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Database: PDB
Entry: 6F57
LinkDB: 6F57
Original site: 6F57 
HEADER    TRANSFERASE/DNA                         01-DEC-17   6F57              
TITLE     CRYSTAL STRUCTURE OF DNMT3A-DNMT3L IN COMPLEX WITH SINGLE CPG-        
TITLE    2 CONTAINING DNA                                                       
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 (5'-D(*AP*GP*AP*GP*CP*GP*CP*AP*TP*G)-3');              
COMPND  13 CHAIN: E, G;                                                         
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 4;                                                           
COMPND  16 MOLECULE: DNA (5'-D(*CP*AP*TP*GP*ZP*GP*CP*TP*CP*T)-3');              
COMPND  17 CHAIN: F, H;                                                         
COMPND  18 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 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: DNMT3L;                                                        
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 SYNTHETIC: YES;                                                      
SOURCE  17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  18 ORGANISM_COMMON: HUMAN;                                              
SOURCE  19 ORGANISM_TAXID: 9606;                                                
SOURCE  20 MOL_ID: 4;                                                           
SOURCE  21 SYNTHETIC: YES;                                                      
SOURCE  22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  23 ORGANISM_COMMON: HUMAN;                                              
SOURCE  24 ORGANISM_TAXID: 9606                                                 
KEYWDS    DNMT3A, DNMT3L, DNA METHYLATION, DNA BINDING PROTEIN, TRANSFERASE-DNA 
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.M.ZHANG,J.SONG                                                      
REVDAT   4   28-FEB-18 6F57    1       JRNL                                     
REVDAT   3   21-FEB-18 6F57    1       JRNL                                     
REVDAT   2   07-FEB-18 6F57    1       JRNL                                     
REVDAT   1   31-JAN-18 6F57    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.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.72                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 26650                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.213                           
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.580                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2020                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 47.7216 -  7.4568    1.00     1945   157  0.1880 0.2229        
REMARK   3     2  7.4568 -  5.9222    1.00     1818   154  0.2111 0.2754        
REMARK   3     3  5.9222 -  5.1746    1.00     1809   141  0.2021 0.2249        
REMARK   3     4  5.1746 -  4.7020    1.00     1765   151  0.1810 0.2086        
REMARK   3     5  4.7020 -  4.3652    1.00     1779   140  0.1710 0.2035        
REMARK   3     6  4.3652 -  4.1080    1.00     1751   141  0.1700 0.2042        
REMARK   3     7  4.1080 -  3.9024    1.00     1774   141  0.1961 0.1981        
REMARK   3     8  3.9024 -  3.7326    0.99     1737   147  0.2002 0.1984        
REMARK   3     9  3.7326 -  3.5889    0.99     1712   150  0.2209 0.2694        
REMARK   3    10  3.5889 -  3.4651    0.99     1752   128  0.2415 0.2734        
REMARK   3    11  3.4651 -  3.3568    0.99     1725   144  0.2665 0.3472        
REMARK   3    12  3.3568 -  3.2609    0.99     1721   148  0.2773 0.3028        
REMARK   3    13  3.2609 -  3.1750    0.99     1723   137  0.3117 0.3024        
REMARK   3    14  3.1750 -  3.0976    0.96     1619   141  0.3367 0.3657        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.380            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.670           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           7899                                  
REMARK   3   ANGLE     :  0.776          10895                                  
REMARK   3   CHIRALITY :  0.030           1193                                  
REMARK   3   PLANARITY :  0.003           1267                                  
REMARK   3   DIHEDRAL  : 17.688           2864                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 6F57 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-DEC-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200007765.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-OCT-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.1                              
