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Database: PDB
Entry: 5MCV
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HEADER    TRANSCRIPTION                           10-NOV-16   5MCV              
TITLE     NEW INSIGHTS INTO THE ROLE OF DNA SHAPE ON ITS RECOGNITION BY P53     
TITLE    2 PROTEINS (COMPLEX P53DBD-LWC1)                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELLULAR TUMOR ANTIGEN P53;                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: P53 DNA BINDING DOMAIN;                                    
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;                                                       
COMPND   9 CHAIN: C;                                                            
COMPND  10 FRAGMENT: DNA;                                                       
COMPND  11 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 BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET27-B;                                  
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  13 ORGANISM_TAXID: 32630;                                               
SOURCE  14 OTHER_DETAILS: SYNTHESISED BY IDT                                    
KEYWDS    TRANSCRIPTION, P53, TRANSCRIPTION FACTOR, DNA BINDING, DNA            
KEYWDS   2 RECOGNITION, WATSON-CRICK BASE-PAIRING, INOSINE, 5-METHYLCYTOSINE,   
KEYWDS   3 TRANSCRIPTION REGULATION, APOPTOSIS, BIOLOGICAL RHYTHMS, CELL CYCLE, 
KEYWDS   4 NUCLEUS, TUMOR SUPPRESSOR, ANTIGEN NY-CO-13, PHOSPHOPROTEIN          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.GOLOVENKO,H.ROZENBERG,Z.SHAKKED                                     
REVDAT   3   02-JAN-19 5MCV    1       TITLE  JRNL                              
REVDAT   2   27-JUN-18 5MCV    1       REMARK                                   
REVDAT   1   13-JUN-18 5MCV    0                                                
JRNL        AUTH   D.GOLOVENKO,B.BRAUNING,P.VYAS,T.E.HARAN,H.ROZENBERG,         
JRNL        AUTH 2 Z.SHAKKED                                                    
JRNL        TITL   NEW INSIGHTS INTO THE ROLE OF DNA SHAPE ON ITS RECOGNITION   
JRNL        TITL 2 BY P53 PROTEINS.                                             
JRNL        REF    STRUCTURE                     V.  26  1237 2018              
JRNL        REFN                   ISSN 1878-4186                               
JRNL        PMID   30057026                                                     
JRNL        DOI    10.1016/J.STR.2018.06.006                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.48                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 60229                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.156                           
REMARK   3   R VALUE            (WORKING SET) : 0.154                           
REMARK   3   FREE R VALUE                     : 0.188                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3007                            
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 34.4831 -  3.5562    0.97     5255   286  0.1306 0.1608        
REMARK   3     2  3.5562 -  2.8231    0.99     5251   271  0.1392 0.1676        
REMARK   3     3  2.8231 -  2.4664    0.99     5252   280  0.1422 0.1820        
REMARK   3     4  2.4664 -  2.2409    0.99     5224   271  0.1464 0.1735        
REMARK   3     5  2.2409 -  2.0803    0.99     5195   268  0.1507 0.1887        
REMARK   3     6  2.0803 -  1.9577    1.00     5235   268  0.1591 0.1908        
REMARK   3     7  1.9577 -  1.8596    0.99     5175   274  0.1718 0.2188        
REMARK   3     8  1.8596 -  1.7787    0.99     5161   281  0.1825 0.2235        
REMARK   3     9  1.7787 -  1.7102    0.99     5172   275  0.1993 0.2427        
REMARK   3    10  1.7102 -  1.6512    0.99     5171   266  0.2130 0.2666        
REMARK   3    11  1.6512 -  1.5996    0.98     5131   267  0.2375 0.2655        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.160            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.850           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 14.48                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.42                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           3906                                  
REMARK   3   ANGLE     :  0.968           5391                                  
REMARK   3   CHIRALITY :  0.058            583                                  
REMARK   3   PLANARITY :  0.005            644                                  
REMARK   3   DIHEDRAL  : 14.487           2344                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 18                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 94 THROUGH 112 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): 166.6903  14.6912  87.6660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0956 T22:   0.1002                                     
REMARK   3      T33:   0.1760 T12:   0.0785                                     
REMARK   3      T13:  -0.0033 T23:   0.0663                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0458 L22:   0.0134                                     
