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Database: PDB
Entry: 2R7G
LinkDB: 2R7G
Original site: 2R7G 
HEADER    TRANSCRIPTION REPRESSOR, CELL CYCLE     07-SEP-07   2R7G              
TITLE     STRUCTURE OF THE RETINOBLASTOMA PROTEIN POCKET DOMAIN IN COMPLEX WITH 
TITLE    2 ADENOVIRUS E1A CR1 DOMAIN                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RETINOBLASTOMA-ASSOCIATED PROTEIN;                         
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: POCKET DOMAIN, DELETION OF RESIDUES 582-642;               
COMPND   5 SYNONYM: PP110; P105-RB; RB;                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: EARLY E1A 32 KDA PROTEIN;                                  
COMPND   9 CHAIN: B, D, E;                                                      
COMPND  10 FRAGMENT: CR1 DOMAIN;                                                
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: RB1;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX4T-1;                                 
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HUMAN ADENOVIRUS 5;                             
SOURCE  13 ORGANISM_TAXID: 28285;                                               
SOURCE  14 STRAIN: TYPE 5;                                                      
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PGEX4T-1                                  
KEYWDS    RETINOBLASTOMA PROTEIN, E1A, E2F DISPLACEMENT, TRANSCRIPTION          
KEYWDS   2 REPRESSOR, CELL CYCLE                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.LIU,R.MARMORSTEIN                                                   
REVDAT   7   21-FEB-24 2R7G    1       REMARK                                   
REVDAT   6   25-OCT-17 2R7G    1       REMARK                                   
REVDAT   5   26-JUL-17 2R7G    1       SOURCE REMARK                            
REVDAT   4   13-JUL-11 2R7G    1       VERSN                                    
REVDAT   3   24-FEB-09 2R7G    1       VERSN                                    
REVDAT   2   20-NOV-07 2R7G    1       JRNL                                     
REVDAT   1   02-OCT-07 2R7G    0                                                
JRNL        AUTH   X.LIU,R.MARMORSTEIN                                          
JRNL        TITL   STRUCTURE OF THE RETINOBLASTOMA PROTEIN BOUND TO ADENOVIRUS  
JRNL        TITL 2 E1A REVEALS THE MOLECULAR BASIS FOR VIRAL ONCOPROTEIN        
JRNL        TITL 3 INACTIVATION OF A TUMOR SUPPRESSOR                           
JRNL        REF    GENES DEV.                    V.  21  2711 2007              
JRNL        REFN                   ISSN 0890-9369                               
JRNL        PMID   17974914                                                     
JRNL        DOI    10.1101/GAD.1590607                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.67 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.67                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.82                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 115475                         
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) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 11573                           
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) : 1.67                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.71                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3627                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 81.81                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2710                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 403                          
REMARK   3   BIN FREE R VALUE                    : 0.3210                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5775                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 482                                     
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) : 28.03                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.16000                                             
REMARK   3    B22 (A**2) : 0.32000                                              
REMARK   3    B33 (A**2) : -0.09000                                             
REMARK   3    B12 (A**2) : 0.01000                                              
REMARK   3    B13 (A**2) : 0.09000                                              
