GenomeNet

Database: PDB
Entry: 6A5N
LinkDB: 6A5N
Original site: 6A5N 
HEADER    GENE REGULATION/DNA                     24-JUN-18   6A5N              
TITLE     CRYSTAL STRUCTURE OF ARABIDOPSIS THALIANA SUVH6 IN COMPLEX WITH       
TITLE    2 METHYLATED DNA                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-9 SPECIFIC   
COMPND   3 SUVH6;                                                               
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: HISTONE H3-K9 METHYLTRANSFERASE 6,H3-K9-HMTASE 6,PROTEIN SET
COMPND   6 DOMAIN GROUP 23,SUPPRESSOR OF VARIEGATION 3-9 HOMOLOG PROTEIN 6,     
COMPND   7 SU(VAR)3-9 HOMOLOG PROTEIN 6;                                        
COMPND   8 EC: 2.1.1.43;                                                        
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: YES;                                                       
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: DNA (5'-D(*GP*AP*GP*TP*AP*CP*TP*(5CM)P*AP*GP*CP*AP*GP*T)-  
COMPND  13 3');                                                                 
COMPND  14 CHAIN: C;                                                            
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 OTHER_DETAILS: METHYLATED DNA;                                       
COMPND  17 MOL_ID: 3;                                                           
COMPND  18 MOLECULE: DNA (5'-D(*CP*AP*CP*TP*GP*CP*TP*GP*AP*GP*TP*AP*CP*T)-3');  
COMPND  19 CHAIN: D;                                                            
COMPND  20 ENGINEERED: YES;                                                     
COMPND  21 OTHER_DETAILS: COMPLEMENTARY DNA                                     
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;                           
SOURCE   3 ORGANISM_COMMON: MOUSE-EAR CRESS;                                    
SOURCE   4 ORGANISM_TAXID: 3702;                                                
SOURCE   5 GENE: SUVH6, SDG23, SET23, AT2G22740, T9I22.18;                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: 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 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  14 ORGANISM_TAXID: 32630;                                               
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 SYNTHETIC: YES;                                                      
SOURCE  17 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  18 ORGANISM_TAXID: 32630                                                
KEYWDS    SRA, SET, HISTONE METHYLTRANSFERASE, DNA METHYLATION, GENE            
KEYWDS   2 REGULATION, GENE REGULATION-DNA COMPLEX                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.LI,J.DU                                                             
REVDAT   3   26-SEP-18 6A5N    1       JRNL                                     
REVDAT   2   19-SEP-18 6A5N    1       JRNL                                     
REVDAT   1   29-AUG-18 6A5N    0                                                
JRNL        AUTH   X.LI,C.J.HARRIS,Z.ZHONG,W.CHEN,R.LIU,B.JIA,Z.WANG,S.LI,      
JRNL        AUTH 2 S.E.JACOBSEN,J.DU                                            
JRNL        TITL   MECHANISTIC INSIGHTS INTO PLANT SUVH FAMILY H3K9             
JRNL        TITL 2 METHYLTRANSFERASES AND THEIR BINDING TO CONTEXT-BIASED       
JRNL        TITL 3 NON-CG DNA METHYLATION.                                      