REMARK   3      L33:   0.0793 L12:  -0.0130                                     
REMARK   3      L13:   0.0053 L23:  -0.0188                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0851 S12:  -0.0219 S13:   0.0999                       
REMARK   3      S21:   0.0731 S22:   0.0091 S23:  -0.1288                       
REMARK   3      S31:   0.0294 S32:   0.0051 S33:  -0.2215                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 113 THROUGH 123 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 152.2873  28.5186  72.3337              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1458 T22:   0.2053                                     
REMARK   3      T33:   0.2208 T12:   0.0558                                     
REMARK   3      T13:   0.0099 T23:   0.0332                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0030 L22:   0.0228                                     
REMARK   3      L33:   0.0023 L12:   0.0093                                     
REMARK   3      L13:  -0.0032 L23:  -0.0098                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0285 S12:   0.1436 S13:   0.1890                       
REMARK   3      S21:  -0.1447 S22:  -0.0609 S23:   0.0883                       
REMARK   3      S31:  -0.1139 S32:  -0.1329 S33:  -0.0079                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 124 THROUGH 155 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 159.7050  19.6161  76.7133              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0791 T22:   0.1032                                     
REMARK   3      T33:   0.1282 T12:   0.0136                                     
REMARK   3      T13:  -0.0107 T23:  -0.0114                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1529 L22:   0.2637                                     
REMARK   3      L33:   0.0344 L12:  -0.1918                                     
REMARK   3      L13:   0.0692 L23:  -0.0923                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0545 S12:   0.2221 S13:   0.0923                       
REMARK   3      S21:  -0.1411 S22:  -0.1220 S23:  -0.0856                       
REMARK   3      S31:  -0.0049 S32:  -0.0239 S33:  -0.1100                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 156 THROUGH 176 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 151.9271  11.9112  89.6453              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0576 T22:   0.0935                                     
REMARK   3      T33:   0.0640 T12:   0.0134                                     
REMARK   3      T13:   0.0242 T23:  -0.0037                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1994 L22:   0.1227                                     
REMARK   3      L33:   0.0061 L12:  -0.0728                                     
REMARK   3      L13:  -0.0032 L23:  -0.0115                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0501 S12:  -0.0958 S13:  -0.1204                       
REMARK   3      S21:   0.0345 S22:  -0.0087 S23:   0.0701                       
REMARK   3      S31:  -0.0045 S32:  -0.0911 S33:  -0.0749                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 177 THROUGH 203 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 147.1903   6.2661  75.8480              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0579 T22:   0.1164                                     
REMARK   3      T33:   0.0169 T12:   0.0366                                     
REMARK   3      T13:  -0.0826 T23:  -0.0866                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0101 L22:   0.2790                                     
REMARK   3      L33:   0.1494 L12:   0.0086                                     
REMARK   3      L13:   0.0410 L23:   0.0517                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0603 S12:   0.1160 S13:  -0.0752                       
REMARK   3      S21:  -0.1556 S22:  -0.0993 S23:   0.1526                       
REMARK   3      S31:   0.0526 S32:  -0.0714 S33:   0.1145                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 204 THROUGH 277 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 156.4920  12.3389  81.6655              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0795 T22:   0.0699                                     
REMARK   3      T33:   0.0261 T12:   0.0102                                     
REMARK   3      T13:  -0.0024 T23:  -0.0190                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3762 L22:   0.5361                                     
REMARK   3      L33:   0.4685 L12:  -0.0058                                     
REMARK   3      L13:   0.0871 L23:   0.0908                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0437 S12:   0.0526 S13:  -0.0173                       
REMARK   3      S21:  -0.0295 S22:   0.0271 S23:   0.0110                       
REMARK   3      S31:   0.0998 S32:  -0.0500 S33:   0.0063                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 278 THROUGH 293 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 150.2964  35.2444  83.6119              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1351 T22:   0.1121                                     
