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Database: PDB
Entry: 4HJE
LinkDB: 4HJE
Original site: 4HJE 
HEADER    TRANSCRIPTION/DNA                       12-OCT-12   4HJE              
TITLE     CRYSTAL STRUCTURE OF P53 CORE DOMAIN IN COMPLEX WITH DNA              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELLULAR TUMOR ANTIGEN P53;                                
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 92-291;                                       
COMPND   5 SYNONYM: ANTIGEN NY-CO-13, PHOSPHOPROTEIN P53, TUMOR SUPPRESSOR P53; 
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: DNA (5'-                                                   
COMPND   9 D(*TP*CP*AP*CP*AP*AP*GP*TP*TP*AP*GP*AP*GP*AP*CP*AP*AP*GP*CP*CP*T)-   
COMPND  10 3');                                                                 
COMPND  11 CHAIN: E;                                                            
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: DNA (5'-                                                   
COMPND  15 D(*AP*GP*GP*CP*TP*TP*GP*TP*CP*TP*CP*TP*AP*AP*CP*TP*TP*GP*TP*GP*A)-   
COMPND  16 3');                                                                 
COMPND  17 CHAIN: F;                                                            
COMPND  18 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: TP53, P53;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS;             
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS              
KEYWDS    TUMOR SUPPRESSOR, TRANSCRIPTION-DNA COMPLEX                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.CHEN,L.CHEN                                                         
REVDAT   2   09-OCT-13 4HJE    1       JRNL                                     
REVDAT   1   17-JUL-13 4HJE    0                                                
JRNL        AUTH   Y.CHEN,X.ZHANG,A.C.DANTAS MACHADO,Y.DING,Z.CHEN,P.Z.QIN,     
JRNL        AUTH 2 R.ROHS,L.CHEN                                                
JRNL        TITL   STRUCTURE OF P53 BINDING TO THE BAX RESPONSE ELEMENT REVEALS 
JRNL        TITL 2 DNA UNWINDING AND COMPRESSION TO ACCOMMODATE BASE-PAIR       
JRNL        TITL 3 INSERTION.                                                   
JRNL        REF    NUCLEIC ACIDS RES.            V.  41  8368 2013              
JRNL        REFN                   ISSN 0305-1048                               
JRNL        PMID   23836939                                                     
JRNL        DOI    10.1093/NAR/GKT584                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.91 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.91                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.66                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.110                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 67896                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.830                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1924                            
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 48.6804 -  4.5942    0.99     5152   151  0.1884 0.2180        
REMARK   3     2  4.5942 -  3.6469    1.00     4974   146  0.1681 0.1951        
REMARK   3     3  3.6469 -  3.1860    1.00     4936   143  0.1696 0.2478        
REMARK   3     4  3.1860 -  2.8947    0.99     4879   143  0.1924 0.2121        
REMARK   3     5  2.8947 -  2.6873    0.98     4817   142  0.1962 0.2138        
REMARK   3     6  2.6873 -  2.5289    0.98     4795   140  0.1908 0.2297        
REMARK   3     7  2.5289 -  2.4022    0.98     4757   142  0.1959 0.2595        
REMARK   3     8  2.4022 -  2.2976    0.97     4756   140  0.1920 0.2479        
REMARK   3     9  2.2976 -  2.2092    0.96     4686   136  0.1868 0.2392        
REMARK   3    10  2.2092 -  2.1330    0.95     4627   132  0.1775 0.2092        
REMARK   3    11  2.1330 -  2.0663    0.94     4548   137  0.1780 0.2150        
REMARK   3    12  2.0663 -  2.0072    0.93     4469   132  0.1776 0.2313        
REMARK   3    13  2.0072 -  1.9544    0.91     4409   125  0.1887 0.2320        
REMARK   3    14  1.9544 -  1.9070    0.86     4167   115  0.2082 0.2521        
