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Database: PDB
Entry: 6MBL
LinkDB: 6MBL
Original site: 6MBL 
HEADER    TRANSFERASE/STRUCTURAL PROTEIN          30-AUG-18   6MBL              
TITLE     SETD3, A HISTIDINE METHYLTRANSFERASE, IN COMPLEX WITH AN ACTIN PEPTIDE
TITLE    2 AND SAH, SECOND P212121 CRYSTAL FORM                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACTIN PEPTIDE;                                             
COMPND   3 CHAIN: Y;                                                            
COMPND   4 FRAGMENT: RESIDUES 66-80;                                            
COMPND   5 SYNONYM: BETA-ACTIN;                                                 
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SETD3;                  
COMPND   9 CHAIN: A;                                                            
COMPND  10 SYNONYM: SET DOMAIN-CONTAINING PROTEIN 3;                            
COMPND  11 EC: 2.1.1.43;                                                        
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   4 ORGANISM_COMMON: HUMAN;                                              
SOURCE   5 ORGANISM_TAXID: 9606;                                                
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   8 ORGANISM_COMMON: HUMAN;                                              
SOURCE   9 ORGANISM_TAXID: 9606;                                                
SOURCE  10 GENE: SETD3, C14ORF154;                                              
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  13 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    TRANSFERASE, TRANSFERASE-STRUCTURAL PROTEIN COMPLEX                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.R.HORTON,S.DAI,X.CHENG                                              
REVDAT   2   16-JAN-19 6MBL    1       JRNL                                     
REVDAT   1   19-DEC-18 6MBL    0                                                
JRNL        AUTH   A.W.WILKINSON,J.DIEP,S.DAI,S.LIU,Y.S.OOI,D.SONG,T.-M.LI,     
JRNL        AUTH 2 J.R.HORTON,X.ZHANG,C.LIU,D.V.TRIVEDI,K.M.RUPPEL,             
JRNL        AUTH 3 J.G.VILCHES-MOURE,K.M.CASEY,J.MAK,T.COWAN,J.E.ELIAS,         
JRNL        AUTH 4 C.M.NAGAMINE,J.A.SPUDICH,X.CHENG,J.E.CARETTE,O.GOZANI        
JRNL        TITL   SETD3 IS AN ACTIN HISTIDINE METHYLTRANSFERASE THAT PREVENTS  
JRNL        TITL 2 PRIMARY DYSTOCIA                                             
JRNL        REF    NATURE                        V. 565   372 2018              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        DOI    10.1038/S41586-018-0821-8                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.13_2998)                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.30                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 30334                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.185                           
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.227                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1520                            
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 48.3106 -  4.8838    0.99     2802   149  0.1711 0.1998        
REMARK   3     2  4.8838 -  3.8770    1.00     2698   141  0.1421 0.1651        
REMARK   3     3  3.8770 -  3.3870    1.00     2660   141  0.1656 0.2196        
REMARK   3     4  3.3870 -  3.0774    0.99     2650   139  0.1930 0.2449        
REMARK   3     5  3.0774 -  2.8569    1.00     2615   138  0.1908 0.2430        
REMARK   3     6  2.8569 -  2.6885    1.00     2623   138  0.1936 0.2703        
REMARK   3     7  2.6885 -  2.5538    1.00     2623   138  0.2056 0.2579        
REMARK   3     8  2.5538 -  2.4427    1.00     2607   138  0.2072 0.2594        
REMARK   3     9  2.4427 -  2.3486    1.00     2612   137  0.2279 0.2945        
REMARK   3    10  2.3486 -  2.2676    0.99     2583   136  0.2457 0.3021        
REMARK   3    11  2.2676 -  2.1967    0.90     2341   125  0.2770 0.3408        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.230            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.940           
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      :  0.004           4209                                  
REMARK   3   ANGLE     :  0.683           5698                                  
REMARK   3   CHIRALITY :  0.042            622                                  
REMARK   3   PLANARITY :  0.004            729                                  
REMARK   3   DIHEDRAL  : 16.879           2549                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'Y' AND (RESID 66 THROUGH 80 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.3572  14.5038  30.1804              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2042 T22:   0.1967                                     