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   : 26661                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.090                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.720                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.17600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.09                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.20                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.98200                            
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   (%): 56.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 7% PEG4000, 0.1 M TRIS-HCL (PH 8.5),     
REMARK 280  100 MM MGCL2, 166 MM IMIDAZOLE (PH 7.0), VAPOR DIFFUSION,           
REMARK 280  HANGING DROP, TEMPERATURE 296K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       88.30550            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.77950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       88.30550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       24.77950            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5650 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21590 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5650 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21050 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, G, H                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET B   178                                                      
REMARK 465     PHE B   179                                                      
REMARK 465     GLU B   180                                                      
REMARK 465     THR B   181                                                      
REMARK 465     VAL B   182                                                      
REMARK 465     PRO B   183                                                      
REMARK 465     VAL B   184                                                      
REMARK 465     TRP B   185                                                      
REMARK 465     ARG B   186                                                      
REMARK 465     ARG B   187                                                      
REMARK 465     SER B   211                                                      
REMARK 465     GLY B   212                                                      
REMARK 465     SER B   213                                                      
REMARK 465     ASP B   214                                                      
REMARK 465     PRO B   215                                                      
REMARK 465     HIS B   313                                                      
REMARK 465     GLY B   314                                                      
REMARK 465     GLY B   315                                                      
REMARK 465     SER B   316                                                      
REMARK 465     LEU B   317                                                      
REMARK 465     ALA B   329                                                      
REMARK 465     ILE B   330                                                      
REMARK 465     ARG B   331                                                      
REMARK 465     SER B   332                                                      
REMARK 465     ARG B   333                                                      
REMARK 465     HIS B   334                                                      
REMARK 465     TRP B   335                                                      
REMARK 465     ALA B   336                                                      
REMARK 465     LEU B   337                                                      
REMARK 465     VAL B   338                                                      
REMARK 465     SER B   339                                                      
REMARK 465     GLU B   340                                                      
REMARK 465     GLU B   341                                                      
REMARK 465     GLU B   342                                                      
REMARK 465     LEU B   343                                                      
REMARK 465     SER B   344                                                      
REMARK 465     LEU B   345                                                      
REMARK 465     LEU B   346                                                      
REMARK 465     ALA B   347                                                      
REMARK 465     GLN B   348                                                      
