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Database: PDB
Entry: 4QEO
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Original site: 4QEO 
HEADER    TRANSCRIPTION/DNA                       17-MAY-14   4QEO              
TITLE     CRYSTAL STRUCTURE OF KRYPTONITE IN COMPLEX WITH MCHH DNA, H3(1-15)    
TITLE    2 PEPTIDE AND SAH                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-9 SPECIFIC   
COMPND   3 SUVH4;                                                               
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: FUNCTIONAL FRAGMENT;                                       
COMPND   6 SYNONYM: HISTONE H3-K9 METHYLTRANSFERASE 4, H3-K9-HMTASE 4, PROTEIN  
COMPND   7 KRYPTONITE, PROTEIN SET DOMAIN GROUP 33, SUPPRESSOR OF VARIEGATION 3-
COMPND   8 9 HOMOLOG PROTEIN 4, SU(VAR)3-9 HOMOLOG PROTEIN 4;                   
COMPND   9 EC: 2.1.1.43;                                                        
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: DNA 5'-GGTACT(5CM)ATCAGTAT-3';                             
COMPND  13 CHAIN: C;                                                            
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: DNA 5'-ACTGATGAGTACCAT-3';                                 
COMPND  17 CHAIN: D;                                                            
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 MOL_ID: 4;                                                           
COMPND  20 MOLECULE: HISTONE H3;                                                
COMPND  21 CHAIN: P;                                                            
COMPND  22 FRAGMENT: UNP RESIDUES 2-16;                                         
COMPND  23 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;                           
SOURCE   3 ORGANISM_COMMON: MOUSE-EAR CRESS,THALE-CRESS;                        
SOURCE   4 ORGANISM_TAXID: 3702;                                                
SOURCE   5 GENE: SUVH4, KYP, SDG33, SET33, AT5G13960, MAC12.7;                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) RIL;                             
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-SUMO;                                 
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 SYNTHETIC: YES;                                                      
SOURCE  15 MOL_ID: 4;                                                           
SOURCE  16 SYNTHETIC: YES;                                                      
SOURCE  17 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;                                 
SOURCE  18 ORGANISM_COMMON: CLAWED FROG,COMMON PLATANNA,PLATANNA;               
SOURCE  19 ORGANISM_TAXID: 8355;                                                
SOURCE  20 OTHER_DETAILS: SAH WAS ORDERED FROM SIGMA.                           
KEYWDS    SRA, SET, HISTONE METHYLATION, METHYLATED DNA, METHYLATION,           
KEYWDS   2 TRANSCRIPTION-DNA COMPLEX                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.DU,S.LI,D.J.PATEL                                                   
REVDAT   2   20-AUG-14 4QEO    1       JRNL                                     
REVDAT   1   30-JUL-14 4QEO    0                                                
JRNL        AUTH   J.DU,L.M.JOHNSON,M.GROTH,S.FENG,C.J.HALE,S.LI,A.A.VASHISHT,  
JRNL        AUTH 2 J.GALLEGO-BARTOLOME,J.A.WOHLSCHLEGEL,D.J.PATEL,S.E.JACOBSEN  
JRNL        TITL   MECHANISM OF DNA METHYLATION-DIRECTED HISTONE METHYLATION BY 
JRNL        TITL 2 KRYPTONITE.                                                  
JRNL        REF    MOL.CELL                      V.  55   495 2014              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   25018018                                                     
JRNL        DOI    10.1016/J.MOLCEL.2014.06.009                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.1_1168)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.10                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 45207                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.188                           
REMARK   3   R VALUE            (WORKING SET) : 0.186                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2271                            
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 41.1063 -  5.0377    0.98     2840   146  0.1925 0.2472        
REMARK   3     2  5.0377 -  3.9996    1.00     2734   154  0.1523 0.1821        
REMARK   3     3  3.9996 -  3.4944    1.00     2733   136  0.1626 0.1884        
