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Database: PDB
Entry: 4QEN
LinkDB: 4QEN
Original site: 4QEN 
HEADER    TRANSCRIPTION/DNA                       17-MAY-14   4QEN              
TITLE     CRYSTAL STRUCTURE OF KRYPTONITE IN COMPLEX WITH MCHH DNA 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'-D(*GP*GP*TP*AP*CP*TP*(5CM)                         
COMPND  13 P*AP*TP*CP*AP*GP*TP*AP*T)-3');                                       
COMPND  14 CHAIN: C;                                                            
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MOL_ID: 3;                                                           
COMPND  17 MOLECULE: DNA (5'-D(*AP*CP*TP*GP*AP*TP*GP*AP*GP*TP*AP*CP*CP*AP*T)-   
COMPND  18 3');                                                                 
COMPND  19 CHAIN: D;                                                            
COMPND  20 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                                                       
KEYWDS    SRA, SET, HISTONE METHYLATION, METHYLATED DNA, TRANSCRIPTION-DNA      
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.DU,S.LI,D.J.PATEL                                                   
REVDAT   2   20-AUG-14 4QEN    1       JRNL                                     
REVDAT   1   30-JUL-14 4QEN    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) : 40.68                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 44884                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.178                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.211                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2261                            
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 40.6919 -  6.2137    0.99     2691   125  0.2019 0.2202        
REMARK   3     2  6.2137 -  4.9348    1.00     2693   148  0.1713 0.2005        
REMARK   3     3  4.9348 -  4.3118    1.00     2683   139  0.1424 0.1764        
REMARK   3     4  4.3118 -  3.9179    1.00     2689   136  0.1479 0.1761        
REMARK   3     5  3.9179 -  3.6373    1.00     2680   157  0.1584 0.1902        
REMARK   3     6  3.6373 -  3.4229    1.00     2719   136  0.1643 0.1794        
REMARK   3     7  3.4229 -  3.2516    1.00     2727   126  0.1653 0.2111        
REMARK   3     8  3.2516 -  3.1101    1.00     2710   148  0.1793 0.2087        
REMARK   3     9  3.1101 -  2.9904    1.00     2656   164  0.1776 0.2138        
REMARK   3    10  2.9904 -  2.8872    1.00     2694   147  0.1843 0.2246        
REMARK   3    11  2.8872 -  2.7970    1.00     2691   141  0.1836 0.2422        
REMARK   3    12  2.7970 -  2.7171    1.00     2715   126  0.1857 0.1707        
REMARK   3    13  2.7171 -  2.6455    1.00     2735   148  0.1832 0.2501        
REMARK   3    14  2.6455 -  2.5810    1.00     2669   130  0.1858 0.2448        
REMARK   3    15  2.5810 -  2.5223    1.00     2738   139  0.1807 0.2246        
REMARK   3    16  2.5223 -  2.4687    1.00     2681   172  0.1797 0.2305        
REMARK   3    17  2.4687 -  2.4193    1.00     2735   131  0.1804 0.2274        
REMARK   3    18  2.4193 -  2.3736    1.00     2626   151  0.1843 0.2115        
REMARK   3    19  2.3736 -  2.3313    1.00     2721   156  0.1866 0.2023        
REMARK   3    20  2.3313 -  2.2917    1.00     2703   129  0.1827 0.2586        
REMARK   3    21  2.2917 -  2.2548    1.00     2701   167  0.1853 0.2233        
REMARK   3    22  2.2548 -  2.2201    1.00     2691   125  0.1912 0.2691        
REMARK   3    23  2.2201 -  2.1874    1.00     2688   120  0.1901 0.2059        
REMARK   3    24  2.1874 -  2.1566    1.00     2706   136  0.1887 0.2639        
REMARK   3    25  2.1566 -  2.1275    1.00     2743   134  0.1910 0.2258        
REMARK   3    26  2.1275 -  2.0999    1.00     2661   146  0.2058 0.2669        
REMARK   3    27  2.0999 -  2.0736    1.00     2651   190  0.2161 0.2835        
REMARK   3    28  2.0736 -  2.0486    1.00     2756   131  0.2182 0.2408        
REMARK   3    29  2.0486 -  2.0248    1.00     2687   154  0.2343 0.2782        
REMARK   3    30  2.0248 -  2.0021    0.99     2633   136  0.2458 0.2571        
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) : 21.100           
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      :  0.008           4377                                  
REMARK   3   ANGLE     :  1.410           6011                                  
REMARK   3   CHIRALITY :  0.099            654                                  
REMARK   3   PLANARITY :  0.005            689                                  
REMARK   3   DIHEDRAL  : 18.268           1666                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resid 99 through 186 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -16.3681  22.0365  25.1445              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2612 T22:   0.2665                                     
REMARK   3      T33:   0.1976 T12:   0.0486                                     
REMARK   3      T13:  -0.0313 T23:  -0.0014                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2101 L22:   1.2382                                     
REMARK   3      L33:   3.2760 L12:  -0.2056                                     
REMARK   3      L13:   0.5473 L23:  -1.1205                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1616 S12:  -0.2655 S13:   0.0796                       
REMARK   3      S21:   0.1465 S22:   0.1278 S23:   0.0113                       
