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Database: PDB
Entry: 5O1B
LinkDB: 5O1B
Original site: 5O1B 
HEADER    DNA BINDING PROTEIN                     18-MAY-17   5O1B              
TITLE     P53 CANCER MUTANT Y220C IN COMPLEX WITH COMPOUND MB84                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELLULAR TUMOR ANTIGEN P53;                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 94-312;                                       
COMPND   5 SYNONYM: ANTIGEN NY-CO-13,PHOSPHOPROTEIN P53,TUMOR SUPPRESSOR P53;   
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: TP53, P53;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    P53, TUMOR SUPPRESSOR, CANCER MUTATION, PROTEIN STABILIZATION, SMALL- 
KEYWDS   2 MOLECULE STABILIZERS, CANCER THERAPY, DNA BINDING PROTEIN, MOLECULAR 
KEYWDS   3 CHAPERONES                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.C.JOERGER,M.R.BAUER,M.G.J.BAUD,A.R.FERSHT                           
REVDAT   1   09-MAY-18 5O1B    0                                                
JRNL        AUTH   M.G.J.BAUD,M.R.BAUER,L.VERDUCI,F.A.DINGLER,K.J.PATEL,        
JRNL        AUTH 2 D.HORIL ROY,A.C.JOERGER,A.R.FERSHT                           
JRNL        TITL   AMINOBENZOTHIAZOLE DERIVATIVES STABILIZE THE THERMOLABILE    
JRNL        TITL 2 P53 CANCER MUTANT Y220C AND SHOW ANTICANCER ACTIVITY IN      
JRNL        TITL 3 P53-Y220C CELL LINES.                                        
JRNL        REF    EUR J MED CHEM                V. 152   101 2018              
JRNL        REFN                   ISSN 1768-3254                               
JRNL        PMID   29702446                                                     
JRNL        DOI    10.1016/J.EJMECH.2018.04.035                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.43 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.43                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.52                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 89795                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.152                           
REMARK   3   R VALUE            (WORKING SET) : 0.151                           
REMARK   3   FREE R VALUE                     : 0.174                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.920                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4421                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 28.5202 -  4.4379    0.99     3104   140  0.1810 0.1690        
REMARK   3     2  4.4379 -  3.5246    0.99     2969   146  0.1487 0.1707        
REMARK   3     3  3.5246 -  3.0797    0.99     2917   147  0.1543 0.1707        
REMARK   3     4  3.0797 -  2.7984    0.99     2920   145  0.1585 0.1682        
REMARK   3     5  2.7984 -  2.5979    1.00     2877   160  0.1585 0.1949        
REMARK   3     6  2.5979 -  2.4449    1.00     2909   146  0.1601 0.1756        
REMARK   3     7  2.4449 -  2.3225    0.99     2907   141  0.1519 0.1775        
REMARK   3     8  2.3225 -  2.2214    1.00     2874   141  0.1447 0.1575        
REMARK   3     9  2.2214 -  2.1359    0.99     2871   162  0.1395 0.1861        
REMARK   3    10  2.1359 -  2.0622    0.99     2828   173  0.1422 0.1819        
REMARK   3    11  2.0622 -  1.9978    0.99     2868   133  0.1386 0.1612        
REMARK   3    12  1.9978 -  1.9407    0.99     2879   149  0.1391 0.1610        
REMARK   3    13  1.9407 -  1.8896    0.99     2862   143  0.1322 0.1837        
REMARK   3    14  1.8896 -  1.8435    0.99     2817   160  0.1407 0.1573        
REMARK   3    15  1.8435 -  1.8016    0.99     2808   183  0.1282 0.1856        
REMARK   3    16  1.8016 -  1.7633    0.99     2807   149  0.1276 0.1586        
REMARK   3    17  1.7633 -  1.7280    0.99     2852   146  0.1289 0.1524        
REMARK   3    18  1.7280 -  1.6954    0.99     2807   166  0.1293 0.1754        
REMARK   3    19  1.6954 -  1.6651    0.98     2814   154  0.1282 0.1758        
REMARK   3    20  1.6651 -  1.6369    0.98     2867   119  0.1298 0.1403        
REMARK   3    21  1.6369 -  1.6105    0.99     2795   143  0.1350 0.1526        
REMARK   3    22  1.6105 -  1.5857    0.99     2842   139  0.1416 0.1713        
REMARK   3    23  1.5857 -  1.5624    0.98     2790   154  0.1448 0.2040        
REMARK   3    24  1.5624 -  1.5404    0.99     2848   132  0.1462 0.1836        