REMARK   3     4  3.4944 -  3.1750    1.00     2729   127  0.1817 0.2245        
REMARK   3     5  3.1750 -  2.9475    1.00     2677   133  0.1985 0.2508        
REMARK   3     6  2.9475 -  2.7738    1.00     2667   161  0.1957 0.2191        
REMARK   3     7  2.7738 -  2.6349    1.00     2665   154  0.1966 0.2456        
REMARK   3     8  2.6349 -  2.5202    1.00     2661   153  0.1961 0.2464        
REMARK   3     9  2.5202 -  2.4232    1.00     2668   121  0.1972 0.2524        
REMARK   3    10  2.4232 -  2.3396    1.00     2697   140  0.2102 0.2601        
REMARK   3    11  2.3396 -  2.2664    1.00     2627   154  0.2073 0.2434        
REMARK   3    12  2.2664 -  2.2016    1.00     2632   155  0.2133 0.2512        
REMARK   3    13  2.2016 -  2.1437    1.00     2643   141  0.2155 0.2348        
REMARK   3    14  2.1437 -  2.0914    1.00     2692   131  0.2260 0.2588        
REMARK   3    15  2.0914 -  2.0438    1.00     2631   128  0.2326 0.2517        
REMARK   3    16  2.0438 -  2.0004    0.99     2640   137  0.2447 0.2856        
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)     : 0.200            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.700           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 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      :  0.011           4420                                  
REMARK   3   ANGLE     :  1.367           6065                                  
REMARK   3   CHIRALITY :  0.092            660                                  
REMARK   3   PLANARITY :  0.008            695                                  
REMARK   3   DIHEDRAL  : 20.907           1682                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resid 99 through 278 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -17.1488  19.7069  16.5122              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1760 T22:   0.1542                                     
REMARK   3      T33:   0.1837 T12:   0.0249                                     
REMARK   3      T13:   0.0072 T23:   0.0216                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5926 L22:   0.9178                                     
REMARK   3      L33:   3.4594 L12:  -0.2455                                     
REMARK   3      L13:   0.5770 L23:  -0.5814                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1230 S12:  -0.1525 S13:  -0.0169                       
REMARK   3      S21:   0.2263 S22:   0.0354 S23:   0.0619                       
REMARK   3      S31:  -0.1904 S32:  -0.2550 S33:   0.0699                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resid 279 through 337 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -10.1914   9.5762   7.1217              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2309 T22:   0.2247                                     
REMARK   3      T33:   0.2725 T12:   0.0198                                     
REMARK   3      T13:   0.0386 T23:   0.0613                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3534 L22:   0.5128                                     
REMARK   3      L33:   1.3837 L12:  -0.3208                                     
REMARK   3      L13:   0.1279 L23:   0.1024                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0836 S12:   0.1484 S13:  -0.1824                       
REMARK   3      S21:   0.0474 S22:  -0.0628 S23:  -0.1019                       
REMARK   3      S31:   0.3381 S32:   0.1439 S33:  -0.0214                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resid 338 through 589 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.9105   3.7034  45.1636              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3533 T22:   0.2931                                     
REMARK   3      T33:   0.3639 T12:  -0.0657                                     
REMARK   3      T13:  -0.0019 T23:   0.1261                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9621 L22:   2.7049                                     
REMARK   3      L33:   3.8275 L12:  -0.2258                                     
REMARK   3      L13:   0.1029 L23:  -1.7476                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0040 S12:  -0.0136 S13:   0.0922                       
REMARK   3      S21:   0.0931 S22:  -0.1893 S23:  -0.3975                       