REMARK 465     ASN B   349                                                      
REMARK 465     LYS B   350                                                      
REMARK 465     GLN B   351                                                      
REMARK 465     SER B   352                                                      
REMARK 465     SER B   353                                                      
REMARK 465     LYS B   354                                                      
REMARK 465     LEU B   355                                                      
REMARK 465     ALA B   356                                                      
REMARK 465     ALA B   357                                                      
REMARK 465     LYS B   358                                                      
REMARK 465     TRP B   359                                                      
REMARK 465     PRO B   360                                                      
REMARK 465     THR B   380                                                      
REMARK 465     GLU B   381                                                      
REMARK 465     LEU B   382                                                      
REMARK 465     THR B   383                                                      
REMARK 465     SER B   384                                                      
REMARK 465     SER B   385                                                      
REMARK 465     LEU B   386                                                      
REMARK 465     MET C   178                                                      
REMARK 465     PHE C   179                                                      
REMARK 465     GLU C   180                                                      
REMARK 465     SER C   211                                                      
REMARK 465     GLY C   212                                                      
REMARK 465     SER C   213                                                      
REMARK 465     ASP C   214                                                      
REMARK 465     PRO C   215                                                      
REMARK 465     PRO C   310                                                      
REMARK 465     ASP C   311                                                      
REMARK 465     VAL C   312                                                      
REMARK 465     HIS C   313                                                      
REMARK 465     GLY C   314                                                      
REMARK 465     GLY C   315                                                      
REMARK 465     SER C   316                                                      
REMARK 465     LEU C   317                                                      
REMARK 465     ALA C   329                                                      
REMARK 465     ILE C   330                                                      
REMARK 465     ARG C   331                                                      
REMARK 465     SER C   332                                                      
REMARK 465     ARG C   333                                                      
REMARK 465     HIS C   334                                                      
REMARK 465     TRP C   335                                                      
REMARK 465     ALA C   336                                                      
REMARK 465     LEU C   337                                                      
REMARK 465     VAL C   338                                                      
REMARK 465     SER C   339                                                      
REMARK 465     GLU C   340                                                      
REMARK 465     GLU C   341                                                      
REMARK 465     GLU C   342                                                      
REMARK 465     LEU C   343                                                      
REMARK 465     SER C   344                                                      
REMARK 465     LEU C   345                                                      
REMARK 465     LEU C   346                                                      
REMARK 465     ALA C   347                                                      
REMARK 465     GLN C   348                                                      
REMARK 465     ASN C   349                                                      
REMARK 465     LYS C   350                                                      
REMARK 465     GLN C   351                                                      
