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Database: PDB
Entry: 2J1Y
LinkDB: 2J1Y
Original site: 2J1Y 
HEADER    NUCLEAR PROTEIN                         15-AUG-06   2J1Y              
TITLE     HUMAN P53 CORE DOMAIN MUTANT M133L-V203A-N239Y-G245S-N268D            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELLULAR TUMOR ANTIGEN P53;                                
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: DNA-BINDING CORE DOMAIN, RESIDUES 94-293;                  
COMPND   5 SYNONYM: P53, TUMOR SUPPRESSOR P53, PHOSPHOPROTEIN P53,              
COMPND   6  ANTIGEN NY-CO-13;                                                   
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    SECOND-SITE SUPPRESSOR MUTATION, DISEASE MUTATION, NUCLEAR            
KEYWDS   2 PROTEIN, PHOSPHORYLATION, TUMOR SUPPRESSOR, ALTERNATIVE              
KEYWDS   3 SPLICING, LI-FRAUMENI SYNDROME, LI- FRAUMENI SYNDROME,               
KEYWDS   4 HOST-VIRUS INTERACTION, TRANSCRIPTION, METAL-BINDING,                
KEYWDS   5 ANTI-ONCOGENE, DNA-BINDING, TRANSFERASE, POLYMORPHISM,               
KEYWDS   6 GLYCOPROTEIN, ZINC, ACTIVATOR, APOPTOSIS, CELL CYCLE,                
KEYWDS   7 ACETYLATION, P53 DNA-BINDING DOMAIN, TRANSCRIPTION                   
KEYWDS   8 REGULATION, SUPERSTABLE MUTANT, DNA-BINDING PROTEIN                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.C.JOERGER,A.R.FERSHT                                                
REVDAT   3   24-FEB-09 2J1Y    1       VERSN                                    
REVDAT   2   18-OCT-06 2J1Y    1       JRNL                                     
REVDAT   1   20-SEP-06 2J1Y    0                                                
JRNL        AUTH   A.C.JOERGER,H.C.ANG,A.R.FERSHT                               
JRNL        TITL   STRUCTURAL BASIS FOR UNDERSTANDING ONCOGENIC P53             
JRNL        TITL 2 MUTATIONS AND DESIGNING RESCUE DRUGS.                        
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 103 15056 2006              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   17015838                                                     
JRNL        DOI    10.1073/PNAS.0607286103                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.C.JOERGER,M.D.ALLEN,A.R.FERSHT                             
REMARK   1  TITL   CRYSTAL STRUCTURE OF A SUPERSTABLE MUTANT OF HUMAN           
REMARK   1  TITL 2 P53 CORE DOMAIN. INSIGHTS INTO THE MECHANISM OF              
REMARK   1  TITL 3 RESCUING ONCOGENIC MUTATIONS.                                
REMARK   1  REF    J.BIOL.CHEM.                  V. 279  1291 2004              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1  PMID   14534297                                                     
REMARK   1  DOI    10.1074/JBC.M309732200                                       
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   A.C.JOERGER,H.C.ANG,D.B.VEPRINTSEV,C.M.BLAIR,                
REMARK   1  AUTH 2 A.R.FERSHT                                                   
REMARK   1  TITL   STRUCTURES OF P53 CANCER MUTANTS AND MECHANISM OF            
REMARK   1  TITL 2 RESCUE BY SECOND-SITE SUPPRESSOR MUTATIONS.                  
REMARK   1  REF    J.BIOL.CHEM.                  V. 280 16030 2005              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1  PMID   15703170                                                     
REMARK   1  DOI    10.1074/JBC.M500179200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.69 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) : 1.69                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.4                           
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)   (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 93295                          
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 SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
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            : 6072                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 754                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.4                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.6                           
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) : 1.5                             
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 2J1Y COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-AUG-06.                  
REMARK 100 THE PDBE ID CODE IS EBI-29156.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX10.1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.284                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 93315                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.690                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.400                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.69                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.78                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.27000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1UOL                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       36.53800            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 GENERATING THE BIOMOLECULE                                           