REMARK   3      S31:  -0.3502 S32:  -0.1647 S33:   0.1200                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resid 187 through 302 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -18.9878  17.1507   6.2399              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2182 T22:   0.1658                                     
REMARK   3      T33:   0.1885 T12:  -0.0063                                     
REMARK   3      T13:   0.0109 T23:   0.0016                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6513 L22:   1.4138                                     
REMARK   3      L33:   2.7042 L12:  -0.3481                                     
REMARK   3      L13:   0.4883 L23:  -0.2424                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0356 S12:   0.0256 S13:  -0.0740                       
REMARK   3      S21:   0.0434 S22:   0.0091 S23:   0.0845                       
REMARK   3      S31:   0.0818 S32:  -0.0809 S33:  -0.0130                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resid 303 through 368 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   5.6574  -2.4157  30.8512              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4273 T22:   0.4358                                     
REMARK   3      T33:   0.4003 T12:   0.1008                                     
REMARK   3      T13:   0.0483 T23:   0.0663                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1182 L22:   1.5390                                     
REMARK   3      L33:   2.1880 L12:  -0.2972                                     
REMARK   3      L13:   0.5644 L23:  -1.3475                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0699 S12:   0.1764 S13:  -0.0702                       
REMARK   3      S21:  -0.5023 S22:  -0.2533 S23:  -0.3239                       
REMARK   3      S31:   0.8714 S32:   0.5704 S33:   0.1637                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'A' and (resid 369 through 624 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.1408   7.8797  46.1133              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2220 T22:   0.1950                                     
REMARK   3      T33:   0.2750 T12:  -0.0103                                     
REMARK   3      T13:  -0.0467 T23:   0.0595                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3855 L22:   2.0041                                     
REMARK   3      L33:   2.6710 L12:  -0.4719                                     
REMARK   3      L13:   0.1417 L23:  -1.1081                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0405 S12:   0.0549 S13:   0.1639                       
REMARK   3      S21:   0.1602 S22:  -0.0662 S23:  -0.2918                       
REMARK   3      S31:  -0.1749 S32:   0.1312 S33:   0.0966                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'C' and (resid 1 through 11 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -31.5501  18.3260  18.3796              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2756 T22:   0.3887                                     
REMARK   3      T33:   0.3344 T12:  -0.0232                                     
REMARK   3      T13:   0.0244 T23:   0.0458                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5866 L22:   2.3607                                     
REMARK   3      L33:   4.2315 L12:  -0.7774                                     
REMARK   3      L13:   0.1728 L23:   0.2686                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0282 S12:  -0.7427 S13:  -0.3919                       
REMARK   3      S21:   0.2014 S22:   0.1601 S23:   0.7068                       
REMARK   3      S31:   0.0897 S32:  -0.7429 S33:  -0.2566                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'D' and (resid 3 through 7 )                     
REMARK   3    ORIGIN FOR THE GROUP (A): -34.5878   8.0115  21.1245              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4526 T22:   0.6825                                     
REMARK   3      T33:   0.6117 T12:  -0.1759                                     
REMARK   3      T13:   0.0438 T23:  -0.0181                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9070 L22:   6.7484                                     
REMARK   3      L33:   2.6129 L12:  -3.8835                                     
REMARK   3      L13:  -0.9737 L23:  -1.4179                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2483 S12:   0.3520 S13:  -1.1088                       
REMARK   3      S21:  -0.4905 S22:  -0.2328 S23:   0.7623                       
REMARK   3      S31:   0.8544 S32:  -1.0813 S33:  -0.2126                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain 'D' and (resid 8 through 15 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -33.3561  30.3679  15.8184              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4572 T22:   0.4881                                     
REMARK   3      T33:   0.4222 T12:   0.1479                                     
REMARK   3      T13:  -0.1110 T23:   0.0374                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7158 L22:   1.9118                                     
REMARK   3      L33:   1.7759 L12:   0.9028                                     
REMARK   3      L13:  -0.7164 L23:  -0.0640                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4453 S12:   0.1005 S13:   0.3290                       
REMARK   3      S21:   0.2301 S22:   0.1972 S23:   0.6676                       
REMARK   3      S31:  -0.8043 S32:  -0.7334 S33:  -0.0248                       
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 4QEN 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 RCSB085958.                                      