REMARK   3      T33:   0.2562 T12:  -0.0065                                     
REMARK   3      T13:  -0.0239 T23:  -0.0292                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2087 L22:   6.0259                                     
REMARK   3      L33:   8.7552 L12:   1.6804                                     
REMARK   3      L13:  -2.2084 L23:   0.3455                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0355 S12:  -0.5731 S13:   0.1155                       
REMARK   3      S21:   0.2571 S22:  -0.0655 S23:  -0.0239                       
REMARK   3      S31:   0.2094 S32:   0.3626 S33:   0.1867                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 20 THROUGH 61 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  25.2252   2.4841  24.2450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1719 T22:   0.3152                                     
REMARK   3      T33:   0.4679 T12:   0.0625                                     
REMARK   3      T13:  -0.0088 T23:   0.0386                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2510 L22:   5.5803                                     
REMARK   3      L33:   5.3454 L12:   2.4165                                     
REMARK   3      L13:   2.0772 L23:   2.3565                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1124 S12:   0.2352 S13:  -0.5697                       
REMARK   3      S21:   0.0059 S22:   0.1106 S23:  -0.5221                       
REMARK   3      S31:   0.2630 S32:   0.4788 S33:  -0.3079                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 62 THROUGH 126 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.8197  18.9421  10.0566              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4017 T22:   0.5242                                     
REMARK   3      T33:   0.3491 T12:   0.0639                                     
REMARK   3      T13:  -0.1233 T23:   0.0444                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1433 L22:   3.5229                                     
REMARK   3      L33:   1.7516 L12:  -1.7492                                     
REMARK   3      L13:  -0.2871 L23:   0.4246                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2590 S12:   0.9006 S13:   0.1912                       
REMARK   3      S21:  -0.7717 S22:  -0.3035 S23:   0.4665                       
REMARK   3      S31:  -0.3089 S32:  -0.1982 S33:   0.0455                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 127 THROUGH 225 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   8.5603   5.2873  21.2820              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1924 T22:   0.2068                                     
REMARK   3      T33:   0.2439 T12:   0.0402                                     
REMARK   3      T13:   0.0244 T23:  -0.0397                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6177 L22:   2.6609                                     
REMARK   3      L33:   1.6978 L12:   0.9341                                     
REMARK   3      L13:   0.9525 L23:   0.2554                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0739 S12:   0.3536 S13:  -0.4628                       
REMARK   3      S21:  -0.1636 S22:  -0.0485 S23:   0.0475                       
REMARK   3      S31:   0.2067 S32:   0.0217 S33:  -0.0205                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 226 THROUGH 334 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.6942  16.1740  22.3893              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1871 T22:   0.2024                                     
REMARK   3      T33:   0.2741 T12:   0.0025                                     
REMARK   3      T13:  -0.0482 T23:   0.0111                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7367 L22:   1.8399                                     
REMARK   3      L33:   2.5470 L12:  -0.6112                                     
REMARK   3      L13:  -0.3093 L23:   0.5990                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0032 S12:   0.2236 S13:   0.0405                       
REMARK   3      S21:  -0.0534 S22:  -0.0654 S23:   0.4386                       
REMARK   3      S31:  -0.0476 S32:  -0.1636 S33:   0.0753                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 335 THROUGH 408 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   8.2753  24.7345  57.0144              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4306 T22:   0.3416                                     
REMARK   3      T33:   0.2653 T12:   0.0774                                     