REMARK 465     SER C   352                                                      
REMARK 465     SER C   353                                                      
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     THR C   361                                                      
REMARK 465     LYS C   362                                                      
REMARK 465     SER C   379                                                      
REMARK 465     THR C   380                                                      
REMARK 465     GLU C   381                                                      
REMARK 465     LEU C   382                                                      
REMARK 465     THR C   383                                                      
REMARK 465     SER C   384                                                      
REMARK 465     SER C   385                                                      
REMARK 465     LEU C   386                                                      
REMARK 465     ALA D   628                                                      
REMARK 465     GLU D   629                                                      
REMARK 465      DC F   433                                                      
REMARK 465      DC H   433                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 629    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 630    CG   CD   CE   NZ                                   
REMARK 470     LYS A 632    CE   NZ                                             
REMARK 470     LYS A 693    CG   CD   CE   NZ                                   
REMARK 470     GLN A 696    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 744    CG   CD   CE   NZ                                   
REMARK 470     GLU A 745    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 748    OD1  OD2                                            
REMARK 470     LYS A 783    CG   CD   CE   NZ                                   
REMARK 470     LYS A 855    CG   CD   CE   NZ                                   
REMARK 470     VAL A 912    CG1  CG2                                            
REMARK 470     GLN B 188    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 197    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 198    CB   CG   OD1  OD2                                  
REMARK 470     LYS B 200    CE   NZ                                             
REMARK 470     LYS B 201    CG   CD   CE   NZ                                   
REMARK 470     GLU B 202    CD   OE1  OE2                                       
REMARK 470     LEU B 203    CG   CD1  CD2                                       
REMARK 470     LEU B 206    CG   CD1  CD2                                       
REMARK 470     GLN B 217    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 230    CG   CD   CE   NZ                                   
REMARK 470     GLU B 234    CD   OE1  OE2                                       
REMARK 470     PHE B 238    O                                                   
REMARK 470     ASP B 239    CG   OD1  OD2                                       
REMARK 470     LEU B 240    CG   CD1  CD2                                       
REMARK 470     HIS B 250    CG   ND1  CD2  CE1  NE2                             
REMARK 470     THR B 251    OG1  CG2                                            
REMARK 470     CYS B 252    SG                                                  
REMARK 470     ASP B 253    CG   OD1  OD2                                       
REMARK 470     ARG B 254    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 273    CG   CD   CE   NZ                                   
REMARK 470     ARG B 278    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     LEU B 288    CG   CD1  CD2                                       
REMARK 470     LYS B 292    CD   CE   NZ                                        
REMARK 470     GLU B 293    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 311    CG   OD1  OD2                                       
REMARK 470     GLN B 318    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     ASN B 366    CG   OD1  ND2                                       
REMARK 470     CYS B 367    CB   SG                                             
REMARK 470     LEU B 369    CB   CG   CD1  CD2                                  
REMARK 470     LEU B 371    CB   CG   CD1  CD2                                  
REMARK 470     ARG B 372    CD   NE   CZ   NH1  NH2                             
REMARK 470     PHE B 375    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B 376    CG   CD   CE   NZ                                   
