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Database: PDB
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HEADER    TRANSFERASE/STRUCTURAL PROTEIN          30-AUG-18   6MBK              
TITLE     SETD3, A HISTIDINE METHYLTRANSFERASE, IN COMPLEX WITH AN ACTIN PEPTIDE
TITLE    2 AND SAH, FIRST P212121 CRYSTAL FORM                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACTIN PEPTIDE;                                             
COMPND   3 CHAIN: Y, Z;                                                         
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, B;                                                         
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;                            
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  13 EXPRESSION_SYSTEM_STRAIN: BL21                                       
KEYWDS    TRANSFERASE, TRANSFERASE-STRUCTURAL PROTEIN COMPLEX                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.R.HORTON,S.DAI,X.CHENG                                              
REVDAT   2   16-JAN-19 6MBK    1       JRNL                                     
REVDAT   1   19-DEC-18 6MBK    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.    1.69 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) : 1.69                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.73                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 135110                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.228                           
REMARK   3   R VALUE            (WORKING SET) : 0.228                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.480                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1996                            
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 37.7418 -  4.0716    0.98     9959   147  0.2239 0.1993        
REMARK   3     2  4.0716 -  3.2323    1.00     9787   148  0.2135 0.2557        
REMARK   3     3  3.2323 -  2.8239    1.00     9616   143  0.2246 0.2550        
REMARK   3     4  2.8239 -  2.5658    0.99     9602   144  0.2177 0.2045        
REMARK   3     5  2.5658 -  2.3819    0.99     9540   144  0.2173 0.2727        
REMARK   3     6  2.3819 -  2.2415    1.00     9533   143  0.2134 0.2173        
REMARK   3     7  2.2415 -  2.1293    1.00     9591   143  0.2138 0.2603        
REMARK   3     8  2.1293 -  2.0366    1.00     9546   144  0.2185 0.2540        
REMARK   3     9  2.0366 -  1.9582    0.98     9346   140  0.2325 0.2321        
REMARK   3    10  1.9582 -  1.8906    0.99     9448   141  0.2431 0.2791        
REMARK   3    11  1.8906 -  1.8315    0.99     9418   142  0.2654 0.2700        
REMARK   3    12  1.8315 -  1.7791    0.99     9405   141  0.2776 0.3102        
REMARK   3    13  1.7791 -  1.7323    0.99     9358   141  0.2955 0.2978        
REMARK   3    14  1.7323 -  1.6900    0.94     8965   135  0.3287 0.3770        
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)     : 0.180            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.360           
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      :  0.010           8556                                  
REMARK   3   ANGLE     :  0.942          11587                                  
REMARK   3   CHIRALITY :  0.057           1253                                  
REMARK   3   PLANARITY :  0.007           1478                                  
REMARK   3   DIHEDRAL  : 15.090           3231                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'Y' AND (RESID 66 THROUGH 80 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  30.7292 -10.1462 -20.0638              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1662 T22:   0.4454                                     
REMARK   3      T33:   0.1619 T12:  -0.1033                                     
REMARK   3      T13:  -0.0785 T23:  -0.0817                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1181 L22:   5.1050                                     
REMARK   3      L33:   4.8425 L12:   0.6856                                     
REMARK   3      L13:   2.7255 L23:   0.0787                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0906 S12:  -0.3782 S13:   0.0071                       
REMARK   3      S21:   0.5214 S22:  -0.1923 S23:  -0.2307                       
REMARK   3      S31:   0.0628 S32:   0.2643 S33:   0.1402                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 20 THROUGH 334 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  22.9779  -2.8684 -28.0793              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1873 T22:   0.2283                                     