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) : 1.2830                             
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   : 44950                              
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                : 13.600                             
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : 0.06700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 48.1000                            
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       : 12.70                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.61000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.61000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.14                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG200, 5% PEG3000, AND 0.1 M MES,   
REMARK 280  PH 6.0, 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       27.19750            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       61.29050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       49.00450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       61.29050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.19750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       49.00450            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4160 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25410 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A    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 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     DC D  12   O3'    DC D  12   C3'    -0.039                       
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     DA C   8   O4' -  C1' -  N9  ANGL. DEV. =  -5.2 DEGREES          
REMARK 500     DA C  11   O4' -  C1' -  N9  ANGL. DEV. =   2.2 DEGREES          
REMARK 500     DC D  12   O4' -  C1' -  N1  ANGL. DEV. =   3.9 DEGREES          
REMARK 500     DT D  15   O4' -  C1' -  N1  ANGL. DEV. =   2.1 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       61.13   -117.51                                   
REMARK 500    ALA A 214      -96.76     65.94                                   
REMARK 500    ARG A 241     -128.52     51.37                                   
REMARK 500    ASP A 353       62.08   -114.64                                   
REMARK 500    SER A 565      -51.69   -144.60                                   
REMARK 500    MET A 586       -0.46     80.20                                   
REMARK 500    ASP A 604     -120.02   -165.54                                   
REMARK 500    ASN A 618       40.08    -99.43                                   
REMARK 500    ARG A 620      -22.36     63.45                                   
REMARK 500    LYS A 621        2.30     82.00                                   
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    5CM C   7       -13.9      D          D   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1227        DISTANCE =  5.22 ANGSTROMS                       
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  115.5                                              
REMARK 620 3 CYS A 425   SG  109.8 114.1                                        
REMARK 620 4 CYS A 429   SG   99.4 104.3 112.7                                  
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 389   SG                                                     
REMARK 620 2 CYS A 395   SG  120.2                                              
REMARK 620 3 CYS A 385   SG  103.0 109.9                                        
REMARK 620 4 CYS A 383   SG   98.1 114.4 110.1                                  
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 431   SG                                                     
REMARK 620 2 CYS A 425   SG  107.7                                              
REMARK 620 3 CYS A 435   SG  116.0 116.3                                        
REMARK 620 4 CYS A 389   SG  109.9 103.3 102.6                                  
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 614   SG  107.5                                              
REMARK 620 3 CYS A 619   SG  107.3 109.8                                        
REMARK 620 4 CYS A 554   SG  109.0 107.1 115.9                                  
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 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4QEO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4QEP   RELATED DB: PDB                                   
DBREF  4QEN A   93   624  UNP    Q8GZB6   SUVH4_ARATH     93    624             
DBREF  4QEN C    1    15  PDB    4QEN     4QEN             1     15             
DBREF  4QEN D    1    15  PDB    4QEN     4QEN             1     15             
SEQADV 4QEN 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                                                      
MODRES 4QEN 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   4  SAH    C14 H20 N6 O5 S                                              
FORMUL   5   ZN    4(ZN 2+)                                                     
FORMUL   9  HOH   *383(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  GLY A  170  1                                   9    
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  HIS A 262   O  VAL A 272           
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  VAL A 295   N  GLN A 287           
SHEET    4   B 5 THR A 216  THR A 220 -1  N  VAL A 217   O  LEU A 300           
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           
LINK         O3'  DT C   6                 P   5CM C   7     1555   1555  1.61  
LINK         O3' 5CM C   7                 P    DA C   8     1555   1555  1.61  
LINK         SG  CYS A 397                ZN    ZN A 802     1555   1555  2.25  
LINK         SG  CYS A 389                ZN    ZN A 804     1555   1555  2.30  
LINK         SG  CYS A 431                ZN    ZN A 803     1555   1555  2.31  
LINK         SG  CYS A 612                ZN    ZN A 805     1555   1555  2.31  
LINK         SG  CYS A 383                ZN    ZN A 802     1555   1555  2.33  
LINK         SG  CYS A 425                ZN    ZN A 803     1555   1555  2.35  
LINK         SG  CYS A 614                ZN    ZN A 805     1555   1555  2.36  
LINK         SG  CYS A 619                ZN    ZN A 805     1555   1555  2.36  
LINK         SG  CYS A 395                ZN    ZN A 804     1555   1555  2.39  
LINK         SG  CYS A 385                ZN    ZN A 804     1555   1555  2.40  
LINK         SG  CYS A 435                ZN    ZN A 803     1555   1555  2.40  
LINK         SG  CYS A 383                ZN    ZN A 804     1555   1555  2.41  
LINK         SG  CYS A 425                ZN    ZN A 802     1555   1555  2.42  
LINK         SG  CYS A 554                ZN    ZN A 805     1555   1555  2.43  
LINK         SG  CYS A 389                ZN    ZN A 803     1555   1555  2.43  
LINK         SG  CYS A 429                ZN    ZN A 802     1555   1555  2.45  
CISPEP   1 LEU A  195    PRO A  196          0         1.82                     
SITE     1 AC1 15 LYS A 456  GLY A 457  TRP A 458  GLU A 492                    
SITE     2 AC1 15 TYR A 493  ARG A 548  ASN A 551  HIS A 552                    
SITE     3 AC1 15 TYR A 593  ALA A 611  CYS A 612  TYR A 613                    
SITE     4 AC1 15 LEU A 623  HOH A 993  HOH A1174                               
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                    
CRYST1   54.395   98.009  122.581  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      0.018384  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010203  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008158        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system