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 BIOMOLECULE:  2                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 BIOMOLECULE:  3                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 BIOMOLECULE:  4                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, MET 133 TO LEU                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, VAL 203 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 239 TO TYR                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, GLY 245 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 268 TO ASP                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, MET 133 TO LEU                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, VAL 203 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, ASN 239 TO TYR                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, GLY 245 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, ASN 268 TO ASP                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, MET 133 TO LEU                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, VAL 203 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, ASN 239 TO TYR                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, GLY 245 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, ASN 268 TO ASP                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, MET 133 TO LEU                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, VAL 203 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, ASN 239 TO TYR                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, GLY 245 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, ASN 268 TO ASP                        
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    94                                                      
REMARK 465     CYS A   182                                                      
REMARK 465     SER A   183                                                      
REMARK 465     ASP A   184                                                      
REMARK 465     ARG A   290                                                      
REMARK 465     LYS A   291                                                      
REMARK 465     LYS A   292                                                      
REMARK 465     GLY A   293                                                      
REMARK 465     SER B    94                                                      
REMARK 465     SER B    95                                                      
REMARK 465     ASP B   184                                                      
REMARK 465     ARG B   290                                                      
REMARK 465     LYS B   291                                                      
REMARK 465     LYS B   292                                                      
REMARK 465     GLY B   293                                                      
REMARK 465     SER C    94                                                      
REMARK 465     SER C    95                                                      
REMARK 465     CYS C   182                                                      
REMARK 465     SER C   183                                                      
REMARK 465     ASP C   184                                                      
REMARK 465     ARG C   290                                                      
REMARK 465     LYS C   291                                                      
REMARK 465     LYS C   292                                                      
REMARK 465     GLY C   293                                                      
REMARK 465     SER D    94                                                      
REMARK 465     SER D    95                                                      
REMARK 465     SER D   183                                                      
REMARK 465     ASP D   184                                                      
REMARK 465     ARG D   290                                                      
REMARK 465     LYS D   291                                                      
REMARK 465     LYS D   292                                                      
REMARK 465     GLY D   293                                                      
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    MET D 246   CG  -  SD  -  CE  ANGL. DEV. =  -9.9 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 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 245     -101.59   -141.06                                   
REMARK 500    ARG A 248       -0.93     74.63                                   
REMARK 500    ALA B 138        7.36     59.91                                   
REMARK 500    CYS B 182       66.00   -116.38                                   
REMARK 500    SER B 245     -100.62   -140.33                                   
REMARK 500    ARG B 248       -0.01     72.89                                   
REMARK 500    CYS C 242      109.06    -52.97                                   
REMARK 500    SER C 245     -106.26   -136.31                                   
REMARK 500    ASN C 288        4.95    -68.84                                   
REMARK 500    ALA D 138       -2.21     64.02                                   
REMARK 500    SER D 245     -100.15   -141.72                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR C 107         0.07    SIDE CHAIN                              
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 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 A1290  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 238   SG                                                     
REMARK 620 2 CYS A 176   SG  110.7                                              
REMARK 620 3 HIS A 179   ND1 116.4 100.6                                        
REMARK 620 4 CYS A 242   SG  112.0 117.3  99.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1290  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 238   SG                                                     
