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Database: PDB
Entry: 2AZE
LinkDB: 2AZE
Original site: 2AZE 
HEADER    CELL CYCLE, TRANSCRIPTION               10-SEP-05   2AZE              
TITLE     STRUCTURE OF THE RB C-TERMINAL DOMAIN BOUND TO AN E2F1-DP1            
TITLE    2 HETERODIMER                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRANSCRIPTION FACTOR DP-1;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: COILED COIL AND MARKED BOX DOMAINS (RESIDUES 199-          
COMPND   5 350);                                                                
COMPND   6 SYNONYM: E2F DIMERIZATION PARTNER 1, DRTF1-POLYPEPTIDE-1,            
COMPND   7 DRTF1;                                                               
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: TRANSCRIPTION FACTOR E2F1;                                 
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: COILED COIL AND MARKED BOX DOMAINS (RESIDUES 200-          
COMPND  13 301);                                                                
COMPND  14 SYNONYM: E2F-1, RETINOBLASTOMA BINDING PROTEIN 3, RBBP-3,            
COMPND  15 PRB-BINDING PROTEIN E2F-1, PBR3, RETINOBLASTOMA-ASSOCIATED           
COMPND  16 PROTEIN 1, RBAP-1;                                                   
COMPND  17 ENGINEERED: YES;                                                     
COMPND  18 MOL_ID: 3;                                                           
COMPND  19 MOLECULE: RETINOBLASTOMA-ASSOCIATED PROTEIN;                         
COMPND  20 CHAIN: C;                                                            
COMPND  21 FRAGMENT: C-TERMINAL CORE DOMAIN (RESIDUES 829-874);                 
COMPND  22 SYNONYM: PP110, P105-RB, RB;                                         
COMPND  23 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: TFDP1, DP1;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: E2F1, RBBP3;                                                   
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_COMMON: HUMAN;                                              
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 GENE: RB1;                                                           
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    COILED COIL, BETA SANDWICH, CELL CYCLE, TRANSCRIPTION                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.M.RUBIN,A.L.GALL,N.ZHENG,N.P.PAVLETICH                              
REVDAT   2   24-FEB-09 2AZE    1       VERSN                                    
REVDAT   1   31-JAN-06 2AZE    0                                                
JRNL        AUTH   S.M.RUBIN,A.L.GALL,N.ZHENG,N.P.PAVLETICH                     
JRNL        TITL   STRUCTURE OF THE RB C-TERMINAL DOMAIN BOUND TO               
JRNL        TITL 2 E2F1-DP1: A MECHANISM FOR PHOSPHORYLATION-INDUCED            
JRNL        TITL 3 E2F RELEASE.                                                 
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 123  1093 2005              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   16360038                                                     
JRNL        DOI    10.1016/J.CELL.2005.09.044                                   
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 17600                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.262                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 872                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.55                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.62                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 82.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1104                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2730                       
REMARK   3   BIN FREE R VALUE                    : 0.2840                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2325                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 131                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.16                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.470 ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.580 ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: REFMAC WAS ALSO USED FOR REFINEMENT.      
REMARK   4                                                                      
REMARK   4 2AZE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-SEP-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB034484.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-APR-05; 23-JAN-04               
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : APS; NSLS                          
REMARK 200  BEAMLINE                       : 24-ID-C; X4A                       
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9498; 0.97916, 0.97241,          
REMARK 200                                   0.97929                            
REMARK 200  MONOCHROMATOR                  : INSERTION DEVICE; NULL             
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315; ADSC             
REMARK 200                                   QUANTUM 4                          
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19350                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD                         
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.49                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, AMMONIUM SULFATE,        
REMARK 280  PEG 400, PH 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE         
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       24.15000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       24.15000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       73.40000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       84.30000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       73.40000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       84.30000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       24.15000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       73.40000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       84.30000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       24.15000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       73.40000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       84.30000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8850 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 20820 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 30470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -145.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       96.60000            
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   196                                                      
REMARK 465     GLU A   197                                                      
REMARK 465     ILE A   347                                                      
