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Entry: 6A5K
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HEADER    GENE REGULATION                         24-JUN-18   6A5K              
TITLE     CRYSTAL STRUCTURE OF ARABIDOPSIS THALIANA SUVH6 IN COMPLEX WITH SAM,  
TITLE    2 FORM 1                                                               
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                                                        
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_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VARIANT: RIL;                                      
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET-SUMO                                  
KEYWDS    SRA, SET, HISTONE METHYLTRANSFERASE, DNA METHYLATION, GENE REGULATION 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.LI,J.DU                                                             
REVDAT   3   26-SEP-18 6A5K    1       JRNL                                     
REVDAT   2   19-SEP-18 6A5K    1       JRNL                                     
REVDAT   1   29-AUG-18 6A5K    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.    1.90 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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.88                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 41533                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.214                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2098                            
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 47.8930 -  5.7663    0.98     2717   147  0.2198 0.2528        
REMARK   3     2  5.7663 -  4.5780    1.00     2736   150  0.1857 0.1903        
REMARK   3     3  4.5780 -  3.9997    1.00     2711   161  0.1499 0.1775        
REMARK   3     4  3.9997 -  3.6341    1.00     2802   125  0.1577 0.1826        
REMARK   3     5  3.6341 -  3.3737    1.00     2747   126  0.1603 0.1818        
REMARK   3     6  3.3737 -  3.1749    1.00     2727   152  0.1666 0.2087        
REMARK   3     7  3.1749 -  3.0159    1.00     2735   171  0.1777 0.1906        
REMARK   3     8  3.0159 -  2.8846    1.00     2750   153  0.1821 0.1912        
REMARK   3     9  2.8846 -  2.7736    1.00     2730   134  0.1841 0.2172        
REMARK   3    10  2.7736 -  2.6779    1.00     2736   142  0.1822 0.2073        
REMARK   3    11  2.6779 -  2.5942    1.00     2795   136  0.1762 0.2230        
REMARK   3    12  2.5942 -  2.5200    1.00     2730   167  0.1930 0.2156        
REMARK   3    13  2.5200 -  2.4537    1.00     2671   170  0.1778 0.2263        
REMARK   3    14  2.4537 -  2.3938    1.00     2764   148  0.1899 0.2718        
REMARK   3    15  2.3938 -  2.3394    1.00     2759   120  0.1938 0.1949        
REMARK   3    16  2.3394 -  2.2896    1.00     2769   142  0.1899 0.2652        
REMARK   3    17  2.2896 -  2.2438    1.00     2711   134  0.2019 0.2416        
REMARK   3    18  2.2438 -  2.2015    1.00     2770   146  0.1871 0.2373        
REMARK   3    19  2.2015 -  2.1621    1.00     2691   170  0.1923 0.1891        
REMARK   3    20  2.1621 -  2.1255    1.00     2791   139  0.1910 0.2239        
REMARK   3    21  2.1255 -  2.0912    1.00     2720   152  0.1959 0.2234        
REMARK   3    22  2.0912 -  2.0590    1.00     2763   153  0.2019 0.2563        
REMARK   3    23  2.0590 -  2.0288    1.00     2697   144  0.2054 0.2493        
REMARK   3    24  2.0288 -  2.0002    0.99     2790   137  0.2171 0.2584        
REMARK   3    25  2.0002 -  1.9731    0.96     2655   136  0.2148 0.2187        
REMARK   3    26  1.9731 -  1.9475    0.88     2382   135  0.2274 0.2635        
REMARK   3    27  1.9475 -  1.9232    0.80     2223   102  0.2393 0.3206        
REMARK   3    28  1.9232 -  1.9000    0.66     1834    84  0.2456 0.2937        
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)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.790           
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      :  0.005           3780                                  
REMARK   3   ANGLE     :  0.945           5091                                  
REMARK   3   CHIRALITY :  0.038            547                                  
REMARK   3   PLANARITY :  0.003            657                                  
REMARK   3   DIHEDRAL  : 15.419           1439                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 267 THROUGH 317 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  38.5493  43.7999  27.8461              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1949 T22:   0.2372                                     
REMARK   3      T33:   0.1353 T12:   0.0276                                     
REMARK   3      T13:   0.0133 T23:   0.0651                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2795 L22:   1.2366                                     
REMARK   3      L33:   1.7240 L12:  -0.3700                                     
REMARK   3      L13:   0.6622 L23:   0.1683                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0912 S12:   0.5458 S13:   0.2666                       
REMARK   3      S21:  -0.2202 S22:  -0.0410 S23:  -0.2082                       
REMARK   3      S31:  -0.1311 S32:   0.2888 S33:   0.1082                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 318 THROUGH 418 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  16.9525  44.2023  25.0745              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2219 T22:   0.1513                                     
REMARK   3      T33:   0.1885 T12:   0.0558                                     