REMARK   3      S31:  -0.2705 S32:   0.2311 S33:   0.0972                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'A' and (resid 590 through 624 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  15.2605  17.5072  40.0777              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9116 T22:   1.1546                                     
REMARK   3      T33:   1.3215 T12:  -0.3270                                     
REMARK   3      T13:  -0.0966 T23:   0.3947                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2223 L22:   3.6161                                     
REMARK   3      L33:   0.5977 L12:  -0.1253                                     
REMARK   3      L13:  -0.9464 L23:  -0.8121                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1448 S12:   0.2109 S13:   1.3049                       
REMARK   3      S21:   0.2229 S22:  -0.0309 S23:  -1.2801                       
REMARK   3      S31:  -1.1702 S32:   1.4463 S33:  -0.1316                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'C' and (resid 1 through 11 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -31.4898  19.1266  18.4422              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3520 T22:   0.5114                                     
REMARK   3      T33:   0.4255 T12:   0.0685                                     
REMARK   3      T13:   0.1190 T23:   0.0194                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8432 L22:   2.8357                                     
REMARK   3      L33:   2.3990 L12:  -0.3770                                     
REMARK   3      L13:   0.3047 L23:   1.0770                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1268 S12:  -0.5538 S13:  -0.2413                       
REMARK   3      S21:   0.5416 S22:   0.0033 S23:   0.8875                       
REMARK   3      S31:  -0.2518 S32:  -0.9046 S33:   0.0255                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'D' and (resid 3 through 7 )                     
REMARK   3    ORIGIN FOR THE GROUP (A): -34.6279   8.7422  21.8361              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5929 T22:   0.8268                                     
REMARK   3      T33:   0.8107 T12:  -0.2196                                     
REMARK   3      T13:   0.0437 T23:   0.1153                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6243 L22:   2.0151                                     
REMARK   3      L33:   0.8516 L12:   0.2697                                     
REMARK   3      L13:   0.7174 L23:   0.9207                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0834 S12:   0.1229 S13:  -0.4519                       
REMARK   3      S21:  -0.1511 S22:  -0.0974 S23:   1.1243                       
REMARK   3      S31:   1.0323 S32:  -1.0548 S33:  -0.0674                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain 'D' and (resid 8 through 15 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -32.7866  30.5763  15.2873              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6962 T22:   0.7319                                     
REMARK   3      T33:   0.6419 T12:   0.2025                                     
REMARK   3      T13:  -0.0787 T23:   0.1446                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6116 L22:   1.5569                                     
REMARK   3      L33:   1.0274 L12:   0.5717                                     
REMARK   3      L13:  -0.9428 L23:   0.1517                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4346 S12:   0.8319 S13:   0.6528                       
REMARK   3      S21:  -0.1341 S22:  -0.3513 S23:   0.3520                       
REMARK   3      S31:  -1.1329 S32:  -0.3141 S33:   0.9276                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain 'P' and (resid 9 through 15 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):   0.7352  16.3923  46.6034              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7381 T22:   0.9355                                     
REMARK   3      T33:   0.9803 T12:  -0.0531                                     
REMARK   3      T13:   0.1870 T23:   0.1337                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0389 L22:   0.5717                                     
REMARK   3      L33:   1.0819 L12:   0.0859                                     
REMARK   3      L13:   0.1608 L23:   0.7730                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5768 S12:  -0.2625 S13:  -0.2711                       
REMARK   3      S21:   0.1269 S22:   0.2465 S23:  -0.3622                       