REMARK   3    25  1.5404 -  1.5196    0.98     2769   149  0.1458 0.1963        
REMARK   3    26  1.5196 -  1.4999    0.98     2788   156  0.1513 0.1676        
REMARK   3    27  1.4999 -  1.4811    0.98     2796   124  0.1588 0.1690        
REMARK   3    28  1.4811 -  1.4633    0.97     2789   137  0.1706 0.2369        
REMARK   3    29  1.4633 -  1.4462    0.96     2699   159  0.1796 0.2178        
REMARK   3    30  1.4462 -  1.4300    0.94     2701   125  0.1985 0.2380        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.110            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.450           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 11.60                          
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           3255                                  
REMARK   3   ANGLE     :  0.783           4436                                  
REMARK   3   CHIRALITY :  0.082            487                                  
REMARK   3   PLANARITY :  0.006            582                                  
REMARK   3   DIHEDRAL  : 16.083           1225                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5O1B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-MAY-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200003269.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-MAR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.976250                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 89897                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.430                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.43                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.51                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 2J1X                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 6 MG/ML PROTEIN IN     
REMARK 280  25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR     
REMARK 280  BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000,   
REMARK 280  5 MM DTT. SOAKING BUFFER: 30 MM COMPOUND IN 100 MM HEPES, PH        
REMARK 280  7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE         
REMARK 280  GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL., VAPOR DIFFUSION,     
REMARK 280  SITTING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       32.57600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       52.67200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.58300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       52.67200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.57600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.58300            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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 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     SER A    95                                                      
REMARK 465     GLY A   293                                                      
REMARK 465     GLU A   294                                                      
REMARK 465     PRO A   295                                                      
REMARK 465     HIS A   296                                                      
REMARK 465     HIS A   297                                                      
REMARK 465     GLU A   298                                                      
REMARK 465     LEU A   299                                                      
REMARK 465     PRO A   300                                                      
REMARK 465     PRO A   301                                                      
REMARK 465     GLY A   302                                                      
REMARK 465     SER A   303                                                      
REMARK 465     THR A   304                                                      
REMARK 465     LYS A   305                                                      
REMARK 465     ARG A   306                                                      
REMARK 465     ALA A   307                                                      
REMARK 465     LEU A   308                                                      
REMARK 465     PRO A   309                                                      
REMARK 465     ASN A   310                                                      
REMARK 465     ASN A   311                                                      