JRNL        REF    PROC. NATL. ACAD. SCI.        V. 115 E8793 2018              
JRNL        REF  2 U.S.A.                                                       
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   30150382                                                     
JRNL        DOI    10.1073/PNAS.1809841115                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.59                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 24873                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.233                           
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.279                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.090                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1267                            
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 33.5949 -  4.9876    0.96     2735   139  0.1873 0.2277        
REMARK   3     2  4.9876 -  3.9608    0.97     2632   166  0.1811 0.2270        
REMARK   3     3  3.9608 -  3.4607    0.90     2434   126  0.2346 0.2946        
REMARK   3     4  3.4607 -  3.1445    0.99     2674   160  0.2532 0.3078        
REMARK   3     5  3.1445 -  2.9193    1.00     2641   142  0.2729 0.3158        
REMARK   3     6  2.9193 -  2.7473    1.00     2640   152  0.2864 0.3504        
REMARK   3     7  2.7473 -  2.6097    0.96     2602   129  0.3838 0.4755        
REMARK   3     8  2.6097 -  2.4962    1.00     2633   136  0.3178 0.3879        
REMARK   3     9  2.4962 -  2.4001    0.99     2615   117  0.3129 0.3753        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.330            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.830           
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      :  0.009           4615                                  
REMARK   3   ANGLE     :  1.314           6331                                  
REMARK   3   CHIRALITY :  0.077            678                                  
REMARK   3   PLANARITY :  0.005            737                                  
REMARK   3   DIHEDRAL  : 22.034           1784                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 266 THROUGH 469 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -29.9449  -1.4330 104.8948              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3304 T22:   0.3812                                     
REMARK   3      T33:   0.3914 T12:  -0.0174                                     
REMARK   3      T13:   0.0388 T23:   0.0990                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0180 L22:   1.4121                                     
REMARK   3      L33:   1.2209 L12:  -2.2509                                     
REMARK   3      L13:   0.0408 L23:   0.4829                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0460 S12:  -0.1152 S13:  -0.4590                       
REMARK   3      S21:   0.1012 S22:   0.0635 S23:   0.1634                       
REMARK   3      S31:   0.1304 S32:  -0.1417 S33:  -0.0006                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 470 THROUGH 518 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -30.7228  -6.8370 124.8953              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7108 T22:   0.5914                                     
REMARK   3      T33:   0.6337 T12:   0.1376                                     
REMARK   3      T13:   0.0344 T23:   0.1198                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1903 L22:   0.8296                                     
REMARK   3      L33:   2.8406 L12:  -2.2419                                     
REMARK   3      L13:  -3.6521 L23:   1.5910                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6438 S12:  -0.6115 S13:  -0.5331                       
REMARK   3      S21:   0.6726 S22:   0.2150 S23:   0.1852                       
REMARK   3      S31:   0.7806 S32:   0.0881 S33:   0.4792                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 519 THROUGH 780 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -51.2210  14.4849 123.4487              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3363 T22:   0.6223                                     
REMARK   3      T33:   0.5026 T12:   0.0419                                     
REMARK   3      T13:   0.0645 T23:  -0.0091                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6902 L22:   1.9706                                     
REMARK   3      L33:   1.7011 L12:  -0.5545                                     
REMARK   3      L13:   0.0865 L23:  -0.3234                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1245 S12:  -0.3849 S13:   0.2533                       
REMARK   3      S21:   0.1637 S22:   0.0488 S23:   0.1655                       
REMARK   3      S31:  -0.1628 S32:  -0.0577 S33:   0.0681                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 2 THROUGH 14 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -36.3662  -9.4074  93.1175              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5315 T22:   0.4251                                     
REMARK   3      T33:   0.7180 T12:   0.0360                                     
REMARK   3      T13:  -0.0050 T23:   0.0930                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.6676 L22:   5.8746                                     
REMARK   3      L33:   5.8863 L12:   0.8839                                     
REMARK   3      L13:  -0.9363 L23:   0.0275                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1088 S12:   0.9968 S13:   0.2007                       
REMARK   3      S21:  -0.7590 S22:  -0.0566 S23:   0.3916                       
REMARK   3      S31:   0.4391 S32:  -1.0897 S33:  -0.0987                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 2 THROUGH 8 )                     
REMARK   3    ORIGIN FOR THE GROUP (A): -41.7594 -16.6493  97.4900              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3401 T22:   0.7509                                     
REMARK   3      T33:   0.9317 T12:  -0.0012                                     
REMARK   3      T13:   0.2750 T23:   0.0370                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.8885 L22:   4.6020                                     
REMARK   3      L33:   4.4422 L12:   5.4794                                     
REMARK   3      L13:  -5.3934 L23:  -4.4715                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6721 S12:   0.2138 S13:  -2.1893                       
REMARK   3      S21:  -1.9563 S22:  -0.1656 S23:  -0.5157                       
REMARK   3      S31:   1.8001 S32:   1.7004 S33:   0.9358                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 9 THROUGH 14 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -26.6718  -1.4973  89.0387              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0677 T22:   1.0834                                     
REMARK   3      T33:   0.7921 T12:   0.1615                                     
REMARK   3      T13:   0.3115 T23:   0.1680                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5970 L22:   9.3564                                     
REMARK   3      L33:   3.8933 L12:   5.4843                                     
REMARK   3      L13:   2.4726 L23:   0.3619                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1545 S12:   1.1694 S13:  -0.4136                       
REMARK   3      S21:   1.1864 S22:   0.7337 S23:   0.2324                       
REMARK   3      S31:   0.1303 S32:   0.7509 S33:  -0.4365                       
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 6A5N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-JUL-18.                  