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              : 0.36                                          
REMARK   3   B_SOL              : 42.31                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.250            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.900           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.32320                                              
REMARK   3    B22 (A**2) : -5.79540                                             
REMARK   3    B33 (A**2) : 3.47220                                              
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : -0.00000                                             
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           7386                                  
REMARK   3   ANGLE     :  1.446          10187                                  
REMARK   3   CHIRALITY :  0.090           1114                                  
REMARK   3   PLANARITY :  0.005           1194                                  
REMARK   3   DIHEDRAL  : 18.953           2840                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain A                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -31.5452  14.5470  15.9247              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0562 T22:   0.1218                                     
REMARK   3      T33:   0.0590 T12:   0.0258                                     
REMARK   3      T13:  -0.0193 T23:   0.0100                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8383 L22:   1.6576                                     
REMARK   3      L33:   1.5511 L12:  -0.5761                                     
REMARK   3      L13:   0.1350 L23:  -0.3579                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0513 S12:   0.0209 S13:  -0.0278                       
REMARK   3      S21:  -0.0248 S22:  -0.0343 S23:   0.0903                       
REMARK   3      S31:  -0.0411 S32:  -0.2187 S33:  -0.0561                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain B                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -34.0777 -28.5197  17.1450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1438 T22:   0.1890                                     
REMARK   3      T33:   0.2068 T12:   0.0114                                     
REMARK   3      T13:  -0.0215 T23:  -0.0179                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0709 L22:   2.1941                                     
REMARK   3      L33:   2.0363 L12:   0.2189                                     
REMARK   3      L13:  -0.4336 L23:   0.1772                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0056 S12:   0.0959 S13:  -0.0609                       
REMARK   3      S21:   0.0545 S22:   0.0889 S23:   0.1279                       
REMARK   3      S31:   0.1990 S32:   0.0141 S33:  -0.0677                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain C                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.0217 -42.6310  17.2557              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1675 T22:   0.1766                                     
REMARK   3      T33:   0.2084 T12:   0.0490                                     
REMARK   3      T13:   0.0108 T23:  -0.0208                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1103 L22:   3.4563                                     
REMARK   3      L33:   2.1077 L12:  -0.6811                                     
REMARK   3      L13:  -0.4374 L23:  -0.5685                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0618 S12:   0.1011 S13:  -0.0098                       
REMARK   3      S21:  -0.2377 S22:  -0.1742 S23:  -0.3252                       
REMARK   3      S31:   0.1319 S32:   0.1774 S33:   0.0971                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain D                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   1.4959   0.4784  16.2461              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0552 T22:   0.1149                                     
REMARK   3      T33:   0.1078 T12:   0.0111                                     
