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Database: PDB
Entry: 5AOK
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HEADER    CELL CYCLE                              10-SEP-15   5AOK              
TITLE     STRUCTURE OF THE P53 CANCER MUTANT Y220C WITH BOUND SMALL MOLECULE    
TITLE    2 PHIKAN7099                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELLULAR TUMOR ANTIGEN P53;                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: DNA-BINDING DOMAIN, UNP RESIDUES 94-312;                   
COMPND   5 SYNONYM: ANTIGEN NY-CO-13, PHOSPHOPROTEIN P53, TUMOR SUPPRESSOR P53, 
COMPND   6 P53;                                                                 
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    CELL CYCLE, P53, CANCER, TUMOR SUPPRESSION, DNA BINDING, CANCER       
KEYWDS   2 THERAPY, SMALL-MOLECULE STABILIZERS, MOLECULAR CHAPERONE             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.C.JOERGER                                                           
REVDAT   3   15-MAY-19 5AOK    1       REMARK                                   
REVDAT   2   08-MAY-19 5AOK    1       REMARK                                   
REVDAT   1   16-DEC-15 5AOK    0                                                
JRNL        AUTH   A.C.JOERGER,M.R.BAUER,R.WILCKEN,M.G.J.BAUD,H.HARBRECHT,      
JRNL        AUTH 2 T.E.EXNER,F.M.BOECKLER,J.SPENCER,A.R.FERSHT                  
JRNL        TITL   EXPLOITING TRANSIENT PROTEIN STATES FOR THE DESIGN OF        
JRNL        TITL 2 SMALL-MOLECULE STABILIZERS OF MUTANT P53.                    
JRNL        REF    STRUCTURE                     V.  23  2246 2015              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   26636255                                                     
JRNL        DOI    10.1016/J.STR.2015.10.016                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.42                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 103279                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.146                           
REMARK   3   R VALUE            (WORKING SET) : 0.145                           
REMARK   3   FREE R VALUE                     : 0.169                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5183                            
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 29.4273 -  4.1909    0.97     3587   157  0.1637 0.1469        
REMARK   3     2  4.1909 -  3.3279    0.98     3444   178  0.1454 0.1727        
REMARK   3     3  3.3279 -  2.9077    0.98     3413   164  0.1554 0.1804        
REMARK   3     4  2.9077 -  2.6420    0.99     3383   176  0.1566 0.1750        
REMARK   3     5  2.6420 -  2.4527    0.98     3391   175  0.1527 0.1601        
REMARK   3     6  2.4527 -  2.3082    0.98     3353   168  0.1484 0.1695        
REMARK   3     7  2.3082 -  2.1926    0.98     3342   162  0.1452 0.1751        
REMARK   3     8  2.1926 -  2.0972    0.98     3306   191  0.1436 0.1770        
REMARK   3     9  2.0972 -  2.0165    0.98     3348   176  0.1402 0.1514        
REMARK   3    10  2.0165 -  1.9469    0.97     3309   163  0.1336 0.1518        
REMARK   3    11  1.9469 -  1.8861    0.97     3301   170  0.1293 0.1876        
REMARK   3    12  1.8861 -  1.8321    0.97     3271   195  0.1319 0.1614        
REMARK   3    13  1.8321 -  1.7839    0.97     3224   196  0.1207 0.1464        
REMARK   3    14  1.7839 -  1.7404    0.97     3254   183  0.1140 0.1479        
REMARK   3    15  1.7404 -  1.7008    0.96     3244   177  0.1180 0.1467        
REMARK   3    16  1.7008 -  1.6647    0.96     3234   178  0.1187 0.1584        
REMARK   3    17  1.6647 -  1.6314    0.96     3242   176  0.1206 0.1540        
REMARK   3    18  1.6314 -  1.6006    0.96     3248   183  0.1224 0.1600        
REMARK   3    19  1.6006 -  1.5720    0.96     3194   188  0.1267 0.1624        
REMARK   3    20  1.5720 -  1.5453    0.95     3217   154  0.1287 0.1667        
REMARK   3    21  1.5453 -  1.5204    0.95     3203   183  0.1318 0.1665        
REMARK   3    22  1.5204 -  1.4970    0.95     3181   176  0.1342 0.1704        
REMARK   3    23  1.4970 -  1.4750    0.95     3221   163  0.1311 0.1844        
REMARK   3    24  1.4750 -  1.4542    0.95     3192   147  0.1374 0.1981        
REMARK   3    25  1.4542 -  1.4346    0.94     3200   160  0.1493 0.1679        
REMARK   3    26  1.4346 -  1.4160    0.95     3168   164  0.1627 0.2218        
REMARK   3    27  1.4160 -  1.3983    0.94     3178   156  0.1692 0.1966        
REMARK   3    28  1.3983 -  1.3814    0.95     3197   156  0.1805 0.2009        
REMARK   3    29  1.3814 -  1.3653    0.94     3108   196  0.2000 0.2352        
REMARK   3    30  1.3653 -  1.3500    0.93     3143   172  0.2090 0.2694        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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) : 15.600           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 10.49                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.50                          
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      :  0.006           3323                                  
REMARK   3   ANGLE     :  1.076           4532                                  
REMARK   3   CHIRALITY :  0.045            490                                  
REMARK   3   PLANARITY :  0.007            599                                  
REMARK   3   DIHEDRAL  : 13.780           1300                                  
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 5AOK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-SEP-15.                  