REMARK 620 2 CYS B 176   SG  107.8                                              
REMARK 620 3 HIS B 179   ND1 110.4 103.0                                        
REMARK 620 4 CYS B 242   SG  114.0 117.4 103.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C1290  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 176   SG                                                     
REMARK 620 2 HIS C 179   ND1 106.5                                              
REMARK 620 3 CYS C 238   SG  110.1 113.3                                        
REMARK 620 4 CYS C 242   SG  115.1  95.2 115.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D1290  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 176   SG                                                     
REMARK 620 2 HIS D 179   ND1 102.9                                              
REMARK 620 3 CYS D 238   SG  107.5 110.9                                        
REMARK 620 4 CYS D 242   SG  116.9 103.0 114.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1291  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 268   OD1                                                    
REMARK 620 2 ASP A 268   OD2  52.0                                              
REMARK 620 3 HOH A2183   O    81.9  74.8                                        
REMARK 620 4 HOH A2041   O   141.0 142.5 131.9                                  
REMARK 620 5 HOH A2047   O   132.3 128.2  59.0  73.1                            
REMARK 620 6 HOH A2184   O    79.5 130.9  93.6  79.5  77.2                      
REMARK 620 7 HOH A2186   O    75.1  88.3 156.7  70.8 142.2  85.4                
REMARK 620 8 HOH A2020   O   127.0  75.1  88.1  79.6  81.1 153.4 103.2          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B1291  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 268   OD1                                                    
REMARK 620 2 ASP B 268   OD2  50.8                                              
REMARK 620 3 HOH B2177   O    79.3 129.6                                        
REMARK 620 4 HOH B2178   O    74.4  74.8  86.8                                  
REMARK 620 5 HOH B2180   O    78.2  84.5  92.6 152.2                            
REMARK 620 6 HOH B2024   O   127.7  76.9 152.2  94.1  99.1                      
REMARK 620 7 HOH B2049   O   130.2 127.6  76.9  61.2 145.4  79.2                
REMARK 620 8 HOH B2050   O   147.5 145.4  80.8 129.8  77.2  77.3  68.6          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C1291  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C2042   O                                                      
REMARK 620 2 HOH C2171   O    77.5                                              
REMARK 620 3 ASP C 268   OD1 142.8  74.1                                        
REMARK 620 4 ASP C 268   OD2 147.4  85.2  52.2                                  
REMARK 620 5 HOH C2016   O    82.2 102.3 126.9  74.8                            
REMARK 620 6 HOH C2043   O    67.4 144.1 132.8 128.9  80.3                      
REMARK 620 7 HOH C2168   O   127.2 154.2  80.3  76.2  90.1  59.8                
REMARK 620 8 HOH C2167   O    78.2  88.1  77.4 129.1 155.2  78.3  89.8          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D1291  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 268   OD1                                                    
REMARK 620 2 ASP D 268   OD2  49.2                                              
REMARK 620 3 HOH D2019   O   127.1  77.9                                        
REMARK 620 4 HOH D2038   O   145.6 146.6  79.0                                  
REMARK 620 5 HOH D2158   O    77.7 126.9 155.2  78.6                            
REMARK 620 6 HOH D2162   O    77.0  81.9  97.5  77.6  88.0                      
REMARK 620 7 HOH D2159   O    74.5  76.1  95.8 130.2  90.5 151.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1290                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A1291                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B1290                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B1291                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN C1290                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA C1291                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN D1290                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA D1291                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1A1U   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE DETERMINATION OF A P53                           
REMARK 900  MUTANT DIMERIZATION DOMAIN, NMR, MINIMIZED                          
REMARK 900  AVERAGE STRUCTURE                                                   
REMARK 900 RELATED ID: 1AIE   RELATED DB: PDB                                   
REMARK 900  P53 TETRAMERIZATION DOMAIN CRYSTAL STRUCTURE                        
REMARK 900 RELATED ID: 1C26   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF P53 TETRAMERIZATION                            
REMARK 900  DOMAIN                                                              
REMARK 900 RELATED ID: 1DT7   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE C-TERMINAL                                
REMARK 900  NEGATIVE REGULATORY DOMAIN OF P53 IN A                              
REMARK 900  COMPLEX WITH CA2+-BOUND S100B(BB)                                   
REMARK 900 RELATED ID: 1GZH   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE BRCT DOMAINS OF                            
REMARK 900  HUMAN 53BP1 BOUND TO THE P53 TUMOR                                  
REMARK 900  SUPRESSOR                                                           
REMARK 900 RELATED ID: 1H26   RELATED DB: PDB                                   
