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Database: PDB
Entry: 1NW3
LinkDB: 1NW3
Original site: 1NW3 
HEADER    TRANSFERASE                             05-FEB-03   1NW3              
TITLE     STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN DOT1L, A NON-SET DOMAIN    
TITLE    2 NUCLEOSOMAL HISTONE METHYLTRANSFERASE                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE METHYLTRANSFERASE DOT1L;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 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: DOT1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX-KG                                   
KEYWDS    HDOT1, HISTONE LYSINE METHYLTRANSFERASE, TRANSFERASE                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.R.MIN,Q.FENG,Z.H.LI,Y.ZHANG,R.M.XU                                  
REVDAT   3   16-APR-14 1NW3    1       REMARK VERSN                             
REVDAT   2   24-FEB-09 1NW3    1       VERSN                                    
REVDAT   1   25-MAR-03 1NW3    0                                                
JRNL        AUTH   J.MIN,Q.FENG,Z.LI,Y.ZHANG,R.M.XU                             
JRNL        TITL   STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN DOT1L, A NON-SET  
JRNL        TITL 2 DOMAIN NUCLEOSOMAL HISTONE METHYLTRANSFERASE                 
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 112   711 2003              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   12628190                                                     
JRNL        DOI    10.1016/S0092-8674(03)00114-4                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 22926                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1810                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2671                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 41                                      
REMARK   3   SOLVENT ATOMS            : 68                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 50.00                          
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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.384                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1NW3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-FEB-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB018270.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-JUL-02; NULL                    
REMARK 200  TEMPERATURE           (KELVIN) : 100; NULL                          
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; NULL                            
REMARK 200  RADIATION SOURCE               : NSLS; NULL                         
REMARK 200  BEAMLINE                       : X26C; NULL                         
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1; NULL                          
REMARK 200  MONOCHROMATOR                  : GRAPHITE; GRAPHITE                 
REMARK 200  OPTICS                         : SI MONOCHROMATOR; NULL             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; NULL                          
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4; NULL               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22926                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.05900                            
REMARK 200  R SYM                      (I) : 0.05900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
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; MAD                         
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.82                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PH 4.6, VAPOR          
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 290K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
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       33.87333            
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       16.93667            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       25.40500            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        8.46833            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       42.34167            
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     LYS A   333                                                      
REMARK 465     LEU A   334                                                      
REMARK 465     ARG A   335                                                      
REMARK 465     GLU A   336                                                      
REMARK 465     GLU A   337                                                      
REMARK 465     GLN A   338                                                      
REMARK 465     GLU A   339                                                      
REMARK 465     ALA A   340                                                      
REMARK 465     ALA A   341                                                      
REMARK 465     ARG A   342                                                      
REMARK 465     ARG A   343                                                      
REMARK 465     ARG A   344                                                      
REMARK 465     GLN A   345                                                      
REMARK 465     GLN A   346                                                      
REMARK 465     ARG A   347                                                      
REMARK 465     GLU A   348                                                      
REMARK 465     SER A   349                                                      
REMARK 465     LYS A   350                                                      
REMARK 465     SER A   351                                                      
REMARK 465     ASN A   352                                                      
REMARK 465     ALA A   353                                                      
REMARK 465     ALA A   354                                                      
REMARK 465     THR A   355                                                      
REMARK 465     PRO A   356                                                      
REMARK 465     THR A   357                                                      
