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Database: PDB
Entry: 5YX2
LinkDB: 5YX2
Original site: 5YX2 
HEADER    TRANSFERASE/TRANSFERASE REGULATOR/DNA   01-DEC-17   5YX2              
TITLE     CRYSTAL STRUCTURE OF DNMT3A-DNMT3L IN COMPLEX WITH DNA CONTAINING TWO 
TITLE    2 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 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: DNA (CYTOSINE-5)-METHYLTRANSFERASE 3-LIKE;                 
COMPND   9 CHAIN: B, C;                                                         
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: DNA (25-MER);                                              
COMPND  13 CHAIN: E, F;                                                         
COMPND  14 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: SYNTHETIC CONSTRUCT;                            
SOURCE  20 ORGANISM_TAXID: 32630                                                
KEYWDS    DNMT3A, DNMT3L, DNA METHYLATION, TRANSFERASE-TRANSFERASE REGULATOR-   
KEYWDS   2 DNA COMPLEX                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.M.ZHANG,J.SONG                                                      
REVDAT   3   28-FEB-18 5YX2    1       JRNL                                     
REVDAT   2   21-FEB-18 5YX2    1       JRNL                                     
REVDAT   1   31-JAN-18 5YX2    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.    2.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.11                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.970                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 40049                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.192                           
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2005                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 33.1170 -  6.3795    0.96     2665   142  0.1738 0.1703        
REMARK   3     2  6.3795 -  5.0694    0.97     2686   143  0.1771 0.2313        
REMARK   3     3  5.0694 -  4.4303    0.98     2686   142  0.1564 0.1773        
REMARK   3     4  4.4303 -  4.0260    0.98     2727   145  0.1582 0.2067        
REMARK   3     5  4.0260 -  3.7379    0.99     2710   141  0.1795 0.2006        
REMARK   3     6  3.7379 -  3.5177    0.98     2719   143  0.1833 0.1988        
REMARK   3     7  3.5177 -  3.3418    0.99     2728   142  0.2048 0.2564        
REMARK   3     8  3.3418 -  3.1964    0.99     2733   141  0.2181 0.2827        
REMARK   3     9  3.1964 -  3.0734    0.99     2727   145  0.2393 0.2944        
REMARK   3    10  3.0734 -  2.9675    0.99     2731   148  0.2505 0.3279        
REMARK   3    11  2.9675 -  2.8747    0.99     2741   143  0.2634 0.2811        
REMARK   3    12  2.8747 -  2.7926    0.99     2748   144  0.2668 0.3105        
REMARK   3    13  2.7926 -  2.7191    0.99     2697   140  0.2679 0.3307        
REMARK   3    14  2.7191 -  2.6528    0.99     2746   146  0.2721 0.2911        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.370            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.350           
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           8618                                  
REMARK   3   ANGLE     :  0.731          11914                                  
REMARK   3   CHIRALITY :  0.030           1301                                  
REMARK   3   PLANARITY :  0.004           1358                                  
REMARK   3   DIHEDRAL  : 20.132           3178                                  
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):  76.9281  28.2134 -16.2972              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3921 T22:   0.6140                                     
REMARK   3      T33:   0.5480 T12:  -0.0159                                     
REMARK   3      T13:  -0.0218 T23:  -0.0051                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2988 L22:   5.5696                                     
REMARK   3      L33:   3.3467 L12:   1.5167                                     
REMARK   3      L13:  -1.0775 L23:  -0.4208                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0690 S12:  -0.8592 S13:  -0.1278                       
REMARK   3      S21:   0.3086 S22:  -0.0117 S23:  -1.1660                       
REMARK   3      S31:   0.0629 S32:   0.7012 S33:   0.0503                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 657 THROUGH 762 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  66.6409  37.2008 -20.1460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5025 T22:   0.3400                                     
REMARK   3      T33:   0.4165 T12:  -0.0569                                     
REMARK   3      T13:  -0.0080 T23:  -0.0328                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2645 L22:   4.5651                                     
REMARK   3      L33:   4.1413 L12:  -0.6512                                     
REMARK   3      L13:   0.1416 L23:  -0.1863                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1039 S12:  -0.1376 S13:   0.6002                       
REMARK   3      S21:  -0.2244 S22:  -0.0308 S23:  -0.1416                       
REMARK   3      S31:  -0.8945 S32:   0.2845 S33:   0.0937                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 763 THROUGH 840 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  67.3687  23.5529 -34.3898              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7608 T22:   0.4535                                     
REMARK   3      T33:   0.3731 T12:  -0.0321                                     
REMARK   3      T13:   0.0195 T23:   0.0272                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8666 L22:   7.3744                                     
REMARK   3      L33:   3.1749 L12:   1.9961                                     
REMARK   3      L13:  -0.6520 L23:   0.9817                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3342 S12:   0.2312 S13:  -0.0304                       
REMARK   3      S21:  -1.5169 S22:   0.2134 S23:  -0.3302                       
