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Database: PDB
Entry: 4IBZ
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Original site: 4IBZ 
HEADER    DNA BINDING PROTEIN                     09-DEC-12   4IBZ              
TITLE     HUMAN P53 CORE DOMAIN WITH HOT SPOT MUTATION R273C AND SECOND-SITE    
TITLE    2 SUPPRESSOR MUTATION T284R                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELLULAR TUMOR ANTIGEN P53;                                
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: DNA BINDING DOMAIN;                                        
COMPND   5 SYNONYM: ANTIGEN NY-CO-13, PHOSPHOPROTEIN P53, TUMOR SUPPRESSOR P53; 
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: P53, TP53;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-27-B                                  
KEYWDS    METAL-BINDING, LOOP-SHEET-HELIX MOTIF, TRANSCRIPTION, ACTIVATOR,      
KEYWDS   2 ANTI-ONCOGENE, APOPTOSIS, CELL CYCLE, DISEASE MUTATION, RESCUE       
KEYWDS   3 MUTATION, TUMOR SUPPRESSOR, DNA BINDING PROTEIN                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.ELDAR,H.ROZENBERG,Y.DISKIN-POSNER,Z.SHAKKED                         
REVDAT   3   15-NOV-17 4IBZ    1       REMARK                                   
REVDAT   2   23-OCT-13 4IBZ    1       JRNL                                     
REVDAT   1   14-AUG-13 4IBZ    0                                                
JRNL        AUTH   A.ELDAR,H.ROZENBERG,Y.DISKIN-POSNER,R.ROHS,Z.SHAKKED         
JRNL        TITL   STRUCTURAL STUDIES OF P53 INACTIVATION BY DNA-CONTACT        
JRNL        TITL 2 MUTATIONS AND ITS RESCUE BY SUPPRESSOR MUTATIONS VIA         
JRNL        TITL 3 ALTERNATIVE PROTEIN-DNA INTERACTIONS.                        
JRNL        REF    NUCLEIC ACIDS RES.            V.  41  8748 2013              
JRNL        REFN                   ISSN 0305-1048                               
JRNL        PMID   23863845                                                     
JRNL        DOI    10.1093/NAR/GKT630                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.92 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.1_1168                                    
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 : TWIN_LSQ_F                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.92                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.69                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 59996                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.181                           
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.233                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.240                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2544                            
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 18.8974 -  5.0107    0.95     3316   148  0.1439 0.1612        
REMARK   3     2  5.0107 -  3.9894    0.95     3305   150  0.1132 0.2000        
REMARK   3     3  3.9894 -  3.4887    0.95     3245   138  0.1292 0.2165        
REMARK   3     4  3.4887 -  3.1714    0.95     3255   140  0.1524 0.2017        
REMARK   3     5  3.1714 -  2.9450    0.95     3261   142  0.1708 0.2444        
REMARK   3     6  2.9450 -  2.7719    0.95     3245   142  0.1939 0.2304        
REMARK   3     7  2.7719 -  2.6335    0.95     3255   132  0.2049 0.2546        
REMARK   3     8  2.6335 -  2.5191    0.95     3212   143  0.2139 0.2287        
REMARK   3     9  2.5191 -  2.4223    0.95     3243   136  0.2219 0.2641        
REMARK   3    10  2.4223 -  2.3389    0.94     3196   138  0.2206 0.2931        
REMARK   3    11  2.3389 -  2.2659    0.94     3221   149  0.2213 0.3016        
REMARK   3    12  2.2659 -  2.2012    0.95     3179   132  0.2186 0.2785        
REMARK   3    13  2.2012 -  2.1434    0.95     3232   134  0.2301 0.2351        
REMARK   3    14  2.1434 -  2.0911    0.94     3203   146  0.2399 0.3040        
REMARK   3    15  2.0911 -  2.0437    0.94     3222   136  0.2290 0.3169        
REMARK   3    16  2.0437 -  2.0002    0.94     3143   134  0.2503 0.2782        
REMARK   3    17  2.0002 -  1.9602    0.92     3146   155  0.2649 0.3097        
REMARK   3    18  1.9602 -  1.9200    0.75     2580    90  0.2881 0.3133        
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)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.390           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.09                          
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: 0.0700                                                   
REMARK   3   OPERATOR: H,-K,-L                                                  
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           6448                                  
REMARK   3   ANGLE     :  1.069           8774                                  
REMARK   3   CHIRALITY :  0.070            949                                  
REMARK   3   PLANARITY :  0.005           1182                                  
REMARK   3   DIHEDRAL  : 14.575           2444                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 21                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 96:109 )                            
REMARK   3    ORIGIN FOR THE GROUP (A): -29.3524  -8.3387 -22.9787              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2646 T22:   0.1396                                     
REMARK   3      T33:   0.2049 T12:  -0.0161                                     
REMARK   3      T13:  -0.0300 T23:   0.0296                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4294 L22:   5.8473                                     
REMARK   3      L33:   5.6798 L12:   1.6758                                     
REMARK   3      L13:   1.3150 L23:   4.0664                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1329 S12:   0.5351 S13:   0.4804                       
REMARK   3      S21:   0.0050 S22:   0.0926 S23:  -0.0242                       
REMARK   3      S31:  -0.5799 S32:   0.0880 S33:   0.0773                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 110:180 )                           