REMARK 465     LYS A   358                                                      
REMARK 465     GLY A   359                                                      
REMARK 465     PRO A   360                                                      
REMARK 465     GLU A   361                                                      
REMARK 465     GLY A   362                                                      
REMARK 465     LYS A   363                                                      
REMARK 465     VAL A   364                                                      
REMARK 465     ALA A   365                                                      
REMARK 465     GLY A   366                                                      
REMARK 465     PRO A   367                                                      
REMARK 465     ALA A   368                                                      
REMARK 465     ASP A   369                                                      
REMARK 465     ALA A   370                                                      
REMARK 465     PRO A   371                                                      
REMARK 465     MET A   372                                                      
REMARK 465     ASP A   373                                                      
REMARK 465     SER A   374                                                      
REMARK 465     GLY A   375                                                      
REMARK 465     ALA A   376                                                      
REMARK 465     GLU A   377                                                      
REMARK 465     GLU A   378                                                      
REMARK 465     GLU A   379                                                      
REMARK 465     LYS A   380                                                      
REMARK 465     ALA A   381                                                      
REMARK 465     GLY A   382                                                      
REMARK 465     ALA A   383                                                      
REMARK 465     ALA A   384                                                      
REMARK 465     THR A   385                                                      
REMARK 465     VAL A   386                                                      
REMARK 465     LYS A   387                                                      
REMARK 465     LYS A   388                                                      
REMARK 465     PRO A   389                                                      
REMARK 465     SER A   390                                                      
REMARK 465     PRO A   391                                                      
REMARK 465     SER A   392                                                      
REMARK 465     LYS A   393                                                      
REMARK 465     ALA A   394                                                      
REMARK 465     ARG A   395                                                      
REMARK 465     LYS A   396                                                      
REMARK 465     LYS A   397                                                      
REMARK 465     LYS A   398                                                      
REMARK 465     LEU A   399                                                      
REMARK 465     ASN A   400                                                      
REMARK 465     LYS A   401                                                      
REMARK 465     LYS A   402                                                      
REMARK 465     GLY A   403                                                      
REMARK 465     ARG A   404                                                      
REMARK 465     LYS A   405                                                      
REMARK 465     MET A   406                                                      
REMARK 465     ALA A   407                                                      
REMARK 465     GLY A   408                                                      
REMARK 465     ARG A   409                                                      
REMARK 465     LYS A   410                                                      
REMARK 465     ARG A   411                                                      
REMARK 465     GLY A   412                                                      
REMARK 465     ARG A   413                                                      
REMARK 465     PRO A   414                                                      
REMARK 465     LYS A   415                                                      
REMARK 465     LYS A   416                                                      
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    HOH A  1046     O    HOH A  1067              0.00            
REMARK 500   O    HOH A  1016     O    HOH A  1048              2.18            
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    ASN A  57       96.74    -54.41                                   
REMARK 500    TYR A  58      -24.87     80.54                                   
REMARK 500    VAL A  59       76.70    -65.23                                   
REMARK 500    LEU A  60       51.12    -90.49                                   
REMARK 500    ILE A  61        2.64     59.29                                   
REMARK 500    ASP A  62       41.36    -61.49                                   
REMARK 500    THR A  65      -11.45    -48.68                                   
REMARK 500    ASN A 178       50.43   -115.41                                   
REMARK 500    SER A 302       89.73   -167.80                                   
REMARK 500    ASN A 331     -159.56   -111.83                                   
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 ACT A 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM A 500                 
DBREF  1NW3 A    1   416  UNP    Q8TEK3   DOT1L_HUMAN      1    416             
SEQRES   1 A  416  MET GLY GLU LYS LEU GLU LEU ARG LEU LYS SER PRO VAL          
SEQRES   2 A  416  GLY ALA GLU PRO ALA VAL TYR PRO TRP PRO LEU PRO VAL          
SEQRES   3 A  416  TYR ASP LYS HIS HIS ASP ALA ALA HIS GLU ILE ILE GLU          
