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Database: PDB
Entry: 4ER6
LinkDB: 4ER6
Original site: 4ER6 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       19-APR-12   4ER6              
TITLE     CRYSTAL STRUCTURE OF HUMAN DOT1L IN COMPLEX WITH INHIBITOR SGC0946    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-79 SPECIFIC; 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: DOT1-LIKE PROTEIN, HISTONE H3-K79 METHYLTRANSFERASE, H3-K79-
COMPND   5 HMTASE, LYSINE N-METHYLTRANSFERASE 4;                                
COMPND   6 EC: 2.1.1.43;                                                        
COMPND   7 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: DOT1L, KIAA1814, KMT4;                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 V2R PRARE2;                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28-MHL                                 
KEYWDS    HISTONE, METHYLTRANSFERASE, EPIGENETICS, TRANSFERASE-TRANSFERASE      
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.K.WERNIMONT,W.TEMPEL,W.YU,A.SCOPTON,Y.LI,K.T.NGUYEN,M.VEDADI,       
AUTHOR   2 J.E.BRADNER,M.SCHAPIRA,C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,         
AUTHOR   3 P.J.BROWN,STRUCTURAL GENOMICS CONSORTIUM (SGC)                       
REVDAT   1   16-MAY-12 4ER6    0                                                
JRNL        AUTH   A.K.WERNIMONT,W.TEMPEL,W.YU,A.SCOPTON,Y.LI,K.T.NGUYEN,       
JRNL        AUTH 2 M.VEDADI,J.E.BRADNER,M.SCHAPIRA,C.H.ARROWSMITH,A.M.EDWARDS,  
JRNL        AUTH 3 C.BOUNTRA,P.J.BROWN                                          
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN DOT1L IN COMPLEX WITH INHIBITOR   
JRNL        TITL 2 SGC0946                                                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 30370                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : PDB ENTRY 3QOW                  
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.217                           
REMARK   3   R VALUE            (WORKING SET) : 0.216                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1479                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2021                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3060                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 85                           
REMARK   3   BIN FREE R VALUE                    : 0.3600                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2600                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 42                                      
REMARK   3   SOLVENT ATOMS            : 25                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 58.95                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.51000                                             
REMARK   3    B22 (A**2) : -0.51000                                             
REMARK   3    B33 (A**2) : 0.76000                                              
REMARK   3    B12 (A**2) : -0.25000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.195         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.164         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.138         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.417        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.935                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2736 ; 0.012 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3733 ; 1.044 ; 1.936       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   340 ; 5.080 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   116 ;32.649 ;23.621       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   424 ;14.338 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;13.223 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   411 ; 0.068 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2084 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     4        A   341                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.4566  57.9540   3.3779              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0607 T22:   0.1052                                     
REMARK   3      T33:   0.0121 T12:   0.0154                                     
REMARK   3      T13:   0.0045 T23:   0.0167                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4689 L22:   1.7620                                     
REMARK   3      L33:   0.4016 L12:  -2.4320                                     
REMARK   3      L13:  -0.0130 L23:   0.0238                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0223 S12:   0.1930 S13:   0.1269                       
REMARK   3      S21:  -0.0330 S22:  -0.0322 S23:  -0.0318                       
REMARK   3      S31:   0.0299 S32:   0.0048 S33:   0.0545                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4ER6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-APR-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB071967.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-NOV-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 31-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979310                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30402                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.148                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 11.100                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08300                            
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) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.30                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.98600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.98600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: RIGID BODY REFINEMENT                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.23                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.5 M NAFORMATE, 0.1 M NAACET, PH 4.5,   
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
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       35.22600            
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       17.61300            
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       26.41950            
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        8.80650            
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       44.03250            
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 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL MOLECULE IS UNKNOWN.       