REMARK   3    ORIGIN FOR THE GROUP (A): -31.0783 -12.5812  -8.6047              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1932 T22:   0.0640                                     
REMARK   3      T33:   0.1815 T12:  -0.0036                                     
REMARK   3      T13:   0.0233 T23:  -0.0060                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4461 L22:   1.3328                                     
REMARK   3      L33:   1.4278 L12:  -0.3648                                     
REMARK   3      L13:  -0.1232 L23:   0.0041                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0179 S12:  -0.1016 S13:  -0.0338                       
REMARK   3      S21:   0.1162 S22:   0.0643 S23:   0.0447                       
REMARK   3      S31:  -0.1404 S32:   0.0260 S33:  -0.0101                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 181:229 )                           
REMARK   3    ORIGIN FOR THE GROUP (A): -20.3690 -18.2885 -10.4002              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1632 T22:   0.0785                                     
REMARK   3      T33:   0.1790 T12:   0.0400                                     
REMARK   3      T13:   0.0199 T23:   0.0080                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7643 L22:   3.1651                                     
REMARK   3      L33:   3.1843 L12:   0.9732                                     
REMARK   3      L13:   0.5511 L23:   1.2499                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0633 S12:  -0.2144 S13:  -0.2062                       
REMARK   3      S21:   0.1014 S22:   0.0162 S23:  -0.0323                       
REMARK   3      S31:   0.2843 S32:   0.3864 S33:  -0.1152                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 230:288 )                           
REMARK   3    ORIGIN FOR THE GROUP (A): -31.6368 -10.8019  -6.3324              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2244 T22:   0.0609                                     
REMARK   3      T33:   0.2039 T12:   0.0040                                     
REMARK   3      T13:   0.0178 T23:  -0.0102                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0249 L22:   0.4748                                     
REMARK   3      L33:   2.2220 L12:   0.3314                                     
REMARK   3      L13:  -0.3138 L23:  -0.1691                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0208 S12:  -0.2373 S13:   0.1040                       
REMARK   3      S21:   0.0701 S22:   0.0280 S23:   0.1343                       
REMARK   3      S31:  -0.1540 S32:   0.1089 S33:  -0.0180                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN B AND (RESID 97:163 )                            
REMARK   3    ORIGIN FOR THE GROUP (A): -36.7726 -14.5673 -55.0074              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2113 T22:   0.0836                                     
REMARK   3      T33:   0.2442 T12:   0.0056                                     
REMARK   3      T13:  -0.0158 T23:  -0.0430                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7101 L22:   0.6807                                     
REMARK   3      L33:   0.8232 L12:   0.0341                                     
REMARK   3      L13:   0.1237 L23:  -0.0079                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0092 S12:  -0.1261 S13:   0.4301                       
REMARK   3      S21:  -0.0818 S22:  -0.0081 S23:   0.1392                       
REMARK   3      S31:  -0.1680 S32:  -0.0670 S33:   0.0612                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN B AND (RESID 164:180 )                           
REMARK   3    ORIGIN FOR THE GROUP (A): -25.2254  -6.6372 -41.1275              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2591 T22:   0.4864                                     
REMARK   3      T33:   0.3883 T12:  -0.0708                                     
REMARK   3      T13:  -0.0184 T23:  -0.2870                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4972 L22:   0.7074                                     
REMARK   3      L33:   0.6014 L12:   1.5369                                     
REMARK   3      L13:  -0.3061 L23:   0.0040                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0671 S12:  -0.7957 S13:   0.9484                       
REMARK   3      S21:   0.2849 S22:  -0.1806 S23:   0.3763                       
REMARK   3      S31:  -0.3080 S32:   0.0667 S33:   0.0748                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN B AND (RESID 181:194 )                           
REMARK   3    ORIGIN FOR THE GROUP (A): -19.3948 -19.4364 -43.1314              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2953 T22:   0.5310                                     
REMARK   3      T33:   0.2319 T12:   0.0816                                     
REMARK   3      T13:   0.0034 T23:   0.0806                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4922 L22:   4.3690                                     
REMARK   3      L33:   4.2695 L12:  -0.6035                                     
REMARK   3      L13:   1.6930 L23:   1.3848                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0772 S12:  -1.1473 S13:  -0.4614                       
REMARK   3      S21:   0.8380 S22:  -0.1530 S23:  -0.2386                       
REMARK   3      S31:   0.7264 S32:   0.4894 S33:   0.1464                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN B AND (RESID 195:274 )                           
REMARK   3    ORIGIN FOR THE GROUP (A): -28.4283 -14.5831 -52.9718              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1742 T22:   0.0547                                     
REMARK   3      T33:   0.2539 T12:   0.0114                                     
REMARK   3      T13:  -0.0049 T23:  -0.0622                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4917 L22:   1.3025                                     
REMARK   3      L33:   2.0311 L12:   0.1836                                     