SEQRES   4 A  416  THR ILE ARG TRP VAL CYS GLU GLU ILE PRO ASP LEU LYS          
SEQRES   5 A  416  LEU ALA MET GLU ASN TYR VAL LEU ILE ASP TYR ASP THR          
SEQRES   6 A  416  LYS SER PHE GLU SER MET GLN ARG LEU CYS ASP LYS TYR          
SEQRES   7 A  416  ASN ARG ALA ILE ASP SER ILE HIS GLN LEU TRP LYS GLY          
SEQRES   8 A  416  THR THR GLN PRO MET LYS LEU ASN THR ARG PRO SER THR          
SEQRES   9 A  416  GLY LEU LEU ARG HIS ILE LEU GLN GLN VAL TYR ASN HIS          
SEQRES  10 A  416  SER VAL THR ASP PRO GLU LYS LEU ASN ASN TYR GLU PRO          
SEQRES  11 A  416  PHE SER PRO GLU VAL TYR GLY GLU THR SER PHE ASP LEU          
SEQRES  12 A  416  VAL ALA GLN MET ILE ASP GLU ILE LYS MET THR ASP ASP          
SEQRES  13 A  416  ASP LEU PHE VAL ASP LEU GLY SER GLY VAL GLY GLN VAL          
SEQRES  14 A  416  VAL LEU GLN VAL ALA ALA ALA THR ASN CYS LYS HIS HIS          
SEQRES  15 A  416  TYR GLY VAL GLU LYS ALA ASP ILE PRO ALA LYS TYR ALA          
SEQRES  16 A  416  GLU THR MET ASP ARG GLU PHE ARG LYS TRP MET LYS TRP          
SEQRES  17 A  416  TYR GLY LYS LYS HIS ALA GLU TYR THR LEU GLU ARG GLY          
SEQRES  18 A  416  ASP PHE LEU SER GLU GLU TRP ARG GLU ARG ILE ALA ASN          
SEQRES  19 A  416  THR SER VAL ILE PHE VAL ASN ASN PHE ALA PHE GLY PRO          
SEQRES  20 A  416  GLU VAL ASP HIS GLN LEU LYS GLU ARG PHE ALA ASN MET          
SEQRES  21 A  416  LYS GLU GLY GLY ARG ILE VAL SER SER LYS PRO PHE ALA          
SEQRES  22 A  416  PRO LEU ASN PHE ARG ILE ASN SER ARG ASN LEU SER ASP          
SEQRES  23 A  416  ILE GLY THR ILE MET ARG VAL VAL GLU LEU SER PRO LEU          
SEQRES  24 A  416  LYS GLY SER VAL SER TRP THR GLY LYS PRO VAL SER TYR          
SEQRES  25 A  416  TYR LEU HIS THR ILE ASP ARG THR ILE LEU GLU ASN TYR          
SEQRES  26 A  416  PHE SER SER LEU LYS ASN PRO LYS LEU ARG GLU GLU GLN          
SEQRES  27 A  416  GLU ALA ALA ARG ARG ARG GLN GLN ARG GLU SER LYS SER          
SEQRES  28 A  416  ASN ALA ALA THR PRO THR LYS GLY PRO GLU GLY LYS VAL          
SEQRES  29 A  416  ALA GLY PRO ALA ASP ALA PRO MET ASP SER GLY ALA GLU          
SEQRES  30 A  416  GLU GLU LYS ALA GLY ALA ALA THR VAL LYS LYS PRO SER          
SEQRES  31 A  416  PRO SER LYS ALA ARG LYS LYS LYS LEU ASN LYS LYS GLY          
SEQRES  32 A  416  ARG LYS MET ALA GLY ARG LYS ARG GLY ARG PRO LYS LYS          
HET    ACT  A 600       4                                                       
HET    SO4  A 601       5                                                       
HET    SO4  A 602       5                                                       
HET    SAM  A 500      27                                                       
HETNAM     ACT ACETATE ION                                                      
HETNAM     SO4 SULFATE ION                                                      
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
FORMUL   2  ACT    C2 H3 O2 1-                                                  
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   5  SAM    C15 H22 N6 O5 S                                              
FORMUL   6  HOH   *68(H2 O)                                                     
HELIX    1   1 ALA A   33  ILE A   48  1                                  16    
HELIX    2   2 ILE A   48  GLU A   56  1                                   9    
HELIX    3   3 SER A   67  GLY A   91  1                                  25    
HELIX    4   4 SER A  103  VAL A  119  1                                  17    
HELIX    5   5 ASP A  121  ASN A  127  5                                   7    
HELIX    6   6 SER A  140  ILE A  151  1                                  12    
HELIX    7   7 GLY A  167  THR A  177  1                                  11    
HELIX    8   8 ALA A  188  GLY A  210  1                                  23    
HELIX    9   9 SER A  225  THR A  235  1                                  11    
HELIX   10  10 GLY A  246  ALA A  258  1                                  13    
HELIX   11  11 ASP A  286  THR A  289  5                                   4    
HELIX   12  12 ARG A  319  ASN A  331  1                                  13    
SHEET    1   A 2 GLU A   6  LEU A   9  0                                        
SHEET    2   A 2 ALA A  18  PRO A  21 -1  O  TYR A  20   N  LEU A   7           
SHEET    1   B 2 VAL A  26  ASP A  28  0                                        
SHEET    2   B 2 HIS A  31  ASP A  32 -1  O  HIS A  31   N  ASP A  28           
SHEET    1   C 7 TYR A 216  ARG A 220  0                                        
SHEET    2   C 7 HIS A 181  GLU A 186  1  N  GLY A 184   O  GLU A 219           
SHEET    3   C 7 LEU A 158  LEU A 162  1  N  PHE A 159   O  TYR A 183           
SHEET    4   C 7 VAL A 237  VAL A 240  1  O  PHE A 239   N  VAL A 160           
SHEET    5   C 7 ARG A 265  SER A 268  1  O  VAL A 267   N  ILE A 238           
SHEET    6   C 7 TYR A 313  ILE A 317 -1  O  HIS A 315   N  ILE A 266           
SHEET    7   C 7 MET A 291  GLU A 295 -1  N  ARG A 292   O  THR A 316           
CISPEP   1 TRP A   22    PRO A   23          0         0.16                     
CISPEP   2 ASN A  331    PRO A  332          0         0.21                     
SITE     1 AC1  4 TYR A 183  ARG A 231  THR A 235  HOH A1047                    
SITE     1 AC2  2 ARG A 203  HIS A 213                                          
SITE     1 AC3  4 ARG A 229  GLN A 252  GLU A 255  ARG A 256                    
SITE     1 AC4 17 PRO A 133  GLY A 137  GLU A 138  THR A 139                    
SITE     2 AC4 17 ASP A 161  GLY A 163  GLN A 168  VAL A 169                    
SITE     3 AC4 17 GLU A 186  LYS A 187  GLY A 221  ASP A 222                    
SITE     4 AC4 17 PHE A 223  PHE A 239  ASN A 241  PHE A 245                    
SITE     5 AC4 17 HOH A1032                                                     
CRYST1  152.800  152.800   50.810  90.00  90.00 120.00 P 65          6          
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      0.006545  0.003778  0.000000        0.00000                         
SCALE2      0.000000  0.007557  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019681        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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