REMARK   3      S31:  -0.5325 S32:  -0.0264 S33:   0.1737                       
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 4QEO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUN-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB085959.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-JAN-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.075                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMETER       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45280                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.100                              
REMARK 200  R MERGE                    (I) : 0.07400                            
REMARK 200  R SYM                      (I) : 0.07400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 36.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.76900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.76900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4QEN                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG200, 5% PEG3000, AND 0.1 M MES,   
REMARK 280  PH 6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       27.73000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       61.20550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       48.38250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       61.20550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.73000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       48.38250            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5230 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25160 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D, P                            
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    92                                                      
REMARK 465     ASN A    93                                                      
REMARK 465     GLY A    94                                                      
REMARK 465     LYS A    95                                                      
REMARK 465     ASP A    96                                                      
REMARK 465     VAL A    97                                                      
REMARK 465     ASN A    98                                                      
REMARK 465     GLN A   313                                                      
REMARK 465     VAL A   314                                                      
REMARK 465     ASN A   315                                                      
REMARK 465     PHE A   316                                                      
REMARK 465     VAL A   317                                                      
REMARK 465     ALA A   318                                                      
REMARK 465     GLY A   319                                                      
REMARK 465     ARG A   320                                                      
REMARK 465     ILE A   321                                                      
REMARK 465     PRO A   322                                                      
REMARK 465     THR A   323                                                      
REMARK 465     SER A   324                                                      
REMARK 465     THR A   325                                                      
REMARK 465     SER A   326                                                      
REMARK 465     GLU A   327                                                      
REMARK 465     ASP A   486                                                      
REMARK 465     THR A   487                                                      
REMARK 465     ILE A   488                                                      
REMARK 465     SER A   489                                                      
REMARK 465     ASP A   490                                                      
REMARK 465     GLN A   500                                                      
REMARK 465     GLN A   501                                                      
REMARK 465     THR A   502                                                      
REMARK 465     MET A   503                                                      
REMARK 465     GLN A   504                                                      
REMARK 465     GLY A   505                                                      
REMARK 465     LEU A   506                                                      
