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Database: PDB
Entry: 6BRR
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Original site: 6BRR 
HEADER    TRANSFERASE/DNA                         30-NOV-17   6BRR              
TITLE     CRYSTAL STRUCTURE OF DNMT3A (R836A)-DNMT3L IN COMPLEX WITH DNA        
TITLE    2 CONTAINING TWO CPG SITES                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA (CYTOSINE-5)-METHYLTRANSFERASE 3A;                     
COMPND   3 CHAIN: A, D;                                                         
COMPND   4 SYNONYM: DNMT3A,DNA METHYLTRANSFERASE HSAIIIA,M.HSAIIIA;             
COMPND   5 EC: 2.1.1.37;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: DNA (CYTOSINE-5)-METHYLTRANSFERASE 3-LIKE;                 
COMPND  10 CHAIN: B, C;                                                         
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: DNA (25-MER);                                              
COMPND  14 CHAIN: E, F;                                                         
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: DNMT3A;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: DNMT3L;                                                        
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 SYNTHETIC: YES;                                                      
SOURCE  19 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  20 ORGANISM_TAXID: 9606                                                 
KEYWDS    DNMT3A, DNMT3L, DNA METHYLATION, TRANSFERASE-DNA COMPLEX              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.M.ZHANG,J.SONG                                                      
REVDAT   2   23-MAY-18 6BRR    1       JRNL                                     
REVDAT   1   31-JAN-18 6BRR    0                                                
JRNL        AUTH   Z.M.ZHANG,R.LU,P.WANG,Y.YU,D.CHEN,L.GAO,S.LIU,D.JI,          
JRNL        AUTH 2 S.B.ROTHBART,Y.WANG,G.G.WANG,J.SONG                          
JRNL        TITL   STRUCTURAL BASIS FOR DNMT3A-MEDIATED DE NOVO DNA             
JRNL        TITL 2 METHYLATION.                                                 
JRNL        REF    NATURE                        V. 554   387 2018              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   29414941                                                     
JRNL        DOI    10.1038/NATURE25477                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.97 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.97                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.96                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.960                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 28270                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.050                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1994                            
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 19.9550 -  7.0590    0.95     1829   137  0.1631 0.1960        
REMARK   3     2  7.0590 -  5.6447    0.98     1878   138  0.2030 0.2395        
REMARK   3     3  5.6447 -  4.9436    0.97     1840   140  0.1882 0.2539        
REMARK   3     4  4.9436 -  4.4972    0.98     1875   143  0.1731 0.2252        
REMARK   3     5  4.4972 -  4.1781    0.98     1880   146  0.1727 0.2007        
REMARK   3     6  4.1781 -  3.9337    0.99     1870   145  0.1888 0.2474        
REMARK   3     7  3.9337 -  3.7381    0.99     1910   145  0.2013 0.2328        
REMARK   3     8  3.7381 -  3.5763    0.99     1876   144  0.2150 0.2732        
REMARK   3     9  3.5763 -  3.4393    0.99     1904   146  0.2332 0.2714        
REMARK   3    10  3.4393 -  3.3212    0.97     1860   143  0.2409 0.2970        
REMARK   3    11  3.3212 -  3.2178    0.99     1893   143  0.2753 0.3082        
REMARK   3    12  3.2178 -  3.1262    0.99     1903   141  0.3057 0.3401        
REMARK   3    13  3.1262 -  3.0442    0.99     1910   148  0.3154 0.3732        
REMARK   3    14  3.0442 -  2.9701    0.97     1848   135  0.3310 0.3436        
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)     : 0.430            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.440           
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           8574                                  
REMARK   3   ANGLE     :  0.665          11868                                  
REMARK   3   CHIRALITY :  0.028           1305                                  
REMARK   3   PLANARITY :  0.003           1352                                  
REMARK   3   DIHEDRAL  : 19.869           3154                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 28                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 628 THROUGH 656 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -13.8993 -80.3761  19.8529              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9777 T22:   0.7918                                     
REMARK   3      T33:   0.9811 T12:  -0.0238                                     
REMARK   3      T13:   0.0348 T23:  -0.0316                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7149 L22:   4.8520                                     
REMARK   3      L33:   1.9607 L12:  -2.3197                                     
REMARK   3      L13:  -0.2886 L23:   2.3306                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0174 S12:   0.1802 S13:  -1.0117                       
REMARK   3      S21:   0.2422 S22:   0.0546 S23:   0.5747                       
REMARK   3      S31:   0.8185 S32:  -0.5450 S33:   0.2607                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 657 THROUGH 784 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.2697 -76.5750  13.2259              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6738 T22:   0.7387                                     
REMARK   3      T33:   0.7385 T12:   0.1120                                     
REMARK   3      T13:  -0.0336 T23:   0.0053                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9350 L22:   3.3055                                     
REMARK   3      L33:   4.2792 L12:  -0.4317                                     
REMARK   3      L13:  -0.4519 L23:   0.4309                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1679 S12:   0.4914 S13:  -0.5705                       
REMARK   3      S21:  -0.1331 S22:  -0.2232 S23:  -0.4054                       
REMARK   3      S31:   0.5590 S32:   0.5556 S33:   0.0652                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 785 THROUGH 852 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -17.8383 -63.9524   1.8312              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7212 T22:   1.0431                                     
REMARK   3      T33:   0.7248 T12:   0.1401                                     
REMARK   3      T13:  -0.0165 T23:  -0.0477                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9786 L22:   4.2991                                     
REMARK   3      L33:   3.8750 L12:  -2.5993                                     
REMARK   3      L13:   0.1914 L23:   1.7722                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5310 S12:   1.3599 S13:  -0.1258                       
REMARK   3      S21:  -0.8776 S22:  -0.6355 S23:   0.3827                       
REMARK   3      S31:  -0.0517 S32:  -0.3503 S33:   0.0555                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 853 THROUGH 912 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -16.5476 -65.0324  12.4621              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6172 T22:   0.8764                                     
REMARK   3      T33:   0.5488 T12:  -0.0293                                     
REMARK   3      T13:  -0.0113 T23:  -0.0113                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7167 L22:   4.6042                                     
REMARK   3      L33:   3.0949 L12:  -0.8080                                     
REMARK   3      L13:  -0.8133 L23:   0.1433                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3046 S12:   0.3221 S13:   0.0389                       
REMARK   3      S21:  -0.0617 S22:  -0.2215 S23:   0.1252                       