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: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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     GLY A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     ASN A   127                                                      
REMARK 465     TYR A   128                                                      
REMARK 465     GLU A   129                                                      
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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A   4    CG   CD   CE   NZ                                   
REMARK 470     GLU A  16    CD   OE1  OE2                                       
REMARK 470     LYS A  29    CD   CE   NZ                                        
REMARK 470     GLU A  56    CD   OE1  OE2                                       
REMARK 470     LEU A  60    CD1  CD2                                            
REMARK 470     GLU A  69    CD   OE1  OE2                                       
REMARK 470     GLN A  94    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  97    CD   CE   NZ                                        
REMARK 470     ASN A  99    CG   OD1  ND2                                       
REMARK 470     VAL A 119    CG1  CG2                                            
REMARK 470     LYS A 124    CD   CE   NZ                                        
REMARK 470     LEU A 125    CG   CD1  CD2                                       
REMARK 470     GLU A 134    CD   OE1  OE2                                       
REMARK 470     GLU A 138    CD   OE1  OE2                                       
REMARK 470     LYS A 152    CG   CD   CE   NZ                                   
REMARK 470     LYS A 180    CG   CD   CE   NZ                                   
REMARK 470     LYS A 187    CE   NZ                                             
REMARK 470     LYS A 193    CD   CE   NZ                                        
REMARK 470     LYS A 207    CD   CE   NZ                                        
REMARK 470     LYS A 212    CD   CE   NZ                                        
REMARK 470     ARG A 220    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A 226    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 230    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 248    CD   OE1  OE2                                       
REMARK 470     GLU A 255    CD   OE1  OE2                                       
REMARK 470     LYS A 261    CE   NZ                                             
REMARK 470     ASN A 276    OD1  ND2                                            
REMARK 470     ARG A 278    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A 282    CD   NE   CZ   NH1  NH2                             
REMARK 470     LEU A 299    CG   CD1  CD2                                       
REMARK 470     LYS A 300    CG   CD   CE   NZ                                   
REMARK 470     SER A 302    OG                                                  
REMARK 470     LYS A 308    CD   CE   NZ                                        
REMARK 470     TYR A 312    CD1  CE1  CE2  CZ   OH                              
REMARK 470     GLU A 323    CD   OE1  OE2                                       
REMARK 470     LYS A 333    NZ                                                  
REMARK 470     GLU A 336    CD   OE1  OE2                                       
REMARK 470     GLU A 337    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 339    CG   CD   OE1  OE2                                  
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    ASP A  62       44.11    -93.49                                   
REMARK 500    THR A 139      -87.29   -131.90                                   
REMARK 500    GLU A 339       41.41    -74.41                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 503  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 625   O                                                      
REMARK 620 2 HOH A 624   O    99.0                                              
REMARK 620 3 MET A  55   O   175.8  81.8                                        
REMARK 620 4 ASN A  57   OD1 100.1  83.3  75.9                                  
REMARK 620 5 LYS A  52   O    93.0 162.4  85.3  81.9                            
REMARK 620 6 LEU A  53   O    95.0 116.4  88.3 153.0  75.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AW2 A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 503                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4EQZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ER0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ER3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ER5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ER7   RELATED DB: PDB                                   
DBREF  4ER6 A    1   412  UNP    Q8TEK3   DOT1L_HUMAN      1    412             
SEQADV 4ER6 GLY A    0  UNP  Q8TEK3              EXPRESSION TAG                 
SEQRES   1 A  413  GLY MET GLY GLU LYS LEU GLU LEU ARG LEU LYS SER PRO          
SEQRES   2 A  413  VAL GLY ALA GLU PRO ALA VAL TYR PRO TRP PRO LEU PRO          
SEQRES   3 A  413  VAL TYR ASP LYS HIS HIS ASP ALA ALA HIS GLU ILE ILE          
SEQRES   4 A  413  GLU THR ILE ARG TRP VAL CYS GLU GLU ILE PRO ASP LEU          
SEQRES   5 A  413  LYS LEU ALA MET GLU ASN TYR VAL LEU ILE ASP TYR ASP          
SEQRES   6 A  413  THR LYS SER PHE GLU SER MET GLN ARG LEU CYS ASP LYS          
SEQRES   7 A  413  TYR ASN ARG ALA ILE ASP SER ILE HIS GLN LEU TRP LYS          
SEQRES   8 A  413  GLY THR THR GLN PRO MET LYS LEU ASN THR ARG PRO SER          
SEQRES   9 A  413  THR GLY LEU LEU ARG HIS ILE LEU GLN GLN VAL TYR ASN          
SEQRES  10 A  413  HIS SER VAL THR ASP PRO GLU LYS LEU ASN ASN TYR GLU          
SEQRES  11 A  413  PRO PHE SER PRO GLU VAL TYR GLY GLU THR SER PHE ASP          