REMARK   3      S31:   0.0688 S32:   0.3608 S33:   0.1258                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 841 THROUGH 857 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  51.7656   7.8333 -37.5049              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3811 T22:   0.5884                                     
REMARK   3      T33:   0.6824 T12:  -0.0520                                     
REMARK   3      T13:  -0.4030 T23:  -0.0312                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5273 L22:   0.0133                                     
REMARK   3      L33:   0.3755 L12:   0.0850                                     
REMARK   3      L13:  -0.4216 L23:  -0.0697                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0607 S12:   0.5899 S13:  -0.0283                       
REMARK   3      S21:  -2.7799 S22:   0.3497 S23:   1.0093                       
REMARK   3      S31:   1.6319 S32:  -0.8875 S33:  -0.4418                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 858 THROUGH 912 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  65.6785  19.5031 -22.9281              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4237 T22:   0.3522                                     
REMARK   3      T33:   0.2466 T12:   0.0765                                     
REMARK   3      T13:   0.0176 T23:   0.0028                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2778 L22:   6.3940                                     
REMARK   3      L33:   2.9843 L12:   1.3090                                     
REMARK   3      L13:  -0.0041 L23:  -0.2001                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0646 S12:   0.0806 S13:  -0.0633                       
REMARK   3      S21:  -0.6049 S22:   0.0872 S23:  -0.2609                       
REMARK   3      S31:  -0.1142 S32:   0.3015 S33:   0.0043                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 178 THROUGH 199 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  74.7364  72.3327 -25.8907              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5604 T22:   0.5152                                     
REMARK   3      T33:   1.3646 T12:  -0.2956                                     
REMARK   3      T13:  -0.0054 T23:   0.0036                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4108 L22:   0.4807                                     
REMARK   3      L33:   2.0298 L12:  -0.7733                                     
REMARK   3      L13:   0.0753 L23:  -0.3253                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7144 S12:   0.0661 S13:   0.4504                       
REMARK   3      S21:   0.1309 S22:  -0.2920 S23:  -0.3378                       
REMARK   3      S31:  -0.9992 S32:   0.3347 S33:  -0.4737                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 200 THROUGH 217 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  68.4723  77.9352 -32.6798              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8129 T22:   0.6191                                     
REMARK   3      T33:   1.4675 T12:  -0.1536                                     
REMARK   3      T13:  -0.1186 T23:   0.1262                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4981 L22:   3.1130                                     
REMARK   3      L33:   0.2027 L12:   2.1703                                     
REMARK   3      L13:   0.7052 L23:   0.0961                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1401 S12:   0.6210 S13:   1.2428                       
REMARK   3      S21:  -1.0221 S22:   0.3643 S23:   0.4669                       
REMARK   3      S31:  -1.7234 S32:   0.0161 S33:  -0.3050                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 218 THROUGH 244 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  71.4412  60.6284 -34.7839              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3047 T22:   0.5735                                     
REMARK   3      T33:   1.0683 T12:  -0.1193                                     
REMARK   3      T13:   0.1075 T23:   0.0513                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0831 L22:   2.6958                                     
REMARK   3      L33:   3.8532 L12:   1.0167                                     
REMARK   3      L13:  -0.2490 L23:   0.9184                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1821 S12:   0.4654 S13:   0.5500                       
REMARK   3      S21:  -1.8971 S22:   0.1545 S23:  -0.0090                       
REMARK   3      S31:  -0.7429 S32:   0.5140 S33:   0.0502                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 245 THROUGH 255 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  52.5631  58.7419 -34.3228              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3068 T22:   0.9458                                     
REMARK   3      T33:   1.5057 T12:   0.0705                                     
REMARK   3      T13:  -0.3970 T23:  -0.1557                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.5527 L22:   2.0018                                     
REMARK   3      L33:   3.4225 L12:  -7.8976                                     
REMARK   3      L13:  -2.3317 L23:   3.8397                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4711 S12:   0.9103 S13:   0.7410                       
REMARK   3      S21:  -0.5470 S22:  -0.1555 S23:  -0.0240                       
REMARK   3      S31:   0.3166 S32:  -0.6486 S33:  -0.3658                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 256 THROUGH 270 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  65.3472  54.4575 -29.1456              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9785 T22:   0.4313                                     
REMARK   3      T33:   0.8262 T12:  -0.0803                                     
REMARK   3      T13:  -0.0300 T23:   0.0937                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7314 L22:   3.3210                                     
REMARK   3      L33:   2.5039 L12:   0.1770                                     