REMARK   3      T13:  -0.0505 T23:  -0.0339                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3000 L22:   1.2159                                     
REMARK   3      L33:   0.9819 L12:  -1.0058                                     
REMARK   3      L13:   0.5404 L23:  -0.3447                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1144 S12:   0.3338 S13:  -0.0520                       
REMARK   3      S21:  -0.2646 S22:  -0.1337 S23:   0.2635                       
REMARK   3      S31:  -0.0434 S32:   0.0568 S33:   0.0161                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 419 THROUGH 498 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  10.4435  50.3725  31.3278              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1535 T22:   0.0954                                     
REMARK   3      T33:   0.2098 T12:   0.0534                                     
REMARK   3      T13:  -0.0211 T23:  -0.0308                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1004 L22:   1.0995                                     
REMARK   3      L33:   1.3713 L12:  -0.9085                                     
REMARK   3      L13:   0.6797 L23:  -0.7543                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0577 S12:  -0.0368 S13:  -0.0323                       
REMARK   3      S21:  -0.0534 S22:   0.0499 S23:   0.1598                       
REMARK   3      S31:  -0.1182 S32:  -0.1459 S33:   0.0226                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 499 THROUGH 537 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  26.1103  48.8810  63.4149              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3115 T22:   0.4067                                     
REMARK   3      T33:   0.2048 T12:   0.2022                                     
REMARK   3      T13:   0.0067 T23:  -0.2939                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7319 L22:   1.0657                                     
REMARK   3      L33:   1.3837 L12:   0.6422                                     
REMARK   3      L13:  -0.1641 L23:  -0.1678                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0366 S12:  -0.9166 S13:   1.0131                       
REMARK   3      S21:   0.7758 S22:  -0.1815 S23:   0.2153                       
REMARK   3      S31:  -0.6200 S32:  -0.5022 S33:   0.0313                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 538 THROUGH 560 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  56.5932  48.2368  54.4970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2496 T22:   0.1720                                     
REMARK   3      T33:   0.4972 T12:  -0.2583                                     
REMARK   3      T13:  -0.1342 T23:   0.1283                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7506 L22:   1.2753                                     
REMARK   3      L33:   0.0597 L12:  -1.2257                                     
REMARK   3      L13:  -0.2420 L23:   0.2399                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4006 S12:  -0.8109 S13:   0.7324                       
REMARK   3      S21:   0.6285 S22:   0.1555 S23:  -0.2065                       
REMARK   3      S31:  -0.2975 S32:   0.4884 S33:   0.4410                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 561 THROUGH 647 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  42.8754  47.1324  47.1443              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1382 T22:   0.0736                                     
REMARK   3      T33:   0.1840 T12:   0.0036                                     
REMARK   3      T13:  -0.0535 T23:   0.0127                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3407 L22:   1.4277                                     
REMARK   3      L33:   1.3456 L12:  -0.0599                                     
REMARK   3      L13:   0.9304 L23:  -0.1625                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1484 S12:  -0.0722 S13:   0.4188                       
REMARK   3      S21:   0.0432 S22:  -0.1226 S23:  -0.3155                       
REMARK   3      S31:  -0.2464 S32:   0.1232 S33:   0.0377                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 648 THROUGH 705 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  44.7581  31.7811  53.7829              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1356 T22:   0.2123                                     
REMARK   3      T33:   0.1778 T12:  -0.0151                                     
REMARK   3      T13:  -0.0055 T23:   0.0154                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7040 L22:   0.9420                                     
REMARK   3      L33:   2.3891 L12:  -0.6784                                     
REMARK   3      L13:   0.4615 L23:  -0.1634                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0438 S12:  -0.1468 S13:  -0.1343                       
REMARK   3      S21:   0.0298 S22:  -0.0004 S23:  -0.0657                       
REMARK   3      S31:   0.1425 S32:  -0.1076 S33:   0.1131                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 706 THROUGH 735 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  40.8729  39.4623  54.4210              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1462 T22:   0.1699                                     
REMARK   3      T33:   0.0697 T12:   0.0190                                     
REMARK   3      T13:  -0.0346 T23:  -0.0084                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1097 L22:   0.9546                                     