REMARK   3      T13:  -0.0048 T23:   0.0173                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3664 L22:   2.6765                                     
REMARK   3      L33:   1.5448 L12:   0.2115                                     
REMARK   3      L13:   0.4158 L23:  -0.2751                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0061 S12:   0.0164 S13:  -0.1323                       
REMARK   3      S21:   0.0811 S22:   0.0509 S23:  -0.2468                       
REMARK   3      S31:   0.0353 S32:   0.0522 S33:  -0.0544                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain A and (resseq 92:223 or resseq 226:   
REMARK   3                          291 )                                       
REMARK   3     SELECTION          : chain B and (resseq 92:223 or resseq 226:   
REMARK   3                          291 )                                       
REMARK   3     ATOM PAIRS NUMBER  : 1555                                        
REMARK   3     RMSD               : 0.058                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: chain A and (resseq 92:223 or resseq 226:   
REMARK   3                          291 )                                       
REMARK   3     SELECTION          : chain C and (resseq 92:223 or resseq 226:   
REMARK   3                          291 )                                       
REMARK   3     ATOM PAIRS NUMBER  : 1555                                        
REMARK   3     RMSD               : 0.044                                       
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: chain A and (resseq 92:223 or resseq 226:   
REMARK   3                          291 )                                       
REMARK   3     SELECTION          : chain D and (resseq 92:223 or resseq 226:   
REMARK   3                          291 )                                       
REMARK   3     ATOM PAIRS NUMBER  : 1555                                        
REMARK   3     RMSD               : 0.054                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4HJE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-OCT-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB075539.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 67896                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.910                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       32.71000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       72.81700            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       46.94000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       72.81700            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.71000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       46.94000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
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 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    99     OE2  GLU D   224              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OG   SER A   183     O    SER D    95     1455     1.97            
REMARK 500   OG   SER B   261     O    LEU D   188     4445     2.10            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 267   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG A 267   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG B 267   CD  -  NE  -  CZ  ANGL. DEV. =  11.8 DEGREES          
REMARK 500    ARG B 267   NE  -  CZ  -  NH1 ANGL. DEV. =  -8.5 DEGREES          
REMARK 500    ARG B 267   NE  -  CZ  -  NH2 ANGL. DEV. =   8.5 DEGREES          
REMARK 500    ARG C 267   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG C 267   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG D 267   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG D 267   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500     DA E   3   O5' -  C5' -  C4' ANGL. DEV. =  -5.7 DEGREES          
REMARK 500     DA E   5   O4' -  C1' -  N9  ANGL. DEV. =  -5.0 DEGREES          
REMARK 500     DA E   6   O4' -  C1' -  N9  ANGL. DEV. =   3.4 DEGREES          
REMARK 500     DG E  11   O4' -  C1' -  N9  ANGL. DEV. =   4.9 DEGREES          
REMARK 500     DA E  12   O5' -  C5' -  C4' ANGL. DEV. =  -5.1 DEGREES          
REMARK 500     DC E  15   P   -  O5' -  C5' ANGL. DEV. = -14.1 DEGREES          