REMARK   3      T13:   0.0253 T23:  -0.0321                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2251 L22:   1.6782                                     
REMARK   3      L33:   6.3226 L12:   1.5302                                     
REMARK   3      L13:  -4.2251 L23:  -2.1622                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0957 S12:  -0.7202 S13:   0.0031                       
REMARK   3      S21:   0.3233 S22:   0.0689 S23:  -0.0435                       
REMARK   3      S31:   0.1247 S32:   0.4466 S33:   0.0625                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 409 THROUGH 500 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  15.6365  35.2342  43.3387              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5107 T22:   0.3149                                     
REMARK   3      T33:   0.4835 T12:  -0.1049                                     
REMARK   3      T13:   0.0601 T23:  -0.0539                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9330 L22:   2.1187                                     
REMARK   3      L33:   2.9266 L12:   0.2109                                     
REMARK   3      L13:  -0.7739 L23:  -0.3974                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2724 S12:  -0.4011 S13:   0.5766                       
REMARK   3      S21:   0.5222 S22:  -0.0561 S23:   0.1435                       
REMARK   3      S31:  -0.9239 S32:   0.3130 S33:  -0.2760                       
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 6MBL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-AUG-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000236560.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-MAR-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30434                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.190                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 10.60                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.27                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
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: 3SMT                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.62                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM CHLORIDE, 0.1 M BIS-TRIS    
REMARK 280  PH 5.5, 25% W/V POLYETHYLENE GLYCOL 3,350, VAPOR DIFFUSION,         
REMARK 280  HANGING DROP, TEMPERATURE 292K                                      
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       28.27850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.81750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       46.41500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       55.81750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.27850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       46.41500            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3750 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22950 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 12.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Y, 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     GLY A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     LEU A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     MET A     0                                                      
REMARK 465     GLY A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     ARG A     5                                                      
REMARK 465     VAL A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     THR A     8                                                      
REMARK 465     GLN A     9                                                      
REMARK 465     LYS A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     THR A    13                                                      
REMARK 465     GLY A    14                                                      
REMARK 465     ALA A    15                                                      
REMARK 465     THR A    16                                                      
REMARK 465     ALA A    17                                                      
REMARK 465     THR A    18                                                      
REMARK 465     VAL A    19                                                      
REMARK 465     TYR A   501                                                      
REMARK 465     GLU A   502                                                      
REMARK 465     GLU A   503                                                      
REMARK 465     SER A   504                                                      
REMARK 465     ASN A   505                                                      
REMARK 465     LEU A   506                                                      