REMARK   3      S31:   0.1597 S32:  -0.1430 S33:   0.0033                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 179 THROUGH 191 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  26.0940-107.5216  14.4607              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9228 T22:   1.4077                                     
REMARK   3      T33:   1.7141 T12:   0.6779                                     
REMARK   3      T13:  -0.3285 T23:  -0.0603                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5256 L22:   4.4415                                     
REMARK   3      L33:   2.8225 L12:  -2.2615                                     
REMARK   3      L13:   1.5516 L23:  -0.1500                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2314 S12:   0.5673 S13:  -1.8346                       
REMARK   3      S21:   1.7551 S22:  -0.1635 S23:  -0.2574                       
REMARK   3      S31:   2.3853 S32:   1.5055 S33:  -0.0765                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 192 THROUGH 205 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  28.4624 -90.8240   3.9043              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9584 T22:   1.7517                                     
REMARK   3      T33:   1.6080 T12:   0.5571                                     
REMARK   3      T13:   0.0089 T23:   0.1979                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5757 L22:   3.4465                                     
REMARK   3      L33:   3.7743 L12:   1.3370                                     
REMARK   3      L13:   0.2520 L23:   1.2137                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.8865 S12:   1.1053 S13:   0.3254                       
REMARK   3      S21:  -0.3187 S22:  -0.9991 S23:  -1.7662                       
REMARK   3      S31:   1.4155 S32:   2.7445 S33:   0.0238                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 206 THROUGH 311 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  19.5763 -86.6278   8.5643              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7381 T22:   1.1196                                     
REMARK   3      T33:   1.1858 T12:   0.2241                                     
REMARK   3      T13:   0.0348 T23:   0.0449                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0897 L22:   4.9443                                     
REMARK   3      L33:   3.4933 L12:  -1.6881                                     
REMARK   3      L13:   0.1268 L23:   0.4292                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2551 S12:   0.2980 S13:  -0.3682                       
REMARK   3      S21:  -0.4106 S22:  -0.4855 S23:  -0.3774                       
REMARK   3      S31:   0.3175 S32:   0.4557 S33:   0.3797                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 312 THROUGH 325 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  32.4517 -79.5985  16.5076              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7668 T22:   1.8396                                     
REMARK   3      T33:   1.6155 T12:   0.2505                                     
REMARK   3      T13:  -0.0912 T23:   0.1077                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.2595 L22:   2.4069                                     
REMARK   3      L33:   7.5513 L12:   4.4442                                     
REMARK   3      L13:   8.3100 L23:   3.9543                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2016 S12:   1.1990 S13:  -1.3193                       
REMARK   3      S21:   1.1782 S22:  -0.0052 S23:   0.2728                       
REMARK   3      S31:  -0.4687 S32:   1.9979 S33:  -0.1684                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 326 THROUGH 349 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  31.7555 -78.7711  20.2921              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3801 T22:   1.2913                                     
REMARK   3      T33:   1.6441 T12:  -0.0868                                     
REMARK   3      T13:  -0.0672 T23:   0.3650                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8921 L22:   2.2655                                     
REMARK   3      L33:   0.2326 L12:   0.6460                                     
REMARK   3      L13:   0.4350 L23:   0.5730                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2965 S12:   0.1065 S13:  -0.0028                       
REMARK   3      S21:   0.0768 S22:  -0.0193 S23:  -0.8948                       
REMARK   3      S31:   0.1044 S32:   0.4956 S33:   0.4493                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 350 THROUGH 379 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  33.9301 -92.2453  12.0676              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3262 T22:   1.3991                                     
REMARK   3      T33:   1.5192 T12:   0.2966                                     
REMARK   3      T13:   0.0361 T23:   0.2716                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6494 L22:   4.2295                                     
REMARK   3      L33:   0.4017 L12:  -3.6401                                     
REMARK   3      L13:   0.5382 L23:  -0.2759                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2308 S12:   0.4037 S13:  -0.2273                       
REMARK   3      S21:  -0.0338 S22:   0.0591 S23:  -0.8071                       
REMARK   3      S31:   0.2304 S32:   0.9118 S33:   0.2566                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 628 THROUGH 698 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -38.9739 -40.7836  18.9241              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7780 T22:   0.6978                                     
REMARK   3      T33:   0.6631 T12:   0.0286                                     
REMARK   3      T13:   0.0830 T23:  -0.0325                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7041 L22:   2.2471                                     
REMARK   3      L33:   2.9996 L12:  -1.1165                                     
REMARK   3      L13:   0.1716 L23:   0.4926                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2097 S12:   0.1962 S13:   0.2119                       
REMARK   3      S21:  -0.1031 S22:   0.0091 S23:   0.0056                       
REMARK   3      S31:  -0.3866 S32:  -0.3301 S33:  -0.0675                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 699 THROUGH 762 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -35.6231 -29.0826  28.6289              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0990 T22:   0.6765                                     
REMARK   3      T33:   0.9774 T12:   0.0391                                     
REMARK   3      T13:   0.1221 T23:  -0.0444                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5524 L22:   1.9938                                     
REMARK   3      L33:   2.1830 L12:  -0.2645                                     
REMARK   3      L13:   0.8794 L23:   0.3341                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0656 S12:  -0.1263 S13:   1.1216                       
REMARK   3      S21:   0.1485 S22:  -0.1013 S23:  -0.1068                       
REMARK   3      S31:  -0.6912 S32:  -0.0379 S33:   0.0558                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 763 THROUGH 784 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -33.5975 -29.5108  39.3048              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3396 T22:   0.8942                                     
REMARK   3      T33:   0.9375 T12:   0.0406                                     
REMARK   3      T13:   0.1274 T23:  -0.1824                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2372 L22:   1.3101                                     
REMARK   3      L33:   1.2031 L12:  -2.2054                                     
REMARK   3      L13:   2.5525 L23:  -1.4270                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.9817 S12:  -0.6918 S13:   0.3490                       
REMARK   3      S21:   1.7133 S22:   1.0909 S23:   0.1596                       