REMARK 100 THE DEPOSITION ID IS D_1290064972.                                   
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                                
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                       : I04                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0163                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 103354                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.5                               
REMARK 200  DATA REDUNDANCY                : 6.100                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 2J1X                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
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: SITTING-DROP VAPOR DIFFUSION AT 21       
REMARK 280  DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM         
REMARK 280  PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100      
REMARK 280  MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT.     
REMARK 280  SOAKING BUFFER: 38 MM COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM       
REMARK 280  SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20    
REMARK 280  % (V/V) GLYCEROL, 150 MM KCL., VAPOR DIFFUSION, SITTING DROP,       
REMARK 280  TEMPERATURE 294K                                                    
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       32.50650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       52.58850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.49450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       52.58850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.50650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.49450            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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     LYS A   291                                                      
REMARK 465     LYS A   292                                                      
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 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   O    HOH A  2075     O    HOH A  2076              2.14            
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    LEU A 188      -46.83   -134.41                                   
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 A1313  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 176   SG                                                     
REMARK 620 2 HIS A 179   ND1 106.3                                              
REMARK 620 3 CYS A 238   SG  109.8 102.7                                        
REMARK 620 4 CYS A 238   SG  108.8 127.1  27.6                                  
REMARK 620 5 CYS A 242   SG  110.5 105.6 120.7  97.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1300  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 238   SG                                                     
REMARK 620 2 CYS B 242   SG  116.2                                              
REMARK 620 3 CYS B 176   SG  110.9 110.8                                        
REMARK 620 4 HIS B 179   ND1 107.3 105.9 104.9                                  
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 GOL A 1291                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1313                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1292                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 1293                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOH A 1292                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOH B 1294                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5AOI   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE P53 CANCER MUTANT Y220C IN COMPLEX WITH AN INDOLE-  
REMARK 900 BASED SMALL MOLECULE                                                 
REMARK 900 RELATED ID: 5AOJ   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE P53 CANCER MUTANT Y220C IN COMPLEX WITH 2-HYDROXY-  
REMARK 900 3,5-DIIODO-4-(1H-PYRROL-1-YL) BENZOIC ACID                           
REMARK 900 RELATED ID: 5AOL   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE P53 CANCER MUTANT Y220C WITH BOUND 3-BROMO-5-       
REMARK 900 (TRIFLUOROMETHYL)BENZENE-1,2-DIAMINE                                 
REMARK 900 RELATED ID: 5AOM   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE P53 CANCER MUTANT Y220C WITH BOUND SMALL MOLECULE   
REMARK 900 PHIKAN883                                                            
DBREF  5AOK A   94   312  UNP    P04637   P53_HUMAN       94    312             
DBREF  5AOK B   94   312  UNP    P04637   P53_HUMAN       94    312             
SEQADV 5AOK LEU A  133  UNP  P04637    MET   133 ENGINEERED MUTATION            