REMARK 465     THR A   312                                                      
REMARK 465     LYS B   292                                                      
REMARK 465     GLY B   293                                                      
REMARK 465     GLU B   294                                                      
REMARK 465     PRO B   295                                                      
REMARK 465     HIS B   296                                                      
REMARK 465     HIS B   297                                                      
REMARK 465     GLU B   298                                                      
REMARK 465     LEU B   299                                                      
REMARK 465     PRO B   300                                                      
REMARK 465     PRO B   301                                                      
REMARK 465     GLY B   302                                                      
REMARK 465     SER B   303                                                      
REMARK 465     THR B   304                                                      
REMARK 465     LYS B   305                                                      
REMARK 465     ARG B   306                                                      
REMARK 465     ALA B   307                                                      
REMARK 465     LEU B   308                                                      
REMARK 465     PRO B   309                                                      
REMARK 465     ASN B   310                                                      
REMARK 465     ASN B   311                                                      
REMARK 465     THR B   312                                                      
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 120    CG   CD   CE   NZ                                   
REMARK 470     ARG A 209    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A 224    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 280    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A 287    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 290    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 291    CG   CD   CE   NZ                                   
REMARK 470     LYS A 292    CG   CD   CE   NZ                                   
REMARK 470     SER B  94    N    CB   OG                                        
REMARK 470     LYS B 101    CD   CE   NZ                                        
REMARK 470     LYS B 120    CG   CD   CE   NZ                                   
REMARK 470     ARG B 209    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU B 224    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 290    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 291    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER A   261     O    HOH A   501              2.19            
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    ASP A 184       31.89    -94.42                                   
REMARK 500    LEU A 188      -46.46   -132.42                                   
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 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 176   SG                                                     
REMARK 620 2 HIS A 179   ND1 105.9                                              
REMARK 620 3 CYS A 238   SG  110.4 106.7                                        
REMARK 620 4 CYS A 242   SG  111.1 105.9 116.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 176   SG                                                     
REMARK 620 2 HIS B 179   ND1 104.3                                              
REMARK 620 3 CYS B 238   SG  110.9 108.1                                        
REMARK 620 4 CYS B 242   SG  111.2 106.2 115.4                                  
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 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9H2 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9H2 B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 404                 
DBREF  5O1B A   94   312  UNP    P04637   P53_HUMAN       94    312             
DBREF  5O1B B   94   312  UNP    P04637   P53_HUMAN       94    312             
SEQADV 5O1B LEU A  133  UNP  P04637    MET   133 ENGINEERED MUTATION            
SEQADV 5O1B ALA A  203  UNP  P04637    VAL   203 ENGINEERED MUTATION            
