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Database: PDB
Entry: 3EXJ
LinkDB: 3EXJ
Original site: 3EXJ 
HEADER    TRANSCRIPTION/DNA                       16-OCT-08   3EXJ              
TITLE     CRYSTAL STRUCTURE OF A P53 CORE TETRAMER BOUND TO DNA                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MOUSE P53 CORE DOMAIN;                                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: 5'-D(P*DGP*DAP*DGP*DCP*DAP*DTP*DGP*DCP*DTP*DCP*DA)-3';     
COMPND   7 CHAIN: C;                                                            
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 OTHER_DETAILS: P53 CONSENSUS SEQUENCE;                               
COMPND  10 MOL_ID: 3;                                                           
COMPND  11 MOLECULE: 5'-D(*DTP*DTP*DGP*DAP*DGP*DCP*DAP*DTP*DGP*DCP*DTP*DC)-3';  
COMPND  12 CHAIN: D;                                                            
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 OTHER_DETAILS: P53 CONSENSUS SEQUENCE                                
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 SYNTHETIC: YES;                                                      
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 SYNTHETIC: YES                                                       
KEYWDS    PROTEIN-DNA COMPLEX, ACETYLATION, ACTIVATOR, ANTI-ONCOGENE,           
KEYWDS   2 APOPTOSIS, CELL CYCLE, COVALENT PROTEIN-RNA LINKAGE, CYTOPLASM,      
KEYWDS   3 DISEASE MUTATION, DNA-BINDING, ENDOPLASMIC RETICULUM, METAL-BINDING, 
KEYWDS   4 METHYLATION, NUCLEUS, PHOSPHOPROTEIN, TRANSCRIPTION, TRANSCRIPTION   
KEYWDS   5 REGULATION, UBL CONJUGATION, ZINC, TRANSCRIPTION-DNA COMPLEX         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.A.MALECKA                                                           
REVDAT   3   25-OCT-17 3EXJ    1       REMARK                                   
REVDAT   2   03-FEB-09 3EXJ    1       JRNL                                     
REVDAT   1   16-DEC-08 3EXJ    0                                                
JRNL        AUTH   K.A.MALECKA,W.C.HO,R.MARMORSTEIN                             
JRNL        TITL   CRYSTAL STRUCTURE OF A P53 CORE TETRAMER BOUND TO DNA.       
JRNL        REF    ONCOGENE                      V.  28   325 2009              
JRNL        REFN                   ISSN 0950-9232                               
JRNL        PMID   18978813                                                     
JRNL        DOI    10.1038/ONC.2008.400                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.70                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 36093                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.225                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
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) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
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            : 3032                                    
REMARK   3   NUCLEIC ACID ATOMS       : 468                                     
REMARK   3   HETEROGEN ATOMS          : 15                                      
REMARK   3   SOLVENT ATOMS            : 578                                     
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) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
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) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; 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: NULL                                      
REMARK   4                                                                      
REMARK   4 3EXJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-NOV-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000049891.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-APR-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
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-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36093                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 70.186                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : 0.08300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.600                              
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   (%): 53.44                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM LITHIUM CITRATE, 20% PEG 3350,    
REMARK 280  PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -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        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       57.37000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.00800            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       57.37000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.00800            
REMARK 290   SMTRY3   4  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: OCTAMERIC                         
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 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        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    96                                                      
REMARK 465     GLN A    97                                                      
REMARK 465     LEU A   292                                                      
REMARK 465     GLU B   290                                                      