REMARK   3      L13:  -1.0785 L23:   0.1070                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0428 S12:   0.1025 S13:   0.0646                       
REMARK   3      S21:  -0.8367 S22:   0.1400 S23:  -0.4167                       
REMARK   3      S31:  -0.0434 S32:  -0.0160 S33:  -0.0751                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 271 THROUGH 280 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  80.1179  62.3313 -21.7450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8858 T22:   0.8829                                     
REMARK   3      T33:   1.1384 T12:  -0.1537                                     
REMARK   3      T13:  -0.1320 T23:  -0.1357                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9606 L22:   3.1573                                     
REMARK   3      L33:   3.7524 L12:  -3.4871                                     
REMARK   3      L13:  -4.2314 L23:   2.6517                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6740 S12:  -1.6963 S13:   1.1357                       
REMARK   3      S21:   0.7925 S22:   0.2498 S23:  -1.5703                       
REMARK   3      S31:  -0.4509 S32:   1.2535 S33:  -0.8847                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 281 THROUGH 332 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  58.5423  61.7702 -19.3850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8160 T22:   0.3955                                     
REMARK   3      T33:   0.9734 T12:   0.0855                                     
REMARK   3      T13:  -0.0983 T23:  -0.0772                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0841 L22:   3.5293                                     
REMARK   3      L33:   5.3119 L12:   0.6892                                     
REMARK   3      L13:   0.0421 L23:  -0.7124                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3096 S12:  -0.4105 S13:   1.2445                       
REMARK   3      S21:  -0.0711 S22:   0.3257 S23:   0.2096                       
REMARK   3      S31:  -1.0240 S32:  -0.3440 S33:   0.0524                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 333 THROUGH 379 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  56.8420  71.9019 -21.1224              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1881 T22:   0.7135                                     
REMARK   3      T33:   1.3742 T12:   0.0228                                     
REMARK   3      T13:  -0.1728 T23:  -0.1693                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6472 L22:   1.5764                                     
REMARK   3      L33:   1.1955 L12:   1.2386                                     
REMARK   3      L13:  -0.9923 L23:  -1.0316                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2278 S12:  -0.0189 S13:   0.2988                       
REMARK   3      S21:   0.1073 S22:  -0.1156 S23:  -0.1148                       
REMARK   3      S31:  -0.9288 S32:  -0.3306 S33:  -0.1497                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 628 THROUGH 784 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  48.2474 -14.8618 -10.3061              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5258 T22:   0.5079                                     
REMARK   3      T33:   0.4450 T12:  -0.1118                                     
REMARK   3      T13:  -0.0735 T23:   0.1314                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4879 L22:   3.3678                                     
REMARK   3      L33:   3.3637 L12:   0.0830                                     
REMARK   3      L13:  -0.7218 L23:   0.1304                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1007 S12:  -0.1974 S13:  -0.2865                       
REMARK   3      S21:   0.0327 S22:  -0.0247 S23:   0.4259                       
REMARK   3      S31:   0.6263 S32:  -0.4974 S33:  -0.1096                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 785 THROUGH 836 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  54.8036   1.2488   2.3449              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4343 T22:   0.5348                                     
REMARK   3      T33:   0.3882 T12:  -0.0141                                     
REMARK   3      T13:   0.0551 T23:   0.0692                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8937 L22:   6.1636                                     
REMARK   3      L33:   2.6037 L12:   1.4526                                     
REMARK   3      L13:   1.1198 L23:   1.0720                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1468 S12:  -0.3761 S13:  -0.2858                       
REMARK   3      S21:   0.5827 S22:  -0.0361 S23:  -0.2969                       
REMARK   3      S31:   0.3235 S32:  -0.1743 S33:  -0.1315                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 837 THROUGH 912 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  53.6749   4.8024  -5.9196              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3757 T22:   0.5385                                     
REMARK   3      T33:   0.3268 T12:  -0.0076                                     
REMARK   3      T13:   0.0384 T23:   0.0506                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7397 L22:   4.4465                                     
REMARK   3      L33:   2.4398 L12:  -0.0144                                     
REMARK   3      L13:  -0.0143 L23:   1.1934                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0116 S12:  -0.2858 S13:   0.1047                       
REMARK   3      S21:   0.2810 S22:  -0.0132 S23:   0.4720                       
REMARK   3      S31:   0.0690 S32:  -0.3643 S33:  -0.0181                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 187 THROUGH 269 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  27.0760 -33.2584  -4.1652              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0101 T22:   1.0127                                     
REMARK   3      T33:   1.3973 T12:  -0.4141                                     