REMARK   3      T33:   0.1900 T12:   0.0094                                     
REMARK   3      T13:  -0.0320 T23:   0.0359                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0272 L22:   0.0164                                     
REMARK   3      L33:   0.0022 L12:   0.0089                                     
REMARK   3      L13:   0.0002 L23:   0.0070                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0620 S12:   0.0251 S13:   0.0565                       
REMARK   3      S21:  -0.1041 S22:  -0.0399 S23:   0.1304                       
REMARK   3      S31:  -0.0171 S32:   0.0025 S33:   0.0003                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 94 THROUGH 112 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): 168.4194  14.6926  53.6875              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1267 T22:   0.1264                                     
REMARK   3      T33:   0.0527 T12:  -0.0306                                     
REMARK   3      T13:  -0.0226 T23:  -0.0405                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3565 L22:   0.5177                                     
REMARK   3      L33:   0.1223 L12:  -0.1379                                     
REMARK   3      L13:  -0.0013 L23:  -0.2293                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1006 S12:  -0.0849 S13:   0.0615                       
REMARK   3      S21:   0.1570 S22:   0.0292 S23:  -0.1325                       
REMARK   3      S31:   0.0335 S32:  -0.0613 S33:  -0.1368                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 113 THROUGH 123 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 154.0117  28.5181  38.3499              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2528 T22:   0.1941                                     
REMARK   3      T33:   0.2171 T12:   0.0502                                     
REMARK   3      T13:  -0.0813 T23:   0.0804                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0432 L22:   0.2273                                     
REMARK   3      L33:   0.2345 L12:   0.0999                                     
REMARK   3      L13:   0.1011 L23:   0.2289                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0022 S12:   0.1255 S13:   0.1393                       
REMARK   3      S21:  -0.1944 S22:  -0.0996 S23:   0.1283                       
REMARK   3      S31:  -0.0548 S32:  -0.1132 S33:  -0.0680                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 124 THROUGH 155)                  
REMARK   3    ORIGIN FOR THE GROUP (A): 161.3395  19.6860  42.6925              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0908 T22:   0.0967                                     
REMARK   3      T33:   0.0438 T12:   0.0000                                     
REMARK   3      T13:   0.0029 T23:   0.0212                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3976 L22:   0.3379                                     
REMARK   3      L33:   0.1299 L12:   0.0941                                     
REMARK   3      L13:   0.1413 L23:  -0.0509                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0172 S12:   0.1292 S13:  -0.0099                       
REMARK   3      S21:  -0.0389 S22:  -0.0149 S23:  -0.0461                       
REMARK   3      S31:  -0.0328 S32:   0.0234 S33:  -0.0711                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 156 THROUGH 176 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 153.6703  12.0210  55.8175              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0839 T22:   0.0515                                     
REMARK   3      T33:   0.0619 T12:   0.0142                                     
REMARK   3      T13:   0.0153 T23:   0.0089                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5509 L22:   0.2285                                     
REMARK   3      L33:   0.1046 L12:  -0.2424                                     
REMARK   3      L13:  -0.0256 L23:   0.1138                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0981 S12:  -0.1163 S13:  -0.1553                       
REMARK   3      S21:   0.0936 S22:   0.0257 S23:   0.1115                       
REMARK   3      S31:   0.0018 S32:  -0.0143 S33:  -0.1567                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 177 THROUGH 203 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 148.8008   6.3470  41.9203              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1470 T22:   0.0708                                     
REMARK   3      T33:   0.1292 T12:  -0.0351                                     
REMARK   3      T13:   0.0079 T23:  -0.0004                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5734 L22:   1.4961                                     
REMARK   3      L33:   0.3604 L12:  -0.2001                                     