REMARK 500     DC E  15   C1' -  O4' -  C4' ANGL. DEV. =  -6.1 DEGREES          
REMARK 500     DC E  15   O4' -  C1' -  N1  ANGL. DEV. =   2.5 DEGREES          
REMARK 500     DA E  16   O4' -  C1' -  N9  ANGL. DEV. =  -8.6 DEGREES          
REMARK 500     DA E  17   C3' -  C2' -  C1' ANGL. DEV. =  -5.3 DEGREES          
REMARK 500     DA E  17   O4' -  C1' -  N9  ANGL. DEV. =   3.8 DEGREES          
REMARK 500     DA E  17   N1  -  C6  -  N6  ANGL. DEV. =   4.5 DEGREES          
REMARK 500     DC E  20   C3' -  C2' -  C1' ANGL. DEV. =  -6.9 DEGREES          
REMARK 500     DC E  20   O4' -  C1' -  N1  ANGL. DEV. =   3.3 DEGREES          
REMARK 500     DT F   5   N3  -  C2  -  O2  ANGL. DEV. =  -5.5 DEGREES          
REMARK 500     DT F   6   O4' -  C1' -  N1  ANGL. DEV. =   3.6 DEGREES          
REMARK 500     DT F   6   N3  -  C2  -  O2  ANGL. DEV. =  -4.1 DEGREES          
REMARK 500     DG F   7   O4' -  C1' -  N9  ANGL. DEV. =   2.3 DEGREES          
REMARK 500     DT F  10   C3' -  C2' -  C1' ANGL. DEV. =  -6.4 DEGREES          
REMARK 500     DC F  11   O4' -  C1' -  N1  ANGL. DEV. =   9.0 DEGREES          
REMARK 500     DT F  12   C5' -  C4' -  C3' ANGL. DEV. =   7.8 DEGREES          
REMARK 500     DC F  11   C3' -  O3' -  P   ANGL. DEV. =  13.5 DEGREES          
REMARK 500     DT F  12   C3' -  O3' -  P   ANGL. DEV. =   7.2 DEGREES          
REMARK 500     DC F  15   C1' -  O4' -  C4' ANGL. DEV. =  -8.1 DEGREES          
REMARK 500     DC F  15   O4' -  C1' -  N1  ANGL. DEV. =   2.3 DEGREES          
REMARK 500     DT F  16   N3  -  C2  -  O2  ANGL. DEV. =  -4.5 DEGREES          
REMARK 500     DT F  17   O4' -  C1' -  N1  ANGL. DEV. =   4.7 DEGREES          
REMARK 500     DG F  18   O4' -  C1' -  N9  ANGL. DEV. =   2.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 121       55.00   -114.97                                   
REMARK 500    ALA A 138       -0.02     73.87                                   
REMARK 500    VAL A 225      120.95    -39.29                                   
REMARK 500    SER B 121       55.04   -115.94                                   
REMARK 500    VAL B 225        8.53    -69.59                                   
REMARK 500    SER C 121       55.40   -114.19                                   
REMARK 500    VAL C 225      114.49    -31.12                                   
REMARK 500    SER D 121       55.49   -115.13                                   
REMARK 500    ALA D 138       -0.09     72.93                                   
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 D 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 179   ND1                                                    
REMARK 620 2 CYS D 176   SG  103.3                                              
REMARK 620 3 CYS D 238   SG  111.6 110.8                                        
REMARK 620 4 CYS D 242   SG  102.6 113.8 114.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 179   ND1                                                    
REMARK 620 2 CYS A 242   SG  105.5                                              
REMARK 620 3 CYS A 238   SG  108.3 114.7                                        
REMARK 620 4 CYS A 176   SG  103.1 113.9 110.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 179   ND1                                                    
REMARK 620 2 CYS C 238   SG  109.2                                              
REMARK 620 3 CYS C 176   SG  103.9 112.3                                        
REMARK 620 4 CYS C 242   SG  103.9 114.1 112.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 179   ND1                                                    
REMARK 620 2 CYS B 238   SG  109.7                                              
REMARK 620 3 CYS B 242   SG  102.7 112.9                                        
REMARK 620 4 CYS B 176   SG  102.9 112.2 115.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 301                  
DBREF  4HJE A   92   291  UNP    P04637   P53_HUMAN       92    291             
DBREF  4HJE B   92   291  UNP    P04637   P53_HUMAN       92    291             
DBREF  4HJE C   92   291  UNP    P04637   P53_HUMAN       92    291             