REMARK   3      T13:  -0.0937 T23:   0.3493                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2535 L22:   2.0080                                     
REMARK   3      L33:   2.3561 L12:   1.8175                                     
REMARK   3      L13:  -1.1671 L23:  -0.2436                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0848 S12:  -0.8062 S13:  -0.9298                       
REMARK   3      S21:   0.2741 S22:   0.2969 S23:   1.6504                       
REMARK   3      S31:   0.9278 S32:  -1.0867 S33:  -0.4145                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 270 THROUGH 291 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  30.3236 -34.0531 -12.9569              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0820 T22:   0.8130                                     
REMARK   3      T33:   1.6377 T12:  -0.3475                                     
REMARK   3      T13:  -0.3497 T23:   0.0863                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7410 L22:   2.9892                                     
REMARK   3      L33:   4.1884 L12:   2.2962                                     
REMARK   3      L13:   0.0108 L23:  -0.3111                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5750 S12:   0.4324 S13:  -1.3780                       
REMARK   3      S21:  -0.2028 S22:   0.2438 S23:   1.8596                       
REMARK   3      S31:   1.2554 S32:  -0.4584 S33:  -0.7670                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 292 THROUGH 301 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  30.6211 -20.0813 -18.4444              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7285 T22:   0.8448                                     
REMARK   3      T33:   1.1989 T12:  -0.2912                                     
REMARK   3      T13:  -0.1866 T23:   0.3183                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.7878 L22:   2.5402                                     
REMARK   3      L33:   5.1103 L12:  -4.9085                                     
REMARK   3      L13:   6.2570 L23:  -2.8462                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3462 S12:  -0.0143 S13:  -0.4317                       
REMARK   3      S21:  -0.7719 S22:   0.4440 S23:   1.1259                       
REMARK   3      S31:   0.4007 S32:  -0.9898 S33:  -0.7030                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 302 THROUGH 332 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  23.1456 -32.0123 -21.7109              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1148 T22:   1.0506                                     
REMARK   3      T33:   1.5366 T12:  -0.3503                                     
REMARK   3      T13:  -0.5390 T23:   0.0732                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0107 L22:  -0.0075                                     
REMARK   3      L33:   0.0221 L12:  -0.0010                                     
REMARK   3      L13:   0.0179 L23:  -0.0130                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4665 S12:   1.0592 S13:  -1.2338                       
REMARK   3      S21:  -0.1463 S22:  -0.0085 S23:   0.5884                       
REMARK   3      S31:   1.2121 S32:  -0.4771 S33:  -0.4809                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 333 THROUGH 350 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  15.3013 -25.4590 -25.9486              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4730 T22:   1.7576                                     
REMARK   3      T33:   1.6930 T12:  -0.2994                                     
REMARK   3      T13:  -0.6345 T23:   0.1658                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7820 L22:   3.9301                                     
REMARK   3      L33:   5.6836 L12:  -1.7590                                     
REMARK   3      L13:   2.1111 L23:  -4.7263                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6612 S12:   0.2002 S13:  -0.1667                       
REMARK   3      S21:  -1.4394 S22:  -1.0202 S23:   1.1175                       
REMARK   3      S31:   0.0251 S32:  -0.6457 S33:   0.4576                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 351 THROUGH 378 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  18.5768 -40.9228 -14.6458              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3986 T22:   1.1030                                     
REMARK   3      T33:   1.6988 T12:  -0.5359                                     
REMARK   3      T13:  -0.2723 T23:   0.1601                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5888 L22:   1.0856                                     
REMARK   3      L33:   2.7336 L12:  -1.5568                                     
REMARK   3      L13:   0.3361 L23:   0.5905                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1084 S12:   0.0163 S13:   0.4807                       
REMARK   3      S21:   0.1686 S22:   0.3301 S23:   0.9080                       
REMARK   3      S31:   0.8763 S32:  -0.3818 S33:  -0.2627                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 422 THROUGH 427 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  38.1072   2.4206   9.0060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8406 T22:   1.4309                                     
REMARK   3      T33:   0.8236 T12:  -0.0268                                     
REMARK   3      T13:   0.2460 T23:  -0.0218                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9937 L22:   6.1359                                     
REMARK   3      L33:   1.3176 L12:   0.7680                                     
REMARK   3      L13:   1.0425 L23:  -2.2993                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4170 S12:  -1.0355 S13:   0.2289                       
REMARK   3      S21:   1.5087 S22:   0.4675 S23:   0.6770                       
REMARK   3      S31:  -0.5616 S32:  -0.9622 S33:  -0.6700                       