REMARK 470     TYR B 377    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     PHE B 378    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     SER B 379    OG                                                  
REMARK 470     ARG C 186    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN C 188    CD   OE1  NE2                                       
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 203    CG   CD1  CD2                                       
REMARK 470     LEU C 206    CG   CD1  CD2                                       
REMARK 470     LEU C 209    CG   CD1  CD2                                       
REMARK 470     GLU C 210    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 219    CD   CE   NZ                                        
REMARK 470     LYS C 230    CE   NZ                                             
REMARK 470     GLU C 234    CD   OE1  OE2                                       
REMARK 470     HIS C 250    CB   CG   ND1  CD2  CE1  NE2                        
REMARK 470     THR C 251    OG1  CG2                                            
REMARK 470     CYS C 252    CB   SG                                             
REMARK 470     ASP C 253    CG   OD1  OD2                                       
REMARK 470     ARG C 254    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    CD   CE   NZ                                        
REMARK 470     GLU C 293    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 318    CG   CD   OE1  NE2                                  
REMARK 470     ASN C 326    OD1  ND2                                            
REMARK 470     ILE C 327    CG1  CG2  CD1                                       
REMARK 470     LEU C 363    CB   CG   CD1  CD2                                  
REMARK 470     VAL C 364    CB   CG1  CG2                                       
REMARK 470     LYS C 365    CG   CD   CE   NZ                                   
REMARK 470     ASN C 366    CB   CG   OD1  ND2                                  
REMARK 470     CYS C 367    SG                                                  
REMARK 470     LEU C 369    CG   CD1  CD2                                       
REMARK 470     ARG C 372    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 373    CD   OE1  OE2                                       
REMARK 470     LYS C 376    CG   CD   CE   NZ                                   
REMARK 470     LYS D 630    CG   CD   CE   NZ                                   
REMARK 470     ARG D 631    NE   CZ   NH1  NH2                                  
REMARK 470     LYS D 632    CG   CD   CE   NZ                                   
REMARK 470     LYS D 693    CG   CD   CE   NZ                                   
REMARK 470     GLN D 696    CD   OE1  NE2                                       
REMARK 470     LYS D 744    CG   CD   CE   NZ                                   
REMARK 470     GLU D 745    CB   CG   CD   OE1  OE2                             
REMARK 470     ASP D 748    CG   OD1  OD2                                       
REMARK 470     LYS D 783    CG   CD   CE   NZ                                   
REMARK 470     GLU D 784    CD   OE1  OE2                                       
REMARK 470     LYS D 906    CG   CD   CE   NZ                                   
REMARK 470      DC H 423    O5'                                                 
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    VAL A   690     NH2  ARG A   736              2.07            
REMARK 500   OG   SER C   194     O    GLU C   197              2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ILE A 643       30.49    -96.72                                   
REMARK 500    ALA A 719       57.34    -95.00                                   
REMARK 500    ARG A 736      -70.87    -29.85                                   
REMARK 500    ALA A 760       49.38    -69.04                                   
REMARK 500    VAL A 785       -1.15   -144.96                                   
REMARK 500    ARG A 790       71.73   -152.94                                   
REMARK 500    ASN A 797       21.66   -141.91                                   
REMARK 500    ASN A 853       68.89     37.20                                   
REMARK 500    PRO B 189     -169.56    -69.67                                   
REMARK 500    PHE B 196       -3.89     62.60                                   
REMARK 500    GLN B 217       -3.52   -141.00                                   
REMARK 500    PRO B 272     -113.36    -72.18                                   
REMARK 500    ASN B 287       47.12    -91.29                                   