SEQRES  12 A  413  LEU VAL ALA GLN MET ILE ASP GLU ILE LYS MET THR ASP          
SEQRES  13 A  413  ASP ASP LEU PHE VAL ASP LEU GLY SER GLY VAL GLY GLN          
SEQRES  14 A  413  VAL VAL LEU GLN VAL ALA ALA ALA THR ASN CYS LYS HIS          
SEQRES  15 A  413  HIS TYR GLY VAL GLU LYS ALA ASP ILE PRO ALA LYS TYR          
SEQRES  16 A  413  ALA GLU THR MET ASP ARG GLU PHE ARG LYS TRP MET LYS          
SEQRES  17 A  413  TRP TYR GLY LYS LYS HIS ALA GLU TYR THR LEU GLU ARG          
SEQRES  18 A  413  GLY ASP PHE LEU SER GLU GLU TRP ARG GLU ARG ILE ALA          
SEQRES  19 A  413  ASN THR SER VAL ILE PHE VAL ASN ASN PHE ALA PHE GLY          
SEQRES  20 A  413  PRO GLU VAL ASP HIS GLN LEU LYS GLU ARG PHE ALA ASN          
SEQRES  21 A  413  MET LYS GLU GLY GLY ARG ILE VAL SER SER LYS PRO PHE          
SEQRES  22 A  413  ALA PRO LEU ASN PHE ARG ILE ASN SER ARG ASN LEU SER          
SEQRES  23 A  413  ASP ILE GLY THR ILE MET ARG VAL VAL GLU LEU SER PRO          
SEQRES  24 A  413  LEU LYS GLY SER VAL SER TRP THR GLY LYS PRO VAL SER          
SEQRES  25 A  413  TYR TYR LEU HIS THR ILE ASP ARG THR ILE LEU GLU ASN          
SEQRES  26 A  413  TYR PHE SER SER LEU LYS ASN PRO LYS LEU ARG GLU GLU          
SEQRES  27 A  413  GLN GLU ALA ALA ARG ARG ARG GLN GLN ARG GLU SER LYS          
SEQRES  28 A  413  SER ASN ALA ALA THR PRO THR LYS GLY PRO GLU GLY LYS          
SEQRES  29 A  413  VAL ALA GLY PRO ALA ASP ALA PRO MET ASP SER GLY ALA          
SEQRES  30 A  413  GLU GLU GLU LYS ALA GLY ALA ALA THR VAL LYS LYS PRO          
SEQRES  31 A  413  SER PRO SER LYS ALA ARG LYS LYS LYS LEU ASN LYS LYS          
SEQRES  32 A  413  GLY ARG LYS MET ALA GLY ARG LYS ARG GLY                      
HET     BR  A 501       1                                                       
HET    AW2  A 502      40                                                       
HET     NA  A 503       1                                                       
HETNAM      BR BROMIDE ION                                                      
HETNAM     AW2 5-BROMO-7-{5-[(3-{[(4-TERT-BUTYLPHENYL)                          
HETNAM   2 AW2  CARBAMOYL]AMINO}PROPYL)(PROPAN-2-YL)AMINO]-5-DEOXY-             
HETNAM   3 AW2  BETA-D-RIBOFURANOSYL}-7H-PYRROLO[2,3-D]PYRIMIDIN-4-             
HETNAM   4 AW2  AMINE                                                           
HETNAM      NA SODIUM ION                                                       
FORMUL   2   BR    BR 1-                                                        
FORMUL   3  AW2    C28 H40 BR N7 O4                                             
FORMUL   4   NA    NA 1+                                                        
FORMUL   5  HOH   *25(H2 O)                                                     
HELIX    1   1 ALA A   33  ILE A   48  1                                  16    
HELIX    2   2 ILE A   48  MET A   55  1                                   8    
HELIX    3   3 TYR A   58  ASP A   62  5                                   5    
HELIX    4   4 SER A   67  GLY A   91  1                                  25    
HELIX    5   5 SER A  103  VAL A  119  1                                  17    
HELIX    6   6 SER A  132  GLU A  138  5                                   7    
HELIX    7   7 THR A  139  ILE A  151  1                                  13    
HELIX    8   8 GLY A  167  THR A  177  1                                  11    
HELIX    9   9 ALA A  188  GLY A  210  1                                  23    
HELIX   10  10 SER A  225  ASN A  234  1                                  10    
HELIX   11  11 GLY A  246  ALA A  258  1                                  13    
HELIX   12  12 ASP A  286  THR A  289  5                                   4    
HELIX   13  13 ARG A  319  ASN A  331  1                                  13    
HELIX   14  14 ASN A  331  GLU A  339  1                                   9    
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  TYR A  27           
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  ASP A 161   O  TYR A 183           
SHEET    4   C 7 VAL A 237  VAL A 240  1  O  PHE A 239   N  LEU A 162           
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 312  ILE A 317 -1  O  HIS A 315   N  ILE A 266           
SHEET    7   C 7 MET A 291  LEU A 296 -1  N  LEU A 296   O  TYR A 312           
LINK        NA    NA A 503                 O   HOH A 625     1555   1555  2.21  
LINK        NA    NA A 503                 O   HOH A 624     1555   1555  2.28  
LINK         O   MET A  55                NA    NA A 503     1555   1555  2.47  
LINK         OD1 ASN A  57                NA    NA A 503     1555   1555  2.53  
LINK         O   LYS A  52                NA    NA A 503     1555   1555  2.81  
LINK         O   LEU A  53                NA    NA A 503     1555   1555  2.98  
CISPEP   1 TRP A   22    PRO A   23          0        -4.46                     
SITE     1 AC1  1 AW2 A 502                                                     
SITE     1 AC2 19 TYR A  58  ASP A 161  GLY A 163  SER A 164                    
SITE     2 AC2 19 GLY A 165  VAL A 169  GLU A 186  LYS A 187                    
SITE     3 AC2 19 ALA A 188  GLY A 221  ASP A 222  PHE A 223                    
SITE     4 AC2 19 PHE A 239  ASN A 241  PHE A 245  VAL A 267                    
SITE     5 AC2 19 SER A 268  TYR A 312   BR A 501                               
SITE     1 AC3  7 LYS A  52  LEU A  53  MET A  55  ASN A  57                    
SITE     2 AC3  7 ARG A 335  HOH A 624  HOH A 625                               
CRYST1  149.907  149.907   52.839  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      0.006671  0.003851  0.000000        0.00000                         
SCALE2      0.000000  0.007703  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018925        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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