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 428 THROUGH 437 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  35.9631  14.6973 -14.4146              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6095 T22:   0.9062                                     
REMARK   3      T33:   1.1823 T12:   0.1342                                     
REMARK   3      T13:  -0.0886 T23:   0.1724                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0736 L22:   4.0058                                     
REMARK   3      L33:   2.8114 L12:   1.3518                                     
REMARK   3      L13:  -0.1961 L23:  -3.0918                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0252 S12:  -0.0149 S13:   1.1107                       
REMARK   3      S21:  -0.0566 S22:   0.7670 S23:   1.7526                       
REMARK   3      S31:  -0.1652 S32:  -0.8988 S33:  -0.7020                       
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 438 THROUGH 446 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  48.6035  27.9203 -40.8078              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3410 T22:   0.7749                                     
REMARK   3      T33:   0.6410 T12:  -0.0899                                     
REMARK   3      T13:  -0.2158 T23:   0.0305                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7608 L22:   9.2943                                     
REMARK   3      L33:   4.3247 L12:   4.6680                                     
REMARK   3      L13:  -0.2489 L23:  -3.4865                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.9802 S12:   1.3287 S13:   0.3952                       
REMARK   3      S21:  -2.0203 S22:   1.3898 S23:   0.6941                       
REMARK   3      S31:  -0.2811 S32:  -0.6393 S33:  -0.3602                       
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 422 THROUGH 431 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  51.6249  27.3006 -39.2539              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8854 T22:   0.5247                                     
REMARK   3      T33:   0.6034 T12:  -0.0109                                     
REMARK   3      T13:  -0.1827 T23:  -0.0109                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2642 L22:   5.6103                                     
REMARK   3      L33:   8.7424 L12:   1.2883                                     
REMARK   3      L13:  -1.7648 L23:   0.2988                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2230 S12:   0.9180 S13:  -0.5169                       
REMARK   3      S21:  -1.5417 S22:   0.0011 S23:   0.6915                       
REMARK   3      S31:   0.3295 S32:  -0.8800 S33:   0.3004                       
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 432 THROUGH 439 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  37.4835  15.9886 -17.8888              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4854 T22:   0.8841                                     
REMARK   3      T33:   1.1400 T12:  -0.0572                                     
REMARK   3      T13:  -0.1420 T23:   0.1330                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1902 L22:   9.9359                                     
REMARK   3      L33:   3.5033 L12:  -2.3691                                     
REMARK   3      L13:  -2.2547 L23:  -0.1398                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0504 S12:  -0.0222 S13:   0.8524                       
REMARK   3      S21:  -0.1775 S22:   0.5704 S23:   2.2089                       
REMARK   3      S31:   0.9417 S32:  -1.1670 S33:  -0.5989                       
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 440 THROUGH 446 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  31.4277   3.0265   4.6658              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7189 T22:   1.4170                                     
REMARK   3      T33:   1.1548 T12:  -0.0656                                     
REMARK   3      T13:   0.2588 T23:   0.1806                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8540 L22:   5.7055                                     
REMARK   3      L33:   4.0476 L12:   1.5626                                     
REMARK   3      L13:  -0.3364 L23:  -3.3376                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4325 S12:  -1.3829 S13:  -0.1588                       
REMARK   3      S21:   1.4698 S22:   0.1153 S23:   1.8234                       
REMARK   3      S31:  -0.6550 S32:  -0.3009 S33:  -0.6032                       
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 5YX2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-DEC-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300006052.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-APR-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9774                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40049                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: PHENIX                                                
REMARK 200 STARTING MODEL: 2QRV                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL (PH 7.0), 200 MM          
REMARK 280  NAH2PO4, 5% PEG 4000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE    
REMARK 280  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      102.71200            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       59.30080            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       29.77900            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000      102.71200            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       59.30080            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       29.77900            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000      102.71200            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       59.30080            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       29.77900            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      118.60160            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       59.55800            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000      118.60160            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       59.55800            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000      118.60160            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       59.55800            