DBREF  4HJE D   92   291  UNP    P04637   P53_HUMAN       92    291             
DBREF  4HJE E    1    21  PDB    4HJE     4HJE             1     21             
DBREF  4HJE F    1    21  PDB    4HJE     4HJE             1     21             
SEQRES   1 A  200  PRO LEU SER SER SER VAL PRO SER GLN LYS THR TYR GLN          
SEQRES   2 A  200  GLY SER TYR GLY PHE ARG LEU GLY PHE LEU HIS SER GLY          
SEQRES   3 A  200  THR ALA LYS SER VAL THR CYS THR TYR SER PRO ALA LEU          
SEQRES   4 A  200  ASN LYS MET PHE CYS GLN LEU ALA LYS THR CYS PRO VAL          
SEQRES   5 A  200  GLN LEU TRP VAL ASP SER THR PRO PRO PRO GLY THR ARG          
SEQRES   6 A  200  VAL ARG ALA MET ALA ILE TYR LYS GLN SER GLN HIS MET          
SEQRES   7 A  200  THR GLU VAL VAL ARG ARG CYS PRO HIS HIS GLU ARG CYS          
SEQRES   8 A  200  SER ASP SER ASP GLY LEU ALA PRO PRO GLN HIS LEU ILE          
SEQRES   9 A  200  ARG VAL GLU GLY ASN LEU ARG VAL GLU TYR LEU ASP ASP          
SEQRES  10 A  200  ARG ASN THR PHE ARG HIS SER VAL VAL VAL PRO TYR GLU          
SEQRES  11 A  200  PRO PRO GLU VAL GLY SER ASP CYS THR THR ILE HIS TYR          
SEQRES  12 A  200  ASN TYR MET CYS ASN SER SER CYS MET GLY GLY MET ASN          
SEQRES  13 A  200  ARG ARG PRO ILE LEU THR ILE ILE THR LEU GLU ASP SER          
SEQRES  14 A  200  SER GLY ASN LEU LEU GLY ARG ASN SER PHE GLU VAL ARG          
SEQRES  15 A  200  VAL CYS ALA CYS PRO GLY ARG ASP ARG ARG THR GLU GLU          
SEQRES  16 A  200  GLU ASN LEU ARG LYS                                          
SEQRES   1 B  200  PRO LEU SER SER SER VAL PRO SER GLN LYS THR TYR GLN          
SEQRES   2 B  200  GLY SER TYR GLY PHE ARG LEU GLY PHE LEU HIS SER GLY          
SEQRES   3 B  200  THR ALA LYS SER VAL THR CYS THR TYR SER PRO ALA LEU          
SEQRES   4 B  200  ASN LYS MET PHE CYS GLN LEU ALA LYS THR CYS PRO VAL          
SEQRES   5 B  200  GLN LEU TRP VAL ASP SER THR PRO PRO PRO GLY THR ARG          
SEQRES   6 B  200  VAL ARG ALA MET ALA ILE TYR LYS GLN SER GLN HIS MET          
SEQRES   7 B  200  THR GLU VAL VAL ARG ARG CYS PRO HIS HIS GLU ARG CYS          
SEQRES   8 B  200  SER ASP SER ASP GLY LEU ALA PRO PRO GLN HIS LEU ILE          
SEQRES   9 B  200  ARG VAL GLU GLY ASN LEU ARG VAL GLU TYR LEU ASP ASP          
SEQRES  10 B  200  ARG ASN THR PHE ARG HIS SER VAL VAL VAL PRO TYR GLU          
SEQRES  11 B  200  PRO PRO GLU VAL GLY SER ASP CYS THR THR ILE HIS TYR          
SEQRES  12 B  200  ASN TYR MET CYS ASN SER SER CYS MET GLY GLY MET ASN          
SEQRES  13 B  200  ARG ARG PRO ILE LEU THR ILE ILE THR LEU GLU ASP SER          
SEQRES  14 B  200  SER GLY ASN LEU LEU GLY ARG ASN SER PHE GLU VAL ARG          
SEQRES  15 B  200  VAL CYS ALA CYS PRO GLY ARG ASP ARG ARG THR GLU GLU          
SEQRES  16 B  200  GLU ASN LEU ARG LYS                                          
SEQRES   1 C  200  PRO LEU SER SER SER VAL PRO SER GLN LYS THR TYR GLN          
SEQRES   2 C  200  GLY SER TYR GLY PHE ARG LEU GLY PHE LEU HIS SER GLY          
SEQRES   3 C  200  THR ALA LYS SER VAL THR CYS THR TYR SER PRO ALA LEU          
SEQRES   4 C  200  ASN LYS MET PHE CYS GLN LEU ALA LYS THR CYS PRO VAL          
SEQRES   5 C  200  GLN LEU TRP VAL ASP SER THR PRO PRO PRO GLY THR ARG          
SEQRES   6 C  200  VAL ARG ALA MET ALA ILE TYR LYS GLN SER GLN HIS MET          
SEQRES   7 C  200  THR GLU VAL VAL ARG ARG CYS PRO HIS HIS GLU ARG CYS          
SEQRES   8 C  200  SER ASP SER ASP GLY LEU ALA PRO PRO GLN HIS LEU ILE          
SEQRES   9 C  200  ARG VAL GLU GLY ASN LEU ARG VAL GLU TYR LEU ASP ASP          
SEQRES  10 C  200  ARG ASN THR PHE ARG HIS SER VAL VAL VAL PRO TYR GLU          
SEQRES  11 C  200  PRO PRO GLU VAL GLY SER ASP CYS THR THR ILE HIS TYR          
SEQRES  12 C  200  ASN TYR MET CYS ASN SER SER CYS MET GLY GLY MET ASN          
SEQRES  13 C  200  ARG ARG PRO ILE LEU THR ILE ILE THR LEU GLU ASP SER          
SEQRES  14 C  200  SER GLY ASN LEU LEU GLY ARG ASN SER PHE GLU VAL ARG          
SEQRES  15 C  200  VAL CYS ALA CYS PRO GLY ARG ASP ARG ARG THR GLU GLU          
SEQRES  16 C  200  GLU ASN LEU ARG LYS                                          
SEQRES   1 D  200  PRO LEU SER SER SER VAL PRO SER GLN LYS THR TYR GLN          
SEQRES   2 D  200  GLY SER TYR GLY PHE ARG LEU GLY PHE LEU HIS SER GLY          