REMARK 900  CDK2/CYCLINA IN COMPLEX WITH AN 11-RESIDUE                          
REMARK 900   RECRUITMENT PEPTIDE FROM P53                                       
REMARK 900 RELATED ID: 1HS5   RELATED DB: PDB                                   
REMARK 900  NMR SOLUTION STRUCTURE OF DESIGNED P53 DIMER                        
REMARK 900 RELATED ID: 1JSP   RELATED DB: PDB                                   
REMARK 900  NMR STRUCTURE OF CBP BROMODOMAIN IN COMPLEX                         
REMARK 900   WITH P53 PEPTIDE                                                   
REMARK 900 RELATED ID: 1KZY   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE 53BP1 BRCT REGION                          
REMARK 900  COMPLEXED TOTUMOR SUPPRESSOR P53                                    
REMARK 900 RELATED ID: 1MA3   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF A SIR2 ENZYME BOUND TO AN                              
REMARK 900  ACETYLATED P53PEPTIDE                                               
REMARK 900 RELATED ID: 1OLG   RELATED DB: PDB                                   
REMARK 900  P53 (OLIGOMERIZATION DOMAIN) (NMR, MINIMIZED                        
REMARK 900  AVERAGE STRUCTURE)                                                  
REMARK 900 RELATED ID: 1OLH   RELATED DB: PDB                                   
REMARK 900  P53 (OLIGOMERIZATION DOMAIN) (NMR, 35                               
REMARK 900  STRUCTURES)                                                         
REMARK 900 RELATED ID: 1PES   RELATED DB: PDB                                   
REMARK 900  TUMOR ANTIGEN P53 (TETRAMERIZATION DOMAIN) (                        
REMARK 900  P53TET) (NMR, MINIMIZED AVERAGE STRUCTURE)                          
REMARK 900 RELATED ID: 1PET   RELATED DB: PDB                                   
REMARK 900  TUMOR ANTIGEN P53 (TETRAMERIZATION DOMAIN) (                        
REMARK 900  P53TET) (NMR, 19 STRUCTURES)                                        
REMARK 900 RELATED ID: 1SAE   RELATED DB: PDB                                   
REMARK 900  HIGH RESOLUTION SOLUTION NMR STRUCTURE OF                           
REMARK 900  THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-                         
REMARK 900  DIMENSIONAL NMR (SAC STRUCTURES)                                    
REMARK 900 RELATED ID: 1SAF   RELATED DB: PDB                                   
REMARK 900  HIGH RESOLUTION SOLUTION NMR STRUCTURE OF                           
REMARK 900  THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-                         
REMARK 900  DIMENSIONAL NMR (SAD STRUCTURES)                                    
REMARK 900 RELATED ID: 1SAG   RELATED DB: PDB                                   
REMARK 900  HIGH RESOLUTION SOLUTION NMR STRUCTURE OF                           
REMARK 900  THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-                         
REMARK 900  DIMENSIONAL NMR (SAC STRUCTURES)                                    
REMARK 900 RELATED ID: 1SAH   RELATED DB: PDB                                   
REMARK 900  HIGH RESOLUTION SOLUTION NMR STRUCTURE OF                           
REMARK 900  THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-                         
REMARK 900  DIMENSIONAL NMR (SAD STRUCTURES)                                    
REMARK 900 RELATED ID: 1SAI   RELATED DB: PDB                                   
REMARK 900  HIGH RESOLUTION SOLUTION NMR STRUCTURE OF                           
REMARK 900  THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-                         
REMARK 900  DIMENSIONAL NMR (SAC STRUCTURES)                                    
REMARK 900 RELATED ID: 1SAJ   RELATED DB: PDB                                   
REMARK 900  HIGH RESOLUTION SOLUTION NMR STRUCTURE OF                           
REMARK 900  THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-                         
REMARK 900  DIMENSIONAL NMR (SAD STRUCTURES)                                    
REMARK 900 RELATED ID: 1SAK   RELATED DB: PDB                                   
REMARK 900  HIGH RESOLUTION SOLUTION NMR STRUCTURE OF                           
REMARK 900  THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-                         
REMARK 900  DIMENSIONAL NMR (SAC STRUCTURES)                                    
REMARK 900 RELATED ID: 1SAL   RELATED DB: PDB                                   
REMARK 900  HIGH RESOLUTION SOLUTION NMR STRUCTURE OF                           
REMARK 900  THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-                         
REMARK 900  DIMENSIONAL NMR (SAD STRUCTURES)                                    
REMARK 900 RELATED ID: 1TSR   RELATED DB: PDB                                   
REMARK 900  P53 CORE DOMAIN IN COMPLEX WITH                                     
REMARK 900  DEOXYRIBONUCLEIC ACID                                               
REMARK 900 RELATED ID: 1TUP   RELATED DB: PDB                                   
REMARK 900  TUMOR SUPPRESSOR P53 COMPLEXED WITH                                 
REMARK 900  DEOXYRIBONUCLEIC ACID                                               
REMARK 900 RELATED ID: 1UOL   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE HUMAN P53 CORE                             
REMARK 900  DOMAIN MUTANT M133L/V203A/N239Y/N268D AT 1                          
REMARK 900  .9 A RESOLUTION.                                                    
REMARK 900 RELATED ID: 1XQH   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF A TERNARY COMPLEX OF                           
REMARK 900  THEMETHYLTRANSFERASE SET9 (ALSO KNOWN AS SET7                       
REMARK 900  /9) WITH A P53PEPTIDE AND SAH                                       
REMARK 900 RELATED ID: 1YCQ   RELATED DB: PDB                                   