REMARK 465     VAL B   291                                                      
REMARK 465     LEU B   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     LYS A  98    CG   CD   CE   NZ                                   
REMARK 470     LYS A 117    CG   CD   CE   NZ                                   
REMARK 470     ARG A 206    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 288    CG   CD   CE   NZ                                   
REMARK 470     LYS A 289    CG   CD   CE   NZ                                   
REMARK 470     VAL A 291    CG1  CG2                                            
REMARK 470     SER B  96    OG                                                  
REMARK 470     GLN B  97    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 162    CG   CD   CE   NZ                                   
REMARK 470     GLN B 189    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 206    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 289    CG   CD   CE   NZ                                   
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   P     DG C    13     O3'   DC D    12     2555     1.60            
REMARK 500   OP2   DG C    13     C3'   DC D    12     2555     2.11            
REMARK 500   OP2   DG C    13     O3'   DC D    12     2555     2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500     DG C  13   O5' -  P   -  OP2 ANGL. DEV. = -16.5 DEGREES          
REMARK 500     DG C  13   P   -  O5' -  C5' ANGL. DEV. = -21.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 180       59.14    -94.67                                   
REMARK 500    LYS A 289      -20.48    173.15                                   
REMARK 500    SER B 180       58.24    -98.34                                   
REMARK 500    ARG B 287       44.64    -63.60                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A   1  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 173   SG                                                     
REMARK 620 2 HIS A 176   ND1 102.1                                              
REMARK 620 3 CYS A 235   SG  111.3 111.6                                        
REMARK 620 4 CYS A 239   SG  114.9 100.5 115.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B   2  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 173   SG                                                     
REMARK 620 2 HIS B 176   ND1 102.0                                              
REMARK 620 3 CYS B 235   SG  110.4 109.3                                        
REMARK 620 4 CYS B 239   SG  115.5 106.5 112.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC B 585                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 2                    
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3EXL   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 THE COMPLETE CRYSTALLIZED DNA SEQUENCE IS                            
REMARK 999 5'-TTGAGCATGCTCGAGCATGCTCA-3'. THE SEQUENCE IN THE                   
REMARK 999 ASYMMETRIC UNIT IS ONLY HALF OF THE COMPLETE SEQUENCE                
REMARK 999 (GAGCATGCTCA FOR CHAIN C AND GAGCATGTCTC FOR CHAIN D.  THE           
REMARK 999 BIOLOGICAL UNIT ISGENERATED BY APPLYING THE (-X, Y, -Z)              
REMARK 999 SYMMETRY.                                                            
DBREF  3EXJ A   96   292  UNP    P02340   P53_MOUSE       93    289             
DBREF  3EXJ B   96   292  UNP    P02340   P53_MOUSE       93    289             
DBREF  3EXJ C   13    23  PDB    3EXJ     3EXJ            13     23             
DBREF  3EXJ D    1    12  PDB    3EXJ     3EXJ             1     12             
SEQRES   1 A  197  SER GLN LYS THR TYR GLN GLY ASN TYR GLY PHE HIS LEU          
SEQRES   2 A  197  GLY PHE LEU GLN SER GLY THR ALA LYS SER VAL MET CYS          
SEQRES   3 A  197  THR TYR SER PRO PRO LEU ASN LYS LEU PHE CYS GLN LEU          
SEQRES   4 A  197  ALA LYS THR CYS PRO VAL GLN LEU TRP VAL SER ALA THR          
SEQRES   5 A  197  PRO PRO ALA GLY SER ARG VAL ARG ALA MET ALA ILE TYR          
SEQRES   6 A  197  LYS LYS SER GLN HIS MET THR GLU VAL VAL ARG ARG CYS          
SEQRES   7 A  197  PRO HIS HIS GLU ARG CYS SER ASP GLY ASP GLY LEU ALA          
SEQRES   8 A  197  PRO PRO GLN HIS LEU ILE ARG VAL GLU GLY ASN LEU TYR          
SEQRES   9 A  197  PRO GLU TYR LEU GLU ASP ARG GLN THR PHE ARG HIS SER          
SEQRES  10 A  197  VAL VAL VAL PRO TYR GLU PRO PRO GLU ALA GLY SER GLU          
SEQRES  11 A  197  TYR THR THR ILE HIS TYR LYS TYR MET CYS ASN SER SER          
SEQRES  12 A  197  CYS MET GLY GLY MET ASN ARG ARG PRO ILE LEU THR ILE          
SEQRES  13 A  197  ILE THR LEU GLU ASP SER SER GLY ASN LEU LEU GLY ARG          
SEQRES  14 A  197  ASP SER PHE GLU VAL ARG VAL CYS ALA CYS PRO GLY ARG          
SEQRES  15 A  197  ASP ARG ARG THR GLU GLU GLU ASN PHE ARG LYS LYS GLU          
SEQRES  16 A  197  VAL LEU                                                      
SEQRES   1 B  197  SER GLN LYS THR TYR GLN GLY ASN TYR GLY PHE HIS LEU          
SEQRES   2 B  197  GLY PHE LEU GLN SER GLY THR ALA LYS SER VAL MET CYS          
SEQRES   3 B  197  THR TYR SER PRO PRO LEU ASN LYS LEU PHE CYS GLN LEU          
SEQRES   4 B  197  ALA LYS THR CYS PRO VAL GLN LEU TRP VAL SER ALA THR          
SEQRES   5 B  197  PRO PRO ALA GLY SER ARG VAL ARG ALA MET ALA ILE TYR          