REMARK 100 THE DEPOSITION ID IS D_1300008194.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-DEC-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL19U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25062                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : 0.08100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 32.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.71500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.400                              
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: 6A5K                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% ETHANOL, 10% W/V GLYCEROL, VAPOR     
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 277K                           
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       37.06850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.92250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.72150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       53.92250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.06850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.72150            
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: 4050 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27680 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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   264                                                      
REMARK 465     SER A   265                                                      
REMARK 465     VAL A   399                                                      
REMARK 465     MET A   400                                                      
REMARK 465     GLN A   401                                                      
REMARK 465     VAL A   402                                                      
REMARK 465     LYS A   403                                                      
REMARK 465     LYS A   404                                                      
REMARK 465     LYS A   405                                                      
REMARK 465     GLY A   406                                                      
REMARK 465     GLU A   407                                                      
REMARK 465     GLU A   408                                                      
REMARK 465     LEU A   409                                                      
REMARK 465     LYS A   410                                                      
REMARK 465     GLU A   411                                                      
REMARK 465     GLY A   781                                                      
REMARK 465     ALA A   782                                                      
REMARK 465     ALA A   783                                                      
REMARK 465     VAL A   784                                                      
REMARK 465     CYS A   785                                                      
REMARK 465     ARG A   786                                                      
REMARK 465     ARG A   787                                                      
REMARK 465     ARG A   788                                                      
REMARK 465     LEU A   789                                                      
REMARK 465     TYR A   790                                                      
REMARK 465      DG C     1                                                      
REMARK 465      DC D     1                                                      
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   2   O4' -  C1' -  N9  ANGL. DEV. =   2.2 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    THR A 419     -114.00     39.97                                   
REMARK 500    ASP A 446       60.57     37.65                                   