REMARK   3      T33:   0.2110 T12:  -0.0964                                     
REMARK   3      T13:   0.0017 T23:  -0.1281                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1744 L22:   0.8004                                     
REMARK   3      L33:   0.9141 L12:   0.0436                                     
REMARK   3      L13:  -0.3189 L23:  -0.0772                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1045 S12:  -0.3412 S13:   0.1917                       
REMARK   3      S21:   0.0754 S22:  -0.0122 S23:  -0.0563                       
REMARK   3      S31:  -0.2403 S32:   0.2286 S33:  -0.0554                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 335 THROUGH 502 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  16.7263 -33.3266  -8.5311              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1489 T22:   0.1357                                     
REMARK   3      T33:   0.1628 T12:  -0.0289                                     
REMARK   3      T13:   0.0030 T23:  -0.0292                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0103 L22:   0.9308                                     
REMARK   3      L33:   3.5044 L12:  -0.9423                                     
REMARK   3      L13:   1.4713 L23:  -1.7474                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0428 S12:  -0.0727 S13:  -0.1397                       
REMARK   3      S21:  -0.1634 S22:   0.0661 S23:   0.0588                       
REMARK   3      S31:   0.3475 S32:  -0.1034 S33:  -0.0905                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'Z' AND (RESID 66 THROUGH 80 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.2030 -10.4077 -66.9869              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2042 T22:   0.4046                                     
REMARK   3      T33:   0.0089 T12:  -0.0145                                     
REMARK   3      T13:   0.0175 T23:  -0.1240                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4583 L22:   4.1744                                     
REMARK   3      L33:   4.2681 L12:   1.2216                                     
REMARK   3      L13:   2.0148 L23:   0.5202                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2216 S12:   0.3588 S13:  -0.1437                       
REMARK   3      S21:  -0.3394 S22:  -0.0355 S23:  -0.1640                       
REMARK   3      S31:   0.0845 S32:  -0.2789 S33:   0.1177                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 20 THROUGH 334 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):   7.3128  -2.9218 -58.7850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1718 T22:   0.2029                                     
REMARK   3      T33:   0.1454 T12:  -0.0104                                     
REMARK   3      T13:   0.0105 T23:  -0.0486                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2165 L22:   0.9981                                     
REMARK   3      L33:   1.2105 L12:   0.3691                                     
REMARK   3      L13:  -0.8797 L23:   0.0113                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1230 S12:   0.2701 S13:   0.2009                       
REMARK   3      S21:  -0.1604 S22:   0.0118 S23:   0.0876                       
REMARK   3      S31:  -0.1552 S32:  -0.1462 S33:  -0.1334                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 335 THROUGH 500 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  13.9748 -33.1170 -77.9716              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3358 T22:   0.2583                                     
REMARK   3      T33:   0.2379 T12:  -0.0188                                     
REMARK   3      T13:  -0.0518 T23:  -0.1463                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6673 L22:   0.6546                                     
REMARK   3      L33:   1.2829 L12:   0.5519                                     
REMARK   3      L13:   0.6846 L23:   1.0432                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0979 S12:   0.1520 S13:  -0.1139                       
REMARK   3      S21:   0.0250 S22:  -0.0849 S23:   0.0170                       
REMARK   3      S31:   0.2151 S32:   0.0498 S33:  -0.0606                       
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 6MBK 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_1000236434.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-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) : 1.0000                             