REMARK   3      S31:  -1.1111 S32:  -0.3564 S33:   0.0151                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 785 THROUGH 818 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -31.8799 -46.2561  39.4425              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9982 T22:   0.8464                                     
REMARK   3      T33:   0.8399 T12:  -0.1024                                     
REMARK   3      T13:   0.0356 T23:  -0.1026                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7703 L22:   2.1236                                     
REMARK   3      L33:   2.4467 L12:  -3.0327                                     
REMARK   3      L13:   0.5595 L23:  -1.5423                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1829 S12:  -0.2446 S13:  -0.2364                       
REMARK   3      S21:   0.3877 S22:   0.2544 S23:   0.5738                       
REMARK   3      S31:  -0.3626 S32:  -0.2214 S33:  -0.0889                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 819 THROUGH 857 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -11.6919 -51.1528  36.7867              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8965 T22:   0.9076                                     
REMARK   3      T33:   0.9617 T12:  -0.1051                                     
REMARK   3      T13:  -0.0568 T23:  -0.1353                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3437 L22:   4.0566                                     
REMARK   3      L33:   2.8997 L12:  -0.3304                                     
REMARK   3      L13:  -0.1900 L23:  -1.1123                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1935 S12:  -0.3768 S13:   0.2218                       
REMARK   3      S21:   0.6765 S22:   0.1409 S23:  -1.1763                       
REMARK   3      S31:  -0.2145 S32:   0.4052 S33:  -0.0566                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 858 THROUGH 912 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -28.1416 -48.2280  27.7322              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7244 T22:   0.6278                                     
REMARK   3      T33:   0.5918 T12:  -0.0371                                     
REMARK   3      T13:   0.0351 T23:  -0.0917                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2451 L22:   3.0367                                     
REMARK   3      L33:   1.9393 L12:  -2.1267                                     
REMARK   3      L13:   1.2132 L23:   0.7309                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0093 S12:  -0.3931 S13:   0.1678                       
REMARK   3      S21:   0.2025 S22:   0.1120 S23:  -0.1238                       
REMARK   3      S31:  -0.5047 S32:  -0.1254 S33:  -0.0288                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 186 THROUGH 201 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -48.4331  -1.1008  30.4658              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7798 T22:   1.0115                                     
REMARK   3      T33:   2.1840 T12:   0.3105                                     
REMARK   3      T13:   0.0016 T23:  -0.1830                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6778 L22:   1.0454                                     
REMARK   3      L33:   1.3398 L12:  -0.7500                                     
REMARK   3      L13:   0.9156 L23:  -1.1352                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4569 S12:  -0.6000 S13:   1.8072                       
REMARK   3      S21:  -0.3325 S22:  -0.0635 S23:  -0.3328                       
REMARK   3      S31:  -1.0728 S32:  -0.3166 S33:   0.0233                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 202 THROUGH 309 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -41.2251  -9.3719  27.0729              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2954 T22:   0.6690                                     
REMARK   3      T33:   1.6183 T12:   0.1674                                     
REMARK   3      T13:   0.2379 T23:  -0.0029                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9251 L22:   3.4478                                     
REMARK   3      L33:   3.9438 L12:   0.0745                                     
REMARK   3      L13:   0.4783 L23:   0.4147                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2480 S12:   0.0516 S13:   1.3769                       
REMARK   3      S21:   0.1624 S22:   0.2397 S23:   0.1257                       
REMARK   3      S31:  -0.8202 S32:  -0.2130 S33:  -0.2483                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 310 THROUGH 325 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -34.8205  -0.6597  14.9841              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7204 T22:   0.8963                                     
REMARK   3      T33:   2.1158 T12:   0.1526                                     
REMARK   3      T13:   0.5946 T23:   0.3272                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9351 L22:   2.0145                                     
REMARK   3      L33:   4.7392 L12:   2.0476                                     
REMARK   3      L13:   1.9908 L23:  -7.3803                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7131 S12:  -0.1278 S13:   1.1476                       
REMARK   3      S21:   0.1098 S22:   0.5087 S23:   2.5611                       
REMARK   3      S31:   0.0743 S32:   2.2213 S33:  -1.5232                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 326 THROUGH 339 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -43.3438  -2.2435  10.2538              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8447 T22:   2.0105                                     
REMARK   3      T33:   1.4383 T12:   0.2515                                     
REMARK   3      T13:   0.4478 T23:   0.0972                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7387 L22:   8.8209                                     
REMARK   3      L33:   7.2422 L12:  -3.1033                                     
REMARK   3      L13:   5.6270 L23:  -2.3562                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3895 S12:   2.3575 S13:   1.0500                       
REMARK   3      S21:  -0.7232 S22:   1.4001 S23:   0.2907                       
REMARK   3      S31:  -2.3651 S32:  -1.7831 S33:  -0.2324                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 340 THROUGH 348 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -24.1171  -1.6071  10.9318              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.0275 T22:   1.1140                                     
REMARK   3      T33:   1.7129 T12:  -0.1122                                     
REMARK   3      T13:   0.5140 T23:   0.4381                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8931 L22:   8.4845                                     
REMARK   3      L33:   0.8664 L12:   6.4047                                     
REMARK   3      L13:  -2.0482 L23:  -2.6009                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.0172 S12:   1.3342 S13:   0.4724                       
REMARK   3      S21:  -0.0590 S22:  -0.0753 S23:  -1.2682                       
REMARK   3      S31:  -1.4707 S32:   0.0267 S33:  -0.3637                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 349 THROUGH 378 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -43.0755   4.0348  20.7668              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9186 T22:   0.9448                                     
REMARK   3      T33:   1.7047 T12:   0.2207                                     
REMARK   3      T13:   0.4063 T23:  -0.0148                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3120 L22:   2.3070                                     
REMARK   3      L33:   1.5957 L12:  -1.8346                                     
REMARK   3      L13:   0.9687 L23:  -1.0474                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4747 S12:  -0.8691 S13:  -1.3710                       
REMARK   3      S21:  -0.6819 S22:  -0.1676 S23:  -0.5462                       