REMARK 465     GLY A   507                                                      
REMARK 465     GLY A   508                                                      
REMARK 465     ARG A   509                                                      
REMARK 465     GLN A   510                                                      
REMARK 465     ARG A   511                                                      
REMARK 465     ARG A   512                                                      
REMARK 465     LEU A   513                                                      
REMARK 465     ARG A   514                                                      
REMARK 465     ASP A   515                                                      
REMARK 465     VAL A   516                                                      
REMARK 465     ALA A   517                                                      
REMARK 465     VAL A   518                                                      
REMARK 465     PRO A   519                                                      
REMARK 465     MET A   520                                                      
REMARK 465     ASN A   521                                                      
REMARK 465     ASN A   522                                                      
REMARK 465     GLY A   523                                                      
REMARK 465     VAL A   524                                                      
REMARK 465     SER A   525                                                      
REMARK 465     GLN A   526                                                      
REMARK 465     SER A   527                                                      
REMARK 465     SER A   528                                                      
REMARK 465     GLU A   529                                                      
REMARK 465     ASP A   530                                                      
REMARK 465     GLU A   531                                                      
REMARK 465     ASN A   532                                                      
REMARK 465     ALA A   533                                                      
REMARK 465      DG C    12                                                      
REMARK 465      DT C    13                                                      
REMARK 465      DA C    14                                                      
REMARK 465      DT C    15                                                      
REMARK 465      DA D     1                                                      
REMARK 465      DC D     2                                                      
REMARK 465     ALA P     1                                                      
REMARK 465     ARG P     2                                                      
REMARK 465     THR P     3                                                      
REMARK 465     LYS P     4                                                      
REMARK 465     GLN P     5                                                      
REMARK 465     THR P     6                                                      
REMARK 465     ALA P     7                                                      
REMARK 465     ARG P     8                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500     DG D   7   O3'    DA D   8   P      -0.083                       
REMARK 500     DA D   8   O3'    DG D   9   P      -0.077                       
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     DC C  10   C3' -  O3' -  P   ANGL. DEV. =  11.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A 190       57.94   -118.68                                   
REMARK 500    ALA A 214     -100.36     68.90                                   
REMARK 500    THR A 228     -158.52   -118.42                                   
REMARK 500    ARG A 241     -128.06     58.85                                   
REMARK 500    ASP A 335      106.65   -176.20                                   
REMARK 500    SER A 354       39.53     90.59                                   
REMARK 500    LYS A 455       28.38   -151.00                                   
REMARK 500    SER A 565      -48.35   -141.49                                   
REMARK 500    MET A 586       -2.17     73.66                                   
REMARK 500    ARG A 620       -1.92     50.99                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    THR P  11        23.5      L          L   OUTSIDE RANGE           