REMARK   3      L13:  -0.2366 L23:  -0.0468                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1103 S12:  -0.4289 S13:   0.3554                       
REMARK   3      S21:  -0.0749 S22:  -0.0714 S23:   0.1578                       
REMARK   3      S31:   0.0539 S32:   0.1907 S33:   0.0215                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN B AND (RESID 275:288 )                           
REMARK   3    ORIGIN FOR THE GROUP (A): -46.1203 -13.8619 -38.9706              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2261 T22:   0.7296                                     
REMARK   3      T33:   0.2791 T12:   0.0491                                     
REMARK   3      T13:   0.0290 T23:  -0.2014                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2102 L22:   0.4231                                     
REMARK   3      L33:   2.3388 L12:   0.0125                                     
REMARK   3      L13:  -0.0349 L23:  -0.5970                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0681 S12:  -1.0994 S13:   0.5052                       
REMARK   3      S21:   0.3243 S22:   0.0688 S23:   0.0125                       
REMARK   3      S31:  -0.3332 S32:   0.1611 S33:  -0.0012                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN C AND (RESID 96:109 )                            
REMARK   3    ORIGIN FOR THE GROUP (A): -63.9793 -25.7426   4.6000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2668 T22:   0.5523                                     
REMARK   3      T33:   0.3116 T12:  -0.0937                                     
REMARK   3      T13:   0.1059 T23:  -0.0405                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3133 L22:   0.9298                                     
REMARK   3      L33:   0.4835 L12:   0.2419                                     
REMARK   3      L13:   0.1448 L23:  -0.4445                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0491 S12:  -0.3522 S13:  -0.2140                       
REMARK   3      S21:  -0.0925 S22:   0.1534 S23:  -0.1627                       
REMARK   3      S31:   0.1949 S32:  -0.5190 S33:  -0.1299                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN C AND (RESID 110:176 )                           
REMARK   3    ORIGIN FOR THE GROUP (A): -66.4198 -21.2334  -9.3572              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1910 T22:   0.3398                                     
REMARK   3      T33:   0.2127 T12:   0.0154                                     
REMARK   3      T13:   0.0377 T23:   0.0029                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4882 L22:   0.8030                                     
REMARK   3      L33:   0.6162 L12:   0.1504                                     
REMARK   3      L13:   0.9910 L23:  -0.3555                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0028 S12:   0.0835 S13:   0.0260                       
REMARK   3      S21:  -0.0643 S22:  -0.0234 S23:   0.0388                       
REMARK   3      S31:   0.0555 S32:  -0.0191 S33:   0.0276                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN C AND (RESID 177:194 )                           
REMARK   3    ORIGIN FOR THE GROUP (A): -51.4075 -20.2078 -19.9772              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3331 T22:   0.6827                                     
REMARK   3      T33:   0.2873 T12:   0.0687                                     
REMARK   3      T13:   0.1235 T23:   0.1083                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7042 L22:   0.2317                                     
REMARK   3      L33:   5.0162 L12:   0.1551                                     
REMARK   3      L13:   1.7582 L23:  -0.1055                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1631 S12:   0.8876 S13:  -0.0257                       
REMARK   3      S21:  -0.6684 S22:  -0.2881 S23:  -0.5638                       
REMARK   3      S31:  -0.5308 S32:   0.2501 S33:   0.0514                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN C AND (RESID 195:289 )                           
REMARK   3    ORIGIN FOR THE GROUP (A): -61.6280 -21.2944  -9.8311              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1768 T22:   0.2932                                     
REMARK   3      T33:   0.1957 T12:   0.0061                                     
REMARK   3      T13:   0.0509 T23:   0.0128                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4456 L22:   0.8861                                     
REMARK   3      L33:   1.0390 L12:  -0.0730                                     
REMARK   3      L13:   1.2329 L23:   0.0669                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0355 S12:   0.2301 S13:   0.0052                       
REMARK   3      S21:  -0.0514 S22:  -0.1335 S23:   0.0397                       
REMARK   3      S31:   0.0434 S32:  -0.1355 S33:   0.0864                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN D AND (RESID 96:112 )                            
REMARK   3    ORIGIN FOR THE GROUP (A): -68.7325 -28.7013 -41.8036              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3843 T22:   0.3920                                     
REMARK   3      T33:   0.4935 T12:   0.0775                                     
REMARK   3      T13:   0.2002 T23:   0.1589                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9492 L22:   0.2817                                     
REMARK   3      L33:   1.5181 L12:  -0.6202                                     
REMARK   3      L13:   1.6871 L23:  -0.4739                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1481 S12:  -0.8155 S13:  -0.9146                       
REMARK   3      S21:   0.1747 S22:   0.1780 S23:   0.1914                       
REMARK   3      S31:   0.5151 S32:  -0.2383 S33:   0.0423                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN D AND (RESID 113:140 )                           
REMARK   3    ORIGIN FOR THE GROUP (A): -76.2176 -17.4153 -57.6510              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1991 T22:   0.3048                                     