REMARK 500    ASN C 287       47.07    -94.44                                   
REMARK 500    TRP D 698       30.41    -83.61                                   
REMARK 500    ALA D 719       59.01    -93.52                                   
REMARK 500    ASN D 797       18.43   -144.93                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH D 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-nucleotide DG F 426 and Z F    
REMARK 800  427                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-nucleotide Z F 427 and DG F    
REMARK 800  428                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-nucleotide DG H 426 and Z H    
REMARK 800  427                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-nucleotide Z H 427 and DG H    
REMARK 800  428                                                                 
DBREF  6F57 A  628   912  UNP    Q9Y6K1   DNM3A_HUMAN    628    912             
DBREF  6F57 B  178   386  UNP    Q9UJW3   DNM3L_HUMAN    178    386             
DBREF  6F57 C  178   386  UNP    Q9UJW3   DNM3L_HUMAN    178    386             
DBREF  6F57 D  628   912  UNP    Q9Y6K1   DNM3A_HUMAN    628    912             
DBREF  6F57 E  403   412  PDB    6F57     6F57           403    412             
DBREF  6F57 F  423   433  PDB    6F57     6F57           423    433             
DBREF  6F57 G  403   412  PDB    6F57     6F57           403    412             
DBREF  6F57 H  423   433  PDB    6F57     6F57           423    433             
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  209  MET PHE GLU THR VAL PRO VAL TRP ARG ARG GLN PRO VAL          
SEQRES   2 B  209  ARG VAL LEU SER LEU PHE GLU ASP ILE LYS LYS GLU LEU          
SEQRES   3 B  209  THR SER LEU GLY PHE LEU GLU SER GLY SER ASP PRO GLY          
SEQRES   4 B  209  GLN LEU LYS HIS VAL VAL ASP VAL THR ASP THR VAL ARG          
SEQRES   5 B  209  LYS ASP VAL GLU GLU TRP GLY PRO PHE ASP LEU VAL TYR          
SEQRES   6 B  209  GLY ALA THR PRO PRO LEU GLY HIS THR CYS ASP ARG PRO          
SEQRES   7 B  209  PRO SER TRP TYR LEU PHE GLN PHE HIS ARG LEU LEU GLN          
SEQRES   8 B  209  TYR ALA ARG PRO LYS PRO GLY SER PRO ARG PRO PHE PHE          
SEQRES   9 B  209  TRP MET PHE VAL ASP ASN LEU VAL LEU ASN LYS GLU ASP          
SEQRES  10 B  209  LEU ASP VAL ALA SER ARG PHE LEU GLU MET GLU PRO VAL          
SEQRES  11 B  209  THR ILE PRO ASP VAL HIS GLY GLY SER LEU GLN ASN ALA          
SEQRES  12 B  209  VAL ARG VAL TRP SER ASN ILE PRO ALA ILE ARG SER ARG          
SEQRES  13 B  209  HIS TRP ALA LEU VAL SER GLU GLU GLU LEU SER LEU LEU          
SEQRES  14 B  209  ALA GLN ASN LYS GLN SER SER LYS LEU ALA ALA LYS TRP          
SEQRES  15 B  209  PRO THR LYS LEU VAL LYS ASN CYS PHE LEU PRO LEU ARG          
SEQRES  16 B  209  GLU TYR PHE LYS TYR PHE SER THR GLU LEU THR SER SER          
SEQRES  17 B  209  LEU                                                          
SEQRES   1 C  209  MET PHE GLU THR VAL PRO VAL TRP ARG ARG GLN PRO VAL          
SEQRES   2 C  209  ARG VAL LEU SER LEU PHE GLU ASP ILE LYS LYS GLU LEU          
SEQRES   3 C  209  THR SER LEU GLY PHE LEU GLU SER GLY SER ASP PRO GLY          
SEQRES   4 C  209  GLN LEU LYS HIS VAL VAL ASP VAL THR ASP THR VAL ARG          
SEQRES   5 C  209  LYS ASP VAL GLU GLU TRP GLY PRO PHE ASP LEU VAL TYR          
SEQRES   6 C  209  GLY ALA THR PRO PRO LEU GLY HIS THR CYS ASP ARG PRO          
SEQRES   7 C  209  PRO SER TRP TYR LEU PHE GLN PHE HIS ARG LEU LEU GLN          
SEQRES   8 C  209  TYR ALA ARG PRO LYS PRO GLY SER PRO ARG PRO PHE PHE          
SEQRES   9 C  209  TRP MET PHE VAL ASP ASN LEU VAL LEU ASN LYS GLU ASP          
SEQRES  10 C  209  LEU ASP VAL ALA SER ARG PHE LEU GLU MET GLU PRO VAL          
SEQRES  11 C  209  THR ILE PRO ASP VAL HIS GLY GLY SER LEU GLN ASN ALA          
SEQRES  12 C  209  VAL ARG VAL TRP SER ASN ILE PRO ALA ILE ARG SER ARG          
SEQRES  13 C  209  HIS TRP ALA LEU VAL SER GLU GLU GLU LEU SER LEU LEU          
SEQRES  14 C  209  ALA GLN ASN LYS GLN SER SER LYS LEU ALA ALA LYS TRP          
SEQRES  15 C  209  PRO THR LYS LEU VAL LYS ASN CYS PHE LEU PRO LEU ARG          
SEQRES  16 C  209  GLU TYR PHE LYS TYR PHE SER THR GLU LEU THR SER SER          
SEQRES  17 C  209  LEU                                                          
SEQRES   1 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 E   10   DA  DG  DA  DG  DC  DG  DC  DA  DT  DG                      
SEQRES   1 F   11   DC  DA  DT  DG   Z  DG  DC  DT  DC  DT  DC                  
SEQRES   1 G   10   DA  DG  DA  DG  DC  DG  DC  DA  DT  DG                      
SEQRES   1 H   11   DC  DA  DT  DG   Z  DG  DC  DT  DC  DT  DC                  
