRO ASN VAL VAL ARG          
SEQRES   7 C  308  LEU MET ASP VAL CYS ALA THR SER ARG THR ASP ARG GLU          
SEQRES   8 C  308  ILE LYS VAL THR LEU VAL PHE GLU HIS VAL ASP GLN ASP          
SEQRES   9 C  308  LEU ARG THR TYR LEU ASP LYS ALA PRO PRO PRO GLY LEU          
SEQRES  10 C  308  PRO ALA GLU THR ILE LYS ASP LEU MET ARG GLN PHE LEU          
SEQRES  11 C  308  ARG GLY LEU ASP PHE LEU HIS ALA ASN CYS ILE VAL HIS          
SEQRES  12 C  308  ARG ASP LEU LYS PRO GLU ASN ILE LEU VAL THR SER GLY          
SEQRES  13 C  308  GLY THR VAL LYS LEU ALA ASP PHE GLY LEU ALA ARG ILE          
SEQRES  14 C  308  TYR SER TYR GLN MET ALA LEU THR PRO VAL VAL VAL THR          
SEQRES  15 C  308  LEU TRP TYR ARG ALA PRO GLU VAL LEU LEU GLN SER THR          
SEQRES  16 C  308  TYR ALA THR PRO VAL ASP MET TRP SER VAL GLY CYS ILE          
SEQRES  17 C  308  PHE ALA GLU MET PHE ARG ARG LYS PRO LEU PHE CYS GLY          
SEQRES  18 C  308  ASN SER GLU ALA ASP GLN LEU GLY LYS ILE PHE ASP LEU          
SEQRES  19 C  308  ILE GLY LEU PRO PRO GLU ASP ASP TRP PRO ARG ASP VAL          
SEQRES  20 C  308  SER LEU PRO ARG GLY ALA PHE PRO PRO ARG GLY PRO ARG          
SEQRES  21 C  308  PRO VAL GLN SER VAL VAL PRO GLU MET GLU GLU SER GLY          
SEQRES  22 C  308  ALA GLN LEU LEU LEU GLU MET LEU THR PHE ASN PRO HIS          
SEQRES  23 C  308  LYS ARG ILE SER ALA PHE ARG ALA LEU GLN HIS SER TYR          
SEQRES  24 C  308  LEU HIS LYS ASP GLU GLY ASN PRO GLU                          
SEQRES   1 D  306  MET ASP TYR LYS ASP ASP ASP ASP LYS SER PRO GLY GLY          
SEQRES   2 D  306  SER MET GLU LEU LEU CYS CYS GLU GLY THR ARG HIS ALA          
SEQRES   3 D  306  PRO ARG ALA GLY PRO ASP PRO ARG LEU LEU GLY ASP GLN          
SEQRES   4 D  306  ARG VAL LEU GLN SER LEU LEU ARG LEU GLU GLU ARG TYR          
SEQRES   5 D  306  VAL PRO ARG ALA SER TYR PHE GLN CYS VAL GLN ARG GLU          
SEQRES   6 D  306  ILE LYS PRO HIS MET ARG LYS MET LEU ALA TYR TRP MET          
SEQRES   7 D  306  LEU GLU VAL CYS GLU GLU GLN ARG CYS GLU GLU GLU VAL          
SEQRES   8 D  306  PHE PRO LEU ALA MET ASN TYR LEU ASP ARG TYR LEU SER          
SEQRES   9 D  306  CYS VAL PRO THR ARG LYS ALA GLN LEU GLN LEU LEU GLY          
SEQRES  10 D  306  ALA VAL CYS MET LEU LEU ALA SER LYS LEU ARG GLU THR          
SEQRES  11 D  306  THR PRO LEU THR ILE GLU LYS LEU CYS ILE TYR THR ASP          
SEQRES  12 D  306  HIS ALA VAL SER PRO ARG GLN LEU ARG ASP TRP GLU VAL          
SEQRES  13 D  306  LEU VAL LEU GLY LYS LEU LYS TRP ASP LEU ALA ALA VAL          
SEQRES  14 D  306  ILE ALA HIS ASP PHE LEU ALA PHE ILE LEU HIS ARG LEU          
SEQRES  15 D  306  SER LEU PRO ARG ASP ARG GLN ALA LEU VAL LYS LYS HIS          
SEQRES  16 D  306  ALA GLN THR PHE LEU ALA LEU CYS ALA THR ASP TYR THR          
SEQRES  17 D  306  PHE ALA MET TYR PRO PRO SER MET ILE ALA THR GLY SER          
SEQRES  18 D  306  ILE GLY ALA ALA VAL GLN GLY LEU GLY ALA CYS SER MET          
SEQRES  19 D  306  SER GLY ASP GLU LEU THR GLU LEU LEU ALA GLY ILE THR          
SEQRES  20 D  306  GLY THR GLU VAL ASP CYS LEU ARG ALA CYS GLN GLU GLN          
SEQRES  21 D  306  ILE GLU ALA ALA LEU ARG GLU SER LEU ARG GLU ALA ALA          
SEQRES  22 D  306  GLN THR SER SER SER PRO ALA PRO LYS ALA PRO ARG GLY          
SEQRES  23 D  306  SER SER SER GLN GLY PRO SER GLN THR SER THR PRO THR          
SEQRES  24 D  306  ASP VAL THR ALA ILE HIS LEU                                  
HELIX    1   1 PRO A   55  GLU A   72  1                                  18    
HELIX    2   2 ASP A  104  LYS A  111  1                                   8    
HELIX    3   3 PRO A  118  ASN A  139  1                                  22    
HELIX    4   4 LEU A  176  VAL A  181  5                                   6    
HELIX    5   5 ALA A  187  GLN A  193  1                                   7    
HELIX    6   6 PRO A  199  MET A  212  1                                  14    
HELIX    7   7 SER A  223  GLY A  236  1                                  14    
HELIX    8   8 PRO A  250  PHE A  254  5                                   5    
HELIX    9   9 PRO A  261  VAL A  266  1                                   6    
HELIX   10  10 GLU A  270  LEU A  281  1                                  12    
HELIX   11  11 SER A  290  GLN A  296  1                                   7    
HELIX   12  12 GLY B   23  GLU B   35  1                                  13    
HELIX   13  13 GLU B   36  VAL B   39  5                                   4    
HELIX   14  14 LYS B   53  GLN B   71  1                                  19    