REMARK 465     GLY A   507                                                      
REMARK 465     LEU A   508                                                      
REMARK 465     LEU A   509                                                      
REMARK 465     GLU A   510                                                      
REMARK 465     SER A   511                                                      
REMARK 465     SER A   512                                                      
REMARK 465     VAL A   513                                                      
REMARK 465     GLY A   514                                                      
REMARK 465     ASP A   515                                                      
REMARK 465     SER A   516                                                      
REMARK 465     ARG A   517                                                      
REMARK 465     LEU A   518                                                      
REMARK 465     PRO A   519                                                      
REMARK 465     LEU A   520                                                      
REMARK 465     VAL A   521                                                      
REMARK 465     LEU A   522                                                      
REMARK 465     ARG A   523                                                      
REMARK 465     ASN A   524                                                      
REMARK 465     LEU A   525                                                      
REMARK 465     GLU A   526                                                      
REMARK 465     GLU A   527                                                      
REMARK 465     GLU A   528                                                      
REMARK 465     ALA A   529                                                      
REMARK 465     GLY A   530                                                      
REMARK 465     VAL A   531                                                      
REMARK 465     GLN A   532                                                      
REMARK 465     ASP A   533                                                      
REMARK 465     ALA A   534                                                      
REMARK 465     LEU A   535                                                      
REMARK 465     ASN A   536                                                      
REMARK 465     ILE A   537                                                      
REMARK 465     ARG A   538                                                      
REMARK 465     GLU A   539                                                      
REMARK 465     ALA A   540                                                      
REMARK 465     ILE A   541                                                      
REMARK 465     SER A   542                                                      
REMARK 465     LYS A   543                                                      
REMARK 465     ALA A   544                                                      
REMARK 465     LYS A   545                                                      
REMARK 465     ALA A   546                                                      
REMARK 465     THR A   547                                                      
REMARK 465     GLU A   548                                                      
REMARK 465     ASN A   549                                                      
REMARK 465     GLY A   550                                                      
REMARK 465     LEU A   551                                                      
REMARK 465     VAL A   552                                                      
REMARK 465     ASN A   553                                                      
REMARK 465     GLY A   554                                                      
REMARK 465     GLU A   555                                                      
REMARK 465     ASN A   556                                                      
REMARK 465     SER A   557                                                      
REMARK 465     ILE A   558                                                      
REMARK 465     PRO A   559                                                      
REMARK 465     ASN A   560                                                      
REMARK 465     GLY A   561                                                      
REMARK 465     THR A   562                                                      
REMARK 465     ARG A   563                                                      
REMARK 465     SER A   564                                                      
REMARK 465     GLU A   565                                                      
REMARK 465     ASN A   566                                                      