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     ASP B   214                                                      
REMARK 465     PRO B   215                                                      
REMARK 465     GLY B   216                                                      
REMARK 465     HIS B   313                                                      
REMARK 465     GLY B   314                                                      
REMARK 465     GLY B   315                                                      
REMARK 465     SER B   316                                                      
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     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     ARG C   186                                                      
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     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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 630    CD   CE   NZ                                        
REMARK 470     LYS A 632    CE   NZ                                             
REMARK 470     LYS A 693    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     ILE A 824    CD1                                                 
REMARK 470     LYS A 826    NZ                                                  
REMARK 470     LYS A 844    CE   NZ                                             
REMARK 470     GLN A 846    CD   OE1  NE2                                       
REMARK 470     GLU A 854    CD   OE1  OE2                                       
REMARK 470     LYS A 855    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     MET B 178    CG   SD   CE                                        
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     GLU B 197    CD   OE1  OE2                                       
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    CD   OE1  OE2                                       
REMARK 470     GLN B 217    CD   OE1  NE2                                       
REMARK 470     LYS B 230    CG   CD   CE   NZ                                   
REMARK 470     GLU B 234    CD   OE1  OE2                                       
REMARK 470     LEU B 248    CG   CD1  CD2                                       
REMARK 470     HIS B 250    CG   ND1  CD2  CE1  NE2                             
REMARK 470     THR B 251    OG1  CG2                                            
REMARK 470     ASP B 253    CG   OD1  OD2                                       
REMARK 470     LYS B 273    CE   NZ                                             
REMARK 470     SER B 276    CB   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     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     ASN B 349    OD1  ND2                                            
REMARK 470     LYS B 350    CG   CD   CE   NZ                                   
REMARK 470     GLN B 351    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 362    CG   CD   CE   NZ                                   
REMARK 470     LEU B 363    CG   CD1  CD2                                       
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    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     LYS D 783    CG   CD   CE   NZ                                   
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 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     PRO C 215    N    CB   CG   CD                                   
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     ARG C 271    CZ   NH1  NH2                                       
REMARK 470     LYS C 273    CG   CD   CE   NZ                                   
REMARK 470     SER C 276    OG                                                  
REMARK 470     ARG C 278    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     LYS C 292    CE   NZ                                             
REMARK 470     ASP C 311    CG   OD1  OD2                                       
REMARK 470     HIS C 313    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU C 317    CB   CG   CD1  CD2                                  
REMARK 470     GLN C 318    CG   CD   OE1  NE2                                  
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    CG   CD   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: 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    ARG A 790       85.28   -154.15                                   
REMARK 500    PHE B 196      -58.86     71.49                                   
REMARK 500    ASN B 287       42.49    -97.79                                   
REMARK 500    LYS B 362      -70.57    -56.48                                   
REMARK 500    PRO B 370        6.17    -66.24                                   
REMARK 500    ILE D 643       30.93    -99.11                                   
REMARK 500    ARG D 790       86.89   -168.10                                   
REMARK 500    PRO C 189     -172.38    -64.41                                   
REMARK 500    PHE C 196      -57.49     65.08                                   
REMARK 500    TRP C 235       21.85    -77.85                                   
REMARK 500    ARG C 278     -143.57   -139.65                                   
REMARK 500    GLN C 318      -71.40   -128.11                                   
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 GOL A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH A 1005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH D 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
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: AD1                                                 
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: AD2                                                 