REMARK   3      S31:  -0.6187 S32:  -0.2232 S33:  -0.2850                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 422 THROUGH 426 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -15.8014 -33.7029  47.5066              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7237 T22:   1.4885                                     
REMARK   3      T33:   1.4319 T12:  -0.1098                                     
REMARK   3      T13:  -0.2320 T23:  -0.3247                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9464 L22:   0.3566                                     
REMARK   3      L33:   0.2636 L12:   0.0015                                     
REMARK   3      L13:  -0.0713 L23:   0.4264                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   2.2031 S12:  -2.4194 S13:   0.5092                       
REMARK   3      S21:   1.1819 S22:   1.4519 S23:  -1.3265                       
REMARK   3      S31:  -0.1243 S32:   0.3542 S33:  -0.3375                       
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 428 THROUGH 435 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.9897 -36.3326  23.9749              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0499 T22:   1.1809                                     
REMARK   3      T33:   1.5533 T12:  -0.2239                                     
REMARK   3      T13:   0.1324 T23:   0.0331                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4294 L22:   0.7902                                     
REMARK   3      L33:  -0.1669 L12:  -0.8117                                     
REMARK   3      L13:  -0.4066 L23:   0.4302                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6062 S12:  -0.1140 S13:   0.9490                       
REMARK   3      S21:  -0.1671 S22:  -0.0416 S23:  -1.1553                       
REMARK   3      S31:  -0.5230 S32:   0.4106 S33:  -0.3663                       
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 436 THROUGH 440 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.3271 -46.9435   5.8017              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0576 T22:   1.4577                                     
REMARK   3      T33:   1.1661 T12:  -0.0573                                     
REMARK   3      T13:   0.1847 T23:   0.1574                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1773 L22:   1.5928                                     
REMARK   3      L33:   7.7849 L12:  -0.5314                                     
REMARK   3      L13:  -2.9604 L23:   2.5053                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.1657 S12:   0.7431 S13:   0.7864                       
REMARK   3      S21:  -0.2615 S22:   0.0091 S23:  -0.6175                       
REMARK   3      S31:  -0.9293 S32:   0.4538 S33:  -0.7713                       
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 441 THROUGH 446 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   2.0133 -60.8387  -7.8463              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3647 T22:   1.7475                                     
REMARK   3      T33:   1.3003 T12:   0.2584                                     
REMARK   3      T13:   0.1471 T23:   0.0510                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6272 L22:   6.5576                                     
REMARK   3      L33:   5.5665 L12:  -4.4931                                     
REMARK   3      L13:  -1.1622 L23:   0.6016                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6631 S12:   0.4818 S13:   0.6052                       
REMARK   3      S21:  -2.1039 S22:  -0.3429 S23:   0.4051                       
REMARK   3      S31:  -0.2206 S32:   0.0342 S33:  -0.6246                       
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 422 THROUGH 433 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.8795 -55.1659  -1.2477              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7786 T22:   1.1532                                     
REMARK   3      T33:   1.0323 T12:   0.0752                                     
REMARK   3      T13:   0.2088 T23:   0.2061                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2527 L22:   4.3092                                     
REMARK   3      L33:   5.4086 L12:  -1.6416                                     
REMARK   3      L13:  -3.4310 L23:  -1.4528                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2617 S12:   0.8275 S13:   0.7751                       
REMARK   3      S21:  -0.3293 S22:  -0.5027 S23:  -0.4624                       
REMARK   3      S31:  -0.1862 S32:   0.4911 S33:   0.1462                       
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 434 THROUGH 446 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -10.1057 -34.2426  31.8373              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4465 T22:   1.0406                                     
REMARK   3      T33:   1.4531 T12:  -0.2279                                     
REMARK   3      T13:  -0.0751 T23:  -0.1583                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7217 L22:   3.1693                                     
REMARK   3      L33:   1.2993 L12:  -1.2106                                     
REMARK   3      L13:  -1.8030 L23:   3.0250                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2556 S12:  -0.4020 S13:   1.2926                       
REMARK   3      S21:   0.6366 S22:   0.4296 S23:  -1.0719                       
REMARK   3      S31:  -0.0133 S32:   0.1561 S33:  -0.7742                       
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 6BRR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-DEC-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000231338.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-JUN-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28270                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.970                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.97                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.20500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 2QRV                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL (PH 7.0), 200 MM          
REMARK 280  NAH2PO4 AND 5% PEG4000, VAPOR DIFFUSION, HANGING DROP,              
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000      102.50250            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       59.17985            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       29.78600            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000      102.50250            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       59.17985            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       29.78600            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000      102.50250            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       59.17985            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       29.78600            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      118.35969            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       59.57200            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000      118.35969            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       59.57200            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000      118.35969            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       59.57200            
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: HEXAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, C, E, F                      
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     MET B   178                                                      
REMARK 465     ASP B   214                                                      
REMARK 465     PRO B   215                                                      
REMARK 465     GLY B   216                                                      
REMARK 465     LEU B   248                                                      
REMARK 465     GLY B   249                                                      
REMARK 465     HIS B   313                                                      
REMARK 465     GLY B   314                                                      
REMARK 465     LYS B   354                                                      