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 802  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 397   SG                                                     
REMARK 620 2 CYS A 383   SG  113.8                                              
REMARK 620 3 CYS A 429   SG  101.6 105.6                                        
REMARK 620 4 CYS A 425   SG  112.7 108.6 114.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 803  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 389   SG                                                     
REMARK 620 2 CYS A 425   SG  105.7                                              
REMARK 620 3 CYS A 435   SG  102.1 113.9                                        
REMARK 620 4 CYS A 431   SG  114.1 105.2 115.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 804  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 395   SG                                                     
REMARK 620 2 CYS A 383   SG  108.8                                              
REMARK 620 3 CYS A 389   SG  118.2  96.5                                        
REMARK 620 4 CYS A 385   SG  113.0 113.8 105.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 805  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 612   SG                                                     
REMARK 620 2 CYS A 619   SG  106.7                                              
REMARK 620 3 CYS A 614   SG  106.9 110.5                                        
REMARK 620 4 CYS A 554   SG  112.0 120.0  99.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 802                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 803                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 804                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 805                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN P OF HISTONE H3             
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4QEN   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH MCHH DNA AND SAH                     
REMARK 900 RELATED ID: 4QEP   RELATED DB: PDB                                   
DBREF  4QEO A   93   624  UNP    Q8GZB6   SUVH4_ARATH     93    624             
DBREF  4QEO P    1    15  UNP    Q92133   Q92133_XENLA     2     16             
DBREF  4QEO C    1    15  PDB    4QEO     4QEO             1     15             
DBREF  4QEO D    1    15  PDB    4QEO     4QEO             1     15             
SEQADV 4QEO SER A   92  UNP  Q8GZB6              EXPRESSION TAG                 
SEQRES   1 A  533  SER ASN GLY LYS ASP VAL ASN LEU GLU PRO HIS LEU LYS          
SEQRES   2 A  533  VAL THR LYS CYS LEU ARG LEU PHE ASN LYS GLN TYR LEU          
SEQRES   3 A  533  LEU CYS VAL GLN ALA LYS LEU SER ARG PRO ASP LEU LYS          
SEQRES   4 A  533  GLY VAL THR GLU MET ILE LYS ALA LYS ALA ILE LEU TYR          
SEQRES   5 A  533  PRO ARG LYS ILE ILE GLY ASP LEU PRO GLY ILE ASP VAL          
SEQRES   6 A  533  GLY HIS ARG PHE PHE SER ARG ALA GLU MET CYS ALA VAL          
SEQRES   7 A  533  GLY PHE HIS ASN HIS TRP LEU ASN GLY ILE ASP TYR MET          
SEQRES   8 A  533  SER MET GLU TYR GLU LYS GLU TYR SER ASN TYR LYS LEU          
SEQRES   9 A  533  PRO LEU ALA VAL SER ILE VAL MET SER GLY GLN TYR GLU          
SEQRES  10 A  533  ASP ASP LEU ASP ASN ALA ASP THR VAL THR TYR THR GLY          
SEQRES  11 A  533  GLN GLY GLY HIS ASN LEU THR GLY ASN LYS ARG GLN ILE          
SEQRES  12 A  533  LYS ASP GLN LEU LEU GLU ARG GLY ASN LEU ALA LEU LYS          
SEQRES  13 A  533  HIS CYS CYS GLU TYR ASN VAL PRO VAL ARG VAL THR ARG          
SEQRES  14 A  533  GLY HIS ASN CYS LYS SER SER TYR THR LYS ARG VAL TYR          
SEQRES  15 A  533  THR TYR ASP GLY LEU TYR LYS VAL GLU LYS PHE TRP ALA          
SEQRES  16 A  533  GLN LYS GLY VAL SER GLY PHE THR VAL TYR LYS TYR ARG          
SEQRES  17 A  533  LEU LYS ARG LEU GLU GLY GLN PRO GLU LEU THR THR ASP          
SEQRES  18 A  533  GLN VAL ASN PHE VAL ALA GLY ARG ILE PRO THR SER THR          
SEQRES  19 A  533  SER GLU ILE GLU GLY LEU VAL CYS GLU ASP ILE SER GLY          
SEQRES  20 A  533  GLY LEU GLU PHE LYS GLY ILE PRO ALA THR ASN ARG VAL          
SEQRES  21 A  533  ASP ASP SER PRO VAL SER PRO THR SER GLY PHE THR TYR          
SEQRES  22 A  533  ILE LYS SER LEU ILE ILE GLU PRO ASN VAL ILE ILE PRO          
SEQRES  23 A  533  LYS SER SER THR GLY CYS ASN CYS ARG GLY SER CYS THR          
SEQRES  24 A  533  ASP SER LYS LYS CYS ALA CYS ALA LYS LEU ASN GLY GLY          
SEQRES  25 A  533  ASN PHE PRO TYR VAL ASP LEU ASN ASP GLY ARG LEU ILE          