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   : 135382                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.690                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.380                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 19.20                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.69                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.75                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.90                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
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   (%): 43.61                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 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       30.13950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       86.79450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.98500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       86.79450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.13950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       57.98500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 3680 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 4090 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23550 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Z, B                                  
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     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 465     GLY B    -5                                                      
REMARK 465     PRO B    -4                                                      
REMARK 465     LEU B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     MET B     0                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     LYS B     2                                                      
REMARK 465     LYS B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     ARG B     5                                                      
REMARK 465     VAL B     6                                                      
REMARK 465     LYS B     7                                                      
REMARK 465     THR B     8                                                      
REMARK 465     GLN B     9                                                      
REMARK 465     LYS B    10                                                      
REMARK 465     SER B    11                                                      
REMARK 465     GLY B    12                                                      
REMARK 465     THR B    13                                                      
REMARK 465     GLY B    14                                                      
REMARK 465     ALA B    15                                                      
REMARK 465     THR B    16                                                      
REMARK 465     ALA B    17                                                      
REMARK 465     THR B    18                                                      
REMARK 465     VAL B    19                                                      
REMARK 465     TYR B   501                                                      
REMARK 465     GLU B   502                                                      
REMARK 465     GLU B   503                                                      
REMARK 465     SER B   504                                                      
REMARK 465     ASN B   505                                                      
REMARK 465     LEU B   506                                                      
REMARK 465     GLY B   507                                                      
REMARK 465     LEU B   508                                                      
REMARK 465     LEU B   509                                                      
REMARK 465     GLU B   510                                                      
REMARK 465     SER B   511                                                      
REMARK 465     SER B   512                                                      
REMARK 465     VAL B   513                                                      
REMARK 465     GLY B   514                                                      
REMARK 465     ASP B   515                                                      
REMARK 465     SER B   516                                                      
REMARK 465     ARG B   517                                                      
REMARK 465     LEU B   518                                                      
REMARK 465     PRO B   519                                                      
REMARK 465     LEU B   520                                                      
REMARK 465     VAL B   521                                                      