REMARK 465     GLU A   567                                                      
REMARK 465     SER A   568                                                      
REMARK 465     LEU A   569                                                      
REMARK 465     ASN A   570                                                      
REMARK 465     GLN A   571                                                      
REMARK 465     GLU A   572                                                      
REMARK 465     SER A   573                                                      
REMARK 465     LYS A   574                                                      
REMARK 465     ARG A   575                                                      
REMARK 465     ALA A   576                                                      
REMARK 465     VAL A   577                                                      
REMARK 465     GLU A   578                                                      
REMARK 465     ASP A   579                                                      
REMARK 465     ALA A   580                                                      
REMARK 465     LYS A   581                                                      
REMARK 465     GLY A   582                                                      
REMARK 465     SER A   583                                                      
REMARK 465     SER A   584                                                      
REMARK 465     SER A   585                                                      
REMARK 465     ASP A   586                                                      
REMARK 465     SER A   587                                                      
REMARK 465     THR A   588                                                      
REMARK 465     ALA A   589                                                      
REMARK 465     GLY A   590                                                      
REMARK 465     VAL A   591                                                      
REMARK 465     LYS A   592                                                      
REMARK 465     GLU A   593                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     THR Y  66    OG1  CG2                                            
REMARK 470     LYS A  64    CG   CD   CE   NZ                                   
REMARK 470     LYS A 221    CG   CD   CE   NZ                                   
REMARK 470     HIS A 228    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASN A 230    CG   OD1  ND2                                       
REMARK 470     LYS A 231    CG   CD   CE   NZ                                   
REMARK 470     LYS A 235    CG   CD   CE   NZ                                   
REMARK 470     GLU A 414    CD   OE1  OE2                                       
REMARK 470     GLU A 493    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 495    CG   CD   CE   NZ                                   
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    HIS A 228     -137.21   -126.28                                   
REMARK 500    LYS A 231       -9.14    -57.26                                   
REMARK 500    SER A 237      119.14   -161.82                                   
REMARK 500    LEU A 272      -63.62     70.68                                   
REMARK 500    LYS A 344       -8.05    -59.87                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1011                
DBREF  6MBL Y   66    80  UNP    P60709   ACTB_HUMAN      66     80             
DBREF  6MBL A    0   593  UNP    Q86TU7   SETD3_HUMAN      1    594             
SEQADV 6MBL GLY A   -5  UNP  Q86TU7              EXPRESSION TAG                 
SEQADV 6MBL PRO A   -4  UNP  Q86TU7              EXPRESSION TAG                 
SEQADV 6MBL LEU A   -3  UNP  Q86TU7              EXPRESSION TAG                 
SEQADV 6MBL GLY A   -2  UNP  Q86TU7              EXPRESSION TAG                 
SEQADV 6MBL SER A   -1  UNP  Q86TU7              EXPRESSION TAG                 
SEQRES   1 Y   15  THR LEU LYS TYR PRO ILE GLU HIS GLY ILE VAL THR ASN          
SEQRES   2 Y   15  TRP ASP                                                      
SEQRES   1 A  599  GLY PRO LEU GLY SER MET GLY LYS LYS SER ARG VAL LYS          
SEQRES   2 A  599  THR GLN LYS SER GLY THR GLY ALA THR ALA THR VAL SER          
SEQRES   3 A  599  PRO LYS GLU ILE LEU ASN LEU THR SER GLU LEU LEU GLN          
SEQRES   4 A  599  LYS CYS SER SER PRO ALA PRO GLY PRO GLY LYS GLU TRP          
SEQRES   5 A  599  GLU GLU TYR VAL GLN ILE ARG THR LEU VAL GLU LYS ILE          
SEQRES   6 A  599  ARG LYS LYS GLN LYS GLY LEU SER VAL THR PHE ASP GLY          
SEQRES   7 A  599  LYS ARG GLU ASP TYR PHE PRO ASP LEU MET LYS TRP ALA          