SEQRES  26 A  533  GLU SER ARG ASP VAL VAL PHE GLU CYS GLY PRO HIS CYS          
SEQRES  27 A  533  GLY CYS GLY PRO LYS CYS VAL ASN ARG THR SER GLN LYS          
SEQRES  28 A  533  ARG LEU ARG PHE ASN LEU GLU VAL PHE ARG SER ALA LYS          
SEQRES  29 A  533  LYS GLY TRP ALA VAL ARG SER TRP GLU TYR ILE PRO ALA          
SEQRES  30 A  533  GLY SER PRO VAL CYS GLU TYR ILE GLY VAL VAL ARG ARG          
SEQRES  31 A  533  THR ALA ASP VAL ASP THR ILE SER ASP ASN GLU TYR ILE          
SEQRES  32 A  533  PHE GLU ILE ASP CYS GLN GLN THR MET GLN GLY LEU GLY          
SEQRES  33 A  533  GLY ARG GLN ARG ARG LEU ARG ASP VAL ALA VAL PRO MET          
SEQRES  34 A  533  ASN ASN GLY VAL SER GLN SER SER GLU ASP GLU ASN ALA          
SEQRES  35 A  533  PRO GLU PHE CYS ILE ASP ALA GLY SER THR GLY ASN PHE          
SEQRES  36 A  533  ALA ARG PHE ILE ASN HIS SER CYS GLU PRO ASN LEU PHE          
SEQRES  37 A  533  VAL GLN CYS VAL LEU SER SER HIS GLN ASP ILE ARG LEU          
SEQRES  38 A  533  ALA ARG VAL VAL LEU PHE ALA ALA ASP ASN ILE SER PRO          
SEQRES  39 A  533  MET GLN GLU LEU THR TYR ASP TYR GLY TYR ALA LEU ASP          
SEQRES  40 A  533  SER VAL HIS GLY PRO ASP GLY LYS VAL LYS GLN LEU ALA          
SEQRES  41 A  533  CYS TYR CYS GLY ALA LEU ASN CYS ARG LYS ARG LEU TYR          
SEQRES   1 C   15   DG  DG  DT  DA  DC  DT 5CM  DA  DT  DC  DA  DG  DT          
SEQRES   2 C   15   DA  DT                                                      
SEQRES   1 D   15   DA  DC  DT  DG  DA  DT  DG  DA  DG  DT  DA  DC  DC          
SEQRES   2 D   15   DA  DT                                                      
SEQRES   1 P   15  ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY GLY          
SEQRES   2 P   15  LYS ALA                                                      
MODRES 4QEO 5CM C    7   DC                                                     
HET    5CM  C   7      20                                                       
HET    SAH  A 801      26                                                       
HET     ZN  A 802       1                                                       
HET     ZN  A 803       1                                                       
HET     ZN  A 804       1                                                       
HET     ZN  A 805       1                                                       
HETNAM     5CM 5-METHYL-2'-DEOXY-CYTIDINE-5'-MONOPHOSPHATE                      
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
HETNAM      ZN ZINC ION                                                         
FORMUL   2  5CM    C10 H16 N3 O7 P                                              
FORMUL   5  SAH    C14 H20 N6 O5 S                                              
FORMUL   6   ZN    4(ZN 2+)                                                     
FORMUL  10  HOH   *285(H2 O)                                                    
HELIX    1   1 GLU A  100  ALA A  122  1                                  23    
HELIX    2   2 ARG A  126  ALA A  138  1                                  13    
HELIX    3   3 SER A  162  VAL A  169  1                                   8    
HELIX    4   4 SER A  183  GLU A  187  5                                   5    
HELIX    5   5 ARG A  241  ASN A  253  1                                  13    
HELIX    6   6 CYS A  395  ASN A  401  1                                   7    
HELIX    7   7 CYS A  435  LYS A  442  5                                   8    
HELIX    8   8 ALA A  483  VAL A  485  5                                   3    
HELIX    9   9 ASN A  545  ILE A  550  5                                   6    
HELIX   10  10 ASP A  569  ALA A  573  5                                   5    
SHEET    1   A 5 ARG A 159  PHE A 160  0                                        
SHEET    2   A 5 ARG A 271  LYS A 288 -1  O  TYR A 273   N  PHE A 160           
SHEET    3   A 5 VAL A 256  ASN A 263 -1  N  VAL A 258   O  ASP A 276           
SHEET    4   A 5 LEU A 197  MET A 203  1  N  MET A 203   O  THR A 259           
SHEET    5   A 5 ILE A 179  MET A 182 -1  N  ASP A 180   O  SER A 200           
SHEET    1   B 5 ARG A 159  PHE A 160  0                                        
SHEET    2   B 5 ARG A 271  LYS A 288 -1  O  TYR A 273   N  PHE A 160           
SHEET    3   B 5 THR A 294  ARG A 302 -1  O  ARG A 299   N  GLU A 282           
SHEET    4   B 5 THR A 216  THR A 220 -1  N  TYR A 219   O  TYR A 298           
SHEET    5   B 5 LEU A 211  ASN A 213 -1  N  LEU A 211   O  THR A 218           
SHEET    1   C 4 LEU A 331  CYS A 333  0                                        