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: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-nucleotide PYO F 427 and DG    
REMARK 800  F 428                                                               
DBREF  5YX2 A  628   912  UNP    Q9Y6K1   DNM3A_HUMAN    628    912             
DBREF  5YX2 B  178   385  UNP    Q9UJW3   DNM3L_HUMAN    178    385             
DBREF  5YX2 D  628   912  UNP    Q9Y6K1   DNM3A_HUMAN    628    912             
DBREF  5YX2 C  178   385  UNP    Q9UJW3   DNM3L_HUMAN    178    385             
DBREF  5YX2 E  422   446  PDB    5YX2     5YX2           422    446             
DBREF  5YX2 F  422   446  PDB    5YX2     5YX2           422    446             
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  ARG 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  208  MET PHE GLU THR VAL PRO VAL TRP ARG ARG GLN PRO VAL          
SEQRES   2 B  208  ARG VAL LEU SER LEU PHE GLU ASP ILE LYS LYS GLU LEU          
SEQRES   3 B  208  THR SER LEU GLY PHE LEU GLU SER GLY SER ASP PRO GLY          
SEQRES   4 B  208  GLN LEU LYS HIS VAL VAL ASP VAL THR ASP THR VAL ARG          
SEQRES   5 B  208  LYS ASP VAL GLU GLU TRP GLY PRO PHE ASP LEU VAL TYR          
SEQRES   6 B  208  GLY ALA THR PRO PRO LEU GLY HIS THR CYS ASP ARG PRO          
SEQRES   7 B  208  PRO SER TRP TYR LEU PHE GLN PHE HIS ARG LEU LEU GLN          
SEQRES   8 B  208  TYR ALA ARG PRO LYS PRO GLY SER PRO ARG PRO PHE PHE          
SEQRES   9 B  208  TRP MET PHE VAL ASP ASN LEU VAL LEU ASN LYS GLU ASP          
SEQRES  10 B  208  LEU ASP VAL ALA SER ARG PHE LEU GLU MET GLU PRO VAL          
SEQRES  11 B  208  THR ILE PRO ASP VAL HIS GLY GLY SER LEU GLN ASN ALA          
SEQRES  12 B  208  VAL ARG VAL TRP SER ASN ILE PRO ALA ILE ARG SER ARG          
SEQRES  13 B  208  HIS TRP ALA LEU VAL SER GLU GLU GLU LEU SER LEU LEU          
SEQRES  14 B  208  ALA GLN ASN LYS GLN SER SER LYS LEU ALA ALA LYS TRP          
SEQRES  15 B  208  PRO THR LYS LEU VAL LYS ASN CYS PHE LEU PRO LEU ARG          
SEQRES  16 B  208  GLU TYR PHE LYS TYR PHE SER THR GLU LEU THR SER SER          
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  ARG 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  208  MET PHE GLU THR VAL PRO VAL TRP ARG ARG GLN PRO VAL          
SEQRES   2 C  208  ARG VAL LEU SER LEU PHE GLU ASP ILE LYS LYS GLU LEU          
SEQRES   3 C  208  THR SER LEU GLY PHE LEU GLU SER GLY SER ASP PRO GLY          
SEQRES   4 C  208  GLN LEU LYS HIS VAL VAL ASP VAL THR ASP THR VAL ARG          
SEQRES   5 C  208  LYS ASP VAL GLU GLU TRP GLY PRO PHE ASP LEU VAL TYR          
SEQRES   6 C  208  GLY ALA THR PRO PRO LEU GLY HIS THR CYS ASP ARG PRO          
SEQRES   7 C  208  PRO SER TRP TYR LEU PHE GLN PHE HIS ARG LEU LEU GLN          
SEQRES   8 C  208  TYR ALA ARG PRO LYS PRO GLY SER PRO ARG PRO PHE PHE          
SEQRES   9 C  208  TRP MET PHE VAL ASP ASN LEU VAL LEU ASN LYS GLU ASP          
SEQRES  10 C  208  LEU ASP VAL ALA SER ARG PHE LEU GLU MET GLU PRO VAL          
SEQRES  11 C  208  THR ILE PRO ASP VAL HIS GLY GLY SER LEU GLN ASN ALA          
SEQRES  12 C  208  VAL ARG VAL TRP SER ASN ILE PRO ALA ILE ARG SER ARG          
SEQRES  13 C  208  HIS TRP ALA LEU VAL SER GLU GLU GLU LEU SER LEU LEU          
SEQRES  14 C  208  ALA GLN ASN LYS GLN SER SER LYS LEU ALA ALA LYS TRP          
SEQRES  15 C  208  PRO THR LYS LEU VAL LYS ASN CYS PHE LEU PRO LEU ARG          
SEQRES  16 C  208  GLU TYR PHE LYS TYR PHE SER THR GLU LEU THR SER SER          
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    GOL  A1001       6                                                       
HET    GOL  A1002       6                                                       
HET    GOL  A1003       6                                                       
HET    GOL  A1004       6                                                       
HET    SAH  A1005      26                                                       
HET    GOL  D1001       6                                                       
HET    SAH  D1002      26                                                       
HET    GOL  E 501       6                                                       
HETNAM     PYO 1-(BETA-D-RIBOFURANOSYL)-PYRIMIDIN-2-ONE-5'-PHOSPHATE            
HETNAM     GOL GLYCEROL                                                         
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  PYO    2(C9 H13 N2 O8 P)                                            
FORMUL   7  GOL    6(C3 H8 O3)                                                  
FORMUL  11  SAH    2(C14 H20 N6 O5 S)                                           
FORMUL  15  HOH   *75(H2 O)                                                     
HELIX    1 AA1 ALA A  644  LEU A  653  1                                  10    
HELIX    2 AA2 CYS A  666  HIS A  677  1                                  12    
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 ARG A  836  LYS A  841  5                                   6    
HELIX   11 AB2 TRP A  860  GLY A  869  1                                  10    
HELIX   12 AB3 SER A  881  SER A  892  1                                  12    
HELIX   13 AB4 SER A  894  ALA A  903  1                                  10    
HELIX   14 AB5 PRO A  904  LYS A  906  5                                   3    
HELIX   15 AB6 PRO B  183  ARG B  187  5                                   5    
HELIX   16 AB7 ILE B  199  GLY B  207  1                                   9    
HELIX   17 AB8 VAL B  228  TRP B  235  1                                   8    
HELIX   18 AB9 PRO B  255  ALA B  270  1                                  16    
HELIX   19 AC1 ASN B  291  LEU B  302  1                                  12    
HELIX   20 AC2 ILE B  327  ARG B  333  1                                   7    
HELIX   21 AC3 SER B  339  SER B  353  1                                  15    
HELIX   22 AC4 LYS B  362  ASN B  366  5                                   5    
HELIX   23 AC5 PHE B  368  ARG B  372  5                                   5    
HELIX   24 AC6 ALA D  644  GLY D  654  1                                  11    