REMARK   3    B23 (A**2) : 0.37000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.097         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.094         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.056         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.237         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5955 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8025 ; 1.256 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   699 ; 4.631 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   269 ;36.808 ;23.858       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1144 ;15.904 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    36 ;12.195 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   910 ; 0.104 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4326 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3281 ; 0.212 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4157 ; 0.308 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   552 ; 0.115 ; 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):    53 ; 0.213 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 0.212 ; 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):  3646 ; 0.860 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5766 ; 1.405 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2594 ; 2.206 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2259 ; 3.332 ; 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  : 5                                          
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   380        A   785                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.1055   0.2593   0.6307              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0437 T22:  -0.0448                                     
REMARK   3      T33:  -0.0399 T12:  -0.0009                                     
REMARK   3      T13:  -0.0189 T23:   0.0263                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8530 L22:   0.6726                                     
REMARK   3      L33:   1.2205 L12:  -0.0569                                     
REMARK   3      L13:  -0.0979 L23:   0.0403                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0388 S12:   0.1643 S13:   0.0659                       
REMARK   3      S21:  -0.2048 S22:  -0.0212 S23:   0.0906                       
REMARK   3      S31:   0.0317 S32:  -0.1991 S33:  -0.0176                       
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    40        B    49                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.6310  -5.2427  14.1492              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0571 T22:  -0.0612                                     
REMARK   3      T33:  -0.0494 T12:  -0.0373                                     
REMARK   3      T13:  -0.0242 T23:   0.0015                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.8664 L22:   3.4987                                     
REMARK   3      L33:   9.6675 L12:  -3.2532                                     
REMARK   3      L13:  -0.4844 L23:  -1.2412                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2488 S12:  -0.0847 S13:   0.0306                       
REMARK   3      S21:  -0.3015 S22:   0.0190 S23:   0.1953                       
REMARK   3      S31:   0.4032 S32:  -0.4823 S33:  -0.2678                       
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   380        C   785                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.9239 -13.6436  32.4229              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0549 T22:  -0.0291                                     
REMARK   3      T33:  -0.0414 T12:  -0.0015                                     
REMARK   3      T13:  -0.0258 T23:   0.0283                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9331 L22:   0.8510                                     
REMARK   3      L33:   1.1186 L12:  -0.0566                                     
REMARK   3      L13:  -0.0979 L23:   0.0049                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0003 S12:  -0.2900 S13:  -0.1018                       
REMARK   3      S21:   0.1523 S22:   0.0133 S23:  -0.0890                       
REMARK   3      S31:   0.1675 S32:   0.0427 S33:  -0.0131                       
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    40        D    49                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.7209 -21.4607  18.9919              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0344 T22:  -0.0686                                     
REMARK   3      T33:  -0.0559 T12:  -0.0408                                     
REMARK   3      T13:  -0.0084 T23:   0.0379                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7954 L22:   6.0318                                     
REMARK   3      L33:  10.4035 L12:  -4.4347                                     
REMARK   3      L13:   0.8894 L23:   0.5912                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0633 S12:  -0.4209 S13:  -0.1232                       
REMARK   3      S21:   0.0020 S22:   0.1471 S23:  -0.0427                       
REMARK   3      S31:   0.5732 S32:  -0.1259 S33:  -0.2103                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E    40        E    48                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.1919 -13.0292 -30.0390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0003 T22:   0.0002                                     
REMARK   3      T33:   0.0000 T12:   0.0001                                     
REMARK   3      T13:  -0.0003 T23:   0.0002                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.7415 L22:  13.8033                                     