REMARK 500    LYS A 500      -51.83     70.26                                   
REMARK 500    VAL A 609      -57.71   -131.22                                   
REMARK 500    ILE A 642      -72.71    -89.63                                   
REMARK 500    ARG A 658      -11.39     87.35                                   
REMARK 500    ASP A 662      -48.77     72.83                                   
REMARK 500    ASN A 711     -154.75   -104.80                                   
REMARK 500    ASP A 732      -44.87     71.53                                   
REMARK 500    ASP A 735      109.79    -55.02                                   
REMARK 500    LEU A 752      -12.72     72.51                                   
REMARK 500    TYR A 761      165.11     83.19                                   
REMARK 500    LEU A 763      -10.10     80.75                                   
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 803  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 553   SG                                                     
REMARK 620 2 CYS A 555   SG  117.5                                              
REMARK 620 3 CYS A 559   SG   87.3 104.2                                        
REMARK 620 4 CYS A 567   SG  110.6 122.1 108.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 801  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 553   SG                                                     
REMARK 620 2 CYS A 569   SG  127.1                                              
REMARK 620 3 CYS A 595   SG   95.6 107.6                                        
REMARK 620 4 CYS A 599   SG  111.2 103.8 110.9                                  
REMARK 620 N                    1     2     3                                   
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 559   SG                                                     
REMARK 620 2 CYS A 595   SG  113.0                                              
REMARK 620 3 CYS A 601   SG  123.0 102.4                                        
REMARK 620 4 CYS A 605   SG  100.8 108.5 108.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 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                  
DBREF  6A5N A  264   790  UNP    Q8VZ17   SUVH6_ARATH    264    790             
DBREF  6A5N C    1    14  PDB    6A5N     6A5N             1     14             
DBREF  6A5N D    1    14  PDB    6A5N     6A5N             1     14             
SEQADV 6A5N LEU A  777  UNP  Q8VZ17    PRO   777 ENGINEERED MUTATION            
SEQRES   1 A  527  SER SER GLY ASP SER SER ARG ASN LYS VAL LYS GLU THR          
SEQRES   2 A  527  LEU ARG LEU PHE HIS GLY VAL CYS ARG LYS ILE LEU GLN          
SEQRES   3 A  527  GLU ASP GLU ALA LYS PRO GLU ASP GLN ARG ARG LYS GLY          
SEQRES   4 A  527  LYS GLY LEU ARG ILE ASP PHE GLU ALA SER THR ILE LEU          
SEQRES   5 A  527  LYS ARG ASN GLY LYS PHE LEU ASN SER GLY VAL HIS ILE          
SEQRES   6 A  527  LEU GLY GLU VAL PRO GLY VAL GLU VAL GLY ASP GLU PHE          
SEQRES   7 A  527  GLN TYR ARG MET GLU LEU ASN ILE LEU GLY ILE HIS LYS          
SEQRES   8 A  527  PRO SER GLN ALA GLY ILE ASP TYR MET LYS TYR GLY LYS          
SEQRES   9 A  527  ALA LYS VAL ALA THR SER ILE VAL ALA SER GLY GLY TYR          
SEQRES  10 A  527  ASP ASP HIS LEU ASP ASN SER ASP VAL LEU THR TYR THR          
SEQRES  11 A  527  GLY GLN GLY GLY ASN VAL MET GLN VAL LYS LYS LYS GLY          
SEQRES  12 A  527  GLU GLU LEU LYS GLU PRO GLU ASP GLN LYS LEU ILE THR          
SEQRES  13 A  527  GLY ASN LEU ALA LEU ALA THR SER ILE GLU LYS GLN THR          
SEQRES  14 A  527  PRO VAL ARG VAL ILE ARG GLY LYS HIS LYS SER THR HIS          
SEQRES  15 A  527  ASP LYS SER LYS GLY GLY ASN TYR VAL TYR ASP GLY LEU          
SEQRES  16 A  527  TYR LEU VAL GLU LYS TYR TRP GLN GLN VAL GLY SER HIS          