REMARK   3      T33:   0.2224 T12:   0.0159                                     
REMARK   3      T13:   0.0221 T23:  -0.0138                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3899 L22:   0.7061                                     
REMARK   3      L33:   1.1372 L12:  -0.1771                                     
REMARK   3      L13:  -0.0639 L23:   0.8193                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0898 S12:   0.5337 S13:  -0.1371                       
REMARK   3      S21:  -0.0249 S22:   0.0287 S23:   0.0451                       
REMARK   3      S31:  -0.0296 S32:  -0.0092 S33:   0.0861                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN D AND (RESID 141:155 )                           
REMARK   3    ORIGIN FOR THE GROUP (A): -69.2846 -17.0077 -40.1726              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2655 T22:   0.3861                                     
REMARK   3      T33:   0.2295 T12:   0.0769                                     
REMARK   3      T13:   0.0671 T23:  -0.0269                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0890 L22:   1.9259                                     
REMARK   3      L33:   2.8238 L12:   0.0324                                     
REMARK   3      L13:  -1.2822 L23:  -0.5323                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2219 S12:  -0.8350 S13:  -0.0464                       
REMARK   3      S21:   0.3906 S22:   0.1795 S23:   0.3353                       
REMARK   3      S31:  -0.2686 S32:  -0.2983 S33:   0.0099                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN D AND (RESID 156:176 )                           
REMARK   3    ORIGIN FOR THE GROUP (A): -60.9935 -29.4117 -57.0448              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2331 T22:   0.1913                                     
REMARK   3      T33:   0.4027 T12:   0.0272                                     
REMARK   3      T13:   0.0745 T23:  -0.0954                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0870 L22:   1.5835                                     
REMARK   3      L33:   2.2816 L12:   0.0666                                     
REMARK   3      L13:  -0.2409 L23:  -0.5664                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2475 S12:   0.2992 S13:  -0.6919                       
REMARK   3      S21:  -0.0449 S22:  -0.0829 S23:   0.0982                       
REMARK   3      S31:   0.5918 S32:   0.1064 S33:   0.0596                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN D AND (RESID 177:194 )                           
REMARK   3    ORIGIN FOR THE GROUP (A): -54.2727 -16.9293 -62.6766              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2736 T22:   0.3041                                     
REMARK   3      T33:   0.2227 T12:  -0.0270                                     
REMARK   3      T13:   0.0140 T23:   0.0277                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9043 L22:   0.7353                                     
REMARK   3      L33:   5.2282 L12:   1.0538                                     
REMARK   3      L13:   2.9068 L23:   1.9256                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0371 S12:   0.6118 S13:   0.2080                       
REMARK   3      S21:  -0.3750 S22:  -0.0485 S23:  -0.1518                       
REMARK   3      S31:  -0.7355 S32:   0.5667 S33:   0.0628                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN D AND (RESID 195:229 )                           
REMARK   3    ORIGIN FOR THE GROUP (A): -59.2462 -17.7971 -47.1402              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1763 T22:   0.1630                                     
REMARK   3      T33:   0.2200 T12:   0.0624                                     
REMARK   3      T13:  -0.0251 T23:  -0.0087                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0025 L22:   2.2522                                     
REMARK   3      L33:   3.5120 L12:   0.4398                                     
REMARK   3      L13:  -1.0663 L23:   0.6940                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2214 S12:  -0.4255 S13:   0.0894                       
REMARK   3      S21:   0.1373 S22:   0.2018 S23:  -0.0516                       
REMARK   3      S31:  -0.1301 S32:   0.0177 S33:   0.0050                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN D AND (RESID 230:274 )                           
REMARK   3    ORIGIN FOR THE GROUP (A): -65.3483 -24.0747 -53.4357              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1435 T22:   0.2053                                     
REMARK   3      T33:   0.3335 T12:   0.0211                                     
REMARK   3      T13:   0.0410 T23:  -0.0540                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2715 L22:   1.6323                                     
REMARK   3      L33:   2.9643 L12:  -0.5244                                     
REMARK   3      L13:  -0.6901 L23:  -0.0468                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1984 S12:   0.3540 S13:  -0.6870                       
REMARK   3      S21:  -0.0130 S22:  -0.1423 S23:   0.1871                       
REMARK   3      S31:   0.2990 S32:   0.1451 S33:   0.2539                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: CHAIN D AND (RESID 275:288 )                           
REMARK   3    ORIGIN FOR THE GROUP (A): -80.8434 -21.7372 -65.0987              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2867 T22:   0.6588                                     
REMARK   3      T33:   0.3267 T12:   0.0069                                     
REMARK   3      T13:   0.0141 T23:  -0.2061                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6826 L22:   1.6049                                     
REMARK   3      L33:   2.2788 L12:  -0.3369                                     
REMARK   3      L13:  -1.6986 L23:  -1.1574                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3692 S12:   1.5996 S13:  -0.9232                       