REMARK   3      L33:  28.1912 L12:   5.5691                                     
REMARK   3      L13:  -3.0062 L23:  -0.2428                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0211 S12:   0.5892 S13:   0.0746                       
REMARK   3      S21:   0.5535 S22:   0.2573 S23:  -0.4185                       
REMARK   3      S31:   0.9577 S32:   0.0877 S33:  -0.2362                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2R7G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-SEP-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000044519.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-JUL-06                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.980                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 121240                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.671                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.0                               
REMARK 200  DATA REDUNDANCY                : 2.500                              
REMARK 200  R MERGE                    (I) : 0.03500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.67                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.73                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 56.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39200                            
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: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.43                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15MM MAGNESIUM ACETATE TETRAHYDRATE,     
REMARK 280  50MM SODIUM CACODYLATE TRIHYDRATE, PH 6.0 AND 1.7M AMMONIUM         
REMARK 280  SULFATE, VAPOR DIFFUSION, TEMPERATURE 293K                          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7240 ANGSTROM**2                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E                         
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     SER A   503                                                      
REMARK 465     GLN A   504                                                      
REMARK 465     ASN A   505                                                      
REMARK 465     LEU A   506                                                      
REMARK 465     ASP A   507                                                      
REMARK 465     SER A   508                                                      
REMARK 465     ARG A   579                                                      
REMARK 465     GLU A   580                                                      
REMARK 465     GLY A   581                                                      
REMARK 465     PRO A   786                                                      
REMARK 465     ARG A   787                                                      
REMARK 465     SER C   503                                                      
REMARK 465     GLN C   504                                                      
REMARK 465     ASN C   505                                                      
REMARK 465     LEU C   506                                                      
REMARK 465     ASP C   507                                                      
REMARK 465     SER C   508                                                      
REMARK 465     GLU C   580                                                      
REMARK 465     GLY C   581                                                      
REMARK 465     PRO C   786                                                      
REMARK 465     ARG C   787                                                      
REMARK 465     LEU E    49                                                      
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     GLN A 436    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 440    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 436    CG   CD   OE1  NE2                                  
REMARK 470     GLU C 440    CG   CD   OE1  OE2                                  
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    SER A 501      -95.15    -66.54                                   
REMARK 500    SER A 560      -47.03   -154.58                                   
REMARK 500    ILE A 744      -74.33    -95.68                                   
REMARK 500    GLU A 746      -87.60   -119.84                                   
REMARK 500    SER C 501      -86.78    -68.83                                   
REMARK 500    SER C 560      -48.16   -157.69                                   
REMARK 500    ASP C 718      -90.77    -52.81                                   
REMARK 500    LEU C 719       85.37     47.63                                   
REMARK 500    ILE C 744      -84.66   -101.33                                   
REMARK 500    GLU C 746     -108.31     52.40                                   
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 A 902                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 901                 
DBREF  2R7G A  380   581  UNP    P06400   RB_HUMAN       380    581             