SEQRES  17 A  527  GLY MET ASN VAL PHE LYS PHE GLN LEU ARG ARG ILE PRO          
SEQRES  18 A  527  GLY GLN PRO GLU LEU SER TRP VAL GLU VAL LYS LYS SER          
SEQRES  19 A  527  LYS SER LYS TYR ARG GLU GLY LEU CYS LYS LEU ASP ILE          
SEQRES  20 A  527  SER GLU GLY LYS GLU GLN SER PRO ILE SER ALA VAL ASN          
SEQRES  21 A  527  GLU ILE ASP ASP GLU LYS PRO PRO LEU PHE THR TYR THR          
SEQRES  22 A  527  VAL LYS LEU ILE TYR PRO ASP TRP CYS ARG PRO VAL PRO          
SEQRES  23 A  527  PRO LYS SER CYS CYS CYS THR THR ARG CYS THR GLU ALA          
SEQRES  24 A  527  GLU ALA ARG VAL CYS ALA CYS VAL GLU LYS ASN GLY GLY          
SEQRES  25 A  527  GLU ILE PRO TYR ASN PHE ASP GLY ALA ILE VAL GLY ALA          
SEQRES  26 A  527  LYS PRO THR ILE TYR GLU CYS GLY PRO LEU CYS LYS CYS          
SEQRES  27 A  527  PRO SER SER CYS TYR LEU ARG VAL THR GLN HIS GLY ILE          
SEQRES  28 A  527  LYS LEU PRO LEU GLU ILE PHE LYS THR LYS SER ARG GLY          
SEQRES  29 A  527  TRP GLY VAL ARG CYS LEU LYS SER ILE PRO ILE GLY SER          
SEQRES  30 A  527  PHE ILE CYS GLU TYR VAL GLY GLU LEU LEU GLU ASP SER          
SEQRES  31 A  527  GLU ALA GLU ARG ARG ILE GLY ASN ASP GLU TYR LEU PHE          
SEQRES  32 A  527  ASP ILE GLY ASN ARG TYR ASP ASN SER LEU ALA GLN GLY          
SEQRES  33 A  527  MET SER GLU LEU MET LEU GLY THR GLN ALA GLY ARG SER          
SEQRES  34 A  527  MET ALA GLU GLY ASP GLU SER SER GLY PHE THR ILE ASP          
SEQRES  35 A  527  ALA ALA SER LYS GLY ASN VAL GLY ARG PHE ILE ASN HIS          
SEQRES  36 A  527  SER CYS SER PRO ASN LEU TYR ALA GLN ASN VAL LEU TYR          
SEQRES  37 A  527  ASP HIS GLU ASP SER ARG ILE PRO HIS VAL MET PHE PHE          
SEQRES  38 A  527  ALA GLN ASP ASN ILE PRO PRO LEU GLN GLU LEU CYS TYR          
SEQRES  39 A  527  ASP TYR ASN TYR ALA LEU ASP GLN VAL ARG ASP SER LYS          
SEQRES  40 A  527  GLY ASN ILE LYS GLN LYS LEU CYS PHE CYS GLY ALA ALA          
SEQRES  41 A  527  VAL CYS ARG ARG ARG LEU TYR                                  
SEQRES   1 C   14   DG  DA  DG  DT  DA  DC  DT 5CM  DA  DG  DC  DA  DG          
SEQRES   2 C   14   DT                                                          
SEQRES   1 D   14   DC  DA  DC  DT  DG  DC  DT  DG  DA  DG  DT  DA  DC          
SEQRES   2 D   14   DT                                                          
HET    5CM  C   8      20                                                       
HET     ZN  A 801       1                                                       
HET     ZN  A 802       1                                                       
HET     ZN  A 803       1                                                       
HETNAM     5CM 5-METHYL-2'-DEOXY-CYTIDINE-5'-MONOPHOSPHATE                      
HETNAM      ZN ZINC ION                                                         
FORMUL   2  5CM    C10 H16 N3 O7 P                                              
FORMUL   4   ZN    3(ZN 2+)                                                     
FORMUL   7  HOH   *40(H2 O)                                                     
HELIX    1 AA1 GLY A  266  LYS A  294  1                                  29    
HELIX    2 AA2 PRO A  295  ARG A  299  5                                   5    
HELIX    3 AA3 ARG A  306  ASN A  318  1                                  13    
HELIX    4 AA4 TYR A  343  GLY A  351  1                                   9    
HELIX    5 AA5 ILE A  418  GLN A  431  1                                  14    
HELIX    6 AA6 SER A  490  SER A  499  1                                  10    
HELIX    7 AA7 CYS A  567  ASN A  573  1                                   7    
HELIX    8 AA8 ASN A  674  LEU A  685  1                                  12    
HELIX    9 AA9 ASN A  711  ILE A  716  5                                   6    
SHEET    1 AA1 5 GLU A 340  PHE A 341  0                                        