REMARK   3      S21:  -0.3858 S22:   0.2897 S23:  -0.0846                       
REMARK   3      S31:   0.5747 S32:   0.3440 S33:   0.1066                       
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 4IBZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JAN-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000076562.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-JUL-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.1                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97590                            
REMARK 200  MONOCHROMATOR                  : SILICON (111)                      
REMARK 200  OPTICS                         : TOROIDAL MIRROR                    
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 60012                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.920                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 27.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.08100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.92                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35600                            
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: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1ACO, CHAIN A                              
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 3350, 0.12M NH4-ACETATE, PH      
REMARK 280  6.1, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       35.20650            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
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: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     LEU A   289                                                      
REMARK 465     ARG A   290                                                      
REMARK 465     LYS A   291                                                      
REMARK 465     LYS A   292                                                      
REMARK 465     GLY A   293                                                      
REMARK 465     SER B    94                                                      
REMARK 465     SER B    95                                                      
REMARK 465     SER B    96                                                      
REMARK 465     LEU B   289                                                      
REMARK 465     ARG B   290                                                      
REMARK 465     LYS B   291                                                      
REMARK 465     LYS B   292                                                      
REMARK 465     GLY B   293                                                      
REMARK 465     SER C    94                                                      
REMARK 465     SER C    95                                                      
REMARK 465     SER C   183                                                      
REMARK 465     ASP C   184                                                      
REMARK 465     ARG C   290                                                      
REMARK 465     LYS C   291                                                      
REMARK 465     LYS C   292                                                      
REMARK 465     GLY C   293                                                      
REMARK 465     SER D    94                                                      
REMARK 465     SER D    95                                                      
REMARK 465     GLY D   226                                                      
REMARK 465     LEU D   289                                                      
REMARK 465     ARG D   290                                                      
REMARK 465     LYS D   291                                                      
REMARK 465     LYS D   292                                                      
REMARK 465     GLY D   293                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 101    CG   CD   CE   NZ                                   
REMARK 470     LYS A 120    CG   CD   CE   NZ                                   
REMARK 470     ARG A 181    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 201    CD1  CD2                                            
REMARK 470     ARG A 209    NH1  NH2                                            
REMARK 470     VAL A 225    CG1  CG2                                            
REMARK 470     ARG A 284    NH1  NH2                                            
REMARK 470     LYS B 101    CE   NZ                                             
REMARK 470     LYS B 120    CD   CE   NZ                                        
REMARK 470     LYS B 139    CE   NZ                                             
REMARK 470     LYS B 164    NZ                                                  
REMARK 470     SER B 166    CB   OG                                             
REMARK 470     ARG B 181    NE   CZ   NH1  NH2                                  
REMARK 470     ARG B 209    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 284    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU B 287    CD   OE1  OE2                                       
REMARK 470     ASN B 288    CG   OD1  ND2                                       
REMARK 470     LYS C 120    CD   CE   NZ                                        
REMARK 470     ARG C 174    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG C 181    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 224    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 228    CG   OD1  OD2                                       
REMARK 470     LEU C 264    CD1  CD2                                            
REMARK 470     ARG C 280    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 284    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 287    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 101    CE   NZ                                             
REMARK 470     LYS D 120    CD   CE   NZ                                        
REMARK 470     LYS D 164    CG   CD   CE   NZ                                   
REMARK 470     ASP D 184    CG   OD1  OD2                                       