REMARK 900  XENOPUS LAEVIS MDM2 BOUND TO THE                                    
REMARK 900  TRANSACTIVATION DOMAIN OF HUMAN P53                                 
REMARK 900 RELATED ID: 1YCR   RELATED DB: PDB                                   
REMARK 900  MDM2 BOUND TO THE TRANSACTIVATION DOMAIN OF                         
REMARK 900   P53                                                                
REMARK 900 RELATED ID: 1YCS   RELATED DB: PDB                                   
REMARK 900  P53-53BP2 COMPLEX                                                   
REMARK 900 RELATED ID: 2AC0   RELATED DB: PDB                                   
REMARK 900  STRUCTURAL BASIS OF DNA RECOGNITION BY P53                          
REMARK 900  TETRAMERS(COMPLEX I)                                                
REMARK 900 RELATED ID: 2ADY   RELATED DB: PDB                                   
REMARK 900  STRUCTURAL BASIS OF DNA RECOGNITION BY P53                          
REMARK 900  TETRAMERS(COMPLEX IV)                                               
REMARK 900 RELATED ID: 2AHI   RELATED DB: PDB                                   
REMARK 900  STRUCTURAL BASIS OF DNA RECOGNITION BY P53                          
REMARK 900  TETRAMERS(COMPLEX III)                                              
REMARK 900 RELATED ID: 2ATA   RELATED DB: PDB                                   
REMARK 900  STRUCTURAL BASIS OF DNA RECOGNITION BY P53                          
REMARK 900  TETRAMERS(COMPLEX II)                                               
REMARK 900 RELATED ID: 2B3G   RELATED DB: PDB                                   
REMARK 900  P53N (FRAGMENT 33-60) BOUND TO RPA70N                               
REMARK 900 RELATED ID: 2BIM   RELATED DB: PDB                                   
REMARK 900  HUMAN P53 CORE DOMAIN MUTANT M133L-V203A-                           
REMARK 900  N239Y-N268D-R273H                                                   
REMARK 900 RELATED ID: 2BIN   RELATED DB: PDB                                   
REMARK 900  HUMAN P53 CORE DOMAIN MUTANT M133L-H168R-                           
REMARK 900  V203A-N239Y-N268D                                                   
REMARK 900 RELATED ID: 2BIO   RELATED DB: PDB                                   
REMARK 900  HUMAN P53 CORE DOMAIN MUTANT M133L-V203A-                           
REMARK 900  N239Y-R249S-N268D                                                   
REMARK 900 RELATED ID: 2BIP   RELATED DB: PDB                                   
REMARK 900  HUMAN P53 CORE DOMAIN MUTANT M133L-H168R-                           
REMARK 900  V203A-N239Y-R249S-N268D                                             
REMARK 900 RELATED ID: 2BIQ   RELATED DB: PDB                                   
REMARK 900  HUMAN P53 CORE DOMAIN MUTANT T123A-M133L-                           
REMARK 900  H168R-V203A-N239Y-R249S-N268D                                       
REMARK 900 RELATED ID: 2F1X   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE TRAF-LIKE DOMAIN                           
REMARK 900  OF HAUSP/USP7BOUND TO A P53 PEPTIDE                                 
REMARK 900 RELATED ID: 2FEJ   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF HUMAN P53 DNA BINDING                         
REMARK 900   DOMAIN.                                                            
REMARK 900 RELATED ID: 2J0Z   RELATED DB: PDB                                   
REMARK 900  P53 TETRAMERIZATION DOMAIN WILD TYPE                                
REMARK 900 RELATED ID: 2J10   RELATED DB: PDB                                   
REMARK 900  P53 TETRAMERIZATION DOMAIN MUTANT T329F Q331K                       
REMARK 900 RELATED ID: 2J11   RELATED DB: PDB                                   
REMARK 900  P53 TETRAMERIZATION DOMAIN MUTANT Y327S T329G                       
REMARK 900   Q331G                                                              
REMARK 900 RELATED ID: 2J1W   RELATED DB: PDB                                   
REMARK 900  HUMAN P53 CORE DOMAIN MUTANT M133L-V143A-                           
REMARK 900  V203A-N239Y-N268D                                                   
REMARK 900 RELATED ID: 2J1X   RELATED DB: PDB                                   
REMARK 900  HUMAN P53 CORE DOMAIN MUTANT M133L-V203A-                           
REMARK 900  Y220C-N239Y-N268D                                                   
REMARK 900 RELATED ID: 2J1Z   RELATED DB: PDB                                   
REMARK 900  HUMAN P53 CORE DOMAIN MUTANT M133L-V203A-                           
REMARK 900  N239Y-N268D-F270L                                                   
REMARK 900 RELATED ID: 2J20   RELATED DB: PDB                                   
REMARK 900  HUMAN P53 CORE DOMAIN MUTANT M133L-V203A-                           
REMARK 900  N239Y-N268D-R273C                                                   
REMARK 900 RELATED ID: 2J21   RELATED DB: PDB                                   
REMARK 900  HUMAN P53 CORE DOMAIN MUTANT M133L-V203A-                           
REMARK 900  N239Y-N268D-R282W                                                   
REMARK 900 RELATED ID: 3SAK   RELATED DB: PDB                                   
REMARK 900  HIGH RESOLUTION SOLUTION NMR STRUCTURE OF                           
REMARK 900  THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-                         
REMARK 900  DIMENSIONAL NMR (SAC STRUCTURES)                                    
DBREF  2J1Y A   94   293  UNP    P04637   P53_HUMAN       94    293             
DBREF  2J1Y B   94   293  UNP    P04637   P53_HUMAN       94    293             
DBREF  2J1Y C   94   293  UNP    P04637   P53_HUMAN       94    293             
DBREF  2J1Y D   94   293  UNP    P04637   P53_HUMAN       94    293             