SHEET    2 AA1 5 TYR A 453  VAL A 468 -1  O  TYR A 453   N  PHE A 341           
SHEET    3 AA1 5 VAL A 434  GLY A 439 -1  N  VAL A 436   O  ASP A 456           
SHEET    4 AA1 5 ALA A 368  ALA A 376  1  N  ILE A 374   O  ARG A 435           
SHEET    5 AA1 5 ILE A 360  TYR A 365 -1  N  ASP A 361   O  SER A 373           
SHEET    1 AA2 4 GLU A 340  PHE A 341  0                                        
SHEET    2 AA2 4 TYR A 453  VAL A 468 -1  O  TYR A 453   N  PHE A 341           
SHEET    3 AA2 4 ASN A 474  ARG A 482 -1  O  VAL A 475   N  GLN A 467           
SHEET    4 AA2 4 VAL A 389  THR A 393 -1  N  LEU A 390   O  LEU A 480           
SHEET    1 AA3 4 LEU A 505  LYS A 507  0                                        
SHEET    2 AA3 4 SER A 520  VAL A 522 -1  O  ALA A 521   N  CYS A 506           
SHEET    3 AA3 4 LEU A 618  THR A 623  1  O  ILE A 620   N  VAL A 522           
SHEET    4 AA3 4 GLY A 627  CYS A 632 -1  O  ARG A 631   N  GLU A 619           
SHEET    1 AA4 2 THR A 534  TYR A 535  0                                        
SHEET    2 AA4 2 LYS A 709  GLY A 710  1  O  GLY A 710   N  THR A 534           
SHEET    1 AA5 4 ILE A 592  TYR A 593  0                                        
SHEET    2 AA5 4 LEU A 724  LEU A 730  1  O  LEU A 730   N  ILE A 592           
SHEET    3 AA5 4 HIS A 740  ALA A 745 -1  O  MET A 742   N  GLN A 727           
SHEET    4 AA5 4 PHE A 641  GLU A 644 -1  N  ILE A 642   O  PHE A 743           
SHEET    1 AA6 3 GLU A 648  GLU A 651  0                                        
SHEET    2 AA6 3 PHE A 702  ASP A 705 -1  O  ASP A 705   N  GLU A 648           
SHEET    3 AA6 3 LEU A 665  ASP A 667 -1  N  PHE A 666   O  ILE A 704           
SHEET    1 AA7 2 TYR A 672  ASP A 673  0                                        
SHEET    2 AA7 2 MET A 693  ALA A 694 -1  O  ALA A 694   N  TYR A 672           
SHEET    1 AA8 2 ASN A 717  HIS A 718  0                                        
SHEET    2 AA8 2 CYS A 756  TYR A 757  1  O  TYR A 757   N  ASN A 717           
SHEET    1 AA9 2 GLN A 765  ARG A 767  0                                        
SHEET    2 AA9 2 ILE A 773  GLN A 775 -1  O  LYS A 774   N  VAL A 766           
LINK         SG  CYS A 553                ZN    ZN A 803     1555   1555  2.57  
LINK         SG  CYS A 553                ZN    ZN A 801     1555   1555  2.42  
LINK         SG  CYS A 555                ZN    ZN A 803     1555   1555  2.46  
LINK         SG  CYS A 559                ZN    ZN A 803     1555   1555  2.46  
LINK         SG  CYS A 559                ZN    ZN A 802     1555   1555  2.18  
LINK         SG  CYS A 567                ZN    ZN A 803     1555   1555  2.29  
LINK         SG  CYS A 569                ZN    ZN A 801     1555   1555  2.17  
LINK         SG  CYS A 595                ZN    ZN A 802     1555   1555  2.11  
LINK         SG  CYS A 595                ZN    ZN A 801     1555   1555  2.62  
LINK         SG  CYS A 599                ZN    ZN A 801     1555   1555  2.41  
LINK         SG  CYS A 601                ZN    ZN A 802     1555   1555  2.44  
LINK         SG  CYS A 605                ZN    ZN A 802     1555   1555  2.65  
LINK         O3'  DT C   7                 P   5CM C   8     1555   1555  1.60  
LINK         O3' 5CM C   8                 P    DA C   9     1555   1555  1.62  
SITE     1 AC1  4 CYS A 553  CYS A 569  CYS A 595  CYS A 599                    
SITE     1 AC2  4 CYS A 559  CYS A 595  CYS A 601  CYS A 605                    
SITE     1 AC3  4 CYS A 553  CYS A 555  CYS A 559  CYS A 567                    
CRYST1   74.137   79.443  107.845  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      0.013489  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012588  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009273        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system