REMARK   3      L13:  -0.0602 L23:   0.0264                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0181 S12:   0.1049 S13:  -0.1523                       
REMARK   3      S21:  -0.1394 S22:  -0.0480 S23:   0.5042                       
REMARK   3      S31:   0.1110 S32:  -0.1651 S33:   0.0545                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 204 THROUGH 277 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 158.1666  12.2440  47.7178              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0532 T22:   0.0574                                     
REMARK   3      T33:   0.0974 T12:   0.0120                                     
REMARK   3      T13:   0.0120 T23:   0.0278                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2664 L22:   0.5893                                     
REMARK   3      L33:   0.3202 L12:   0.0155                                     
REMARK   3      L13:   0.2554 L23:   0.1603                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0229 S12:  -0.0032 S13:   0.0721                       
REMARK   3      S21:   0.0802 S22:  -0.0069 S23:  -0.0221                       
REMARK   3      S31:  -0.0140 S32:   0.0475 S33:  -0.0628                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 278 THROUGH 293)                  
REMARK   3    ORIGIN FOR THE GROUP (A): 152.0273  35.2435  49.6422              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1343 T22:   0.1078                                     
REMARK   3      T33:   0.1780 T12:  -0.0023                                     
REMARK   3      T13:  -0.0078 T23:  -0.0158                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0245 L22:   0.0188                                     
REMARK   3      L33:   0.0030 L12:   0.0018                                     
REMARK   3      L13:  -0.0012 L23:   0.0088                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0527 S12:   0.0158 S13:   0.0699                       
REMARK   3      S21:  -0.1298 S22:  -0.0630 S23:   0.1332                       
REMARK   3      S31:   0.0191 S32:   0.0138 S33:   0.0002                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 6 )                     
REMARK   3    ORIGIN FOR THE GROUP (A): 134.1819  34.8610  92.2921              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2156 T22:   0.1423                                     
REMARK   3      T33:   0.1486 T12:  -0.0163                                     
REMARK   3      T13:   0.0196 T23:  -0.0462                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0281 L22:   0.0254                                     
REMARK   3      L33:   0.0238 L12:   0.0205                                     
REMARK   3      L13:   0.0209 L23:   0.0267                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2098 S12:  -0.1906 S13:   0.0957                       
REMARK   3      S21:   0.1013 S22:  -0.0901 S23:  -0.0935                       
REMARK   3      S31:   0.0423 S32:  -0.0049 S33:   0.0002                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 7 THROUGH 10 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): 132.8350  28.2922  75.0343              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1947 T22:   0.2222                                     
REMARK   3      T33:   0.2056 T12:   0.0913                                     
REMARK   3      T13:  -0.1096 T23:  -0.0080                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0089 L22:   0.7259                                     
REMARK   3      L33:   0.0106 L12:  -0.0803                                     
REMARK   3      L13:  -0.0099 L23:   0.0873                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1415 S12:   0.2300 S13:  -0.1703                       
REMARK   3      S21:  -0.3542 S22:   0.1049 S23:  -0.0393                       
REMARK   3      S31:   0.0066 S32:  -0.1388 S33:   0.0572                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 11 THROUGH 16 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): 135.9102  34.8571  58.3119              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1350 T22:   0.2077                                     
REMARK   3      T33:   0.1371 T12:  -0.0493                                     
REMARK   3      T13:   0.0302 T23:  -0.0561                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0674 L22:   0.0332                                     
REMARK   3      L33:   0.0717 L12:   0.0178                                     
REMARK   3      L13:   0.0016 L23:   0.0484                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1694 S12:  -0.1300 S13:   0.0675                       
REMARK   3      S21:   0.1279 S22:   0.0051 S23:  -0.0830                       
REMARK   3      S31:  -0.0494 S32:   0.0008 S33:   0.0055                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 17 THROUGH 20 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): 134.5660  28.2883  41.0594              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2403 T22:   0.2404                                     