REMARK 465     LEU B   522                                                      
REMARK 465     ARG B   523                                                      
REMARK 465     ASN B   524                                                      
REMARK 465     LEU B   525                                                      
REMARK 465     GLU B   526                                                      
REMARK 465     GLU B   527                                                      
REMARK 465     GLU B   528                                                      
REMARK 465     ALA B   529                                                      
REMARK 465     GLY B   530                                                      
REMARK 465     VAL B   531                                                      
REMARK 465     GLN B   532                                                      
REMARK 465     ASP B   533                                                      
REMARK 465     ALA B   534                                                      
REMARK 465     LEU B   535                                                      
REMARK 465     ASN B   536                                                      
REMARK 465     ILE B   537                                                      
REMARK 465     ARG B   538                                                      
REMARK 465     GLU B   539                                                      
REMARK 465     ALA B   540                                                      
REMARK 465     ILE B   541                                                      
REMARK 465     SER B   542                                                      
REMARK 465     LYS B   543                                                      
REMARK 465     ALA B   544                                                      
REMARK 465     LYS B   545                                                      
REMARK 465     ALA B   546                                                      
REMARK 465     THR B   547                                                      
REMARK 465     GLU B   548                                                      
REMARK 465     ASN B   549                                                      
REMARK 465     GLY B   550                                                      
REMARK 465     LEU B   551                                                      
REMARK 465     VAL B   552                                                      
REMARK 465     ASN B   553                                                      
REMARK 465     GLY B   554                                                      
REMARK 465     GLU B   555                                                      
REMARK 465     ASN B   556                                                      
REMARK 465     SER B   557                                                      
REMARK 465     ILE B   558                                                      
REMARK 465     PRO B   559                                                      
REMARK 465     ASN B   560                                                      
REMARK 465     GLY B   561                                                      
REMARK 465     THR B   562                                                      
REMARK 465     ARG B   563                                                      
REMARK 465     SER B   564                                                      
REMARK 465     GLU B   565                                                      
REMARK 465     ASN B   566                                                      
REMARK 465     GLU B   567                                                      
REMARK 465     SER B   568                                                      
REMARK 465     LEU B   569                                                      
REMARK 465     ASN B   570                                                      
REMARK 465     GLN B   571                                                      
REMARK 465     GLU B   572                                                      
REMARK 465     SER B   573                                                      
REMARK 465     LYS B   574                                                      
REMARK 465     ARG B   575                                                      
REMARK 465     ALA B   576                                                      
REMARK 465     VAL B   577                                                      
REMARK 465     GLU B   578                                                      
REMARK 465     ASP B   579                                                      
REMARK 465     ALA B   580                                                      