REMARK 465     LEU B   355                                                      
REMARK 465     ALA B   356                                                      
REMARK 465     ALA B   357                                                      
REMARK 465     LYS B   358                                                      
REMARK 465     TRP B   359                                                      
REMARK 465     PRO B   360                                                      
REMARK 465     THR B   380                                                      
REMARK 465     GLU B   381                                                      
REMARK 465     LEU B   382                                                      
REMARK 465     THR B   383                                                      
REMARK 465     SER B   384                                                      
REMARK 465     SER B   385                                                      
REMARK 465     LEU B   386                                                      
REMARK 465     MET C   178                                                      
REMARK 465     PHE C   179                                                      
REMARK 465     GLU C   180                                                      
REMARK 465     THR C   181                                                      
REMARK 465     VAL C   182                                                      
REMARK 465     PRO C   183                                                      
REMARK 465     VAL C   184                                                      
REMARK 465     TRP C   185                                                      
REMARK 465     LEU C   209                                                      
REMARK 465     GLU C   210                                                      
REMARK 465     SER C   211                                                      
REMARK 465     GLY C   212                                                      
REMARK 465     SER C   213                                                      
REMARK 465     ASP C   214                                                      
REMARK 465     THR C   251                                                      
REMARK 465     CYS C   252                                                      
REMARK 465     HIS C   313                                                      
REMARK 465     GLY C   314                                                      
REMARK 465     GLY C   315                                                      
REMARK 465     SER C   316                                                      
REMARK 465     LYS C   354                                                      
REMARK 465     LEU C   355                                                      
REMARK 465     ALA C   356                                                      
REMARK 465     ALA C   357                                                      
REMARK 465     LYS C   358                                                      
REMARK 465     TRP C   359                                                      
REMARK 465     PRO C   360                                                      
REMARK 465     SER C   379                                                      
REMARK 465     THR C   380                                                      
REMARK 465     GLU C   381                                                      
REMARK 465     LEU C   382                                                      
REMARK 465     THR C   383                                                      
REMARK 465     SER C   384                                                      
REMARK 465     SER C   385                                                      
REMARK 465     LEU C   386                                                      
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     GLU A 629    CD   OE1  OE2                                       
REMARK 470     LYS A 630    CD   CE   NZ                                        
REMARK 470     LYS A 632    CE   NZ                                             
REMARK 470     LYS A 693    CG   CD   CE   NZ                                   
REMARK 470     LYS A 721    NZ                                                  
REMARK 470     LYS A 744    CG   CD   CE   NZ                                   
REMARK 470     GLU A 745    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 812    NZ                                                  
REMARK 470     ILE A 824    CD1                                                 
REMARK 470     LYS A 844    CG   CD   CE   NZ                                   
REMARK 470     GLN A 846    CD   OE1  NE2                                       
REMARK 470     GLU A 854    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 855    CG   CD   CE   NZ                                   
REMARK 470     LYS A 906    NZ                                                  
REMARK 470     GLU A 907    CD   OE1  OE2                                       
REMARK 470     VAL A 912    CG1  CG2                                            
REMARK 470     PHE B 179    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU B 180    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 186    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 198    CG   OD1  OD2                                       
REMARK 470     LYS B 200    CG   CD   CE   NZ                                   
REMARK 470     LYS B 201    CG   CD   CE   NZ                                   
REMARK 470     LEU B 206    CD1  CD2                                            
REMARK 470     GLU B 210    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 217    CD   OE1  NE2                                       
REMARK 470     ASP B 223    CG   OD1  OD2                                       
REMARK 470     LYS B 230    CG   CD   CE   NZ                                   
REMARK 470     GLU B 234    CD   OE1  OE2                                       
REMARK 470     HIS B 250    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP B 253    CG   OD1  OD2                                       
REMARK 470     LYS B 273    CD   CE   NZ                                        
REMARK 470     SER B 276    OG                                                  
REMARK 470     ARG B 278    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     LYS B 292    CE   NZ                                             
REMARK 470     GLU B 293    CD   OE1  OE2                                       
REMARK 470     ASP B 311    CG   OD1  OD2                                       
REMARK 470     VAL B 312    CG1  CG2                                            
REMARK 470     SER B 316    OG                                                  
REMARK 470     LEU B 317    CG   CD1  CD2                                       
REMARK 470     GLN B 318    CG   CD   OE1  NE2                                  
REMARK 470     ASN B 319    CG   OD1  ND2                                       
REMARK 470     ARG B 331    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B 332    OG                                                  
REMARK 470     ARG B 333    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 337    CG   CD1  CD2                                       
REMARK 470     VAL B 338    CG1  CG2                                            
REMARK 470     SER B 339    OG                                                  
REMARK 470     GLU B 341    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 342    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 345    CG   CD1  CD2                                       
REMARK 470     LYS B 350    CE   NZ                                             
REMARK 470     GLN B 351    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 362    CG   CD   CE   NZ                                   
REMARK 470     LYS B 365    CG   CD   CE   NZ                                   
REMARK 470     CYS B 367    CB   SG                                             
REMARK 470     LEU B 369    CB   CG   CD1  CD2                                  
REMARK 470     ARG B 372    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU B 373    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 376    CG   CD   CE   NZ                                   