REMARK   3      L33:   0.9295 L12:  -0.1867                                     
REMARK   3      L13:  -0.0645 L23:  -0.4573                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1559 S12:  -0.4101 S13:   0.0534                       
REMARK   3      S21:   0.1213 S22:  -0.0559 S23:  -0.2486                       
REMARK   3      S31:  -0.2411 S32:  -0.0079 S33:   0.1154                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 736 THROUGH 790 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  33.9697  32.0740  51.5507              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1158 T22:   0.1382                                     
REMARK   3      T33:   0.1097 T12:   0.0067                                     
REMARK   3      T13:   0.0163 T23:   0.0167                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0596 L22:   0.7217                                     
REMARK   3      L33:   1.1178 L12:   0.3711                                     
REMARK   3      L13:   0.0477 L23:  -0.2586                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0305 S12:  -0.2839 S13:  -0.2286                       
REMARK   3      S21:   0.0623 S22:  -0.0815 S23:  -0.1203                       
REMARK   3      S31:   0.0726 S32:  -0.0989 S33:   0.0243                       
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 6A5K 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_1300008192.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-JAN-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.2827                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42734                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
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     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 16.90                              
REMARK 200  R MERGE                    (I) : 0.07100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 41.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.93                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.90                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.87400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
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   (%): 45.18                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M POTASSIUM SODIUM TARTRATE, 20%      
REMARK 280  PEG 3350, PH 7, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       38.55650            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       61.07600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.55650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       61.07600            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLY A   266                                                      
REMARK 465     GLY A   378                                                      
REMARK 465     GLY A   379                                                      
REMARK 465     TYR A   380                                                      
REMARK 465     ASP A   381                                                      
REMARK 465     ASP A   382                                                      
REMARK 465     HIS A   383                                                      
REMARK 465     LEU A   384                                                      
REMARK 465     ASP A   385                                                      
REMARK 465     GLY A   396                                                      
REMARK 465     GLY A   397                                                      
REMARK 465     ASN A   398                                                      
REMARK 465     VAL A   399                                                      
REMARK 465     MSE 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     PRO A   412                                                      
REMARK 465     LYS A   442                                                      
REMARK 465     SER A   443                                                      
REMARK 465     THR A   444                                                      
REMARK 465     HIS A   445                                                      
REMARK 465     ASP A   446                                                      
REMARK 465     LYS A   447                                                      
REMARK 465     SER A   470                                                      
REMARK 465     HIS A   471                                                      
REMARK 465     GLU A   563                                                      
REMARK 465     ALA A   564                                                      
REMARK 465     ARG A   565                                                      
REMARK 465     LEU A   685                                                      
REMARK 465     GLY A   686                                                      
REMARK 465     THR A   687                                                      
REMARK 465     GLN A   688                                                      
REMARK 465     ALA A   689                                                      
REMARK 465     GLY A   690                                                      
REMARK 465     ARG A   691                                                      
REMARK 465     SER A   692                                                      
REMARK 465     MSE A   693                                                      
REMARK 465     ALA A   694                                                      
REMARK 465     GLU A   695                                                      