REMARK 465     LYS B   581                                                      
REMARK 465     GLY B   582                                                      
REMARK 465     SER B   583                                                      
REMARK 465     SER B   584                                                      
REMARK 465     SER B   585                                                      
REMARK 465     ASP B   586                                                      
REMARK 465     SER B   587                                                      
REMARK 465     THR B   588                                                      
REMARK 465     ALA B   589                                                      
REMARK 465     GLY B   590                                                      
REMARK 465     VAL B   591                                                      
REMARK 465     LYS B   592                                                      
REMARK 465     GLU B   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     LYS A  22    CG   CD   CE   NZ                                   
REMARK 470     LYS B  22    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O4   SO4 B  1012     O    HOH B  1101              1.92            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A 116       -0.42     75.97                                   
REMARK 500    SER A 198        5.55     81.21                                   
REMARK 500    LEU A 272      -59.09     71.87                                   
REMARK 500    LEU B 272      -64.95     76.38                                   
REMARK 500    THR B 314       42.91    -81.83                                   
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 Z 115        DISTANCE =  6.11 ANGSTROMS                       
REMARK 525    HOH B1482        DISTANCE =  7.93 ANGSTROMS                       
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 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH B 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 1005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 1006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 1007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 1008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 1009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 1010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 1011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 1012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 1013                
DBREF  6MBK Y   66    80  UNP    P60709   ACTB_HUMAN      66     80             
DBREF  6MBK A    0   593  UNP    Q86TU7   SETD3_HUMAN      1    594             
DBREF  6MBK Z   66    80  UNP    P60709   ACTB_HUMAN      66     80             
DBREF  6MBK B    0   593  UNP    Q86TU7   SETD3_HUMAN      1    594             
SEQADV 6MBK GLY A   -5  UNP  Q86TU7              EXPRESSION TAG                 
SEQADV 6MBK PRO A   -4  UNP  Q86TU7              EXPRESSION TAG                 
SEQADV 6MBK LEU A   -3  UNP  Q86TU7              EXPRESSION TAG                 
SEQADV 6MBK GLY A   -2  UNP  Q86TU7              EXPRESSION TAG                 
SEQADV 6MBK SER A   -1  UNP  Q86TU7              EXPRESSION TAG                 
SEQADV 6MBK GLY B   -5  UNP  Q86TU7              EXPRESSION TAG                 
SEQADV 6MBK PRO B   -4  UNP  Q86TU7              EXPRESSION TAG                 
SEQADV 6MBK LEU B   -3  UNP  Q86TU7              EXPRESSION TAG                 
SEQADV 6MBK GLY B   -2  UNP  Q86TU7              EXPRESSION TAG                 
SEQADV 6MBK SER B   -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                                                          
SEQRES   1 Z   15  THR LEU LYS TYR PRO ILE GLU HIS GLY ILE VAL THR ASN          
SEQRES   2 Z   15  TRP ASP                                                      
SEQRES   1 B  599  GLY PRO LEU GLY SER MET GLY LYS LYS SER ARG VAL LYS          
SEQRES   2 B  599  THR GLN LYS SER GLY THR GLY ALA THR ALA THR VAL SER          
SEQRES   3 B  599  PRO LYS GLU ILE LEU ASN LEU THR SER GLU LEU LEU GLN          
SEQRES   4 B  599  LYS CYS SER SER PRO ALA PRO GLY PRO GLY LYS GLU TRP          
SEQRES   5 B  599  GLU GLU TYR VAL GLN ILE ARG THR LEU VAL GLU LYS ILE          
SEQRES   6 B  599  ARG LYS LYS GLN LYS GLY LEU SER VAL THR PHE ASP GLY          
SEQRES   7 B  599  LYS ARG GLU ASP TYR PHE PRO ASP LEU MET LYS TRP ALA          
SEQRES   8 B  599  SER GLU ASN GLY ALA SER VAL GLU GLY PHE GLU MET VAL          
SEQRES   9 B  599  ASN PHE LYS GLU GLU GLY PHE GLY LEU ARG ALA THR ARG          
SEQRES  10 B  599  ASP ILE LYS ALA GLU GLU LEU PHE LEU TRP VAL PRO ARG          