REMARK 470     ARG D 209    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU D 221    CD   OE1  OE2                                       
REMARK 470     GLU D 224    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 248    NH1  NH2                                            
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 B   467     O    HOH B   514              2.11            
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   O    HOH A   530     O    HOH B   546     2444     2.08            
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    ALA A 138       -1.63     71.17                                   
REMARK 500    ARG A 181       43.43    -82.05                                   
REMARK 500    ARG A 248       -8.03     73.24                                   
REMARK 500    ARG B 181       63.44    -66.89                                   
REMARK 500    CYS B 182     -136.45     63.29                                   
REMARK 500    SER B 183      -59.92     59.89                                   
REMARK 500    ARG C 181       68.11   -107.29                                   
REMARK 500    LEU C 188      -34.86   -139.11                                   
REMARK 500    CYS C 242      109.97    -59.59                                   
REMARK 500    ARG C 248       -0.67     68.98                                   
REMARK 500    SER D 183       37.68    -73.42                                   
REMARK 500    GLU D 224       39.07    -81.58                                   
REMARK 500    ARG D 248       -7.05     71.29                                   
REMARK 500    ARG D 248       -6.38     71.29                                   
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  108.2                                              
REMARK 620 3 CYS D 242   SG  104.1 113.2                                        
REMARK 620 4 CYS D 238   SG  114.0 108.1 109.5                                  
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 242   SG   99.0                                              
REMARK 620 3 CYS B 176   SG  106.2 117.9                                        
REMARK 620 4 CYS B 238   SG  124.1  98.3 111.2                                  
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 176   SG  102.9                                              
REMARK 620 3 CYS C 242   SG  122.6 122.3                                        
REMARK 620 4 CYS C 238   SG   89.5 107.1 106.8                                  
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  102.5                                              
REMARK 620 3 CYS A 238   SG  108.5 114.4                                        
REMARK 620 4 CYS A 176   SG  108.9 111.5 110.6                                  
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 EDO A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 308                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4IBQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4IBS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4IBT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4IBU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4IBV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4IBW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4IBY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4IJT   RELATED DB: PDB                                   
DBREF  4IBZ A   94   293  UNP    P04637   P53_HUMAN       94    293             
DBREF  4IBZ B   94   293  UNP    P04637   P53_HUMAN       94    293             
DBREF  4IBZ C   94   293  UNP    P04637   P53_HUMAN       94    293             
DBREF  4IBZ D   94   293  UNP    P04637   P53_HUMAN       94    293             
SEQADV 4IBZ CYS A  273  UNP  P04637    ARG   273 ENGINEERED MUTATION            
SEQADV 4IBZ ARG A  284  UNP  P04637    THR   284 ENGINEERED MUTATION            
SEQADV 4IBZ CYS B  273  UNP  P04637    ARG   273 ENGINEERED MUTATION            
SEQADV 4IBZ ARG B  284  UNP  P04637    THR   284 ENGINEERED MUTATION            
SEQADV 4IBZ CYS C  273  UNP  P04637    ARG   273 ENGINEERED MUTATION            
SEQADV 4IBZ ARG C  284  UNP  P04637    THR   284 ENGINEERED MUTATION            
SEQADV 4IBZ CYS D  273  UNP  P04637    ARG   273 ENGINEERED MUTATION            
SEQADV 4IBZ ARG D  284  UNP  P04637    THR   284 ENGINEERED MUTATION            
SEQRES   1 A  200  SER SER SER VAL PRO SER GLN LYS THR TYR GLN GLY SER          
SEQRES   2 A  200  TYR GLY PHE ARG LEU GLY PHE LEU HIS SER GLY THR ALA          
SEQRES   3 A  200  LYS SER VAL THR CYS THR TYR SER PRO ALA LEU ASN LYS          
SEQRES   4 A  200  MET PHE CYS GLN LEU ALA LYS THR CYS PRO VAL GLN LEU          
SEQRES   5 A  200  TRP VAL ASP SER THR PRO PRO PRO GLY THR ARG VAL ARG          
SEQRES   6 A  200  ALA MET ALA ILE TYR LYS GLN SER GLN HIS MET THR GLU          
SEQRES   7 A  200  VAL VAL ARG ARG CYS PRO HIS HIS GLU ARG CYS SER ASP          
SEQRES   8 A  200  SER ASP GLY LEU ALA PRO PRO GLN HIS LEU ILE ARG VAL          
SEQRES   9 A  200  GLU GLY ASN LEU ARG VAL GLU TYR LEU ASP ASP ARG ASN          
SEQRES  10 A  200  THR PHE ARG HIS SER VAL VAL VAL PRO TYR GLU PRO PRO          
SEQRES  11 A  200  GLU VAL GLY SER ASP CYS THR THR ILE HIS TYR ASN TYR          
SEQRES  12 A  200  MET CYS ASN SER SER CYS MET GLY GLY MET ASN ARG ARG          
SEQRES  13 A  200  PRO ILE LEU THR ILE ILE THR LEU GLU ASP SER SER GLY          
SEQRES  14 A  200  ASN LEU LEU GLY ARG ASN SER PHE GLU VAL CYS VAL CYS          
SEQRES  15 A  200  ALA CYS PRO GLY ARG ASP ARG ARG ARG GLU GLU GLU ASN          
SEQRES  16 A  200  LEU ARG LYS LYS GLY                                          
SEQRES   1 B  200  SER SER SER VAL PRO SER GLN LYS THR TYR GLN GLY SER          
SEQRES   2 B  200  TYR GLY PHE ARG LEU GLY PHE LEU HIS SER GLY THR ALA          
SEQRES   3 B  200  LYS SER VAL THR CYS THR TYR SER PRO ALA LEU ASN LYS          
SEQRES   4 B  200  MET PHE CYS GLN LEU ALA LYS THR CYS PRO VAL GLN LEU          
SEQRES   5 B  200  TRP VAL ASP SER THR PRO PRO PRO GLY THR ARG VAL ARG          
SEQRES   6 B  200  ALA MET ALA ILE TYR LYS GLN SER GLN HIS MET THR GLU          