DBREF  2R7G A  643   787  UNP    P06400   RB_HUMAN       643    787             
DBREF  2R7G B   40    49  UNP    P03255   E1A_ADE05       40     49             
DBREF  2R7G C  380   581  UNP    P06400   RB_HUMAN       380    581             
DBREF  2R7G C  643   787  UNP    P06400   RB_HUMAN       643    787             
DBREF  2R7G D   40    49  UNP    P03255   E1A_ADE05       40     49             
DBREF  2R7G E   40    49  UNP    P03255   E1A_ADE05       40     49             
SEQRES   1 A  347  ASN THR ILE GLN GLN LEU MET MET ILE LEU ASN SER ALA          
SEQRES   2 A  347  SER ASP GLN PRO SER GLU ASN LEU ILE SER TYR PHE ASN          
SEQRES   3 A  347  ASN CYS THR VAL ASN PRO LYS GLU SER ILE LEU LYS ARG          
SEQRES   4 A  347  VAL LYS ASP ILE GLY TYR ILE PHE LYS GLU LYS PHE ALA          
SEQRES   5 A  347  LYS ALA VAL GLY GLN GLY CYS VAL GLU ILE GLY SER GLN          
SEQRES   6 A  347  ARG TYR LYS LEU GLY VAL ARG LEU TYR TYR ARG VAL MET          
SEQRES   7 A  347  GLU SER MET LEU LYS SER GLU GLU GLU ARG LEU SER ILE          
SEQRES   8 A  347  GLN ASN PHE SER LYS LEU LEU ASN ASP ASN ILE PHE HIS          
SEQRES   9 A  347  MET SER LEU LEU ALA CYS ALA LEU GLU VAL VAL MET ALA          
SEQRES  10 A  347  THR TYR SER ARG SER THR SER GLN ASN LEU ASP SER GLY          
SEQRES  11 A  347  THR ASP LEU SER PHE PRO TRP ILE LEU ASN VAL LEU ASN          
SEQRES  12 A  347  LEU LYS ALA PHE ASP PHE TYR LYS VAL ILE GLU SER PHE          
SEQRES  13 A  347  ILE LYS ALA GLU GLY ASN LEU THR ARG GLU MET ILE LYS          
SEQRES  14 A  347  HIS LEU GLU ARG CYS GLU HIS ARG ILE MET GLU SER LEU          
SEQRES  15 A  347  ALA TRP LEU SER ASP SER PRO LEU PHE ASP LEU ILE LYS          
SEQRES  16 A  347  GLN SER LYS ASP ARG GLU GLY LYS SER THR SER LEU SER          
SEQRES  17 A  347  LEU PHE TYR LYS LYS VAL TYR ARG LEU ALA TYR LEU ARG          
SEQRES  18 A  347  LEU ASN THR LEU CYS GLU ARG LEU LEU SER GLU HIS PRO          
SEQRES  19 A  347  GLU LEU GLU HIS ILE ILE TRP THR LEU PHE GLN HIS THR          
SEQRES  20 A  347  LEU GLN ASN GLU TYR GLU LEU MET ARG ASP ARG HIS LEU          
SEQRES  21 A  347  ASP GLN ILE MET MET CYS SER MET TYR GLY ILE CYS LYS          
SEQRES  22 A  347  VAL LYS ASN ILE ASP LEU LYS PHE LYS ILE ILE VAL THR          
SEQRES  23 A  347  ALA TYR LYS ASP LEU PRO HIS ALA VAL GLN GLU THR PHE          
SEQRES  24 A  347  LYS ARG VAL LEU ILE LYS GLU GLU GLU TYR ASP SER ILE          
SEQRES  25 A  347  ILE VAL PHE TYR ASN SER VAL PHE MET GLN ARG LEU LYS          
SEQRES  26 A  347  THR ASN ILE LEU GLN TYR ALA SER THR ARG PRO PRO THR          
SEQRES  27 A  347  LEU SER PRO ILE PRO HIS ILE PRO ARG                          
SEQRES   1 B   10  PRO PRO THR LEU HIS GLU LEU TYR ASP LEU                      
SEQRES   1 C  347  ASN THR ILE GLN GLN LEU MET MET ILE LEU ASN SER ALA          
SEQRES   2 C  347  SER ASP GLN PRO SER GLU ASN LEU ILE SER TYR PHE ASN          
SEQRES   3 C  347  ASN CYS THR VAL ASN PRO LYS GLU SER ILE LEU LYS ARG          
SEQRES   4 C  347  VAL LYS ASP ILE GLY TYR ILE PHE LYS GLU LYS PHE ALA          
SEQRES   5 C  347  LYS ALA VAL GLY GLN GLY CYS VAL GLU ILE GLY SER GLN          
SEQRES   6 C  347  ARG TYR LYS LEU GLY VAL ARG LEU TYR TYR ARG VAL MET          
SEQRES   7 C  347  GLU SER MET LEU LYS SER GLU GLU GLU ARG LEU SER ILE          
SEQRES   8 C  347  GLN ASN PHE SER LYS LEU LEU ASN ASP ASN ILE PHE HIS          
SEQRES   9 C  347  MET SER LEU LEU ALA CYS ALA LEU GLU VAL VAL MET ALA          
SEQRES  10 C  347  THR TYR SER ARG SER THR SER GLN ASN LEU ASP SER GLY          
SEQRES  11 C  347  THR ASP LEU SER PHE PRO TRP ILE LEU ASN VAL LEU ASN          
SEQRES  12 C  347  LEU LYS ALA PHE ASP PHE TYR LYS VAL ILE GLU SER PHE          
SEQRES  13 C  347  ILE LYS ALA GLU GLY ASN LEU THR ARG GLU MET ILE LYS          
SEQRES  14 C  347  HIS LEU GLU ARG CYS GLU HIS ARG ILE MET GLU SER LEU          
SEQRES  15 C  347  ALA TRP LEU SER ASP SER PRO LEU PHE ASP LEU ILE LYS          
SEQRES  16 C  347  GLN SER LYS ASP ARG GLU GLY LYS SER THR SER LEU SER          
SEQRES  17 C  347  LEU PHE TYR LYS LYS VAL TYR ARG LEU ALA TYR LEU ARG          
SEQRES  18 C  347  LEU ASN THR LEU CYS GLU ARG LEU LEU SER GLU HIS PRO          
SEQRES  19 C  347  GLU LEU GLU HIS ILE ILE TRP THR LEU PHE GLN HIS THR          
SEQRES  20 C  347  LEU GLN ASN GLU TYR GLU LEU MET ARG ASP ARG HIS LEU          
SEQRES  21 C  347  ASP GLN ILE MET MET CYS SER MET TYR GLY ILE CYS LYS          
SEQRES  22 C  347  VAL LYS ASN ILE ASP LEU LYS PHE LYS ILE ILE VAL THR          
SEQRES  23 C  347  ALA TYR LYS ASP LEU PRO HIS ALA VAL GLN GLU THR PHE          
SEQRES  24 C  347  LYS ARG VAL LEU ILE LYS GLU GLU GLU TYR ASP SER ILE          
SEQRES  25 C  347  ILE VAL PHE TYR ASN SER VAL PHE MET GLN ARG LEU LYS          
SEQRES  26 C  347  THR ASN ILE LEU GLN TYR ALA SER THR ARG PRO PRO THR          
SEQRES  27 C  347  LEU SER PRO ILE PRO HIS ILE PRO ARG                          
SEQRES   1 D   10  PRO PRO THR LEU HIS GLU LEU TYR ASP LEU                      
SEQRES   1 E   10  PRO PRO THR LEU HIS GLU LEU TYR ASP LEU                      
HET    SO4  A 902       5                                                       