REMARK 470     GLU D 629    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 630    CG   CD   CE   NZ                                   
REMARK 470     LYS D 632    CE   NZ                                             
REMARK 470     GLU D 667    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 693    NZ                                                  
REMARK 470     LYS D 721    CE   NZ                                             
REMARK 470     LYS D 744    CG   CD   CE   NZ                                   
REMARK 470     ASP D 748    OD1  OD2                                            
REMARK 470     LYS D 844    CE   NZ                                             
REMARK 470     LYS D 855    NZ                                                  
REMARK 470     ARG D 899    CZ   NH1  NH2                                       
REMARK 470     VAL D 912    CG1  CG2                                            
REMARK 470     ARG C 186    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 187    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 197    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 198    CB   CG   OD1  OD2                                  
REMARK 470     LYS C 200    CG   CD   CE   NZ                                   
REMARK 470     LYS C 201    CG   CD   CE   NZ                                   
REMARK 470     GLU C 202    CG   CD   OE1  OE2                                  
REMARK 470     LEU C 206    CG   CD1  CD2                                       
REMARK 470     LYS C 219    CD   CE   NZ                                        
REMARK 470     VAL C 221    CG1  CG2                                            
REMARK 470     VAL C 222    CG1  CG2                                            
REMARK 470     LYS C 230    CG   CD   CE   NZ                                   
REMARK 470     GLU C 234    CD   OE1  OE2                                       
REMARK 470     LEU C 248    CG   CD1  CD2                                       
REMARK 470     HIS C 250    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP C 253    CG   OD1  OD2                                       
REMARK 470     LYS C 273    CG   CD   CE   NZ                                   
REMARK 470     ARG C 278    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     LYS C 292    CD   CE   NZ                                        
REMARK 470     ASP C 311    CG   OD1  OD2                                       
REMARK 470     LEU C 317    CB   CG   CD1  CD2                                  
REMARK 470     GLN C 318    CG   CD   OE1  NE2                                  
REMARK 470     ASN C 319    CG   OD1  ND2                                       
REMARK 470     ARG C 331    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 333    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU C 337    CG   CD1  CD2                                       
REMARK 470     GLU C 341    CD   OE1  OE2                                       
REMARK 470     LEU C 343    CG   CD1  CD2                                       
REMARK 470     LEU C 346    CG   CD1  CD2                                       
REMARK 470     GLN C 348    CG   CD   OE1  NE2                                  
REMARK 470     ASN C 349    CG   OD1  ND2                                       
REMARK 470     LYS C 350    CG   CD   CE   NZ                                   
REMARK 470     GLN C 351    OE1  NE2                                            
REMARK 470     LYS C 362    CG   CD   CE   NZ                                   
REMARK 470     VAL C 364    CG1  CG2                                            
REMARK 470     LYS C 365    CG   CD   CE   NZ                                   
REMARK 470     ASN C 366    CG   OD1  ND2                                       
REMARK 470     CYS C 367    CB   SG                                             
REMARK 470     LEU C 369    CB   CG   CD1  CD2                                  
REMARK 470     LEU C 371    CB   CG   CD1  CD2                                  
REMARK 470     ARG C 372    CD   NE   CZ   NH1  NH2                             
REMARK 470     TYR C 374    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS C 376    CG   CD   CE   NZ                                   
REMARK 470     TYR C 377    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     PHE C 378    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470      DG E 422    O5'                                                 
REMARK 470      DG F 422    O5'                                                 
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   O    PRO C   328     OG   SER C   332              2.14            
REMARK 500   OG1  THR D   835     OP1   DG E   428              2.19            
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    ILE A 643       30.61    -93.36                                   
REMARK 500    ARG A 790       80.49   -158.05                                   
REMARK 500    PHE B 196      -47.31     69.20                                   
REMARK 500    TRP B 235       10.31    -68.71                                   
REMARK 500    ASN B 287       58.23    -99.74                                   
REMARK 500    ASP B 311      102.75   -168.35                                   
REMARK 500    PRO B 370        9.78    -69.08                                   
REMARK 500    ILE D 643       34.74    -97.95                                   
REMARK 500    LYS D 744     -165.95    -78.70                                   
REMARK 500    ASP D 748       31.09    -93.18                                   
REMARK 500    ALA D 760       55.80    -90.60                                   
REMARK 500    ARG D 790       83.37   -166.21                                   
REMARK 500    PHE C 196      -62.29     69.63                                   
REMARK 500    ARG C 278     -162.63   -162.79                                   
REMARK 500    ASN C 287       59.38   -111.01                                   
REMARK 500    GLN C 318      -73.61   -136.01                                   
REMARK 500    ARG C 333      104.22    -56.61                                   
REMARK 500    HIS C 334       68.36    -53.96                                   
REMARK 500    PHE C 375     -147.65   -121.84                                   
REMARK 500    TYR C 377      -52.85   -146.28                                   
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 SAH D 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-nucleotide DG E 426 and PYO    
REMARK 800  E 427                                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-nucleotide PYO E 427 and DG    
REMARK 800  E 428                                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-nucleotide DG F 426 and PYO    
REMARK 800  F 427                                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-nucleotide PYO F 427 and DG    
REMARK 800  F 428                                                               
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THERE IS APPARENTLY AN ERROR IN THE REFERENCE SEQUENCE Q9Y6K1, AS    
REMARK 999 SER 332 WAS NOT OBSERVED IN ANY OTHER PUBLISHED DNMT3L STRUCTURES    
DBREF  6BRR A  628   912  UNP    Q9Y6K1   DNM3A_HUMAN    439    723             
DBREF  6BRR B  178   386  UNP    Q9UJW3   DNM3L_HUMAN    178    387             
DBREF  6BRR D  628   912  UNP    Q9Y6K1   DNM3A_HUMAN    439    723             
DBREF  6BRR C  178   386  UNP    Q9UJW3   DNM3L_HUMAN    178    387             
DBREF  6BRR E  422   446  PDB    6BRR     6BRR           422    446             
DBREF  6BRR F  422   446  PDB    6BRR     6BRR           422    446             
SEQADV 6BRR ALA A  836  UNP  Q9Y6K1    ARG   647 ENGINEERED MUTATION            
SEQADV 6BRR     B       UNP  Q9UJW3    SER   332 SEE REMARK 999                 
SEQADV 6BRR ALA D  836  UNP  Q9Y6K1    ARG   647 ENGINEERED MUTATION            
SEQADV 6BRR     C       UNP  Q9UJW3    SER   332 SEE REMARK 999                 
SEQRES   1 A  285  ALA GLU LYS ARG LYS PRO ILE ARG VAL LEU SER LEU PHE          
SEQRES   2 A  285  ASP GLY ILE ALA THR GLY LEU LEU VAL LEU LYS ASP LEU          
SEQRES   3 A  285  GLY ILE GLN VAL ASP ARG TYR ILE ALA SER GLU VAL CYS          