SEQRES   8 A  599  SER GLU ASN GLY ALA SER VAL GLU GLY PHE GLU MET VAL          
SEQRES   9 A  599  ASN PHE LYS GLU GLU GLY PHE GLY LEU ARG ALA THR ARG          
SEQRES  10 A  599  ASP ILE LYS ALA GLU GLU LEU PHE LEU TRP VAL PRO ARG          
SEQRES  11 A  599  LYS LEU LEU MET THR VAL GLU SER ALA LYS ASN SER VAL          
SEQRES  12 A  599  LEU GLY PRO LEU TYR SER GLN ASP ARG ILE LEU GLN ALA          
SEQRES  13 A  599  MET GLY ASN ILE ALA LEU ALA PHE HIS LEU LEU CYS GLU          
SEQRES  14 A  599  ARG ALA SER PRO ASN SER PHE TRP GLN PRO TYR ILE GLN          
SEQRES  15 A  599  THR LEU PRO SER GLU TYR ASP THR PRO LEU TYR PHE GLU          
SEQRES  16 A  599  GLU ASP GLU VAL ARG TYR LEU GLN SER THR GLN ALA ILE          
SEQRES  17 A  599  HIS ASP VAL PHE SER GLN TYR LYS ASN THR ALA ARG GLN          
SEQRES  18 A  599  TYR ALA TYR PHE TYR LYS VAL ILE GLN THR HIS PRO HIS          
SEQRES  19 A  599  ALA ASN LYS LEU PRO LEU LYS ASP SER PHE THR TYR GLU          
SEQRES  20 A  599  ASP TYR ARG TRP ALA VAL SER SER VAL MET THR ARG GLN          
SEQRES  21 A  599  ASN GLN ILE PRO THR GLU ASP GLY SER ARG VAL THR LEU          
SEQRES  22 A  599  ALA LEU ILE PRO LEU TRP ASP MET CYS ASN HIS THR ASN          
SEQRES  23 A  599  GLY LEU ILE THR THR GLY TYR ASN LEU GLU ASP ASP ARG          
SEQRES  24 A  599  CYS GLU CYS VAL ALA LEU GLN ASP PHE ARG ALA GLY GLU          
SEQRES  25 A  599  GLN ILE TYR ILE PHE TYR GLY THR ARG SER ASN ALA GLU          
SEQRES  26 A  599  PHE VAL ILE HIS SER GLY PHE PHE PHE ASP ASN ASN SER          
SEQRES  27 A  599  HIS ASP ARG VAL LYS ILE LYS LEU GLY VAL SER LYS SER          
SEQRES  28 A  599  ASP ARG LEU TYR ALA MET LYS ALA GLU VAL LEU ALA ARG          
SEQRES  29 A  599  ALA GLY ILE PRO THR SER SER VAL PHE ALA LEU HIS PHE          
SEQRES  30 A  599  THR GLU PRO PRO ILE SER ALA GLN LEU LEU ALA PHE LEU          
SEQRES  31 A  599  ARG VAL PHE CYS MET THR GLU GLU GLU LEU LYS GLU HIS          
SEQRES  32 A  599  LEU LEU GLY ASP SER ALA ILE ASP ARG ILE PHE THR LEU          
SEQRES  33 A  599  GLY ASN SER GLU PHE PRO VAL SER TRP ASP ASN GLU VAL          
SEQRES  34 A  599  LYS LEU TRP THR PHE LEU GLU ASP ARG ALA SER LEU LEU          
SEQRES  35 A  599  LEU LYS THR TYR LYS THR THR ILE GLU GLU ASP LYS SER          
SEQRES  36 A  599  VAL LEU LYS ASN HIS ASP LEU SER VAL ARG ALA LYS MET          
SEQRES  37 A  599  ALA ILE LYS LEU ARG LEU GLY GLU LYS GLU ILE LEU GLU          
SEQRES  38 A  599  LYS ALA VAL LYS SER ALA ALA VAL ASN ARG GLU TYR TYR          
SEQRES  39 A  599  ARG GLN GLN MET GLU GLU LYS ALA PRO LEU PRO LYS TYR          
SEQRES  40 A  599  GLU GLU SER ASN LEU GLY LEU LEU GLU SER SER VAL GLY          
SEQRES  41 A  599  ASP SER ARG LEU PRO LEU VAL LEU ARG ASN LEU GLU GLU          
SEQRES  42 A  599  GLU ALA GLY VAL GLN ASP ALA LEU ASN ILE ARG GLU ALA          
SEQRES  43 A  599  ILE SER LYS ALA LYS ALA THR GLU ASN GLY LEU VAL ASN          
SEQRES  44 A  599  GLY GLU ASN SER ILE PRO ASN GLY THR ARG SER GLU ASN          
SEQRES  45 A  599  GLU SER LEU ASN GLN GLU SER LYS ARG ALA VAL GLU ASP          
SEQRES  46 A  599  ALA LYS GLY SER SER SER ASP SER THR ALA GLY VAL LYS          
SEQRES  47 A  599  GLU                                                          
HET    SAH  A1001      26                                                       
HET    EDO  A1002       4                                                       
HET    EDO  A1003       4                                                       
HET    EDO  A1004       4                                                       
HET    EDO  A1005       4                                                       
HET    EDO  A1006       4                                                       
HET    EDO  A1007       4                                                       
HET    EDO  A1008       4                                                       
HET    EDO  A1009       4                                                       
HET    EDO  A1010       4                                                       
HET    EDO  A1011       4                                                       
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  SAH    C14 H20 N6 O5 S                                              
FORMUL   4  EDO    10(C2 H6 O2)                                                 
FORMUL  14  HOH   *139(H2 O)                                                    
HELIX    1 AA1 PRO A   21  SER A   36  1                                  16    
HELIX    2 AA2 GLY A   41  GLY A   43  5                                   3    
HELIX    3 AA3 LYS A   44  LYS A   62  1                                  19    
HELIX    4 AA4 LYS A   73  ASP A   76  5                                   4    
HELIX    5 AA5 TYR A   77  ASN A   88  1                                  12    