HET      Z  F 427      18                                                       
HET      Z  H 427      18                                                       
HET    SAH  A1001      26                                                       
HET    SAH  D1001      26                                                       
HETNAM       Z 1-(2-DEOXY-5-O-PHOSPHONO-BETA-D-ERYTHRO-                         
HETNAM   2   Z  PENTOFURANOSYL)PYRIMIDIN-2(1H)-ONE                              
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
HETSYN       Z 2'-DEOXYZEBULARINE-5'-MONOPHOSPHATE                              
FORMUL   6    Z    2(C9 H13 N2 O7 P)                                            
FORMUL   9  SAH    2(C14 H20 N6 O5 S)                                           
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  TRP A  698  1                                   8    
HELIX    5 AA5 ARG A  729  ARG A  742  1                                  14    
HELIX    6 AA6 GLY A  762  LEU A  773  1                                  12    
HELIX    7 AA7 LYS A  783  VAL A  785  5                                   3    
HELIX    8 AA8 GLU A  814  LEU A  819  1                                   6    
HELIX    9 AA9 ARG A  836  ILE A  840  5                                   5    
HELIX   10 AB1 TRP A  860  GLY A  869  1                                  10    
HELIX   11 AB2 SER A  881  ARG A  891  1                                  11    
HELIX   12 AB3 SER A  894  ALA A  903  1                                  10    
HELIX   13 AB4 PRO A  904  TYR A  908  5                                   5    
HELIX   14 AB5 ILE B  199  LEU B  206  1                                   8    
HELIX   15 AB6 VAL B  228  GLU B  234  1                                   7    
HELIX   16 AB7 PRO B  255  ARG B  271  1                                  17    
HELIX   17 AB8 ASN B  291  LEU B  302  1                                  12    
HELIX   18 AB9 LYS B  362  LEU B  369  1                                   8    
HELIX   19 AC1 PRO B  370  TYR B  374  5                                   5    
HELIX   20 AC2 PRO C  183  ARG C  187  5                                   5    
HELIX   21 AC3 ILE C  199  GLY C  207  1                                   9    
HELIX   22 AC4 VAL C  228  GLU C  234  1                                   7    
HELIX   23 AC5 PRO C  255  ARG C  271  1                                  17    
HELIX   24 AC6 ASN C  291  GLU C  303  1                                  13    
HELIX   25 AC7 VAL C  364  LEU C  369  1                                   6    
HELIX   26 AC8 PRO C  370  TYR C  374  5                                   5    
HELIX   27 AC9 ALA D  644  LEU D  653  1                                  10    
HELIX   28 AD1 CYS D  666  HIS D  677  1                                  12    
HELIX   29 AD2 ASP D  686  VAL D  690  5                                   5    
HELIX   30 AD3 THR D  691  TRP D  698  1                                   8    
HELIX   31 AD4 ARG D  729  ARG D  742  1                                  14    
HELIX   32 AD5 GLY D  762  LEU D  773  1                                  12    
HELIX   33 AD6 LYS D  783  VAL D  785  5                                   3    
HELIX   34 AD7 GLU D  814  LEU D  819  1                                   6    
HELIX   35 AD8 ARG D  836  ILE D  840  5                                   5    
HELIX   36 AD9 TRP D  860  GLY D  869  1                                  10    
HELIX   37 AE1 SER D  881  ARG D  891  1                                  11    
HELIX   38 AE2 SER D  894  ALA D  903  1                                  10    
HELIX   39 AE3 PRO D  904  TYR D  908  5                                   5    
SHEET    1 AA1 7 ILE A 681  VAL A 684  0                                        
SHEET    2 AA1 7 VAL A 657  SER A 663  1  N  TYR A 660   O  MET A 682           
SHEET    3 AA1 7 ILE A 634  LEU A 639  1  N  SER A 638   O  ILE A 661           
SHEET    4 AA1 7 LEU A 703  GLY A 706  1  O  LEU A 703   N  LEU A 637           
SHEET    5 AA1 7 PHE A 752  VAL A 758  1  O  LEU A 754   N  VAL A 704           
SHEET    6 AA1 7 ALA A 791  GLY A 796 -1  O  TRP A 795   N  PHE A 755           
SHEET    7 AA1 7 VAL A 778  ASP A 781 -1  N  ILE A 780   O  ARG A 792           
SHEET    1 AA2 3 ILE A 824  ALA A 825  0                                        
SHEET    2 AA2 3 VAL A 850  MET A 852 -1  O  PHE A 851   N  ILE A 824           
SHEET    3 AA2 3 LYS A 855  ASP A 857 -1  O  ASP A 857   N  VAL A 850           
SHEET    1 AA3 6 LEU B 218  VAL B 221  0                                        
SHEET    2 AA3 6 VAL B 192  LEU B 195  1  N  SER B 194   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  MET B 283   N  VAL B 241           