SEQADV 2J1Y LEU A  133  UNP  P04637    MET   133 ENGINEERED MUTATION            
SEQADV 2J1Y ALA A  203  UNP  P04637    VAL   203 ENGINEERED MUTATION            
SEQADV 2J1Y TYR A  239  UNP  P04637    ASN   239 ENGINEERED MUTATION            
SEQADV 2J1Y SER A  245  UNP  P04637    GLY   245 ENGINEERED MUTATION            
SEQADV 2J1Y ASP A  268  UNP  P04637    ASN   268 ENGINEERED MUTATION            
SEQADV 2J1Y LEU B  133  UNP  P04637    MET   133 ENGINEERED MUTATION            
SEQADV 2J1Y ALA B  203  UNP  P04637    VAL   203 ENGINEERED MUTATION            
SEQADV 2J1Y TYR B  239  UNP  P04637    ASN   239 ENGINEERED MUTATION            
SEQADV 2J1Y SER B  245  UNP  P04637    GLY   245 ENGINEERED MUTATION            
SEQADV 2J1Y ASP B  268  UNP  P04637    ASN   268 ENGINEERED MUTATION            
SEQADV 2J1Y LEU C  133  UNP  P04637    MET   133 ENGINEERED MUTATION            
SEQADV 2J1Y ALA C  203  UNP  P04637    VAL   203 ENGINEERED MUTATION            
SEQADV 2J1Y TYR C  239  UNP  P04637    ASN   239 ENGINEERED MUTATION            
SEQADV 2J1Y SER C  245  UNP  P04637    GLY   245 ENGINEERED MUTATION            
SEQADV 2J1Y ASP C  268  UNP  P04637    ASN   268 ENGINEERED MUTATION            
SEQADV 2J1Y LEU D  133  UNP  P04637    MET   133 ENGINEERED MUTATION            
SEQADV 2J1Y ALA D  203  UNP  P04637    VAL   203 ENGINEERED MUTATION            
SEQADV 2J1Y TYR D  239  UNP  P04637    ASN   239 ENGINEERED MUTATION            
SEQADV 2J1Y SER D  245  UNP  P04637    GLY   245 ENGINEERED MUTATION            
SEQADV 2J1Y ASP D  268  UNP  P04637    ASN   268 ENGINEERED MUTATION            
SEQRES   1 A  200  SER SER SER VAL PRO SER GLN LYS THR TYR GLN GLY SER          
SEQRES   2 A  200  TYR GLY PHE ARG LEU GLY PHE LEU HIS SER GLY THR ALA          
SEQRES   3 A  200  LYS SER VAL THR CYS THR TYR SER PRO ALA LEU ASN LYS          
SEQRES   4 A  200  LEU PHE CYS GLN LEU ALA LYS THR CYS PRO VAL GLN LEU          
SEQRES   5 A  200  TRP VAL ASP SER THR PRO PRO PRO GLY THR ARG VAL ARG          
SEQRES   6 A  200  ALA MET ALA ILE TYR LYS GLN SER GLN HIS MET THR GLU          
SEQRES   7 A  200  VAL VAL ARG ARG CYS PRO HIS HIS GLU ARG CYS SER ASP          
SEQRES   8 A  200  SER ASP GLY LEU ALA PRO PRO GLN HIS LEU ILE ARG VAL          
SEQRES   9 A  200  GLU GLY ASN LEU ARG ALA GLU TYR LEU ASP ASP ARG ASN          
SEQRES  10 A  200  THR PHE ARG HIS SER VAL VAL VAL PRO TYR GLU PRO PRO          
SEQRES  11 A  200  GLU VAL GLY SER ASP CYS THR THR ILE HIS TYR ASN TYR          
SEQRES  12 A  200  MET CYS TYR SER SER CYS MET GLY SER MET ASN ARG ARG          
SEQRES  13 A  200  PRO ILE LEU THR ILE ILE THR LEU GLU ASP SER SER GLY          
SEQRES  14 A  200  ASN LEU LEU GLY ARG ASP SER PHE GLU VAL ARG VAL CYS          
SEQRES  15 A  200  ALA CYS PRO GLY ARG ASP ARG ARG THR GLU GLU GLU ASN          
SEQRES  16 A  200  LEU ARG LYS LYS GLY                                          
SEQRES   1 B  200  SER SER SER VAL PRO SER GLN LYS THR TYR GLN GLY SER          
SEQRES   2 B  200  TYR GLY PHE ARG LEU GLY PHE LEU HIS SER GLY THR ALA          
SEQRES   3 B  200  LYS SER VAL THR CYS THR TYR SER PRO ALA LEU ASN LYS          
SEQRES   4 B  200  LEU PHE CYS GLN LEU ALA LYS THR CYS PRO VAL GLN LEU          
SEQRES   5 B  200  TRP VAL ASP SER THR PRO PRO PRO GLY THR ARG VAL ARG          
SEQRES   6 B  200  ALA MET ALA ILE TYR LYS GLN SER GLN HIS MET THR GLU          
SEQRES   7 B  200  VAL VAL ARG ARG CYS PRO HIS HIS GLU ARG CYS SER ASP          
SEQRES   8 B  200  SER ASP GLY LEU ALA PRO PRO GLN HIS LEU ILE ARG VAL          
SEQRES   9 B  200  GLU GLY ASN LEU ARG ALA GLU TYR LEU ASP ASP ARG ASN          
SEQRES  10 B  200  THR PHE ARG HIS SER VAL VAL VAL PRO TYR GLU PRO PRO          
SEQRES  11 B  200  GLU VAL GLY SER ASP CYS THR THR ILE HIS TYR ASN TYR          
SEQRES  12 B  200  MET CYS TYR SER SER CYS MET GLY SER MET ASN ARG ARG          
SEQRES  13 B  200  PRO ILE LEU THR ILE ILE THR LEU GLU ASP SER SER GLY          
SEQRES  14 B  200  ASN LEU LEU GLY ARG ASP SER PHE GLU VAL ARG VAL CYS          
SEQRES  15 B  200  ALA CYS PRO GLY ARG ASP ARG ARG THR GLU GLU GLU ASN          
SEQRES  16 B  200  LEU ARG LYS LYS GLY                                          
SEQRES   1 C  200  SER SER SER VAL PRO SER GLN LYS THR TYR GLN GLY SER          
SEQRES   2 C  200  TYR GLY PHE ARG LEU GLY PHE LEU HIS SER GLY THR ALA          
SEQRES   3 C  200  LYS SER VAL THR CYS THR TYR SER PRO ALA LEU ASN LYS          
SEQRES   4 C  200  LEU PHE CYS GLN LEU ALA LYS THR CYS PRO VAL GLN LEU          
SEQRES   5 C  200  TRP VAL ASP SER THR PRO PRO PRO GLY THR ARG VAL ARG          
SEQRES   6 C  200  ALA MET ALA ILE TYR LYS GLN SER GLN HIS MET THR GLU          
SEQRES   7 C  200  VAL VAL ARG ARG CYS PRO HIS HIS GLU ARG CYS SER ASP          
SEQRES   8 C  200  SER ASP GLY LEU ALA PRO PRO GLN HIS LEU ILE ARG VAL          
SEQRES   9 C  200  GLU GLY ASN LEU ARG ALA GLU TYR LEU ASP ASP ARG ASN          
SEQRES  10 C  200  THR PHE ARG HIS SER VAL VAL VAL PRO TYR GLU PRO PRO          
SEQRES  11 C  200  GLU VAL GLY SER ASP CYS THR THR ILE HIS TYR ASN TYR          
SEQRES  12 C  200  MET CYS TYR SER SER CYS MET GLY SER MET ASN ARG ARG          
SEQRES  13 C  200  PRO ILE LEU THR ILE ILE THR LEU GLU ASP SER SER GLY          
SEQRES  14 C  200  ASN LEU LEU GLY ARG ASP SER PHE GLU VAL ARG VAL CYS          
SEQRES  15 C  200  ALA CYS PRO GLY ARG ASP ARG ARG THR GLU GLU GLU ASN          
SEQRES  16 C  200  LEU ARG LYS LYS GLY                                          
SEQRES   1 D  200  SER SER SER VAL PRO SER GLN LYS THR TYR GLN GLY SER          
SEQRES   2 D  200  TYR GLY PHE ARG LEU GLY PHE LEU HIS SER GLY THR ALA          
SEQRES   3 D  200  LYS SER VAL THR CYS THR TYR SER PRO ALA LEU ASN LYS          
SEQRES   4 D  200  LEU PHE CYS GLN LEU ALA LYS THR CYS PRO VAL GLN LEU          