REMARK   3      T33:   0.1722 T12:  -0.0346                                     
REMARK   3      T13:  -0.0158 T23:   0.0477                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0288 L22:   0.0314                                     
REMARK   3      L33:   0.0243 L12:  -0.0228                                     
REMARK   3      L13:  -0.0150 L23:   0.0267                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1951 S12:   0.2387 S13:  -0.2480                       
REMARK   3      S21:  -0.4679 S22:   0.0540 S23:  -0.0479                       
REMARK   3      S31:  -0.0913 S32:  -0.1911 S33:   0.0003                       
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 5MCV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-NOV-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200002286.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-JUL-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.88560                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 60494                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 5.700                              
REMARK 200  R MERGE                    (I) : 0.07300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.63                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39400                            
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: PHASER 2.5.7                                          
REMARK 200 STARTING MODEL: PDBID 1TSR                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.22                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.02 M CITRIC ACID, 0.08 M BIS-TRIS      
REMARK 280  PROPANE, 16% W/V POLYETHYLENE GLYCOL 3,350, PH 8.8, EVAPORATION,    
REMARK 280  TEMPERATURE 292K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       69.03900            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.76650            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       69.03900            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       24.76650            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       -6.90912            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      135.91851            
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      DT C     0                                                      
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     HIS A 115    ND1  CE1  NE2                                       
REMARK 470     SER A 183    CB   OG                                             
REMARK 470     SER A 185    OG                                                  
REMARK 470     GLU A 287    CD   OE1  OE2                                       
REMARK 470     LYS A 291    CE   NZ                                             
REMARK 470     LYS A 292    CE   NZ                                             
REMARK 470     HIS B 115    ND1  CE1  NE2                                       
REMARK 470     SER B 183    CB   OG                                             
REMARK 470     SER B 185    CB   OG                                             
REMARK 470     GLU B 287    CD   OE1  OE2                                       
REMARK 470     LYS B 291    CE   NZ                                             
REMARK 470     LYS B 292    CE   NZ                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   643     O    HOH C   165              1.96            
REMARK 500   O    HOH B   651     O    HOH C   164              1.98            
REMARK 500   O    HOH A   580     O    HOH A   647              2.01            
REMARK 500   O    HOH B   408     O    HOH B   621              2.02            
REMARK 500   O    HOH A   486     O    HOH A   526              2.02            
REMARK 500   O    HOH B   489     O    HOH B   532              2.02            
REMARK 500   O    HOH B   577     O    HOH B   578              2.03            
REMARK 500   O    HOH B   573     O    HOH B   652              2.03            
REMARK 500   O    HOH A   585     O    HOH A   587              2.04            
REMARK 500   O    HOH B   568     O    HOH B   626              2.04            
REMARK 500   O    HOH A   408     O    HOH A   612              2.06            
REMARK 500   O    HOH B   529     O    HOH B   588              2.10            
REMARK 500   O    HOH A   505     O    HOH A   582              2.11            
REMARK 500   O    HOH A   568     O    HOH A   620              2.11            
REMARK 500   O    HOH B   625     O    HOH B   636              2.12            
REMARK 500   O    HOH A   618     O    HOH A   628              2.13            
REMARK 500   OP2   DI C    15     O    HOH C   101              2.15            
REMARK 500   O    HOH B   507     O    HOH B   556              2.17            
REMARK 500   O    HOH A   639     O    HOH A   652              2.17            
REMARK 500   OP2   DI C     5     O    HOH C   102              2.18            
REMARK 500   O    HOH A   452     O    HOH A   595              2.19            
REMARK 500   O    HOH A   504     O    HOH A   559              2.19            