HELIX    6 AA6 LYS A  125  LEU A  127  5                                   3    
HELIX    7 AA7 VAL A  130  ASN A  135  1                                   6    
HELIX    8 AA8 LEU A  138  ASP A  145  1                                   8    
HELIX    9 AA9 ASP A  145  MET A  151  1                                   7    
HELIX   10 AB1 MET A  151  ALA A  165  1                                  15    
HELIX   11 AB2 TRP A  171  GLN A  176  1                                   6    
HELIX   12 AB3 THR A  184  PHE A  188  5                                   5    
HELIX   13 AB4 GLU A  189  TYR A  195  1                                   7    
HELIX   14 AB5 ALA A  201  HIS A  226  1                                  26    
HELIX   15 AB6 LEU A  232  ASP A  236  5                                   5    
HELIX   16 AB7 THR A  239  GLN A  254  1                                  16    
HELIX   17 AB8 LEU A  272  CYS A  276  5                                   5    
HELIX   18 AB9 SER A  316  GLY A  325  1                                  10    
HELIX   19 AC1 LEU A  348  ALA A  359  1                                  12    
HELIX   20 AC2 SER A  377  CYS A  388  1                                  12    
HELIX   21 AC3 THR A  390  HIS A  397  1                                   8    
HELIX   22 AC4 SER A  402  THR A  409  1                                   8    
HELIX   23 AC5 SER A  418  LYS A  438  1                                  21    
HELIX   24 AC6 THR A  443  HIS A  454  1                                  12    
HELIX   25 AC7 SER A  457  LYS A  495  1                                  39    
SHEET    1 AA1 4 PHE A  95  PHE A 100  0                                        
SHEET    2 AA1 4 GLY A 104  ALA A 109 -1  O  GLY A 104   N  PHE A 100           
SHEET    3 AA1 4 GLN A 307  ILE A 310 -1  O  ILE A 308   N  LEU A 107           
SHEET    4 AA1 4 ASN A 277  HIS A 278  1  N  ASN A 277   O  ILE A 310           
SHEET    1 AA2 3 LEU A 118  PRO A 123  0                                        
SHEET    2 AA2 3 ARG A 293  VAL A 297 -1  O  CYS A 294   N  VAL A 122           
SHEET    3 AA2 3 THR A 285  ASN A 288 -1  N  ASN A 288   O  ARG A 293           
SHEET    1 AA3 3 MET A 128  THR A 129  0                                        
SHEET    2 AA3 3 VAL A 265  LEU A 269 -1  O  LEU A 269   N  MET A 128           
SHEET    3 AA3 3 ASN A 255  PRO A 258 -1  N  ILE A 257   O  THR A 266           
SHEET    1 AA4 2 ARG A 335  GLY A 341  0                                        
SHEET    2 AA4 2 SER A 364  HIS A 370 -1  O  PHE A 367   N  ILE A 338           
CISPEP   1 PRO A  227    HIS A  228          0        -1.43                     
CISPEP   2 GLU A  373    PRO A  374          0        -4.55                     
SITE     1 AC1 19 ARG A  74  GLU A 102  GLU A 103  PHE A 105                    
SITE     2 AC1 19 THR A 252  ARG A 253  ASP A 274  MET A 275                    
SITE     3 AC1 19 CYS A 276  ASN A 277  HIS A 278  TYR A 312                    
SITE     4 AC1 19 SER A 324  PHE A 326  EDO A1005  HOH A1135                    
SITE     5 AC1 19 HOH A1176  HOH A1202  HIS Y  73                               
SITE     1 AC2  7 PRO A  40  GLU A  45  GLU A  48  HIS A 203                    
SITE     2 AC2  7 SER A 207  EDO A1003  HOH A1153                               
SITE     1 AC3  5 SER A 207  LYS A 210  ASN A 211  ARG A 214                    
SITE     2 AC3  5 EDO A1002                                                     
SITE     1 AC4  6 PHE A  70  ARG A 164  ILE A 175  LEU A 178                    
SITE     2 AC4  6 SER A 180  HOH A1138                                          
SITE     1 AC5  3 GLU A 103  SAH A1001  HOH A1103                               
SITE     1 AC6  3 THR A 443  ILE A 444  HOH A1129                               
SITE     1 AC7  4 ASP A  80  LYS A  83  TRP A  84  GLU A  87                    
SITE     1 AC8  5 LEU A 340  GLY A 341  PHE A 408  ARG A 432                    
SITE     2 AC8  5 EDO A1010                                                     
SITE     1 AC9  5 ALA A  90  SER A  91  VAL A  92  GLU A  93                    
SITE     2 AC9  5 TRP A 121                                                     
SITE     1 AD1  6 LYS A 339  ILE A 404  ASP A 405  PHE A 408                    
SITE     2 AD1  6 ARG A 432  EDO A1008                                          
SITE     1 AD2  5 ASP A 334  PHE A 371  GLU A 472  ILE A 473                    
SITE     2 AD2  5 HOH A1168                                                     
CRYST1   56.557   92.830  111.635  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      0.017681  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010772  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008958        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system