REMARK 465     THR A   348                                                      
REMARK 465     THR A   349                                                      
REMARK 465     ALA A   350                                                      
REMARK 465     GLY B   196                                                      
REMARK 465     SER B   197                                                      
REMARK 465     HIS B   198                                                      
REMARK 465     MET B   199                                                      
REMARK 465     GLY B   200                                                      
REMARK 465     LYS C   873                                                      
REMARK 465     LYS C   874                                                      
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    ALA A 247       97.37     49.67                                   
REMARK 500    ARG A 249      106.14     86.68                                   
REMARK 500    SER A 313       50.12    -97.61                                   
REMARK 500    VAL A 345       89.55     50.11                                   
REMARK 500    ALA B 255      101.69    165.06                                   
REMARK 500    PRO B 257       49.03    -68.38                                   
REMARK 500    GLU B 270      -14.76     76.91                                   
REMARK 500    GLU B 280      -14.22   -153.19                                   
REMARK 500    GLU B 300      -26.24   -175.34                                   
REMARK 500    ARG C 857       49.56    -99.11                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH C 110        DISTANCE =  5.18 ANGSTROMS                       
REMARK 525    HOH B  59        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH B 122        DISTANCE =  5.05 ANGSTROMS                       
DBREF  2AZE A  199   350  UNP    Q14186   TDP1_HUMAN     199    350             
DBREF  2AZE B  200   301  UNP    Q01094   E2F1_HUMAN     200    301             
DBREF  2AZE C  829   874  UNP    P06400   RB_HUMAN       829    874             
SEQADV 2AZE GLY A  196  UNP  Q14186              CLONING ARTIFACT               
SEQADV 2AZE GLU A  197  UNP  Q14186              CLONING ARTIFACT               
SEQADV 2AZE PHE A  198  UNP  Q14186              CLONING ARTIFACT               
SEQADV 2AZE GLY B  196  UNP  Q01094              CLONING ARTIFACT               
SEQADV 2AZE SER B  197  UNP  Q01094              CLONING ARTIFACT               
SEQADV 2AZE HIS B  198  UNP  Q01094              CLONING ARTIFACT               
SEQADV 2AZE MET B  199  UNP  Q01094              CLONING ARTIFACT               
SEQRES   1 A  155  GLY GLU PHE ALA GLN GLU CYS GLN ASN LEU GLU VAL GLU          
SEQRES   2 A  155  ARG GLN ARG ARG LEU GLU ARG ILE LYS GLN LYS GLN SER          
SEQRES   3 A  155  GLN LEU GLN GLU LEU ILE LEU GLN GLN ILE ALA PHE LYS          
SEQRES   4 A  155  ASN LEU VAL GLN ARG ASN ARG HIS ALA GLU GLN GLN ALA          
SEQRES   5 A  155  SER ARG PRO PRO PRO PRO ASN SER VAL ILE HIS LEU PRO          
SEQRES   6 A  155  PHE ILE ILE VAL ASN THR SER LYS LYS THR VAL ILE ASP          
SEQRES   7 A  155  CYS SER ILE SER ASN ASP LYS PHE GLU TYR LEU PHE ASN          
SEQRES   8 A  155  PHE ASP ASN THR PHE GLU ILE HIS ASP ASP ILE GLU VAL          
SEQRES   9 A  155  LEU LYS ARG MET GLY MET ALA CYS GLY LEU GLU SER GLY          
SEQRES  10 A  155  SER CYS SER ALA GLU ASP LEU LYS MET ALA ARG SER LEU          
SEQRES  11 A  155  VAL PRO LYS ALA LEU GLU PRO TYR VAL THR GLU MET ALA          
SEQRES  12 A  155  GLN GLY THR VAL GLY GLY VAL PHE ILE THR THR ALA              
SEQRES   1 B  106  GLY SER HIS MET GLY GLY ARG LEU GLU GLY LEU THR GLN          
SEQRES   2 B  106  ASP LEU ARG GLN LEU GLN GLU SER GLU GLN GLN LEU ASP          
SEQRES   3 B  106  HIS LEU MET ASN ILE CYS THR THR GLN LEU ARG LEU LEU          
SEQRES   4 B  106  SER GLU ASP THR ASP SER GLN ARG LEU ALA TYR VAL THR          
SEQRES   5 B  106  CYS GLN ASP LEU ARG SER ILE ALA ASP PRO ALA GLU GLN          
SEQRES   6 B  106  MET VAL MET VAL ILE LYS ALA PRO PRO GLU THR GLN LEU          
SEQRES   7 B  106  GLN ALA VAL ASP SER SER GLU ASN PHE GLN ILE SER LEU          
SEQRES   8 B  106  LYS SER LYS GLN GLY PRO ILE ASP VAL PHE LEU CYS PRO          
SEQRES   9 B  106  GLU GLU                                                      
SEQRES   1 C   46  SER ARG ILE LEU VAL SER ILE GLY GLU SER PHE GLY THR          
SEQRES   2 C   46  SER GLU LYS PHE GLN LYS ILE ASN GLN MET VAL CYS ASN          
SEQRES   3 C   46  SER ASP ARG VAL LEU LYS ARG SER ALA GLU GLY SER ASN          
SEQRES   4 C   46  PRO PRO LYS PRO LEU LYS LYS                                  
FORMUL   4  HOH   *131(H2 O)                                                    
HELIX    1   1 PHE A  198  GLN A  246  1                                  49    
HELIX    2   2 PRO A  252  ASN A  254  5                                   3    
HELIX    3   3 ASP A  296  MET A  303  1                                   8    
HELIX    4   4 GLY A  308  GLY A  312  5                                   5    
HELIX    5   5 SER A  315  LEU A  325  1                                  11    
HELIX    6   6 VAL A  326  ALA A  329  5                                   4    
HELIX    7   7 LEU A  330  GLY A  340  1                                  11    
HELIX    8   8 GLY B  201  ASP B  237  1                                  37    
HELIX    9   9 ASP B  237  ALA B  244  1                                   8    
HELIX   10  10 CYS B  248  SER B  253  1                                   6    
HELIX   11  11 GLY C  840  ASN C  854  1                                  15    
SHEET    1   A 2 VAL A 256  HIS A 258  0                                        
SHEET    2   A 2 TYR B 245  THR B 247 -1  O  VAL B 246   N  ILE A 257           
SHEET    1   B 4 PHE A 291  ASP A 295  0                                        
SHEET    2   B 4 ILE A 262  SER A 267 -1  N  ILE A 263   O  HIS A 294           
SHEET    3   B 4 GLN B 260  LYS B 266 -1  O  MET B 263   N  VAL A 264           
SHEET    4   B 4 ASP B 294  PHE B 296 -1  O  PHE B 296   N  VAL B 264           
SHEET    1   C 5 ILE A 272  ILE A 276  0                                        
SHEET    2   C 5 GLU A 282  PHE A 287 -1  O  ASN A 286   N  ASP A 273           
SHEET    3   C 5 PHE B 282  LYS B 287 -1  O  PHE B 282   N  PHE A 287           
SHEET    4   C 5 GLN B 272  ASP B 277 -1  N  GLN B 274   O  SER B 285           
SHEET    5   C 5 ARG C 830  SER C 834 -1  O  VAL C 833   N  LEU B 273           
CISPEP   1 LEU A  259    PRO A  260          0        -4.34                     
CRYST1  146.800  168.600   48.300  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006812  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005931  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020704        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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