SEQRES   3 D  200  THR ALA LYS SER VAL THR CYS THR TYR SER PRO ALA LEU          
SEQRES   4 D  200  ASN LYS MET PHE CYS GLN LEU ALA LYS THR CYS PRO VAL          
SEQRES   5 D  200  GLN LEU TRP VAL ASP SER THR PRO PRO PRO GLY THR ARG          
SEQRES   6 D  200  VAL ARG ALA MET ALA ILE TYR LYS GLN SER GLN HIS MET          
SEQRES   7 D  200  THR GLU VAL VAL ARG ARG CYS PRO HIS HIS GLU ARG CYS          
SEQRES   8 D  200  SER ASP SER ASP GLY LEU ALA PRO PRO GLN HIS LEU ILE          
SEQRES   9 D  200  ARG VAL GLU GLY ASN LEU ARG VAL GLU TYR LEU ASP ASP          
SEQRES  10 D  200  ARG ASN THR PHE ARG HIS SER VAL VAL VAL PRO TYR GLU          
SEQRES  11 D  200  PRO PRO GLU VAL GLY SER ASP CYS THR THR ILE HIS TYR          
SEQRES  12 D  200  ASN TYR MET CYS ASN SER SER CYS MET GLY GLY MET ASN          
SEQRES  13 D  200  ARG ARG PRO ILE LEU THR ILE ILE THR LEU GLU ASP SER          
SEQRES  14 D  200  SER GLY ASN LEU LEU GLY ARG ASN SER PHE GLU VAL ARG          
SEQRES  15 D  200  VAL CYS ALA CYS PRO GLY ARG ASP ARG ARG THR GLU GLU          
SEQRES  16 D  200  GLU ASN LEU ARG LYS                                          
SEQRES   1 E   21   DT  DC  DA  DC  DA  DA  DG  DT  DT  DA  DG  DA  DG          
SEQRES   2 E   21   DA  DC  DA  DA  DG  DC  DC  DT                              
SEQRES   1 F   21   DA  DG  DG  DC  DT  DT  DG  DT  DC  DT  DC  DT  DA          
SEQRES   2 F   21   DA  DC  DT  DT  DG  DT  DG  DA                              
HET     ZN  A 301       1                                                       
HET     ZN  B 301       1                                                       
HET     ZN  C 301       1                                                       
HET     ZN  D 301       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   7   ZN    4(ZN 2+)                                                     
FORMUL  11  HOH   *832(H2 O)                                                    
HELIX    1   1 GLN A  165  MET A  169  5                                   5    
HELIX    2   2 CYS A  176  CYS A  182  1                                   7    
HELIX    3   3 CYS A  277  ASN A  288  1                                  12    
HELIX    4   4 LEU A  289  LYS A  291  5                                   3    
HELIX    5   5 GLN B  165  MET B  169  5                                   5    
HELIX    6   6 CYS B  176  CYS B  182  1                                   7    
HELIX    7   7 CYS B  277  LEU B  289  1                                  13    
HELIX    8   8 GLN C  165  MET C  169  5                                   5    
HELIX    9   9 CYS C  176  CYS C  182  1                                   7    
HELIX   10  10 CYS C  277  LEU C  289  1                                  13    
HELIX   11  11 GLN D  165  MET D  169  5                                   5    
HELIX   12  12 CYS D  176  CYS D  182  1                                   7    
HELIX   13  13 CYS D  277  LEU D  289  1                                  13    
SHEET    1   A 4 ARG A 110  GLY A 112  0                                        
SHEET    2   A 4 CYS A 141  TRP A 146 -1  O  TRP A 146   N  ARG A 110           
SHEET    3   A 4 THR A 230  TYR A 236 -1  O  THR A 230   N  LEU A 145           
SHEET    4   A 4 ILE A 195  VAL A 197 -1  N  ARG A 196   O  ASN A 235           
SHEET    1   B 7 CYS A 124  SER A 127  0                                        
SHEET    2   B 7 LYS A 132  CYS A 135 -1  O  PHE A 134   N  THR A 125           
SHEET    3   B 7 LEU A 264  VAL A 274  1  O  GLU A 271   N  MET A 133           
SHEET    4   B 7 ILE A 251  GLU A 258 -1  N  THR A 253   O  PHE A 270           
SHEET    5   B 7 ARG A 156  TYR A 163 -1  N  MET A 160   O  ILE A 254           
SHEET    6   B 7 HIS A 214  PRO A 219 -1  O  VAL A 218   N  VAL A 157           
SHEET    7   B 7 GLU A 204  ASP A 207 -1  N  GLU A 204   O  VAL A 217           
SHEET    1   C 4 ARG B 110  GLY B 112  0                                        
SHEET    2   C 4 CYS B 141  TRP B 146 -1  O  GLN B 144   N  GLY B 112           
SHEET    3   C 4 THR B 230  TYR B 236 -1  O  THR B 230   N  LEU B 145           
SHEET    4   C 4 ILE B 195  VAL B 197 -1  N  ARG B 196   O  ASN B 235           
SHEET    1   D 7 CYS B 124  SER B 127  0                                        