SEQRES   4 A  285  GLU ASP SER ILE THR VAL GLY MET VAL ARG HIS GLN GLY          
SEQRES   5 A  285  LYS ILE MET TYR VAL GLY ASP VAL ARG SER VAL THR GLN          
SEQRES   6 A  285  LYS HIS ILE GLN GLU TRP GLY PRO PHE ASP LEU VAL ILE          
SEQRES   7 A  285  GLY GLY SER PRO CYS ASN ASP LEU SER ILE VAL ASN PRO          
SEQRES   8 A  285  ALA ARG LYS GLY LEU TYR GLU GLY THR GLY ARG LEU PHE          
SEQRES   9 A  285  PHE GLU PHE TYR ARG LEU LEU HIS ASP ALA ARG PRO LYS          
SEQRES  10 A  285  GLU GLY ASP ASP ARG PRO PHE PHE TRP LEU PHE GLU ASN          
SEQRES  11 A  285  VAL VAL ALA MET GLY VAL SER ASP LYS ARG ASP ILE SER          
SEQRES  12 A  285  ARG PHE LEU GLU SER ASN PRO VAL MET ILE ASP ALA LYS          
SEQRES  13 A  285  GLU VAL SER ALA ALA HIS ARG ALA ARG TYR PHE TRP GLY          
SEQRES  14 A  285  ASN LEU PRO GLY MET ASN ARG PRO LEU ALA SER THR VAL          
SEQRES  15 A  285  ASN ASP LYS LEU GLU LEU GLN GLU CYS LEU GLU HIS GLY          
SEQRES  16 A  285  ARG ILE ALA LYS PHE SER LYS VAL ARG THR ILE THR THR          
SEQRES  17 A  285  ALA SER ASN SER ILE LYS GLN GLY LYS ASP GLN HIS PHE          
SEQRES  18 A  285  PRO VAL PHE MET ASN GLU LYS GLU ASP ILE LEU TRP CYS          
SEQRES  19 A  285  THR GLU MET GLU ARG VAL PHE GLY PHE PRO VAL HIS TYR          
SEQRES  20 A  285  THR ASP VAL SER ASN MET SER ARG LEU ALA ARG GLN ARG          
SEQRES  21 A  285  LEU LEU GLY ARG SER TRP SER VAL PRO VAL ILE ARG HIS          
SEQRES  22 A  285  LEU PHE ALA PRO LEU LYS GLU TYR PHE ALA CYS VAL              
SEQRES   1 B  209  MET PHE GLU THR VAL PRO VAL TRP ARG ARG GLN PRO VAL          
SEQRES   2 B  209  ARG VAL LEU SER LEU PHE GLU ASP ILE LYS LYS GLU LEU          
SEQRES   3 B  209  THR SER LEU GLY PHE LEU GLU SER GLY SER ASP PRO GLY          
SEQRES   4 B  209  GLN LEU LYS HIS VAL VAL ASP VAL THR ASP THR VAL ARG          
SEQRES   5 B  209  LYS ASP VAL GLU GLU TRP GLY PRO PHE ASP LEU VAL TYR          
SEQRES   6 B  209  GLY ALA THR PRO PRO LEU GLY HIS THR CYS ASP ARG PRO          
SEQRES   7 B  209  PRO SER TRP TYR LEU PHE GLN PHE HIS ARG LEU LEU GLN          
SEQRES   8 B  209  TYR ALA ARG PRO LYS PRO GLY SER PRO ARG PRO PHE PHE          
SEQRES   9 B  209  TRP MET PHE VAL ASP ASN LEU VAL LEU ASN LYS GLU ASP          
SEQRES  10 B  209  LEU ASP VAL ALA SER ARG PHE LEU GLU MET GLU PRO VAL          
SEQRES  11 B  209  THR ILE PRO ASP VAL HIS GLY GLY SER LEU GLN ASN ALA          
SEQRES  12 B  209  VAL ARG VAL TRP SER ASN ILE PRO ALA ILE ARG SER ARG          
SEQRES  13 B  209  HIS TRP ALA LEU VAL SER GLU GLU GLU LEU SER LEU LEU          
SEQRES  14 B  209  ALA GLN ASN LYS GLN SER SER LYS LEU ALA ALA LYS TRP          
SEQRES  15 B  209  PRO THR LYS LEU VAL LYS ASN CYS PHE LEU PRO LEU ARG          
SEQRES  16 B  209  GLU TYR PHE LYS TYR PHE SER THR GLU LEU THR SER SER          
SEQRES  17 B  209  LEU                                                          
SEQRES   1 D  285  ALA GLU LYS ARG LYS PRO ILE ARG VAL LEU SER LEU PHE          
SEQRES   2 D  285  ASP GLY ILE ALA THR GLY LEU LEU VAL LEU LYS ASP LEU          
SEQRES   3 D  285  GLY ILE GLN VAL ASP ARG TYR ILE ALA SER GLU VAL CYS          
SEQRES   4 D  285  GLU ASP SER ILE THR VAL GLY MET VAL ARG HIS GLN GLY          
SEQRES   5 D  285  LYS ILE MET TYR VAL GLY ASP VAL ARG SER VAL THR GLN          
SEQRES   6 D  285  LYS HIS ILE GLN GLU TRP GLY PRO PHE ASP LEU VAL ILE          
SEQRES   7 D  285  GLY GLY SER PRO CYS ASN ASP LEU SER ILE VAL ASN PRO          
SEQRES   8 D  285  ALA ARG LYS GLY LEU TYR GLU GLY THR GLY ARG LEU PHE          
SEQRES   9 D  285  PHE GLU PHE TYR ARG LEU LEU HIS ASP ALA ARG PRO LYS          
SEQRES  10 D  285  GLU GLY ASP ASP ARG PRO PHE PHE TRP LEU PHE GLU ASN          
SEQRES  11 D  285  VAL VAL ALA MET GLY VAL SER ASP LYS ARG ASP ILE SER          
SEQRES  12 D  285  ARG PHE LEU GLU SER ASN PRO VAL MET ILE ASP ALA LYS          
SEQRES  13 D  285  GLU VAL SER ALA ALA HIS ARG ALA ARG TYR PHE TRP GLY          
SEQRES  14 D  285  ASN LEU PRO GLY MET ASN ARG PRO LEU ALA SER THR VAL          
SEQRES  15 D  285  ASN ASP LYS LEU GLU LEU GLN GLU CYS LEU GLU HIS GLY          
SEQRES  16 D  285  ARG ILE ALA LYS PHE SER LYS VAL ARG THR ILE THR THR          
SEQRES  17 D  285  ALA SER ASN SER ILE LYS GLN GLY LYS ASP GLN HIS PHE          
SEQRES  18 D  285  PRO VAL PHE MET ASN GLU LYS GLU ASP ILE LEU TRP CYS          
SEQRES  19 D  285  THR GLU MET GLU ARG VAL PHE GLY PHE PRO VAL HIS TYR          
SEQRES  20 D  285  THR ASP VAL SER ASN MET SER ARG LEU ALA ARG GLN ARG          
SEQRES  21 D  285  LEU LEU GLY ARG SER TRP SER VAL PRO VAL ILE ARG HIS          
SEQRES  22 D  285  LEU PHE ALA PRO LEU LYS GLU TYR PHE ALA CYS VAL              
SEQRES   1 C  209  MET PHE GLU THR VAL PRO VAL TRP ARG ARG GLN PRO VAL          
SEQRES   2 C  209  ARG VAL LEU SER LEU PHE GLU ASP ILE LYS LYS GLU LEU          
SEQRES   3 C  209  THR SER LEU GLY PHE LEU GLU SER GLY SER ASP PRO GLY          
SEQRES   4 C  209  GLN LEU LYS HIS VAL VAL ASP VAL THR ASP THR VAL ARG          
SEQRES   5 C  209  LYS ASP VAL GLU GLU TRP GLY PRO PHE ASP LEU VAL TYR          
SEQRES   6 C  209  GLY ALA THR PRO PRO LEU GLY HIS THR CYS ASP ARG PRO          
SEQRES   7 C  209  PRO SER TRP TYR LEU PHE GLN PHE HIS ARG LEU LEU GLN          
SEQRES   8 C  209  TYR ALA ARG PRO LYS PRO GLY SER PRO ARG PRO PHE PHE          
SEQRES   9 C  209  TRP MET PHE VAL ASP ASN LEU VAL LEU ASN LYS GLU ASP          
SEQRES  10 C  209  LEU ASP VAL ALA SER ARG PHE LEU GLU MET GLU PRO VAL          
SEQRES  11 C  209  THR ILE PRO ASP VAL HIS GLY GLY SER LEU GLN ASN ALA          
SEQRES  12 C  209  VAL ARG VAL TRP SER ASN ILE PRO ALA ILE ARG SER ARG          
SEQRES  13 C  209  HIS TRP ALA LEU VAL SER GLU GLU GLU LEU SER LEU LEU          
SEQRES  14 C  209  ALA GLN ASN LYS GLN SER SER LYS LEU ALA ALA LYS TRP          
SEQRES  15 C  209  PRO THR LYS LEU VAL LYS ASN CYS PHE LEU PRO LEU ARG          
SEQRES  16 C  209  GLU TYR PHE LYS TYR PHE SER THR GLU LEU THR SER SER          
SEQRES  17 C  209  LEU                                                          
SEQRES   1 E   25   DG  DC  DA  DT  DG PYO  DG  DT  DT  DC  DT  DA  DA          
SEQRES   2 E   25   DT  DT  DA  DG  DA  DA  DC  DG  DC  DA  DT  DG              
SEQRES   1 F   25   DG  DC  DA  DT  DG PYO  DG  DT  DT  DC  DT  DA  DA          
SEQRES   2 F   25   DT  DT  DA  DG  DA  DA  DC  DG  DC  DA  DT  DG              
HET    PYO  E 427      19                                                       
HET    PYO  F 427      19                                                       
HET    SAH  A1001      26                                                       
HET    SAH  D1001      26                                                       
HETNAM     PYO 1-(BETA-D-RIBOFURANOSYL)-PYRIMIDIN-2-ONE-5'-PHOSPHATE            
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
FORMUL   5  PYO    2(C9 H13 N2 O8 P)                                            
FORMUL   7  SAH    2(C14 H20 N6 O5 S)                                           
HELIX    1 AA1 ALA A  644  LEU A  653  1                                  10    
HELIX    2 AA2 CYS A  666  ARG A  676  1                                  11    
HELIX    3 AA3 ASP A  686  VAL A  690  5                                   5    
HELIX    4 AA4 THR A  691  GLY A  699  1                                   9    
HELIX    5 AA5 THR A  727  ARG A  729  5                                   3    
HELIX    6 AA6 LEU A  730  ARG A  742  1                                  13    
HELIX    7 AA7 GLY A  762  GLU A  774  1                                  13    
HELIX    8 AA8 LYS A  783  VAL A  785  5                                   3    
HELIX    9 AA9 GLU A  814  LEU A  819  5                                   6    
HELIX   10 AB1 TRP A  860  GLY A  869  1                                  10    
HELIX   11 AB2 SER A  881  SER A  892  1                                  12    
HELIX   12 AB3 SER A  894  ALA A  903  1                                  10    
HELIX   13 AB4 PRO A  904  GLU A  907  5                                   4    
HELIX   14 AB5 PRO B  183  ARG B  187  5                                   5    
HELIX   15 AB6 ILE B  199  LEU B  206  1                                   8    
HELIX   16 AB7 ASP B  223  THR B  227  5                                   5    
HELIX   17 AB8 VAL B  228  TRP B  235  1                                   8    