REMARK 465     GLY A   696                                                      
REMARK 465     ASP A   697                                                      
REMARK 465     VAL A   766                                                      
REMARK 465     ARG A   767                                                      
REMARK 465     ASP A   768                                                      
REMARK 465     SER A   769                                                      
REMARK 465     LYS A   770                                                      
REMARK 465     GLY A   771                                                      
REMARK 465     ASN A   772                                                      
REMARK 465     ILE A   773                                                      
REMARK 465     LYS A   774                                                      
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    GLU A 296       49.35    -69.59                                   
REMARK 500    ASP A 297      -11.87   -154.91                                   
REMARK 500    GLN A 357      -38.57   -132.62                                   
REMARK 500    THR A 419     -119.44     39.43                                   
REMARK 500    ASP A 526     -159.93   -144.55                                   
REMARK 500    GLU A 561     -171.23    172.92                                   
REMARK 500    VAL A 609      -72.92   -129.39                                   
REMARK 500    ILE A 642      -69.72   -100.74                                   
REMARK 500    ASN A 711     -165.53   -108.21                                   
REMARK 500    TYR A 731      -41.49   -153.17                                   
REMARK 500    ARG A 787      -30.62     77.59                                   
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 A1300        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH A1301        DISTANCE =  6.02 ANGSTROMS                       
REMARK 525    HOH A1302        DISTANCE =  6.05 ANGSTROMS                       
REMARK 525    HOH A1303        DISTANCE =  6.57 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 803  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 553   SG                                                     
REMARK 620 2 CYS A 555   SG  108.3                                              
REMARK 620 3 CYS A 559   SG  104.5 106.5                                        
REMARK 620 4 CYS A 567   SG  118.5 101.5 116.7                                  
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  118.4                                              
REMARK 620 3 CYS A 595   SG  112.9 109.6                                        
REMARK 620 4 CYS A 599   SG  100.8 104.0 110.2                                  
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  108.4                                              
REMARK 620 3 CYS A 601   SG  121.6 104.5                                        
REMARK 620 4 CYS A 605   SG   99.4 112.3 110.9                                  
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 720   SG                                                     
REMARK 620 2 CYS A 778   SG  108.3                                              
REMARK 620 3 CYS A 780   SG  108.1 106.2                                        
REMARK 620 4 CYS A 785   SG  113.9 108.2 111.7                                  
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                  
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 SAM A 805                 
DBREF  6A5K A  264   790  UNP    Q8VZ17   SUVH6_ARATH    264    790             
SEQADV 6A5K 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 MSE GLU LEU ASN ILE LEU GLY ILE HIS LYS          
SEQRES   8 A  527  PRO SER GLN ALA GLY ILE ASP TYR MSE 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 MSE 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 MSE 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  MSE SER GLU LEU MSE LEU GLY THR GLN ALA GLY ARG SER          
SEQRES  34 A  527  MSE 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 MSE 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                                  
MODRES 6A5K MSE A  345  MET  MODIFIED RESIDUE                                   
MODRES 6A5K MSE A  363  MET  MODIFIED RESIDUE                                   
MODRES 6A5K MSE A  473  MET  MODIFIED RESIDUE                                   
MODRES 6A5K MSE A  680  MET  MODIFIED RESIDUE                                   
MODRES 6A5K MSE A  684  MET  MODIFIED RESIDUE                                   
MODRES 6A5K MSE A  742  MET  MODIFIED RESIDUE                                   
HET    MSE  A 345       8                                                       
HET    MSE  A 363       8                                                       
HET    MSE  A 473       8                                                       
HET    MSE  A 680       8                                                       
HET    MSE  A 684       8                                                       
HET    MSE  A 742       8                                                       
HET     ZN  A 801       1                                                       
HET     ZN  A 802       1                                                       
HET     ZN  A 803       1                                                       
HET     ZN  A 804       1                                                       
HET    SAM  A 805      27                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      ZN ZINC ION                                                         