SHEET    2   D 7 LYS B 132  CYS B 135 -1  O  PHE B 134   N  THR B 125           
SHEET    3   D 7 LEU B 264  VAL B 274  1  O  GLU B 271   N  MET B 133           
SHEET    4   D 7 ILE B 251  GLU B 258 -1  N  LEU B 257   O  LEU B 265           
SHEET    5   D 7 ARG B 156  TYR B 163 -1  N  MET B 160   O  ILE B 254           
SHEET    6   D 7 HIS B 214  PRO B 219 -1  O  VAL B 218   N  VAL B 157           
SHEET    7   D 7 GLU B 204  ASP B 207 -1  N  GLU B 204   O  VAL B 217           
SHEET    1   E 4 ARG C 110  GLY C 112  0                                        
SHEET    2   E 4 CYS C 141  TRP C 146 -1  O  TRP C 146   N  ARG C 110           
SHEET    3   E 4 THR C 230  TYR C 236 -1  O  THR C 230   N  LEU C 145           
SHEET    4   E 4 ILE C 195  VAL C 197 -1  N  ARG C 196   O  ASN C 235           
SHEET    1   F 7 CYS C 124  SER C 127  0                                        
SHEET    2   F 7 LYS C 132  CYS C 135 -1  O  LYS C 132   N  SER C 127           
SHEET    3   F 7 LEU C 264  VAL C 274  1  O  GLU C 271   N  MET C 133           
SHEET    4   F 7 ILE C 251  GLU C 258 -1  N  THR C 253   O  PHE C 270           
SHEET    5   F 7 ARG C 156  TYR C 163 -1  N  MET C 160   O  ILE C 254           
SHEET    6   F 7 HIS C 214  PRO C 219 -1  O  VAL C 218   N  VAL C 157           
SHEET    7   F 7 GLU C 204  ASP C 207 -1  N  GLU C 204   O  VAL C 217           
SHEET    1   G 4 ARG D 110  GLY D 112  0                                        
SHEET    2   G 4 CYS D 141  TRP D 146 -1  O  GLN D 144   N  GLY D 112           
SHEET    3   G 4 THR D 230  TYR D 236 -1  O  THR D 230   N  LEU D 145           
SHEET    4   G 4 ILE D 195  VAL D 197 -1  N  ARG D 196   O  ASN D 235           
SHEET    1   H 7 CYS D 124  SER D 127  0                                        
SHEET    2   H 7 LYS D 132  CYS D 135 -1  O  PHE D 134   N  THR D 125           
SHEET    3   H 7 LEU D 264  VAL D 274  1  O  GLU D 271   N  MET D 133           
SHEET    4   H 7 ILE D 251  GLU D 258 -1  N  THR D 253   O  PHE D 270           
SHEET    5   H 7 ARG D 156  TYR D 163 -1  N  ARG D 156   O  GLU D 258           
SHEET    6   H 7 HIS D 214  PRO D 219 -1  O  VAL D 218   N  VAL D 157           
SHEET    7   H 7 GLU D 204  ASP D 207 -1  N  GLU D 204   O  VAL D 217           
LINK         ND1 HIS D 179                ZN    ZN D 301     1555   1555  2.07  
LINK         ND1 HIS A 179                ZN    ZN A 301     1555   1555  2.09  
LINK         ND1 HIS C 179                ZN    ZN C 301     1555   1555  2.11  
LINK         ND1 HIS B 179                ZN    ZN B 301     1555   1555  2.11  
LINK         SG  CYS A 242                ZN    ZN A 301     1555   1555  2.31  
LINK         SG  CYS D 176                ZN    ZN D 301     1555   1555  2.32  
LINK         SG  CYS B 238                ZN    ZN B 301     1555   1555  2.33  
LINK         SG  CYS B 242                ZN    ZN B 301     1555   1555  2.33  
LINK         SG  CYS D 238                ZN    ZN D 301     1555   1555  2.33  
LINK         SG  CYS B 176                ZN    ZN B 301     1555   1555  2.34  
LINK         SG  CYS D 242                ZN    ZN D 301     1555   1555  2.35  
LINK         SG  CYS C 238                ZN    ZN C 301     1555   1555  2.35  
LINK         SG  CYS C 176                ZN    ZN C 301     1555   1555  2.35  
LINK         SG  CYS C 242                ZN    ZN C 301     1555   1555  2.35  
LINK         SG  CYS A 238                ZN    ZN A 301     1555   1555  2.36  
LINK         SG  CYS A 176                ZN    ZN A 301     1555   1555  2.38  
SITE     1 AC1  4 CYS A 176  HIS A 179  CYS A 238  CYS A 242                    
SITE     1 AC2  4 CYS B 176  HIS B 179  CYS B 238  CYS B 242                    
SITE     1 AC3  4 CYS C 176  HIS C 179  CYS C 238  CYS C 242                    
SITE     1 AC4  4 CYS D 176  HIS D 179  CYS D 238  CYS D 242                    
CRYST1   65.420   93.880  145.634  90.00  90.00  90.00 P 21 21 21   16          
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      0.015286  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010652  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006867        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system