HELIX   18 AB9 PRO B  255  ARG B  271  1                                  17    
HELIX   19 AC1 ASN B  291  LEU B  302  1                                  12    
HELIX   20 AC2 SER B  339  LEU B  343  5                                   5    
HELIX   21 AC3 LEU B  345  LYS B  350  1                                   6    
HELIX   22 AC4 LYS B  362  CYS B  367  5                                   6    
HELIX   23 AC5 PHE B  368  ARG B  372  5                                   5    
HELIX   24 AC6 ALA D  644  LEU D  653  1                                  10    
HELIX   25 AC7 CYS D  666  HIS D  677  1                                  12    
HELIX   26 AC8 ASP D  686  VAL D  690  5                                   5    
HELIX   27 AC9 THR D  691  GLY D  699  1                                   9    
HELIX   28 AD1 THR D  727  ARG D  729  5                                   3    
HELIX   29 AD2 LEU D  730  ARG D  742  1                                  13    
HELIX   30 AD3 GLY D  762  LEU D  773  1                                  12    
HELIX   31 AD4 LYS D  783  VAL D  785  5                                   3    
HELIX   32 AD5 GLU D  814  LEU D  819  5                                   6    
HELIX   33 AD6 ALA D  836  LYS D  841  5                                   6    
HELIX   34 AD7 TRP D  860  GLY D  869  1                                  10    
HELIX   35 AD8 SER D  881  ARG D  891  1                                  11    
HELIX   36 AD9 SER D  894  ALA D  903  1                                  10    
HELIX   37 AE1 PRO D  904  TYR D  908  5                                   5    
HELIX   38 AE2 LYS C  201  LEU C  206  1                                   6    
HELIX   39 AE3 VAL C  228  TRP C  235  1                                   8    
HELIX   40 AE4 PRO C  255  GLN C  268  1                                  14    
HELIX   41 AE5 ASN C  291  LEU C  302  1                                  12    
HELIX   42 AE6 SER C  339  ASN C  349  1                                  11    
HELIX   43 AE7 PHE C  368  ARG C  372  5                                   5    
SHEET    1 AA1 7 MET A 682  TYR A 683  0                                        
SHEET    2 AA1 7 VAL A 657  SER A 663  1  N  TYR A 660   O  MET A 682           
SHEET    3 AA1 7 ILE A 634  LEU A 639  1  N  SER A 638   O  ILE A 661           
SHEET    4 AA1 7 LEU A 703  GLY A 706  1  O  LEU A 703   N  LEU A 637           
SHEET    5 AA1 7 PHE A 752  VAL A 758  1  O  PHE A 752   N  VAL A 704           
SHEET    6 AA1 7 ALA A 791  GLY A 796 -1  O  TRP A 795   N  PHE A 755           
SHEET    7 AA1 7 VAL A 778  ASP A 781 -1  N  ILE A 780   O  ARG A 792           
SHEET    1 AA2 3 ILE A 824  ALA A 825  0                                        
SHEET    2 AA2 3 VAL A 850  PHE A 851 -1  O  PHE A 851   N  ILE A 824           
SHEET    3 AA2 3 GLU A 856  ASP A 857 -1  O  ASP A 857   N  VAL A 850           
SHEET    1 AA3 6 LEU B 218  VAL B 221  0                                        
SHEET    2 AA3 6 VAL B 192  LEU B 195  1  N  VAL B 192   O  LYS B 219           
SHEET    3 AA3 6 LEU B 240  ALA B 244  1  O  TYR B 242   N  LEU B 193           
SHEET    4 AA3 6 PHE B 281  ASP B 286  1  O  VAL B 285   N  GLY B 243           
SHEET    5 AA3 6 ASN B 319  SER B 325 -1  O  ARG B 322   N  ASP B 286           
SHEET    6 AA3 6 VAL B 307  ASP B 311 -1  N  ASP B 311   O  ASN B 319           
SHEET    1 AA4 7 MET D 682  TYR D 683  0                                        
SHEET    2 AA4 7 VAL D 657  SER D 663  1  N  ALA D 662   O  MET D 682           
SHEET    3 AA4 7 ILE D 634  LEU D 639  1  N  SER D 638   O  SER D 663           
SHEET    4 AA4 7 LEU D 703  GLY D 706  1  O  ILE D 705   N  LEU D 639           
SHEET    5 AA4 7 PHE D 752  VAL D 758  1  O  PHE D 752   N  VAL D 704           
SHEET    6 AA4 7 ALA D 791  GLY D 796 -1  O  TYR D 793   N  ASN D 757           
SHEET    7 AA4 7 VAL D 778  ASP D 781 -1  N  VAL D 778   O  PHE D 794           
SHEET    1 AA5 3 ILE D 824  ALA D 825  0                                        
SHEET    2 AA5 3 VAL D 850  MET D 852 -1  O  PHE D 851   N  ILE D 824           
SHEET    3 AA5 3 LYS D 855  ASP D 857 -1  O  ASP D 857   N  VAL D 850           
SHEET    1 AA6 6 LEU C 218  VAL C 221  0                                        
SHEET    2 AA6 6 VAL C 192  LEU C 195  1  N  SER C 194   O  LYS C 219           
SHEET    3 AA6 6 LEU C 240  ALA C 244  1  O  LEU C 240   N  LEU C 193           
SHEET    4 AA6 6 PHE C 281  ASP C 286  1  O  VAL C 285   N  GLY C 243           
SHEET    5 AA6 6 VAL C 321  SER C 325 -1  O  ARG C 322   N  ASP C 286           
SHEET    6 AA6 6 VAL C 307  ILE C 309 -1  N  ILE C 309   O  VAL C 321           
LINK         SG  CYS A 710                 C6  PYO F 427     1555   1555  1.79  
LINK         SG  CYS D 710                 C6  PYO E 427     1555   1555  1.79  
LINK         O3'  DG E 426                 P   PYO E 427     1555   1555  1.61  
LINK         O3' PYO E 427                 P    DG E 428     1555   1555  1.61  
LINK         O3'  DG F 426                 P   PYO F 427     1555   1555  1.61  
LINK         O3' PYO F 427                 P    DG F 428     1555   1555  1.61  
CISPEP   1 GLY A  699    PRO A  700          0        -0.97                     
CISPEP   2 ASP B  311    VAL B  312          0        -0.19                     
CISPEP   3 GLY D  699    PRO D  700          0        -1.76                     
CISPEP   4 LYS C  376    TYR C  377          0       -12.17                     
SITE     1 AC1 17 PHE A 640  ASP A 641  GLY A 642  ILE A 643                    
SITE     2 AC1 17 THR A 645  SER A 663  GLU A 664  VAL A 665                    
SITE     3 AC1 17 CYS A 666  ASP A 686  VAL A 687  GLY A 707                    
SITE     4 AC1 17 PRO A 709  LEU A 730  ARG A 891  SER A 892                    
SITE     5 AC1 17 TRP A 893                                                     
SITE     1 AC2 17 PHE D 640  ASP D 641  GLY D 642  ILE D 643                    
SITE     2 AC2 17 THR D 645  SER D 663  GLU D 664  VAL D 665                    
SITE     3 AC2 17 CYS D 666  ASP D 686  VAL D 687  GLY D 707                    
SITE     4 AC2 17 PRO D 709  LEU D 730  ARG D 891  SER D 892                    
SITE     5 AC2 17 TRP D 893                                                     
SITE     1 AC3 18 SER D 708  CYS D 710  SER D 714  ILE D 715                    
SITE     2 AC3 18 VAL D 716  GLU D 756  VAL D 758  ARG D 790                    
SITE     3 AC3 18 ARG D 792  ARG D 831  THR D 832  GLY D 890                    
SITE     4 AC3 18 ARG D 891   DT E 425   DG E 428   DG F 442                    
SITE     5 AC3 18  DC F 443   DA F 444                                          
SITE     1 AC4 19 SER D 708  CYS D 710  ASN D 711  SER D 714                    
SITE     2 AC4 19 VAL D 716  ASN D 717  PRO D 718  GLU D 756                    
SITE     3 AC4 19 VAL D 758  ARG D 790  ARG D 792  THR D 834                    
SITE     4 AC4 19 THR D 835  GLY D 890  ARG D 891   DG E 426                    
SITE     5 AC4 19  DT E 429   DA F 440   DC F 441                               
SITE     1 AC5 18 SER A 708  CYS A 710  SER A 714  ILE A 715                    
SITE     2 AC5 18 VAL A 716  GLU A 756  VAL A 758  ALA A 760                    
SITE     3 AC5 18 ARG A 790  ARG A 792  THR A 832  GLY A 890                    
SITE     4 AC5 18 ARG A 891   DG E 442   DC E 443   DA E 444                    
SITE     5 AC5 18  DT F 425   DG F 428                                          
SITE     1 AC6 20 SER A 708  CYS A 710  ASN A 711  SER A 714                    
SITE     2 AC6 20 VAL A 716  ASN A 717  PRO A 718  GLU A 756                    
SITE     3 AC6 20 VAL A 758  ALA A 760  ARG A 790  ARG A 792                    
SITE     4 AC6 20 THR A 835  GLY A 890  ARG A 891   DA E 440                    
SITE     5 AC6 20  DC E 441   DG E 442   DG F 426   DT F 429                    
CRYST1  205.005  205.005   89.358  90.00  90.00 120.00 H 3          18          
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      0.004878  0.002816  0.000000        0.00000                         
SCALE2      0.000000  0.005633  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011191        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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