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   P     DG C     1     O3'   DC C    20     1556     1.60            
REMARK 500   O    HOH B   592     O    HOH C   140     2557     2.13            
REMARK 500   O    HOH A   472     O    HOH B   435     2557     2.15            
REMARK 500   O    HOH A   591     O    HOH C   151     2557     2.15            
REMARK 500   O    HOH A   458     O    HOH B   499     2557     2.16            
REMARK 500   O    HOH A   509     O    HOH A   633     4557     2.18            
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     DG C   3   O4' -  C1' -  N9  ANGL. DEV. =   2.2 DEGREES          
REMARK 500     DG C  13   O4' -  C1' -  N9  ANGL. DEV. =   2.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 176   SG                                                     
REMARK 620 2 HIS A 179   ND1 101.3                                              
REMARK 620 3 CYS A 238   SG  111.7 113.6                                        
REMARK 620 4 CYS A 242   SG  114.7 100.9 113.5                                  
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 CYS B 176   SG                                                     
REMARK 620 2 HIS B 179   ND1 101.9                                              
REMARK 620 3 CYS B 238   SG  111.1 112.6                                        
REMARK 620 4 CYS B 242   SG  114.5 102.2 113.6                                  
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 EDO A 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 307                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3KZ8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5MCW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5MG7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5MF7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6FJ5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5MCT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5MCU   RELATED DB: PDB                                   
DBREF  5MCV A   94   293  UNP    P04637   P53_HUMAN       55    254             
DBREF  5MCV B   94   293  UNP    P04637   P53_HUMAN       55    254             
DBREF  5MCV C    0    20  PDB    5MCV     5MCV             0     20             
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 ARG VAL CYS          
SEQRES  15 A  200  ALA CYS PRO GLY ARG ASP ARG ARG THR GLU GLU GLU ASN          
SEQRES  16 A  200  LEU ARG LYS LYS GLY                                          
SEQRES   1 B  200  SER SER SER VAL PRO SER GLN LYS THR TYR GLN GLY SER          
SEQRES   2 B  200  TYR GLY PHE ARG LEU GLY PHE LEU HIS SER GLY THR ALA          
SEQRES   3 B  200  LYS SER VAL THR CYS THR TYR SER PRO ALA LEU ASN LYS          
SEQRES   4 B  200  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 ARG VAL CYS          
SEQRES  15 B  200  ALA CYS PRO GLY ARG ASP ARG ARG THR GLU GLU GLU ASN          
SEQRES  16 B  200  LEU ARG LYS LYS GLY                                          
SEQRES   1 C   21   DT  DG  DG  DG  DC  DI 5CM  DG  DC  DC  DC  DG  DG          
SEQRES   2 C   21   DG  DC  DI 5CM  DG  DC  DC  DC                              
HET    5CM  C   6      20                                                       
HET    5CM  C  16      20                                                       
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    EDO  A 306       4                                                       
HET    ACT  A 307       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                                                       
HETNAM     5CM 5-METHYL-2'-DEOXY-CYTIDINE-5'-MONOPHOSPHATE                      
HETNAM      ZN ZINC ION                                                         
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     ACT ACETATE ION                                                      
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  5CM    2(C10 H16 N3 O7 P)                                           
FORMUL   4   ZN    2(ZN 2+)                                                     
FORMUL   5  EDO    10(C2 H6 O2)                                                 
FORMUL  10  ACT    2(C2 H3 O2 1-)                                               
FORMUL  18  HOH   *575(H2 O)                                                    
HELIX    1 AA1 GLN A  165  MET A  169  5                                   5    
HELIX    2 AA2 CYS A  176  ARG A  181  1                                   6    
HELIX    3 AA3 CYS A  277  GLY A  293  1                                  17    
HELIX    4 AA4 GLN B  165  MET B  169  5                                   5    
HELIX    5 AA5 CYS B  176  ARG B  181  1                                   6    
HELIX    6 AA6 CYS B  277  GLY B  293  1                                  17    
SHEET    1 AA1 4 ARG A 110  GLY A 112  0                                        
SHEET    2 AA1 4 CYS A 141  TRP A 146 -1  O  GLN A 144   N  GLY A 112           
SHEET    3 AA1 4 THR A 230  TYR A 236 -1  O  THR A 230   N  LEU A 145           
SHEET    4 AA1 4 ILE A 195  GLU A 198 -1  N  ARG A 196   O  ASN A 235           