HET    SO4  C 901       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   6  SO4    2(O4 S 2-)                                                   
FORMUL   8  HOH   *482(H2 O)                                                    
HELIX    1   1 THR A  381  ALA A  392  1                                  12    
HELIX    2   2 SER A  397  ASN A  406  1                                  10    
HELIX    3   3 PRO A  411  GLY A  435  1                                  25    
HELIX    4   4 CYS A  438  SER A  469  1                                  32    
HELIX    5   5 PHE A  473  ASN A  478  1                                   6    
HELIX    6   6 ASP A  479  THR A  502  1                                  24    
HELIX    7   7 PRO A  515  ASN A  522  1                                   8    
HELIX    8   8 LYS A  524  LYS A  530  1                                   7    
HELIX    9   9 VAL A  531  GLU A  539  1                                   9    
HELIX   10  10 THR A  543  SER A  560  1                                  18    
HELIX   11  11 LEU A  561  LEU A  564  5                                   4    
HELIX   12  12 PRO A  568  ASP A  578  1                                  11    
HELIX   13  13 SER A  644  LEU A  670  1                                  27    
HELIX   14  14 GLU A  675  GLU A  691  1                                  17    
HELIX   15  15 TYR A  692  ARG A  696  5                                   5    
HELIX   16  16 HIS A  699  LYS A  715  1                                  17    
HELIX   17  17 LYS A  720  LYS A  729  1                                  10    
HELIX   18  18 GLN A  736  ARG A  741  1                                   6    
HELIX   19  19 SER A  751  VAL A  759  1                                   9    
HELIX   20  20 VAL A  759  TYR A  771  1                                  13    
HELIX   21  21 THR B   42  TYR B   47  1                                   6    
HELIX   22  22 THR C  381  ALA C  392  1                                  12    
HELIX   23  23 SER C  397  ASN C  406  1                                  10    
HELIX   24  24 PRO C  411  GLY C  435  1                                  25    
HELIX   25  25 CYS C  438  SER C  469  1                                  32    
HELIX   26  26 PHE C  473  ASN C  478  1                                   6    
HELIX   27  27 ASP C  479  THR C  502  1                                  24    
HELIX   28  28 PRO C  515  ASN C  522  1                                   8    
HELIX   29  29 LYS C  524  LYS C  530  1                                   7    
HELIX   30  30 VAL C  531  GLU C  539  1                                   9    
HELIX   31  31 THR C  543  SER C  560  1                                  18    
HELIX   32  32 LEU C  561  LEU C  564  5                                   4    
HELIX   33  33 PRO C  568  ARG C  579  1                                  12    
HELIX   34  34 SER C  644  LEU C  670  1                                  27    
HELIX   35  35 GLU C  675  GLU C  691  1                                  17    
HELIX   36  36 TYR C  692  ARG C  696  5                                   5    
HELIX   37  37 HIS C  699  LYS C  715  1                                  17    
HELIX   38  38 LYS C  720  LYS C  729  1                                  10    
HELIX   39  39 GLN C  736  ARG C  741  1                                   6    
HELIX   40  40 SER C  751  VAL C  759  1                                   9    
HELIX   41  41 VAL C  759  GLN C  770  1                                  12    
HELIX   42  42 TYR C  771  SER C  773  5                                   3    
HELIX   43  43 THR D   42  TYR D   47  1                                   6    
SHEET    1   A 2 VAL A 742  LEU A 743  0                                        
SHEET    2   A 2 TYR A 749  ASP A 750 -1  O  ASP A 750   N  VAL A 742           
SHEET    1   B 2 VAL C 742  LEU C 743  0                                        
SHEET    2   B 2 TYR C 749  ASP C 750 -1  O  ASP C 750   N  VAL C 742           
CISPEP   1 PHE A  514    PRO A  515          0         2.37                     
CISPEP   2 PHE C  514    PRO C  515          0         5.57                     
SITE     1 AC1 11 ASN A 406  CYS A 407  THR A 408  ASN A 472                    
SITE     2 AC1 11 PHE A 473  SER A 474  HOH A1001  HOH A1009                    
SITE     3 AC1 11 HOH A1087  LYS C 574  HOH C1076                               
SITE     1 AC2 11 LYS A 574  HOH A1060  ASN C 406  CYS C 407                    
SITE     2 AC2 11 THR C 408  ASN C 472  PHE C 473  SER C 474                    
SITE     3 AC2 11 HOH C1003  HOH C1011  HOH C1088                               
CRYST1   57.713   57.706   92.268  94.34  92.69 105.79 P 1           3          
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      0.017327  0.004899  0.001271        0.00000                         
SCALE2      0.000000  0.018009  0.001664        0.00000                         
SCALE3      0.000000  0.000000  0.010896        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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