SEQRES  11 B  599  LYS LEU LEU MET THR VAL GLU SER ALA LYS ASN SER VAL          
SEQRES  12 B  599  LEU GLY PRO LEU TYR SER GLN ASP ARG ILE LEU GLN ALA          
SEQRES  13 B  599  MET GLY ASN ILE ALA LEU ALA PHE HIS LEU LEU CYS GLU          
SEQRES  14 B  599  ARG ALA SER PRO ASN SER PHE TRP GLN PRO TYR ILE GLN          
SEQRES  15 B  599  THR LEU PRO SER GLU TYR ASP THR PRO LEU TYR PHE GLU          
SEQRES  16 B  599  GLU ASP GLU VAL ARG TYR LEU GLN SER THR GLN ALA ILE          
SEQRES  17 B  599  HIS ASP VAL PHE SER GLN TYR LYS ASN THR ALA ARG GLN          
SEQRES  18 B  599  TYR ALA TYR PHE TYR LYS VAL ILE GLN THR HIS PRO HIS          
SEQRES  19 B  599  ALA ASN LYS LEU PRO LEU LYS ASP SER PHE THR TYR GLU          
SEQRES  20 B  599  ASP TYR ARG TRP ALA VAL SER SER VAL MET THR ARG GLN          
SEQRES  21 B  599  ASN GLN ILE PRO THR GLU ASP GLY SER ARG VAL THR LEU          
SEQRES  22 B  599  ALA LEU ILE PRO LEU TRP ASP MET CYS ASN HIS THR ASN          
SEQRES  23 B  599  GLY LEU ILE THR THR GLY TYR ASN LEU GLU ASP ASP ARG          
SEQRES  24 B  599  CYS GLU CYS VAL ALA LEU GLN ASP PHE ARG ALA GLY GLU          
SEQRES  25 B  599  GLN ILE TYR ILE PHE TYR GLY THR ARG SER ASN ALA GLU          
SEQRES  26 B  599  PHE VAL ILE HIS SER GLY PHE PHE PHE ASP ASN ASN SER          
SEQRES  27 B  599  HIS ASP ARG VAL LYS ILE LYS LEU GLY VAL SER LYS SER          
SEQRES  28 B  599  ASP ARG LEU TYR ALA MET LYS ALA GLU VAL LEU ALA ARG          
SEQRES  29 B  599  ALA GLY ILE PRO THR SER SER VAL PHE ALA LEU HIS PHE          
SEQRES  30 B  599  THR GLU PRO PRO ILE SER ALA GLN LEU LEU ALA PHE LEU          
SEQRES  31 B  599  ARG VAL PHE CYS MET THR GLU GLU GLU LEU LYS GLU HIS          
SEQRES  32 B  599  LEU LEU GLY ASP SER ALA ILE ASP ARG ILE PHE THR LEU          
SEQRES  33 B  599  GLY ASN SER GLU PHE PRO VAL SER TRP ASP ASN GLU VAL          
SEQRES  34 B  599  LYS LEU TRP THR PHE LEU GLU ASP ARG ALA SER LEU LEU          
SEQRES  35 B  599  LEU LYS THR TYR LYS THR THR ILE GLU GLU ASP LYS SER          
SEQRES  36 B  599  VAL LEU LYS ASN HIS ASP LEU SER VAL ARG ALA LYS MET          
SEQRES  37 B  599  ALA ILE LYS LEU ARG LEU GLY GLU LYS GLU ILE LEU GLU          
SEQRES  38 B  599  LYS ALA VAL LYS SER ALA ALA VAL ASN ARG GLU TYR TYR          
SEQRES  39 B  599  ARG GLN GLN MET GLU GLU LYS ALA PRO LEU PRO LYS TYR          
SEQRES  40 B  599  GLU GLU SER ASN LEU GLY LEU LEU GLU SER SER VAL GLY          
SEQRES  41 B  599  ASP SER ARG LEU PRO LEU VAL LEU ARG ASN LEU GLU GLU          
SEQRES  42 B  599  GLU ALA GLY VAL GLN ASP ALA LEU ASN ILE ARG GLU ALA          
SEQRES  43 B  599  ILE SER LYS ALA LYS ALA THR GLU ASN GLY LEU VAL ASN          
SEQRES  44 B  599  GLY GLU ASN SER ILE PRO ASN GLY THR ARG SER GLU ASN          
SEQRES  45 B  599  GLU SER LEU ASN GLN GLU SER LYS ARG ALA VAL GLU ASP          
SEQRES  46 B  599  ALA LYS GLY SER SER SER ASP SER THR ALA GLY VAL LYS          
SEQRES  47 B  599  GLU                                                          
HET    SAH  A 601      26                                                       
HET    EDO  A 602       4                                                       
HET    EDO  A 603       4                                                       
HET    EDO  A 604       4                                                       
HET    EDO  A 605       4                                                       
HET    EDO  A 606       4                                                       
HET    EDO  A 607       4                                                       
HET    GOL  A 608       6                                                       
HET    GOL  A 609       6                                                       
HET    SO4  A 610       5                                                       
HET    SO4  A 611       5                                                       
HET    SAH  B1001      26                                                       
HET    EDO  B1002       4                                                       
HET    EDO  B1003       4                                                       
HET    EDO  B1004       4                                                       
HET    EDO  B1005       4                                                       
HET    EDO  B1006       4                                                       
HET    EDO  B1007       4                                                       
HET    EDO  B1008       4                                                       
HET    EDO  B1009       4                                                       
HET    GOL  B1010       6                                                       