SHEET    1 AA2 7 CYS A 124  SER A 127  0                                        
SHEET    2 AA2 7 LYS A 132  CYS A 135 -1  O  PHE A 134   N  THR A 125           
SHEET    3 AA2 7 LEU A 264  VAL A 274  1  O  GLU A 271   N  MET A 133           
SHEET    4 AA2 7 ILE A 251  GLU A 258 -1  N  ILE A 255   O  ASN A 268           
SHEET    5 AA2 7 ARG A 156  TYR A 163 -1  N  ARG A 156   O  GLU A 258           
SHEET    6 AA2 7 HIS A 214  PRO A 219 -1  O  VAL A 218   N  VAL A 157           
SHEET    7 AA2 7 GLU A 204  ASP A 207 -1  N  GLU A 204   O  VAL A 217           
SHEET    1 AA3 4 ARG B 110  GLY B 112  0                                        
SHEET    2 AA3 4 CYS B 141  TRP B 146 -1  O  GLN B 144   N  GLY B 112           
SHEET    3 AA3 4 THR B 230  TYR B 236 -1  O  THR B 230   N  LEU B 145           
SHEET    4 AA3 4 ILE B 195  GLU B 198 -1  N  ARG B 196   O  ASN B 235           
SHEET    1 AA4 7 CYS B 124  SER B 127  0                                        
SHEET    2 AA4 7 LYS B 132  CYS B 135 -1  O  PHE B 134   N  THR B 125           
SHEET    3 AA4 7 LEU B 264  VAL B 274  1  O  GLU B 271   N  MET B 133           
SHEET    4 AA4 7 ILE B 251  GLU B 258 -1  N  THR B 253   O  PHE B 270           
SHEET    5 AA4 7 ARG B 156  TYR B 163 -1  N  ARG B 156   O  GLU B 258           
SHEET    6 AA4 7 HIS B 214  PRO B 219 -1  O  VAL B 218   N  VAL B 157           
SHEET    7 AA4 7 GLU B 204  ASP B 207 -1  N  GLU B 204   O  VAL B 217           
LINK         SG  CYS A 176                ZN    ZN A 301     1555   1555  2.31  
LINK         ND1 HIS A 179                ZN    ZN A 301     1555   1555  2.05  
LINK         SG  CYS A 238                ZN    ZN A 301     1555   1555  2.33  
LINK         SG  CYS A 242                ZN    ZN A 301     1555   1555  2.37  
LINK         SG  CYS B 176                ZN    ZN B 301     1555   1555  2.31  
LINK         ND1 HIS B 179                ZN    ZN B 301     1555   1555  2.03  
LINK         SG  CYS B 238                ZN    ZN B 301     1555   1555  2.35  
LINK         SG  CYS B 242                ZN    ZN B 301     1555   1555  2.37  
LINK         O3'  DI C   5                 P   5CM C   6     1555   1555  1.60  
LINK         O3' 5CM C   6                 P    DG C   7     1555   1555  1.59  
LINK         O3'  DI C  15                 P   5CM C  16     1555   1555  1.60  
LINK         O3' 5CM C  16                 P    DG C  17     1555   1555  1.61  
SITE     1 AC1  4 CYS A 176  HIS A 179  CYS A 238  CYS A 242                    
SITE     1 AC2  6 PHE A 113  LEU A 114  SER A 116  CYS A 124                    
SITE     2 AC2  6 MET A 133  PRO A 142                                          
SITE     1 AC3  9 LYS A 132  SER A 240  PRO A 250  GLU A 271                    
SITE     2 AC3  9 VAL A 272  ARG A 273  GLU A 285  HOH A 486                    
SITE     3 AC3  9 HOH A 526                                                     
SITE     1 AC4  5 SER A 260  HOH A 473  GLN B 100  SER B 269                    
SITE     2 AC4  5 EDO B 306                                                     
SITE     1 AC5  8 ASN A 131  LYS A 164  LEU A 252  GLU A 271                    
SITE     2 AC5  8 HOH A 427  HOH A 488  HOH A 528  EDO B 304                    
SITE     1 AC6  4 ARG A 110  LEU A 111  TRP A 146  ACT A 307                    
SITE     1 AC7  9 LEU A 111  TYR A 126  EDO A 306  HOH A 444                    
SITE     2 AC7  9 HOH A 547  HOH A 557  HOH A 561  SER B 261                    
SITE     3 AC7  9 ASN B 263                                                     
SITE     1 AC8  4 CYS B 176  HIS B 179  CYS B 238  CYS B 242                    
SITE     1 AC9  6 PHE B 113  LEU B 114  SER B 116  CYS B 124                    
SITE     2 AC9  6 MET B 133  PRO B 142                                          
SITE     1 AD1  9 LYS B 132  SER B 240  PRO B 250  GLU B 271                    
SITE     2 AD1  9 VAL B 272  ARG B 273  GLU B 285  HOH B 489                    
SITE     3 AD1  9 HOH B 532                                                     
SITE     1 AD2  5 GLN A 100  SER A 269  EDO A 305  SER B 260                    
SITE     2 AD2  5 HOH B 466                                                     
SITE     1 AD3  5 ARG B 110  LEU B 111  GLY B 112  TRP B 146                    
SITE     2 AD3  5 ACT B 307                                                     
SITE     1 AD4  8 EDO A 304  ASN B 131  LYS B 164  LEU B 252                    
SITE     2 AD4  8 GLU B 271  HOH B 421  HOH B 497  HOH B 535                    
SITE     1 AD5  9 SER A 261  ASN A 263  LEU B 111  TYR B 126                    
SITE     2 AD5  9 EDO B 305  HOH B 462  HOH B 545  HOH B 558                    
SITE     3 AD5  9 HOH B 564                                                     
CRYST1  138.078   49.533   68.047  90.00  92.91  90.00 C 1 2 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      0.007242  0.000000  0.000368        0.00000                         
SCALE2      0.000000  0.020189  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014715        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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