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  GLU D  774  1                                  13    
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 ARG D  836  LYS D  841  5                                   6    
HELIX   34 AD7 TRP D  860  GLY D  869  1                                  10    
HELIX   35 AD8 SER D  881  SER D  892  1                                  12    
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 ILE C  199  LEU C  206  1                                   8    
HELIX   39 AE3 VAL C  228  TRP C  235  1                                   8    
HELIX   40 AE4 PRO C  255  ALA C  270  1                                  16    
HELIX   41 AE5 ASN C  291  LEU C  302  1                                  12    
HELIX   42 AE6 ILE C  327  ARG C  333  1                                   7    
HELIX   43 AE7 SER C  339  ASN C  349  1                                  11    
HELIX   44 AE8 PHE C  368  ARG C  372  5                                   5    
SHEET    1 AA1 7 ILE A 681  TYR A 683  0                                        
SHEET    2 AA1 7 VAL A 657  SER A 663  1  N  ALA A 662   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  TYR A 793   N  ASN A 757           
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  MET A 852 -1  O  PHE A 851   N  ILE A 824           
SHEET    3 AA2 3 LYS A 855  ASP A 857 -1  O  LYS A 855   N  MET A 852           
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  TRP B 324   N  PHE B 284           
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  ILE D 661           
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  LYS D 855   N  MET D 852           
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  TYR C 242   N  LEU C 193           
SHEET    4 AA6 6 PHE C 281  ASP C 286  1  O  PHE C 281   N  VAL C 241           
SHEET    5 AA6 6 ASN C 319  SER C 325 -1  O  TRP C 324   N  PHE C 284           
SHEET    6 AA6 6 VAL C 307  ASP C 311 -1  N  ILE C 309   O  VAL C 321           
LINK         SG  CYS A 710                 C6  PYO F 427     1555   1555  1.86  
LINK         SG  CYS D 710                 C6  PYO E 427     1555   1555  1.87  
LINK         O3'  DG E 426                 P   PYO E 427     1555   1555  1.61  
LINK         O3' PYO E 427                 P    DG E 428     1555   1555  1.60  
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        -0.47                     
CISPEP   2 GLY D  699    PRO D  700          0        -1.64                     
SITE     1 AC1  2 HIS A 847  GLU A 856                                          
SITE     1 AC2  5 PRO A 709  ASN A 711  ARG A 891  SAH A1005                    
SITE     2 AC2  5 HOH A1112                                                     
SITE     1 AC3  4 ARG A 866  VAL A 872  GOL A1004  VAL D 809                    
SITE     1 AC4  3 HIS A 873  GOL A1003  ARG D 676                               
SITE     1 AC5 22 PHE A 640  ASP A 641  GLY A 642  ILE A 643                    
SITE     2 AC5 22 THR A 645  SER A 663  GLU A 664  VAL A 665                    
SITE     3 AC5 22 CYS A 666  ASP A 686  VAL A 687  ARG A 688                    
SITE     4 AC5 22 GLY A 707  PRO A 709  LEU A 730  ARG A 891                    
SITE     5 AC5 22 SER A 892  TRP A 893  GOL A1002  HOH A1101                    
SITE     6 AC5 22 HOH A1107  HOH A1108                                          
SITE     1 AC6  4 PHE D 751  PHE D 752  ASN D 797   DC F 423                    
SITE     1 AC7 17 PHE D 640  ASP D 641  GLY D 642  ILE D 643                    
SITE     2 AC7 17 THR D 645  SER D 663  GLU D 664  VAL D 665                    
SITE     3 AC7 17 CYS D 666  ASP D 686  VAL D 687  GLY D 707                    
SITE     4 AC7 17 LEU D 730  ARG D 891  SER D 892  TRP D 893                    
SITE     5 AC7 17 HOH D1104                                                     
SITE     1 AC8  5 ASN D 711  THR D 835  ARG D 891   DG E 428                    
SITE     2 AC8  5  DT E 429                                                     
SITE     1 AC9 20 SER D 708  CYS D 710  SER D 714  ILE D 715                    
SITE     2 AC9 20 VAL D 716  GLU D 756  VAL D 758  ALA D 760                    
SITE     3 AC9 20 ARG D 790  ARG D 792  ARG D 831  THR D 832                    
SITE     4 AC9 20 THR D 834  GLY D 890  ARG D 891   DT E 425                    
SITE     5 AC9 20  DG E 428   DG F 442   DC F 443   DA F 444                    
SITE     1 AD1 21 SER D 708  CYS D 710  ASN D 711  SER D 714                    
SITE     2 AD1 21 VAL D 716  ASN D 717  PRO D 718  GLU D 756                    
SITE     3 AD1 21 VAL D 758  ALA D 760  ARG D 790  ARG D 792                    
SITE     4 AD1 21 THR D 834  THR D 835  ARG D 836  GLY D 890                    
SITE     5 AD1 21 ARG D 891   DG E 426   DT E 429  GOL E 501                    
SITE     6 AD1 21  DC F 441                                                     
SITE     1 AD2 20 SER A 708  CYS A 710  SER A 714  ILE A 715                    
SITE     2 AD2 20 VAL A 716  GLU A 756  VAL A 758  ALA A 760                    
SITE     3 AD2 20 ARG A 790  ARG A 792  ARG A 831  THR A 832                    
SITE     4 AD2 20 THR A 834  GLY A 890  ARG A 891   DG E 442                    
SITE     5 AD2 20  DC E 443   DA E 444   DT F 425   DG F 428                    
SITE     1 AD3 24 SER A 708  CYS A 710  ASN A 711  SER A 714                    
SITE     2 AD3 24 VAL A 716  ASN A 717  PRO A 718  GLU A 756                    
SITE     3 AD3 24 VAL A 758  ALA A 760  ARG A 790  ARG A 792                    
SITE     4 AD3 24 THR A 834  THR A 835  ARG A 836  GLY A 890                    
SITE     5 AD3 24 ARG A 891  HOH A1102   DA E 440   DC E 441                    
SITE     6 AD3 24  DG F 426   DT F 429  HOH F 501  HOH F 506                    
CRYST1  205.424  205.424   89.337  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      0.004868  0.002811  0.000000        0.00000                         
SCALE2      0.000000  0.005621  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011194        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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