SHEET    2   C 4 ALA A 347  THR A 348 -1  O  ALA A 347   N  VAL A 332           
SHEET    3   C 4 LEU A 448  ARG A 452  1  O  VAL A 450   N  THR A 348           
SHEET    4   C 4 TRP A 458  SER A 462 -1  O  ARG A 461   N  GLU A 449           
SHEET    1   D 2 THR A 363  TYR A 364  0                                        
SHEET    2   D 2 THR A 543  GLY A 544  1  O  GLY A 544   N  THR A 363           
SHEET    1   E 4 ILE A 369  ILE A 370  0                                        
SHEET    2   E 4 VAL A 478  ARG A 481  1  O  VAL A 479   N  ILE A 369           
SHEET    3   E 4 PHE A 536  ASP A 539 -1  O  ASP A 539   N  VAL A 478           
SHEET    4   E 4 ILE A 494  GLU A 496 -1  N  PHE A 495   O  ILE A 538           
SHEET    1   F 2 TYR A 407  VAL A 408  0                                        
SHEET    2   F 2 ARG A 414  LEU A 415 -1  O  ARG A 414   N  VAL A 408           
SHEET    1   G 4 VAL A 422  PHE A 423  0                                        
SHEET    2   G 4 LEU A 558  LEU A 564  1  O  LEU A 564   N  VAL A 422           
SHEET    3   G 4 ARG A 574  ALA A 579 -1  O  ARG A 574   N  VAL A 563           
SHEET    4   G 4 PRO A 471  GLU A 474 -1  N  VAL A 472   O  LEU A 577           
SHEET    1   H 2 ASN A 551  HIS A 552  0                                        
SHEET    2   H 2 THR A 590  TYR A 591  1  O  TYR A 591   N  ASN A 551           
SHEET    1   I 2 VAL A 600  HIS A 601  0                                        
SHEET    2   I 2 VAL A 607  LYS A 608 -1  O  LYS A 608   N  VAL A 600           
LINK         O3'  DT C   6                 P   5CM C   7     1555   1555  1.55  
LINK         O3' 5CM C   7                 P    DA C   8     1555   1555  1.54  
LINK         SG  CYS A 397                ZN    ZN A 802     1555   1555  2.14  
LINK         SG  CYS A 389                ZN    ZN A 803     1555   1555  2.17  
LINK         SG  CYS A 425                ZN    ZN A 803     1555   1555  2.22  
LINK         SG  CYS A 383                ZN    ZN A 802     1555   1555  2.28  
LINK         SG  CYS A 395                ZN    ZN A 804     1555   1555  2.30  
LINK         SG  CYS A 383                ZN    ZN A 804     1555   1555  2.35  
LINK         SG  CYS A 435                ZN    ZN A 803     1555   1555  2.38  
LINK         SG  CYS A 429                ZN    ZN A 802     1555   1555  2.38  
LINK         SG  CYS A 389                ZN    ZN A 804     1555   1555  2.38  
LINK         SG  CYS A 431                ZN    ZN A 803     1555   1555  2.40  
LINK         SG  CYS A 612                ZN    ZN A 805     1555   1555  2.40  
LINK         SG  CYS A 619                ZN    ZN A 805     1555   1555  2.40  
LINK         SG  CYS A 385                ZN    ZN A 804     1555   1555  2.40  
LINK         SG  CYS A 614                ZN    ZN A 805     1555   1555  2.46  
LINK         SG  CYS A 425                ZN    ZN A 802     1555   1555  2.48  
LINK         SG  CYS A 554                ZN    ZN A 805     1555   1555  2.51  
CISPEP   1 LEU A  195    PRO A  196          0         0.88                     
CISPEP   2 GLY A  602    PRO A  603          0       -11.27                     
SITE     1 AC1 14 LYS A 456  GLY A 457  TRP A 458  GLU A 492                    
SITE     2 AC1 14 TYR A 493  ARG A 548  ASN A 551  HIS A 552                    
SITE     3 AC1 14 TYR A 593  ALA A 611  CYS A 612  TYR A 613                    
SITE     4 AC1 14 CYS A 614  LYS P   9                                          
SITE     1 AC2  4 CYS A 383  CYS A 397  CYS A 425  CYS A 429                    
SITE     1 AC3  4 CYS A 389  CYS A 425  CYS A 431  CYS A 435                    
SITE     1 AC4  4 CYS A 383  CYS A 385  CYS A 389  CYS A 395                    
SITE     1 AC5  4 CYS A 554  CYS A 612  CYS A 614  CYS A 619                    
SITE     1 AC6 13 SER A 418  ARG A 419  ASP A 420  TYR A 475                    
SITE     2 AC6 13 GLU A 492  ILE A 494  PHE A 495  GLU A 496                    
SITE     3 AC6 13 TYR A 591  TYR A 593  GLY A 594  TYR A 595                    
SITE     4 AC6 13 SAH A 801                                                     
CRYST1   55.460   96.765  122.411  90.00  90.00  90.00 P 21 21 21    4          
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      0.018031  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010334  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008169        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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