SEQRES   5 D  200  TRP VAL ASP SER THR PRO PRO PRO GLY THR ARG VAL ARG          
SEQRES   6 D  200  ALA MET ALA ILE TYR LYS GLN SER GLN HIS MET THR GLU          
SEQRES   7 D  200  VAL VAL ARG ARG CYS PRO HIS HIS GLU ARG CYS SER ASP          
SEQRES   8 D  200  SER ASP GLY LEU ALA PRO PRO GLN HIS LEU ILE ARG VAL          
SEQRES   9 D  200  GLU GLY ASN LEU ARG ALA GLU TYR LEU ASP ASP ARG ASN          
SEQRES  10 D  200  THR PHE ARG HIS SER VAL VAL VAL PRO TYR GLU PRO PRO          
SEQRES  11 D  200  GLU VAL GLY SER ASP CYS THR THR ILE HIS TYR ASN TYR          
SEQRES  12 D  200  MET CYS TYR SER SER CYS MET GLY SER MET ASN ARG ARG          
SEQRES  13 D  200  PRO ILE LEU THR ILE ILE THR LEU GLU ASP SER SER GLY          
SEQRES  14 D  200  ASN LEU LEU GLY ARG ASP SER PHE GLU VAL ARG VAL CYS          
SEQRES  15 D  200  ALA CYS PRO GLY ARG ASP ARG ARG THR GLU GLU GLU ASN          
SEQRES  16 D  200  LEU ARG LYS LYS GLY                                          
HET     ZN  A1290       1                                                       
HET     CA  A1291       1                                                       
HET     ZN  B1290       1                                                       
HET     CA  B1291       1                                                       
HET     ZN  C1290       1                                                       
HET     CA  C1291       1                                                       
HET     ZN  D1290       1                                                       
HET     CA  D1291       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CA CALCIUM ION                                                      
FORMUL   5   ZN    4(ZN 2+)                                                     
FORMUL   6   CA    4(CA 2+)                                                     
FORMUL  13  HOH   *754(H2 O1)                                                   
HELIX    1   1 GLN A  165  MET A  169  5                                   5    
HELIX    2   2 CYS A  176  ARG A  181  1                                   6    
HELIX    3   3 CYS A  277  GLU A  287  1                                  11    
HELIX    4   4 CYS B  176  CYS B  182  1                                   7    
HELIX    5   5 CYS B  277  ASN B  288  1                                  12    
HELIX    6   6 GLN C  104  GLY C  108  5                                   5    
HELIX    7   7 CYS C  176  ARG C  181  1                                   6    
HELIX    8   8 CYS C  277  ASN C  288  1                                  12    
HELIX    9   9 GLN D  165  MET D  169  5                                   5    
HELIX   10  10 CYS D  176  CYS D  182  1                                   7    
HELIX   11  11 CYS D  277  ASN D  288  1                                  12    
SHEET    1  AA 4 ARG A 110  GLY A 112  0                                        
SHEET    2  AA 4 CYS A 141  TRP A 146 -1  O  GLN A 144   N  GLY A 112           
SHEET    3  AA 4 THR A 230  TYR A 236 -1  O  THR A 230   N  LEU A 145           
SHEET    4  AA 4 ILE A 195  GLU A 198 -1  O  ARG A 196   N  ASN A 235           
SHEET    1  AB 7 CYS A 124  SER A 127  0                                        
SHEET    2  AB 7 LYS A 132  CYS A 135 -1  O  LYS A 132   N  SER A 127           
SHEET    3  AB 7 LEU A 264  VAL A 274  1  O  GLU A 271   N  LEU A 133           
SHEET    4  AB 7 ILE A 251  GLU A 258 -1  O  ILE A 251   N  VAL A 272           
SHEET    5  AB 7 ARG A 156  TYR A 163 -1  O  ARG A 156   N  GLU A 258           
SHEET    6  AB 7 HIS A 214  PRO A 219 -1  O  VAL A 216   N  ALA A 159           
SHEET    7  AB 7 GLU A 204  ASP A 207 -1  O  GLU A 204   N  VAL A 217           
SHEET    1  BA 4 ARG B 110  GLY B 112  0                                        
SHEET    2  BA 4 CYS B 141  TRP B 146 -1  O  GLN B 144   N  GLY B 112           
SHEET    3  BA 4 THR B 230  TYR B 236 -1  O  THR B 230   N  LEU B 145           
SHEET    4  BA 4 ILE B 195  GLU B 198 -1  O  ARG B 196   N  ASN B 235           
SHEET    1  BB 7 CYS B 124  SER B 127  0                                        
SHEET    2  BB 7 LYS B 132  CYS B 135 -1  O  LYS B 132   N  SER B 127           
SHEET    3  BB 7 LEU B 264  VAL B 274  1  O  GLU B 271   N  LEU B 133           
SHEET    4  BB 7 ILE B 251  GLU B 258 -1  O  ILE B 251   N  VAL B 272           
SHEET    5  BB 7 ARG B 156  TYR B 163 -1  O  ARG B 156   N  GLU B 258           
SHEET    6  BB 7 HIS B 214  PRO B 219 -1  O  VAL B 216   N  ALA B 159           
SHEET    7  BB 7 GLU B 204  ASP B 207 -1  O  GLU B 204   N  VAL B 217           
SHEET    1  CA 4 ARG C 110  GLY C 112  0                                        
SHEET    2  CA 4 CYS C 141  TRP C 146 -1  O  GLN C 144   N  GLY C 112           
SHEET    3  CA 4 THR C 230  TYR C 236 -1  O  THR C 230   N  LEU C 145           
SHEET    4  CA 4 ILE C 195  GLU C 198 -1  O  ARG C 196   N  ASN C 235           
SHEET    1  CB 7 CYS C 124  SER C 127  0                                        
SHEET    2  CB 7 LYS C 132  CYS C 135 -1  O  LYS C 132   N  SER C 127           
SHEET    3  CB 7 LEU C 264  VAL C 274  1  O  GLU C 271   N  LEU C 133           
SHEET    4  CB 7 ILE C 251  GLU C 258 -1  O  ILE C 251   N  VAL C 272           
SHEET    5  CB 7 ARG C 156  TYR C 163 -1  O  ARG C 156   N  GLU C 258           
SHEET    6  CB 7 HIS C 214  PRO C 219 -1  O  VAL C 216   N  ALA C 159           
SHEET    7  CB 7 GLU C 204  ASP C 207 -1  O  GLU C 204   N  VAL C 217           
SHEET    1  DA 4 ARG D 110  GLY D 112  0                                        
SHEET    2  DA 4 CYS D 141  TRP D 146 -1  O  GLN D 144   N  GLY D 112           
SHEET    3  DA 4 CYS D 229  TYR D 236 -1  O  THR D 230   N  LEU D 145           