HELIX   15  15 GLU B   76  VAL B   92  1                                  17    
HELIX   16  16 ARG B   95  ALA B   97  5                                   3    
HELIX   17  17 GLN B   98  GLU B  115  1                                  18    
HELIX   18  18 GLU B  122  THR B  128  1                                   7    
HELIX   19  19 SER B  133  LEU B  148  1                                  16    
HELIX   20  20 ILE B  156  ASP B  159  5                                   4    
HELIX   21  21 PHE B  160  ARG B  167  1                                   8    
HELIX   22  22 ARG B  174  ASP B  192  1                                  19    
HELIX   23  23 TYR B  193  ALA B  196  5                                   4    
HELIX   24  24 PRO B  199  GLY B  214  1                                  16    
HELIX   25  25 SER B  221  GLY B  234  1                                  14    
HELIX   26  26 GLU B  236  GLU B  253  1                                  18    
HELIX   27  27 PRO C   55  GLU C   72  1                                  18    
HELIX   28  28 ASP C  104  LYS C  111  1                                   8    
HELIX   29  29 PRO C  118  ASN C  139  1                                  22    
HELIX   30  30 LEU C  166  THR C  177  1                                  12    
HELIX   31  31 ALA C  187  LEU C  192  1                                   6    
HELIX   32  32 PRO C  199  MET C  212  1                                  14    
HELIX   33  33 SER C  223  GLY C  236  1                                  14    
HELIX   34  34 PRO C  250  PHE C  254  5                                   5    
HELIX   35  35 PRO C  261  VAL C  266  1                                   6    
HELIX   36  36 GLU C  270  LEU C  281  1                                  12    
HELIX   37  37 SER C  290  GLN C  296  1                                   7    
HELIX   38  38 GLY D   23  GLU D   35  1                                  13    
HELIX   39  39 GLU D   36  VAL D   39  5                                   4    
HELIX   40  40 LYS D   53  GLN D   71  1                                  19    
HELIX   41  41 GLU D   76  VAL D   92  1                                  17    
HELIX   42  42 ARG D   95  ALA D   97  5                                   3    
HELIX   43  43 GLN D   98  GLU D  115  1                                  18    
HELIX   44  44 GLU D  122  THR D  128  1                                   7    
HELIX   45  45 SER D  133  LEU D  148  1                                  16    
HELIX   46  46 ILE D  156  ASP D  159  5                                   4    
HELIX   47  47 PHE D  160  ARG D  167  1                                   8    
HELIX   48  48 ARG D  174  ASP D  192  1                                  19    
HELIX   49  49 TYR D  193  ALA D  196  5                                   4    
HELIX   50  50 PRO D  199  GLY D  214  1                                  16    
HELIX   51  51 GLY D  222  GLY D  234  1                                  13    
HELIX   52  52 GLU D  236  GLU D  253  1                                  18    
SHEET    1   A 5 GLU A  12  ILE A  17  0                                        
SHEET    2   A 5 VAL A  25  ARG A  29 -1  O  ARG A  29   N  GLU A  12           
SHEET    3   A 5 PHE A  36  PRO A  45 -1  O  VAL A  37   N  ALA A  28           
SHEET    4   A 5 GLU A  91  GLU A  99 -1  O  ILE A  92   N  VAL A  44           
SHEET    5   A 5 LEU A  79  THR A  85 -1  N  CYS A  83   O  THR A  95           
SHEET    1   B 2 ILE A 151  VAL A 153  0                                        
SHEET    2   B 2 VAL A 159  LEU A 161 -1  O  LYS A 160   N  LEU A 152           
SHEET    1   C 5 GLU C  12  ILE C  17  0                                        
SHEET    2   C 5 VAL C  25  ARG C  29 -1  O  ARG C  29   N  GLU C  12           
SHEET    3   C 5 PHE C  36  PRO C  45 -1  O  VAL C  37   N  ALA C  28           
SHEET    4   C 5 GLU C  91  GLU C  99 -1  O  ILE C  92   N  VAL C  44           
SHEET    5   C 5 LEU C  79  THR C  85 -1  N  CYS C  83   O  THR C  95           
SHEET    1   D 2 ILE C 151  VAL C 153  0                                        
SHEET    2   D 2 VAL C 159  LEU C 161 -1  O  LYS C 160   N  LEU C 152           
CRYST1  141.297  141.297  143.530  90.00  90.00  90.00 P 42 21 2    16          
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      0.007077  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007077  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006967        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system