SHEET    5 AA3 6 VAL B 321  SER B 325 -1  O  ARG B 322   N  ASP B 286           
SHEET    6 AA3 6 VAL B 307  ILE B 309 -1  N  ILE B 309   O  VAL B 321           
SHEET    1 AA4 6 LYS C 219  VAL C 221  0                                        
SHEET    2 AA4 6 VAL C 192  LEU C 195  1  N  SER C 194   O  VAL C 221           
SHEET    3 AA4 6 LEU C 240  ALA C 244  1  O  TYR C 242   N  LEU C 193           
SHEET    4 AA4 6 PHE C 281  ASP C 286  1  O  MET C 283   N  VAL C 241           
SHEET    5 AA4 6 ARG C 322  SER C 325 -1  O  TRP C 324   N  PHE C 284           
SHEET    6 AA4 6 VAL C 307  THR C 308 -1  N  VAL C 307   O  VAL C 323           
SHEET    1 AA5 7 ILE D 681  VAL D 684  0                                        
SHEET    2 AA5 7 VAL D 657  SER D 663  1  N  ALA D 662   O  MET D 682           
SHEET    3 AA5 7 ILE D 634  LEU D 639  1  N  SER D 638   O  ILE D 661           
SHEET    4 AA5 7 LEU D 703  GLY D 706  1  O  LEU D 703   N  LEU D 637           
SHEET    5 AA5 7 PHE D 752  VAL D 758  1  O  GLU D 756   N  GLY D 706           
SHEET    6 AA5 7 ALA D 791  GLY D 796 -1  O  TRP D 795   N  PHE D 755           
SHEET    7 AA5 7 VAL D 778  ASP D 781 -1  N  ILE D 780   O  ARG D 792           
SHEET    1 AA6 3 ILE D 824  ALA D 825  0                                        
SHEET    2 AA6 3 VAL D 850  PHE D 851 -1  O  PHE D 851   N  ILE D 824           
SHEET    3 AA6 3 GLU D 856  ASP D 857 -1  O  ASP D 857   N  VAL D 850           
LINK         SG  CYS A 710                 C6    Z F 427     1555   1555  1.84  
LINK         SG  CYS D 710                 C6    Z H 427     1555   1555  1.86  
LINK         O3'  DG F 426                 P     Z F 427     1555   1555  1.60  
LINK         O3'   Z F 427                 P    DG F 428     1555   1555  1.61  
LINK         O3'  DG H 426                 P     Z H 427     1555   1555  1.60  
LINK         O3'   Z H 427                 P    DG H 428     1555   1555  1.61  
CISPEP   1 GLU D  745    GLY D  746          0        -1.47                     
SITE     1 AC1 16 PHE A 640  ASP A 641  GLY A 642  ILE A 643                    
SITE     2 AC1 16 THR A 645  SER A 663  GLU A 664  CYS A 666                    
SITE     3 AC1 16 ASP A 686  VAL A 687  GLY A 707  PRO A 709                    
SITE     4 AC1 16 LEU A 730  ARG A 891  SER A 892  TRP A 893                    
SITE     1 AC2 13 PHE D 640  ASP D 641  GLY D 642  THR D 645                    
SITE     2 AC2 13 GLU D 664  CYS D 666  ASP D 686  VAL D 687                    
SITE     3 AC2 13 GLY D 707  LEU D 730  ARG D 891  SER D 892                    
SITE     4 AC2 13 TRP D 893                                                     
SITE     1 AC3 18 SER A 708  CYS A 710  SER A 714  ILE A 715                    
SITE     2 AC3 18 VAL A 716  GLU A 756  VAL A 758  ARG A 790                    
SITE     3 AC3 18 ARG A 792  ARG A 831  THR A 832  THR A 834                    
SITE     4 AC3 18 GLY A 890   DG E 408   DC E 409   DA E 410                    
SITE     5 AC3 18  DT F 425   DG F 428                                          
SITE     1 AC4 19 SER A 708  CYS A 710  ASN A 711  SER A 714                    
SITE     2 AC4 19 VAL A 716  ASN A 717  PRO A 718  GLU A 756                    
SITE     3 AC4 19 VAL A 758  ARG A 790  ARG A 792  THR A 834                    
SITE     4 AC4 19 THR A 835  ARG A 836  GLY A 890   DG E 406                    
SITE     5 AC4 19  DC E 407   DG F 426   DC F 429                               
SITE     1 AC5 17 SER D 708  CYS D 710  SER D 714  ILE D 715                    
SITE     2 AC5 17 VAL D 716  GLU D 756  VAL D 758  ARG D 790                    
SITE     3 AC5 17 ARG D 792  ARG D 831  THR D 832  GLY D 890                    
SITE     4 AC5 17 SER D 892   DG G 408   DC G 409   DT H 425                    
SITE     5 AC5 17  DG H 428                                                     
SITE     1 AC6 20 SER D 708  CYS D 710  ASN D 711  SER D 714                    
SITE     2 AC6 20 VAL D 716  ASN D 717  PRO D 718  GLU D 756                    
SITE     3 AC6 20 VAL D 758  ARG D 790  ARG D 792  THR D 834                    
SITE     4 AC6 20 THR D 835  ARG D 836  GLY D 890  SER D 892                    
SITE     5 AC6 20  DG G 406   DC G 407   DG H 426   DC H 429                    
CRYST1  176.611   49.559  162.259  90.00  90.00  90.00 P 21 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.005662  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.020178  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006163        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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