HET    GOL  B1011       6                                                       
HET    SO4  B1012       5                                                       
HET    SO4  B1013       5                                                       
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     GOL GLYCEROL                                                         
HETNAM     SO4 SULFATE ION                                                      
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  SAH    2(C14 H20 N6 O5 S)                                           
FORMUL   6  EDO    14(C2 H6 O2)                                                 
FORMUL  12  GOL    4(C3 H8 O3)                                                  
FORMUL  14  SO4    4(O4 S 2-)                                                   
FORMUL  29  HOH   *833(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  SER A  143  1                                   6    
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 PRO A  227  ASN A  230  5                                   4    
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  LEU A  399  1                                  10    
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    
HELIX   26 AC8 PRO B   21  SER B   36  1                                  16    
HELIX   27 AC9 GLY B   41  GLY B   43  5                                   3    
HELIX   28 AD1 LYS B   44  LYS B   62  1                                  19    
HELIX   29 AD2 LYS B   73  ASP B   76  5                                   4    
HELIX   30 AD3 TYR B   77  ASN B   88  1                                  12    
HELIX   31 AD4 LYS B  125  LEU B  127  5                                   3    
HELIX   32 AD5 VAL B  130  ASN B  135  1                                   6    
HELIX   33 AD6 LEU B  138  ASP B  145  1                                   8    
HELIX   34 AD7 ASP B  145  MET B  151  1                                   7    
HELIX   35 AD8 MET B  151  ALA B  165  1                                  15    
HELIX   36 AD9 TRP B  171  GLN B  176  1                                   6    
HELIX   37 AE1 THR B  184  PHE B  188  5                                   5    
HELIX   38 AE2 GLU B  189  TYR B  195  1                                   7    
HELIX   39 AE3 ALA B  201  HIS B  226  1                                  26    
HELIX   40 AE4 PRO B  227  ASN B  230  5                                   4    
HELIX   41 AE5 LEU B  232  ASP B  236  5                                   5    
HELIX   42 AE6 THR B  239  GLN B  254  1                                  16    
HELIX   43 AE7 LEU B  272  CYS B  276  5                                   5    
HELIX   44 AE8 SER B  316  GLY B  325  1                                  10    
HELIX   45 AE9 LEU B  348  GLY B  360  1                                  13    
HELIX   46 AF1 SER B  377  CYS B  388  1                                  12    
HELIX   47 AF2 THR B  390  LEU B  399  1                                  10    
HELIX   48 AF3 SER B  402  THR B  409  1                                   8    
HELIX   49 AF4 SER B  418  LYS B  438  1                                  21    
HELIX   50 AF5 THR B  443  HIS B  454  1                                  12    
HELIX   51 AF6 SER B  457  LYS B  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  ARG A 108   N  GLU A  96           
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 296   N  LEU A 120           
SHEET    3 AA2 3 THR A 285  ASN A 288 -1  N  GLY A 286   O  GLU A 295           
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           
SHEET    1 AA5 4 PHE B  95  PHE B 100  0                                        
SHEET    2 AA5 4 GLY B 104  ALA B 109 -1  O  ARG B 108   N  GLU B  96           
SHEET    3 AA5 4 GLN B 307  ILE B 310 -1  O  ILE B 308   N  LEU B 107           
SHEET    4 AA5 4 ASN B 277  HIS B 278  1  N  ASN B 277   O  ILE B 310           
SHEET    1 AA6 3 LEU B 118  PRO B 123  0                                        
SHEET    2 AA6 3 ARG B 293  VAL B 297 -1  O  CYS B 296   N  LEU B 120           
SHEET    3 AA6 3 THR B 285  ASN B 288 -1  N  GLY B 286   O  GLU B 295           
SHEET    1 AA7 3 MET B 128  THR B 129  0                                        
SHEET    2 AA7 3 VAL B 265  LEU B 269 -1  O  LEU B 269   N  MET B 128           
SHEET    3 AA7 3 ASN B 255  PRO B 258 -1  N  ILE B 257   O  THR B 266           
SHEET    1 AA8 2 ARG B 335  GLY B 341  0                                        
SHEET    2 AA8 2 SER B 364  HIS B 370 -1  O  PHE B 367   N  ILE B 338           
CISPEP   1 GLU A  373    PRO A  374          0        -3.48                     
CISPEP   2 GLU B  373    PRO B  374          0        -5.25                     