SHEET    4  DA 4 ILE D 195  GLU D 198 -1  O  ARG D 196   N  ASN D 235           
SHEET    1  DB 7 CYS D 124  SER D 127  0                                        
SHEET    2  DB 7 LYS D 132  CYS D 135 -1  O  LYS D 132   N  SER D 127           
SHEET    3  DB 7 LEU D 264  VAL D 274  1  O  GLU D 271   N  LEU D 133           
SHEET    4  DB 7 ILE D 251  GLU D 258 -1  O  ILE D 251   N  VAL D 272           
SHEET    5  DB 7 ARG D 156  TYR D 163 -1  O  ARG D 156   N  GLU D 258           
SHEET    6  DB 7 HIS D 214  PRO D 219 -1  O  VAL D 216   N  ALA D 159           
SHEET    7  DB 7 GLU D 204  ASP D 207 -1  O  GLU D 204   N  VAL D 217           
LINK        ZN    ZN A1290                 SG  CYS A 238     1555   1555  2.34  
LINK        ZN    ZN A1290                 SG  CYS A 176     1555   1555  2.33  
LINK        ZN    ZN A1290                 ND1 HIS A 179     1555   1555  2.13  
LINK        ZN    ZN A1290                 SG  CYS A 242     1555   1555  2.35  
LINK        CA    CA A1291                 OD1 ASP A 268     1555   1555  2.48  
LINK        CA    CA A1291                 OD2 ASP A 268     1555   1555  2.46  
LINK        CA    CA A1291                 O   HOH A2183     1555   1555  3.06  
LINK        CA    CA A1291                 O   HOH A2041     1555   1555  2.65  
LINK        CA    CA A1291                 O   HOH A2047     1555   1555  2.77  
LINK        CA    CA A1291                 O   HOH A2184     1555   1555  2.58  
LINK        CA    CA A1291                 O   HOH A2186     1555   1555  2.63  
LINK        CA    CA A1291                 O   HOH A2020     1555   1555  2.49  
LINK        ZN    ZN B1290                 SG  CYS B 238     1555   1555  2.37  
LINK        ZN    ZN B1290                 SG  CYS B 176     1555   1555  2.33  
LINK        ZN    ZN B1290                 ND1 HIS B 179     1555   1555  2.03  
LINK        ZN    ZN B1290                 SG  CYS B 242     1555   1555  2.30  
LINK        CA    CA B1291                 O   HOH B2050     1555   1555  2.52  
LINK        CA    CA B1291                 O   HOH B2049     1555   1555  2.71  
LINK        CA    CA B1291                 O   HOH B2024     1555   1555  2.54  
LINK        CA    CA B1291                 O   HOH B2180     1555   1555  2.57  
LINK        CA    CA B1291                 O   HOH B2178     1555   1555  2.76  
LINK        CA    CA B1291                 O   HOH B2177     1555   1555  2.52  
LINK        CA    CA B1291                 OD2 ASP B 268     1555   1555  2.51  
LINK        CA    CA B1291                 OD1 ASP B 268     1555   1555  2.61  
LINK        ZN    ZN C1290                 SG  CYS C 242     1555   1555  2.41  
LINK        ZN    ZN C1290                 SG  CYS C 238     1555   1555  2.30  
LINK        ZN    ZN C1290                 ND1 HIS C 179     1555   1555  2.18  
LINK        ZN    ZN C1290                 SG  CYS C 176     1555   1555  2.35  
LINK        CA    CA C1291                 O   HOH C2042     1555   1555  2.48  
LINK        CA    CA C1291                 O   HOH C2171     1555   1555  2.58  
LINK        CA    CA C1291                 OD1 ASP C 268     1555   1555  2.52  
LINK        CA    CA C1291                 O   HOH C2016     1555   1555  2.50  
LINK        CA    CA C1291                 O   HOH C2043     1555   1555  2.85  
LINK        CA    CA C1291                 O   HOH C2168     1555   1555  2.96  
LINK        CA    CA C1291                 OD2 ASP C 268     1555   1555  2.49  
LINK        CA    CA C1291                 O   HOH C2167     1555   1555  2.60  
LINK        ZN    ZN D1290                 SG  CYS D 242     1555   1555  2.34  
LINK        ZN    ZN D1290                 SG  CYS D 238     1555   1555  2.37  
LINK        ZN    ZN D1290                 ND1 HIS D 179     1555   1555  1.96  
LINK        ZN    ZN D1290                 SG  CYS D 176     1555   1555  2.34  
LINK        CA    CA D1291                 OD2 ASP D 268     1555   1555  2.60  
LINK        CA    CA D1291                 O   HOH D2019     1555   1555  2.53  
LINK        CA    CA D1291                 O   HOH D2038     1555   1555  2.54  
LINK        CA    CA D1291                 O   HOH D2158     1555   1555  2.65  
LINK        CA    CA D1291                 O   HOH D2162     1555   1555  2.64  
LINK        CA    CA D1291                 O   HOH D2159     1555   1555  2.67  
LINK        CA    CA D1291                 OD1 ASP D 268     1555   1555  2.65  
SITE     1 AC1  4 CYS A 176  HIS A 179  CYS A 238  CYS A 242                    
SITE     1 AC2  7 ASP A 268  HOH A2020  HOH A2041  HOH A2047                    
SITE     2 AC2  7 HOH A2183  HOH A2184  HOH A2186                               
SITE     1 AC3  4 CYS B 176  HIS B 179  CYS B 238  CYS B 242                    
SITE     1 AC4  7 ASP B 268  HOH B2024  HOH B2049  HOH B2050                    
SITE     2 AC4  7 HOH B2177  HOH B2178  HOH B2180                               
SITE     1 AC5  4 CYS C 176  HIS C 179  CYS C 238  CYS C 242                    
SITE     1 AC6  7 ASP C 268  HOH C2016  HOH C2042  HOH C2043                    
SITE     2 AC6  7 HOH C2167  HOH C2168  HOH C2171                               
SITE     1 AC7  4 CYS D 176  HIS D 179  CYS D 238  CYS D 242                    
SITE     1 AC8  6 ASP D 268  HOH D2019  HOH D2038  HOH D2158                    
SITE     2 AC8  6 HOH D2159  HOH D2162                                          
CRYST1   68.514   73.076   84.760  90.00  90.05  90.00 P 1 21 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      0.014596  0.000000  0.000013        0.00000                         
SCALE2      0.000000  0.013684  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011798        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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