SEQADV 5O1B CYS A  220  UNP  P04637    TYR   220 ENGINEERED MUTATION            
SEQADV 5O1B TYR A  239  UNP  P04637    ASN   239 ENGINEERED MUTATION            
SEQADV 5O1B ASP A  268  UNP  P04637    ASN   268 ENGINEERED MUTATION            
SEQADV 5O1B LEU B  133  UNP  P04637    MET   133 ENGINEERED MUTATION            
SEQADV 5O1B ALA B  203  UNP  P04637    VAL   203 ENGINEERED MUTATION            
SEQADV 5O1B CYS B  220  UNP  P04637    TYR   220 ENGINEERED MUTATION            
SEQADV 5O1B TYR B  239  UNP  P04637    ASN   239 ENGINEERED MUTATION            
SEQADV 5O1B ASP B  268  UNP  P04637    ASN   268 ENGINEERED MUTATION            
SEQRES   1 A  219  SER SER SER VAL PRO SER GLN LYS THR TYR GLN GLY SER          
SEQRES   2 A  219  TYR GLY PHE ARG LEU GLY PHE LEU HIS SER GLY THR ALA          
SEQRES   3 A  219  LYS SER VAL THR CYS THR TYR SER PRO ALA LEU ASN LYS          
SEQRES   4 A  219  LEU PHE CYS GLN LEU ALA LYS THR CYS PRO VAL GLN LEU          
SEQRES   5 A  219  TRP VAL ASP SER THR PRO PRO PRO GLY THR ARG VAL ARG          
SEQRES   6 A  219  ALA MET ALA ILE TYR LYS GLN SER GLN HIS MET THR GLU          
SEQRES   7 A  219  VAL VAL ARG ARG CYS PRO HIS HIS GLU ARG CYS SER ASP          
SEQRES   8 A  219  SER ASP GLY LEU ALA PRO PRO GLN HIS LEU ILE ARG VAL          
SEQRES   9 A  219  GLU GLY ASN LEU ARG ALA GLU TYR LEU ASP ASP ARG ASN          
SEQRES  10 A  219  THR PHE ARG HIS SER VAL VAL VAL PRO CYS GLU PRO PRO          
SEQRES  11 A  219  GLU VAL GLY SER ASP CYS THR THR ILE HIS TYR ASN TYR          
SEQRES  12 A  219  MET CYS TYR SER SER CYS MET GLY GLY MET ASN ARG ARG          
SEQRES  13 A  219  PRO ILE LEU THR ILE ILE THR LEU GLU ASP SER SER GLY          
SEQRES  14 A  219  ASN LEU LEU GLY ARG ASP SER PHE GLU VAL ARG VAL CYS          
SEQRES  15 A  219  ALA CYS PRO GLY ARG ASP ARG ARG THR GLU GLU GLU ASN          
SEQRES  16 A  219  LEU ARG LYS LYS GLY GLU PRO HIS HIS GLU LEU PRO PRO          
SEQRES  17 A  219  GLY SER THR LYS ARG ALA LEU PRO ASN ASN THR                  
SEQRES   1 B  219  SER SER SER VAL PRO SER GLN LYS THR TYR GLN GLY SER          
SEQRES   2 B  219  TYR GLY PHE ARG LEU GLY PHE LEU HIS SER GLY THR ALA          
SEQRES   3 B  219  LYS SER VAL THR CYS THR TYR SER PRO ALA LEU ASN LYS          
SEQRES   4 B  219  LEU PHE CYS GLN LEU ALA LYS THR CYS PRO VAL GLN LEU          
SEQRES   5 B  219  TRP VAL ASP SER THR PRO PRO PRO GLY THR ARG VAL ARG          
SEQRES   6 B  219  ALA MET ALA ILE TYR LYS GLN SER GLN HIS MET THR GLU          
SEQRES   7 B  219  VAL VAL ARG ARG CYS PRO HIS HIS GLU ARG CYS SER ASP          
SEQRES   8 B  219  SER ASP GLY LEU ALA PRO PRO GLN HIS LEU ILE ARG VAL          
SEQRES   9 B  219  GLU GLY ASN LEU ARG ALA GLU TYR LEU ASP ASP ARG ASN          
SEQRES  10 B  219  THR PHE ARG HIS SER VAL VAL VAL PRO CYS GLU PRO PRO          
SEQRES  11 B  219  GLU VAL GLY SER ASP CYS THR THR ILE HIS TYR ASN TYR          
SEQRES  12 B  219  MET CYS TYR SER SER CYS MET GLY GLY MET ASN ARG ARG          
SEQRES  13 B  219  PRO ILE LEU THR ILE ILE THR LEU GLU ASP SER SER GLY          
SEQRES  14 B  219  ASN LEU LEU GLY ARG ASP SER PHE GLU VAL ARG VAL CYS          
SEQRES  15 B  219  ALA CYS PRO GLY ARG ASP ARG ARG THR GLU GLU GLU ASN          
SEQRES  16 B  219  LEU ARG LYS LYS GLY GLU PRO HIS HIS GLU LEU PRO PRO          
SEQRES  17 B  219  GLY SER THR LYS ARG ALA LEU PRO ASN ASN THR                  
HET     ZN  A 401       1                                                       
HET    9H2  A 402      16                                                       
HET    GOL  A 403       6                                                       
HET    GOL  A 404       6                                                       
HET     ZN  B 401       1                                                       
HET    9H2  B 402      16                                                       
HET    GOL  B 403       6                                                       
HET    GOL  B 404       6                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     9H2 6-(HYDROXYMETHYL)-2,4-BIS(IODANYL)-3-PYRROL-1-YL-PHENOL          
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   4  9H2    2(C11 H9 I2 N O2)                                            
FORMUL   5  GOL    4(C3 H8 O3)                                                  