SEQRES   7 B  200  VAL VAL ARG ARG CYS PRO HIS HIS GLU ARG CYS SER ASP          
SEQRES   8 B  200  SER ASP GLY LEU ALA PRO PRO GLN HIS LEU ILE ARG VAL          
SEQRES   9 B  200  GLU GLY ASN LEU ARG VAL GLU TYR LEU ASP ASP ARG ASN          
SEQRES  10 B  200  THR PHE ARG HIS SER VAL VAL VAL PRO TYR GLU PRO PRO          
SEQRES  11 B  200  GLU VAL GLY SER ASP CYS THR THR ILE HIS TYR ASN TYR          
SEQRES  12 B  200  MET CYS ASN SER SER CYS MET GLY GLY MET ASN ARG ARG          
SEQRES  13 B  200  PRO ILE LEU THR ILE ILE THR LEU GLU ASP SER SER GLY          
SEQRES  14 B  200  ASN LEU LEU GLY ARG ASN SER PHE GLU VAL CYS VAL CYS          
SEQRES  15 B  200  ALA CYS PRO GLY ARG ASP ARG ARG ARG GLU GLU GLU ASN          
SEQRES  16 B  200  LEU ARG LYS LYS GLY                                          
SEQRES   1 C  200  SER SER SER VAL PRO SER GLN LYS THR TYR GLN GLY SER          
SEQRES   2 C  200  TYR GLY PHE ARG LEU GLY PHE LEU HIS SER GLY THR ALA          
SEQRES   3 C  200  LYS SER VAL THR CYS THR TYR SER PRO ALA LEU ASN LYS          
SEQRES   4 C  200  MET PHE CYS GLN LEU ALA LYS THR CYS PRO VAL GLN LEU          
SEQRES   5 C  200  TRP VAL ASP SER THR PRO PRO PRO GLY THR ARG VAL ARG          
SEQRES   6 C  200  ALA MET ALA ILE TYR LYS GLN SER GLN HIS MET THR GLU          
SEQRES   7 C  200  VAL VAL ARG ARG CYS PRO HIS HIS GLU ARG CYS SER ASP          
SEQRES   8 C  200  SER ASP GLY LEU ALA PRO PRO GLN HIS LEU ILE ARG VAL          
SEQRES   9 C  200  GLU GLY ASN LEU ARG VAL GLU TYR LEU ASP ASP ARG ASN          
SEQRES  10 C  200  THR PHE ARG HIS SER VAL VAL VAL PRO TYR GLU PRO PRO          
SEQRES  11 C  200  GLU VAL GLY SER ASP CYS THR THR ILE HIS TYR ASN TYR          
SEQRES  12 C  200  MET CYS ASN SER SER CYS MET GLY GLY MET ASN ARG ARG          
SEQRES  13 C  200  PRO ILE LEU THR ILE ILE THR LEU GLU ASP SER SER GLY          
SEQRES  14 C  200  ASN LEU LEU GLY ARG ASN SER PHE GLU VAL CYS VAL CYS          
SEQRES  15 C  200  ALA CYS PRO GLY ARG ASP ARG ARG ARG GLU GLU GLU ASN          
SEQRES  16 C  200  LEU ARG LYS LYS GLY                                          
SEQRES   1 D  200  SER SER SER VAL PRO SER GLN LYS THR TYR GLN GLY SER          
SEQRES   2 D  200  TYR GLY PHE ARG LEU GLY PHE LEU HIS SER GLY THR ALA          
SEQRES   3 D  200  LYS SER VAL THR CYS THR TYR SER PRO ALA LEU ASN LYS          
SEQRES   4 D  200  MET PHE CYS GLN LEU ALA LYS THR CYS PRO VAL GLN LEU          
SEQRES   5 D  200  TRP VAL ASP SER THR PRO PRO PRO GLY THR ARG VAL ARG          
SEQRES   6 D  200  ALA MET ALA ILE TYR LYS GLN SER GLN HIS MET THR GLU          
SEQRES   7 D  200  VAL VAL ARG ARG CYS PRO HIS HIS GLU ARG CYS SER ASP          
SEQRES   8 D  200  SER ASP GLY LEU ALA PRO PRO GLN HIS LEU ILE ARG VAL          
SEQRES   9 D  200  GLU GLY ASN LEU ARG VAL GLU TYR LEU ASP ASP ARG ASN          
SEQRES  10 D  200  THR PHE ARG HIS SER VAL VAL VAL PRO TYR GLU PRO PRO          
SEQRES  11 D  200  GLU VAL GLY SER ASP CYS THR THR ILE HIS TYR ASN TYR          
SEQRES  12 D  200  MET CYS ASN SER SER CYS MET GLY GLY MET ASN ARG ARG          
SEQRES  13 D  200  PRO ILE LEU THR ILE ILE THR LEU GLU ASP SER SER GLY          
SEQRES  14 D  200  ASN LEU LEU GLY ARG ASN SER PHE GLU VAL CYS VAL CYS          
SEQRES  15 D  200  ALA CYS PRO GLY ARG ASP ARG ARG ARG GLU GLU GLU ASN          
SEQRES  16 D  200  LEU ARG LYS LYS GLY                                          
HET     ZN  A 301       1                                                       
HET    EDO  A 302       4                                                       
HET    EDO  A 303       4                                                       
HET    EDO  A 304       4                                                       
HET    EDO  A 305       4                                                       
HET     ZN  B 301       1                                                       
HET    EDO  B 302       4                                                       
HET    EDO  B 303       4                                                       
HET    EDO  B 304       4                                                       
HET    EDO  B 305       4                                                       
HET    EDO  B 306       4                                                       
HET    ACT  B 307       4                                                       
HET     ZN  C 301       1                                                       
HET    EDO  C 302       4                                                       
HET    EDO  C 303       4                                                       
HET    EDO  C 304       4                                                       
HET    EDO  C 305       4                                                       
HET     ZN  D 301       1                                                       
HET    EDO  D 302       4                                                       
HET    EDO  D 303       4                                                       
HET    EDO  D 304       4                                                       
HET    EDO  D 305       8                                                       
HET    EDO  D 306       4                                                       
HET    EDO  D 307       4                                                       
HET    ACT  D 308       4                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     ACT ACETATE ION                                                      
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   5   ZN    4(ZN 2+)                                                     
FORMUL   6  EDO    19(C2 H6 O2)                                                 
FORMUL  16  ACT    2(C2 H3 O2 1-)                                               
FORMUL  30  HOH   *613(H2 O)                                                    
HELIX    1   1 GLN A  165  MET A  169  5                                   5    
HELIX    2   2 CYS A  176  ARG A  181  1                                   6    
HELIX    3   3 CYS A  277  GLU A  287  1                                  11    
HELIX    4   4 CYS B  176  ARG B  181  1                                   6    