SITE     1 AC1 21 ARG A  74  GLU A 102  GLU A 103  PHE A 105                    
SITE     2 AC1 21 PRO A 179  THR A 252  ARG A 253  ASP A 274                    
SITE     3 AC1 21 MET A 275  CYS A 276  ASN A 277  HIS A 278                    
SITE     4 AC1 21 TYR A 312  SER A 324  PHE A 326  GOL A 609                    
SITE     5 AC1 21 HOH A 764  HOH A 782  HOH A 935  HOH A 944                    
SITE     6 AC1 21 HIS Y  73                                                     
SITE     1 AC2  6 PRO A  42  GLU A  45  ILE A 202  HOH A 787                    
SITE     2 AC2  6 HOH A 840  HOH A 907                                          
SITE     1 AC3  9 PRO A  42  GLY A  43  LEU A 399  GLY A 400                    
SITE     2 AC3  9 ASP A 401  SER A 402  ALA A 403  ARG A 406                    
SITE     3 AC3  9 HOH A 704                                                     
SITE     1 AC4  8 LYS A  64  GLY A  65  LEU A  66  HOH A 703                    
SITE     2 AC4  8 HOH A 707  HOH A 977  ASP B  71  LYS B  73                    
SITE     1 AC5  3 ASN A 135  HOH A 731  HOH A 838                               
SITE     1 AC6  7 PRO A  40  GLU A  45  GLU A  48  HIS A 203                    
SITE     2 AC6  7 SER A 207  LYS A 210  HOH A 717                               
SITE     1 AC7  4 VAL A 458  LYS A 461  LYS A 465  HOH A 982                    
SITE     1 AC8 10 ASN A 317  PHE A 327  ASP A 334  PHE A 371                    
SITE     2 AC8 10 GLY A 469  GLU A 472  HOH A 763  HOH A 793                    
SITE     3 AC8 10 HOH A 900  HOH A 966                                          
SITE     1 AC9  8 GLU A 103  PRO A 179  GLU A 181  TYR A 182                    
SITE     2 AC9  8 SAH A 601  HOH A 748  HOH A 842  HOH A 908                    
SITE     1 AD1  5 ARG A 194  GLN A 197  LYS A 441  HOH A 752                    
SITE     2 AD1  5 HOH A 955                                                     
SITE     1 AD2  7 PHE A 367  ALA A 368  HIS A 370  SER A 377                    
SITE     2 AD2  7 GLN A 379  HOH A 712  HOH A 718                               
SITE     1 AD3 23 ARG B  74  GLU B 102  GLU B 103  PHE B 105                    
SITE     2 AD3 23 PRO B 179  THR B 252  ARG B 253  ASP B 274                    
SITE     3 AD3 23 MET B 275  CYS B 276  ASN B 277  HIS B 278                    
SITE     4 AD3 23 TYR B 312  SER B 324  PHE B 326  HOH B1113                    
SITE     5 AD3 23 HOH B1253  HOH B1264  HOH B1290  HOH B1306                    
SITE     6 AD3 23 HOH B1308  HOH B1358  HIS Z  73                               
SITE     1 AD4  8 PRO B  42  GLU B  45  ILE B 202  PHE B 206                    
SITE     2 AD4  8 EDO B1008  HOH B1115  HOH B1168  HOH B1257                    
SITE     1 AD5  2 VAL B 297  HOH B1341                                          
SITE     1 AD6  8 PHE B  70  ARG B 164  ILE B 175  GLN B 176                    
SITE     2 AD6  8 LEU B 178  PRO B 179  SER B 180  HOH B1231                    
SITE     1 AD7  1 ASN B 484                                                     
SITE     1 AD8  3 ASP B  76  TYR B  77  ASP B  80                               
SITE     1 AD9  6 ASP B 334  PHE B 371  GLY B 469  GLU B 472                    
SITE     2 AD9  6 ILE B 473  HOH B1224                                          
SITE     1 AE1 10 PRO B  42  GLY B  43  LEU B 399  GLY B 400                    
SITE     2 AE1 10 ASP B 401  SER B 402  ALA B 403  ARG B 406                    
SITE     3 AE1 10 EDO B1002  HOH B1106                                          
SITE     1 AE2  6 GLN B 200  LYS B 337  LYS B 339  LEU B 436                    
SITE     2 AE2  6 HOH B1198  HOH B1222                                          
SITE     1 AE3  3 HIS B 203  ASP B 401  HOH B1144                               
SITE     1 AE4  9 HIS B 370  PHE B 371  THR B 372  GLU B 373                    
SITE     2 AE4  9 PRO B 375  LYS B 476  ALA B 477  SER B 480                    
SITE     3 AE4  9 HOH B1136                                                     
SITE     1 AE5  9 PHE B 367  ALA B 368  HIS B 370  SER B 377                    
SITE     2 AE5  9 GLN B 379  HOH B1101  HOH B1110  HOH B1128                    
SITE     3 AE5  9 HOH B1133                                                     
SITE     1 AE6  3 ARG B 194  LYS B 441  HOH B1163                               
CRYST1   60.279  115.970  173.589  90.00  90.00  90.00 P 21 21 21    8          
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      0.016590  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008623  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005761        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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