SEQRES   6 B  197  LYS LYS SER GLN HIS MET THR GLU VAL VAL ARG ARG CYS          
SEQRES   7 B  197  PRO HIS HIS GLU ARG CYS SER ASP GLY ASP GLY LEU ALA          
SEQRES   8 B  197  PRO PRO GLN HIS LEU ILE ARG VAL GLU GLY ASN LEU TYR          
SEQRES   9 B  197  PRO GLU TYR LEU GLU ASP ARG GLN THR PHE ARG HIS SER          
SEQRES  10 B  197  VAL VAL VAL PRO TYR GLU PRO PRO GLU ALA GLY SER GLU          
SEQRES  11 B  197  TYR THR THR ILE HIS TYR LYS TYR MET CYS ASN SER SER          
SEQRES  12 B  197  CYS MET GLY GLY MET ASN ARG ARG PRO ILE LEU THR ILE          
SEQRES  13 B  197  ILE THR LEU GLU ASP SER SER GLY ASN LEU LEU GLY ARG          
SEQRES  14 B  197  ASP SER PHE GLU VAL ARG VAL CYS ALA CYS PRO GLY ARG          
SEQRES  15 B  197  ASP ARG ARG THR GLU GLU GLU ASN PHE ARG LYS LYS GLU          
SEQRES  16 B  197  VAL LEU                                                      
SEQRES   1 C   11   DG  DA  DG  DC  DA  DT  DG  DC  DT  DC  DA                  
SEQRES   1 D   12   DT  DT  DG  DA  DG  DC  DA  DT  DG  DC  DT  DC              
HET     ZN  A   1       1                                                       
HET    FLC  B 585      13                                                       
HET     ZN  B   2       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     FLC CITRATE ANION                                                    
FORMUL   5   ZN    2(ZN 2+)                                                     
FORMUL   6  FLC    C6 H5 O7 3-                                                  
FORMUL   8  HOH   *578(H2 O)                                                    
HELIX    1   1 GLN A  101  GLY A  105  5                                   5    
HELIX    2   2 THR A  115  VAL A  119  5                                   5    
HELIX    3   3 CYS A  173  ARG A  178  1                                   6    
HELIX    4   4 CYS A  274  LYS A  288  1                                  15    
HELIX    5   5 GLN B  101  GLY B  105  5                                   5    
HELIX    6   6 THR B  115  VAL B  119  5                                   5    
HELIX    7   7 CYS B  173  ARG B  178  1                                   6    
HELIX    8   8 CYS B  274  ARG B  287  1                                  14    
SHEET    1   A 4 HIS A 107  PHE A 110  0                                        
SHEET    2   A 4 CYS A 138  TRP A 143 -1  O  GLN A 141   N  GLY A 109           
SHEET    3   A 4 THR A 227  TYR A 233 -1  O  THR A 227   N  LEU A 142           
SHEET    4   A 4 ILE A 192  GLU A 195 -1  N  GLU A 195   O  HIS A 230           
SHEET    1   B 7 CYS A 121  SER A 124  0                                        
SHEET    2   B 7 LYS A 129  CYS A 132 -1  O  PHE A 131   N  THR A 122           
SHEET    3   B 7 LEU A 261  VAL A 271  1  O  GLU A 268   N  LEU A 130           
SHEET    4   B 7 ILE A 248  GLU A 255 -1  N  LEU A 254   O  LEU A 262           
SHEET    5   B 7 ARG A 153  TYR A 160 -1  N  ARG A 153   O  GLU A 255           
SHEET    6   B 7 HIS A 211  PRO A 216 -1  O  VAL A 215   N  VAL A 154           
SHEET    7   B 7 GLU A 201  GLU A 204 -1  N  LEU A 203   O  SER A 212           
SHEET    1   C 4 HIS B 107  PHE B 110  0                                        
SHEET    2   C 4 CYS B 138  TRP B 143 -1  O  GLN B 141   N  GLY B 109           
SHEET    3   C 4 THR B 227  TYR B 233 -1  O  TYR B 231   N  CYS B 138           
SHEET    4   C 4 ILE B 192  GLU B 195 -1  N  GLU B 195   O  HIS B 230           
SHEET    1   D 7 CYS B 121  SER B 124  0                                        
SHEET    2   D 7 LYS B 129  CYS B 132 -1  O  PHE B 131   N  THR B 122           
SHEET    3   D 7 LEU B 261  VAL B 271  1  O  GLU B 268   N  LEU B 130           
SHEET    4   D 7 ILE B 248  GLU B 255 -1  N  LEU B 254   O  LEU B 262           
SHEET    5   D 7 ARG B 153  TYR B 160 -1  N  MET B 157   O  ILE B 251           
SHEET    6   D 7 HIS B 211  PRO B 216 -1  O  VAL B 215   N  VAL B 154           
SHEET    7   D 7 GLU B 201  GLU B 204 -1  N  LEU B 203   O  SER B 212           
LINK         SG  CYS A 173                ZN    ZN A   1     1555   1555  2.37  
LINK         ND1 HIS A 176                ZN    ZN A   1     1555   1555  2.18  
LINK         SG  CYS A 235                ZN    ZN A   1     1555   1555  2.38  
LINK         SG  CYS A 239                ZN    ZN A   1     1555   1555  2.34  
LINK         SG  CYS B 173                ZN    ZN B   2     1555   1555  2.32  
LINK         ND1 HIS B 176                ZN    ZN B   2     1555   1555  2.11  
LINK         SG  CYS B 235                ZN    ZN B   2     1555   1555  2.48  
LINK         SG  CYS B 239                ZN    ZN B   2     1555   1555  2.36  
SITE     1 AC1  4 CYS A 173  HIS A 176  CYS A 235  CYS A 239                    
SITE     1 AC2  8 LYS A 162  SER A 163  HOH A 373  HOH A 423                    
SITE     2 AC2  8 THR B 115  LYS B 117  PRO B 139  HIS B 230                    
SITE     1 AC3  4 CYS B 173  HIS B 176  CYS B 235  CYS B 239                    
CRYST1  114.740   68.016   75.162  90.00 111.12  90.00 C 1 2 1       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      0.008715  0.000000  0.003366        0.00000                         
SCALE2      0.000000  0.014702  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014263        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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