FORMUL  11  HOH   *462(H2 O)                                                    
HELIX    1 AA1 GLN A  165  MET A  169  5                                   5    
HELIX    2 AA2 HIS A  178  CYS A  182  5                                   5    
HELIX    3 AA3 CYS A  277  LYS A  292  1                                  16    
HELIX    4 AA4 HIS B  178  CYS B  182  5                                   5    
HELIX    5 AA5 CYS B  277  LYS B  291  1                                  15    
SHEET    1 AA1 4 ARG A 110  GLY A 112  0                                        
SHEET    2 AA1 4 CYS A 141  TRP A 146 -1  O  GLN A 144   N  GLY A 112           
SHEET    3 AA1 4 THR A 230  TYR A 236 -1  O  THR A 230   N  LEU A 145           
SHEET    4 AA1 4 ILE A 195  VAL A 197 -1  N  ARG A 196   O  ASN A 235           
SHEET    1 AA2 7 CYS A 124  SER A 127  0                                        
SHEET    2 AA2 7 LYS A 132  CYS A 135 -1  O  PHE A 134   N  THR A 125           
SHEET    3 AA2 7 LEU A 264  VAL A 274  1  O  GLU A 271   N  LEU A 133           
SHEET    4 AA2 7 ILE A 251  GLU A 258 -1  N  THR A 253   O  PHE A 270           
SHEET    5 AA2 7 ARG A 156  TYR A 163 -1  N  MET A 160   O  ILE A 254           
SHEET    6 AA2 7 HIS A 214  PRO A 219 -1  O  VAL A 218   N  VAL A 157           
SHEET    7 AA2 7 GLU A 204  ASP A 207 -1  N  GLU A 204   O  VAL A 217           
SHEET    1 AA3 4 ARG B 110  GLY B 112  0                                        
SHEET    2 AA3 4 CYS B 141  TRP B 146 -1  O  GLN B 144   N  GLY B 112           
SHEET    3 AA3 4 THR B 230  TYR B 236 -1  O  THR B 230   N  LEU B 145           
SHEET    4 AA3 4 ILE B 195  VAL B 197 -1  N  ARG B 196   O  ASN B 235           
SHEET    1 AA4 7 CYS B 124  SER B 127  0                                        
SHEET    2 AA4 7 LYS B 132  CYS B 135 -1  O  LYS B 132   N  SER B 127           
SHEET    3 AA4 7 LEU B 264  VAL B 274  1  O  GLU B 271   N  LEU B 133           
SHEET    4 AA4 7 ILE B 251  GLU B 258 -1  N  THR B 253   O  PHE B 270           
SHEET    5 AA4 7 ARG B 156  TYR B 163 -1  N  MET B 160   O  ILE B 254           
SHEET    6 AA4 7 HIS B 214  PRO B 219 -1  O  VAL B 218   N  VAL B 157           
SHEET    7 AA4 7 GLU B 204  ASP B 207 -1  N  LEU B 206   O  SER B 215           
LINK         SG  CYS A 176                ZN    ZN A 401     1555   1555  2.31  
LINK         ND1 HIS A 179                ZN    ZN A 401     1555   1555  1.99  
LINK         SG  CYS A 238                ZN    ZN A 401     1555   1555  2.31  
LINK         SG  CYS A 242                ZN    ZN A 401     1555   1555  2.30  
LINK         SG  CYS B 176                ZN    ZN B 401     1555   1555  2.32  
LINK         ND1 HIS B 179                ZN    ZN B 401     1555   1555  2.06  
LINK         SG  CYS B 238                ZN    ZN B 401     1555   1555  2.32  
LINK         SG  CYS B 242                ZN    ZN B 401     1555   1555  2.31  
SITE     1 AC1  4 CYS A 176  HIS A 179  CYS A 238  CYS A 242                    
SITE     1 AC2  8 LEU A 145  VAL A 147  THR A 150  CYS A 220                    
SITE     2 AC2  8 GLU A 221  PRO A 223  THR A 230  HOH A 525                    
SITE     1 AC3  5 SER A 241  CYS A 275  ALA A 276  HOH A 583                    
SITE     2 AC3  5 HOH A 611                                                     
SITE     1 AC4  6 ARG A 174  GLN A 192  ASP A 207  PHE A 212                    
SITE     2 AC4  6 HIS A 214  HOH A 533                                          
SITE     1 AC5  4 CYS B 176  HIS B 179  CYS B 238  CYS B 242                    
SITE     1 AC6  9 LEU B 145  VAL B 147  THR B 150  CYS B 220                    
SITE     2 AC6  9 GLU B 221  PRO B 223  THR B 230  HOH B 537                    
SITE     3 AC6  9 HOH B 568                                                     
SITE     1 AC7  5 TYR B 239  SER B 241  CYS B 275  ALA B 276                    
SITE     2 AC7  5 HOH B 559                                                     
SITE     1 AC8  7 ARG B 174  GLN B 192  ASP B 207  PHE B 212                    
SITE     2 AC8  7 HIS B 214  HOH B 503  HOH B 565                               
CRYST1   65.152   71.166  105.344  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015349  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014052  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009493        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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