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
FORMUL   1  MSE    6(C5 H11 N O2 SE)                                            
FORMUL   2   ZN    4(ZN 2+)                                                     
FORMUL   6  SAM    C15 H22 N6 O5 S                                              
FORMUL   7  HOH   *403(H2 O)                                                    
HELIX    1 AA1 ASP A  267  ALA A  293  1                                  27    
HELIX    2 AA2 ARG A  306  ASN A  318  1                                  13    
HELIX    3 AA3 TYR A  343  LEU A  350  1                                   8    
HELIX    4 AA4 ILE A  418  GLN A  431  1                                  14    
HELIX    5 AA5 LEU A  489  LYS A  498  1                                  10    
HELIX    6 AA6 PRO A  542  ARG A  546  5                                   5    
HELIX    7 AA7 CYS A  567  ASN A  573  1                                   7    
HELIX    8 AA8 VAL A  609  GLY A  613  5                                   5    
HELIX    9 AA9 ASP A  652  ARG A  658  1                                   7    
HELIX   10 AB1 ASN A  661  GLU A  663  5                                   3    
HELIX   11 AB2 ASN A  674  MSE A  684  1                                  11    
HELIX   12 AB3 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  ARG A 438   O  VAL A 454           
SHEET    4 AA1 5 ALA A 368  ALA A 376  1  N  ALA A 376   O  GLY A 439           
SHEET    5 AA1 5 ILE A 360  TYR A 365 -1  N  TYR A 365   O  ALA A 368           
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 6 LEU A 505  LYS A 507  0                                        
SHEET    2 AA3 6 SER A 520  VAL A 522 -1  O  ALA A 521   N  CYS A 506           
SHEET    3 AA3 6 LEU A 618  LYS A 622  1  O  ILE A 620   N  SER A 520           
SHEET    4 AA3 6 TRP A 628  CYS A 632 -1  O  ARG A 631   N  GLU A 619           
SHEET    5 AA3 6 GLU A 754  TYR A 757 -1  O  LEU A 755   N  VAL A 630           
SHEET    6 AA3 6 ASN A 717  HIS A 718  1  N  ASN A 717   O  TYR A 757           
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 THR A 591  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  MSE 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 SER A 699  ASP A 705 -1  O  ASP A 705   N  GLU A 648           
SHEET    3 AA6 3 LEU A 665  GLY A 669 -1  N  PHE A 666   O  ILE A 704           
SHEET    1 AA7 2 LYS A 776  LEU A 777  0                                        
SHEET    2 AA7 2 ARG A 788  TYR A 790 -1  O  LEU A 789   N  LYS A 776           
LINK         C   ARG A 344                 N   MSE A 345     1555   1555  1.33  
LINK         C   MSE A 345                 N   GLU A 346     1555   1555  1.33  
LINK         C   TYR A 362                 N   MSE A 363     1555   1555  1.33  
LINK         C   MSE A 363                 N   LYS A 364     1555   1555  1.33  
LINK         C   GLY A 472                 N   MSE A 473     1555   1555  1.33  
LINK         C   MSE A 473                 N   ASN A 474     1555   1555  1.33  
LINK         SG  CYS A 553                ZN    ZN A 803     1555   1555  2.54  
LINK         SG  CYS A 553                ZN    ZN A 801     1555   1555  2.40  
LINK         SG  CYS A 555                ZN    ZN A 803     1555   1555  2.53  
LINK         SG  CYS A 559                ZN    ZN A 802     1555   1555  2.38  
LINK         SG  CYS A 559                ZN    ZN A 803     1555   1555  2.31  
LINK         SG  CYS A 567                ZN    ZN A 803     1555   1555  2.31  
LINK         SG  CYS A 569                ZN    ZN A 801     1555   1555  2.31  
LINK         SG  CYS A 595                ZN    ZN A 802     1555   1555  2.41  
LINK         SG  CYS A 595                ZN    ZN A 801     1555   1555  2.41  
LINK         SG  CYS A 599                ZN    ZN A 801     1555   1555  2.35  
LINK         SG  CYS A 601                ZN    ZN A 802     1555   1555  2.32  
LINK         SG  CYS A 605                ZN    ZN A 802     1555   1555  2.40  
LINK         C   GLY A 679                 N   MSE A 680     1555   1555  1.33  
LINK         C   MSE A 680                 N   SER A 681     1555   1555  1.33  
LINK         C   LEU A 683                 N   MSE A 684     1555   1555  1.33  
LINK         SG  CYS A 720                ZN    ZN A 804     1555   1555  2.42  
LINK         C   VAL A 741                 N   MSE A 742     1555   1555  1.33  
LINK         C   MSE A 742                 N   PHE A 743     1555   1555  1.33  
LINK         SG  CYS A 778                ZN    ZN A 804     1555   1555  2.36  
LINK         SG  CYS A 780                ZN    ZN A 804     1555   1555  2.37  
LINK         SG  CYS A 785                ZN    ZN A 804     1555   1555  2.30  
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                    
SITE     1 AC4  4 CYS A 720  CYS A 778  CYS A 780  CYS A 785                    
SITE     1 AC5 17 ARG A 626  TRP A 628  GLU A 663  TYR A 664                    
SITE     2 AC5 17 ARG A 714  PHE A 715  ASN A 717  HIS A 718                    
SITE     3 AC5 17 TYR A 759  LYS A 776  LEU A 777  CYS A 778                    
SITE     4 AC5 17 PHE A 779  HOH A1066  HOH A1135  HOH A1163                    
SITE     5 AC5 17 HOH A1168                                                     
CRYST1   77.113  122.152   56.315  90.00  90.00  90.00 P 21 21 2     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      0.012968  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008187  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017757        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system