SEQADV 5AOK ALA A  203  UNP  P04637    VAL   203 ENGINEERED MUTATION            
SEQADV 5AOK CYS A  220  UNP  P04637    TYR   220 ENGINEERED MUTATION            
SEQADV 5AOK TYR A  239  UNP  P04637    ASN   239 ENGINEERED MUTATION            
SEQADV 5AOK ASP A  268  UNP  P04637    ASN   268 ENGINEERED MUTATION            
SEQADV 5AOK LEU B  133  UNP  P04637    MET   133 ENGINEERED MUTATION            
SEQADV 5AOK ALA B  203  UNP  P04637    VAL   203 ENGINEERED MUTATION            
SEQADV 5AOK CYS B  220  UNP  P04637    TYR   220 ENGINEERED MUTATION            
SEQADV 5AOK TYR B  239  UNP  P04637    ASN   239 ENGINEERED MUTATION            
SEQADV 5AOK 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  A1313       1                                                       
HET    GOL  A1291       6                                                       
HET    GOH  A1292      18                                                       
HET     ZN  B1300       1                                                       
HET    GOL  B1292       6                                                       
HET    PEG  B1293       7                                                       
HET    GOH  B1294      18                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     GOL GLYCEROL                                                         
HETNAM     GOH 5-[2-CYCLOPROPYL-5-(1H-PYRROL-1-YL)-1,3-OXAZOL-4-YL]-            
HETNAM   2 GOH  1H-1,2,3,4-TETRAZOLE                                            
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   4  GOL    2(C3 H8 O3)                                                  
FORMUL   5  GOH    2(C11 H10 N6 O)                                              
FORMUL   8  PEG    C4 H10 O3                                                    
FORMUL  10  HOH   *566(H2 O)                                                    
HELIX    1   1 GLN A  165  MET A  169  5                                   5    
HELIX    2   2 HIS A  178  CYS A  182  5                                   5    
HELIX    3   3 CYS A  277  ARG A  290  1                                  14    
HELIX    4   4 HIS B  178  CYS B  182  5                                   5    
HELIX    5   5 CYS B  277  LYS B  291  1                                  15    
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  VAL A 197 -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  VAL B 197 -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           
LINK        ZN    ZN A1313                 SG  CYS A 176     1555   1555  2.33  
LINK        ZN    ZN A1313                 ND1 HIS A 179     1555   1555  2.01  
LINK        ZN    ZN A1313                 SG ACYS A 238     1555   1555  2.38  
LINK        ZN    ZN A1313                 SG BCYS A 238     1555   1555  2.22  
LINK        ZN    ZN A1313                 SG  CYS A 242     1555   1555  2.31  
LINK        ZN    ZN B1300                 SG  CYS B 238     1555   1555  2.32  
LINK        ZN    ZN B1300                 SG  CYS B 242     1555   1555  2.30  
LINK        ZN    ZN B1300                 SG  CYS B 176     1555   1555  2.33  
LINK        ZN    ZN B1300                 ND1 HIS B 179     1555   1555  2.04  
SITE     1 AC1  8 PRO A 219  GLU A 221  THR A 230  THR A 231                    
SITE     2 AC1  8 ILE A 232  GOH A1292  HOH A2212  HOH A2213                    
SITE     1 AC2  4 CYS A 176  HIS A 179  CYS A 238  CYS A 242                    
SITE     1 AC3  9 PRO B 219  CYS B 220  GLU B 221  THR B 230                    
SITE     2 AC3  9 THR B 231  ILE B 232  GOH B1294  HOH B2196                    
SITE     3 AC3  9 HOH B2197                                                     
SITE     1 AC4  4 HIS B 115  SER B 116  GLY B 117  ARG B 282                    
SITE     1 AC5  4 CYS B 176  HIS B 179  CYS B 238  CYS B 242                    
SITE     1 AC6 12 VAL A 147  THR A 150  PRO A 151  CYS A 220                    
SITE     2 AC6 12 GLU A 221  PRO A 223  THR A 230  GOL A1291                    
SITE     3 AC6 12 HOH A2094  HOH A2095  HOH A2107  HOH A2288                    
SITE     1 AC7 14 VAL B 147  THR B 150  PRO B 151  PRO B 152                    
SITE     2 AC7 14 CYS B 220  GLU B 221  PRO B 223  THR B 230                    
SITE     3 AC7 14 GOL B1292  HOH B2082  HOH B2083  HOH B2084                    
SITE     4 AC7 14 HOH B2097  HOH B2278                                          
CRYST1   65.013   70.989  105.177  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      0.015382  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014087  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009508        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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