HELIX    5   5 CYS B  277  ASN B  288  1                                  12    
HELIX    6   6 CYS C  176  ARG C  181  1                                   6    
HELIX    7   7 CYS C  277  LEU C  289  1                                  13    
HELIX    8   8 GLN D  104  GLY D  108  5                                   5    
HELIX    9   9 CYS D  176  CYS D  182  1                                   7    
HELIX   10  10 CYS D  277  ASN D  288  1                                  12    
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  ARG A 156   O  GLU A 258           
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  TRP B 146   N  ARG B 110           
SHEET    3   C 4 THR B 230  TYR B 236 -1  O  ILE B 232   N  VAL B 143           
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  LYS B 132   N  SER B 127           
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  THR B 253   O  PHE B 270           
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  GLN C 144   N  GLY C 112           
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  GLU D 198 -1  N  GLU D 198   O  HIS D 233           
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  MET D 160   O  ILE D 254           
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  LEU D 206   O  SER D 215           
LINK         ND1 HIS D 179                ZN    ZN D 301     1555   1555  1.86  
LINK         ND1 HIS B 179                ZN    ZN B 301     1555   1555  1.90  
LINK         ND1 HIS C 179                ZN    ZN C 301     1555   1555  2.00  
LINK         ND1 HIS A 179                ZN    ZN A 301     1555   1555  2.01  
LINK         SG  CYS B 242                ZN    ZN B 301     1555   1555  2.25  
LINK         SG  CYS A 242                ZN    ZN A 301     1555   1555  2.29  
LINK         SG  CYS A 238                ZN    ZN A 301     1555   1555  2.33  
LINK         SG  CYS D 176                ZN    ZN D 301     1555   1555  2.35  
LINK         SG  CYS C 176                ZN    ZN C 301     1555   1555  2.35  
LINK         SG  CYS D 242                ZN    ZN D 301     1555   1555  2.37  
LINK         SG  CYS A 176                ZN    ZN A 301     1555   1555  2.39  
LINK         SG  CYS D 238                ZN    ZN D 301     1555   1555  2.41  
LINK         SG  CYS C 242                ZN    ZN C 301     1555   1555  2.45  
LINK         SG  CYS B 176                ZN    ZN B 301     1555   1555  2.45  
LINK         SG  CYS B 238                ZN    ZN B 301     1555   1555  2.50  
LINK         SG  CYS C 238                ZN    ZN C 301     1555   1555  2.54  
SITE     1 AC1  4 CYS A 176  HIS A 179  CYS A 238  CYS A 242                    
SITE     1 AC2  2 THR A 170  VAL A 172                                          
SITE     1 AC3  7 ARG A 158  ALA A 159  MET A 160  ILE A 254                    
SITE     2 AC3  7 THR A 256  HOH A 433  HOH A 439                               
SITE     1 AC4  6 ASP A 186  ARG A 196  VAL A 197  GLU A 198                    
SITE     2 AC4  6 ASN A 235  MET A 237                                          
SITE     1 AC5  2 THR A 102  HOH A 555                                          
SITE     1 AC6  4 CYS B 176  HIS B 179  CYS B 238  CYS B 242                    
SITE     1 AC7  6 SER B 260  SER B 261  HOH B 529  ALA D 119                    
SITE     2 AC7  6 LYS D 120  HOH D 435                                          
SITE     1 AC8  5 ASP B 207  HOH B 470  HOH B 506  LEU D 114                    
SITE     2 AC8  5 HIS D 115                                                     
SITE     1 AC9  8 PRO B 190  PRO B 191  GLN B 192  HIS B 193                    
SITE     2 AC9  8 ASP B 207  HIS B 214  HOH B 456  HIS D 115                    
SITE     1 BC1  6 PHE B 113  HIS B 115  GLN B 144  HOH B 541                    
SITE     2 BC1  6 EDO D 302  EDO D 306                                          
SITE     1 BC2  9 MET B 160  LEU B 206  ASP B 208  THR B 211                    
SITE     2 BC2  9 ARG B 213  HIS B 214  SER B 215  HOH B 503                    
SITE     3 BC2  9 HOH B 562                                                     
SITE     1 BC3  4 ARG B 110  HOH B 505  EDO D 302  EDO D 307                    
SITE     1 BC4  4 CYS C 176  HIS C 179  CYS C 238  CYS C 242                    
SITE     1 BC5  6 PRO C  98  ARG C 158  MET C 160  ILE C 254                    
SITE     2 BC5  6 THR C 256  HOH C 437                                          
SITE     1 BC6  6 LEU A 114  HIS A 115  SER A 116  ASP C 207                    
SITE     2 BC6  6 ARG C 209  HOH C 496                                          
SITE     1 BC7  4 ALA A 119  SER C 261  GLY C 262  HOH C 467                    
SITE     1 BC8  2 ARG C 209  ASN C 210                                          
SITE     1 BC9  4 CYS D 176  HIS D 179  CYS D 238  CYS D 242                    
SITE     1 CC1  7 HIS B 115  TRP B 146  EDO B 305  ACT B 307                    
SITE     2 CC1  7 PRO D 191  GLN D 192  EDO D 307                               
SITE     1 CC2  7 LEU D 114  SER D 116  CYS D 124  THR D 125                    
SITE     2 CC2  7 TYR D 126  HOH D 434  HOH D 527                               
SITE     1 CC3  3 SER D 240  ARG D 248  CYS D 273                               
SITE     1 CC4  9 MET D 160  LEU D 206  ASP D 208  THR D 211                    
SITE     2 CC4  9 ARG D 213  HIS D 214  SER D 215  HOH D 442                    
SITE     3 CC4  9 HOH D 520                                                     
SITE     1 CC5  5 LEU B 114  HIS B 115  EDO B 305  ASP D 207                    
SITE     2 CC5  5 HOH D 432                                                     
SITE     1 CC6  7 TRP B 146  ACT B 307  GLU D 180  PRO D 191                    
SITE     2 CC6  7 EDO D 302  HOH D 526  HOH D 541                               
SITE     1 CC7  3 GLY D 187  HOH D 450  HOH D 482                               
CRYST1   68.742   70.413   84.585  90.00  89.92  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014547  0.000000 -0.000021        0.00000                         
SCALE2      0.000000  0.014202  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011822        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system