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Database: PDB
Entry: 4ER5
LinkDB: 4ER5
Original site: 4ER5 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       19-APR-12   4ER5              
TITLE     CRYSTAL STRUCTURE OF HUMAN DOT1L IN COMPLEX WITH 2 MOLECULES OF       
TITLE    2 EPZ004777                                                            
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: PLASMMID;                             
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,A.FEDERATION,   
AUTHOR   2 J.MARINEAU,J.QI,M.VEDADI,J.E.BRADNER,M.SCHAPIRA,C.H.ARROWSMITH,      
AUTHOR   3 A.M.EDWARDS,C.BOUNTRA,P.J.BROWN,STRUCTURAL GENOMICS CONSORTIUM (SGC) 
REVDAT   1   16-MAY-12 4ER5    0                                                
JRNL        AUTH   A.K.WERNIMONT,W.TEMPEL,W.YU,A.SCOPTON,Y.LI,K.T.NGUYEN,       
JRNL        AUTH 2 A.FEDERATION,J.MARINEAU,J.QI,M.VEDADI,J.E.BRADNER,           
JRNL        AUTH 3 M.SCHAPIRA,C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,P.J.BROWN    
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN DOT1L IN COMPLEX WITH 2 MOLECULES 
JRNL        TITL 2 OF EPZ004777                                                 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.57 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 2.57                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.24                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 22247                          
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) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1100                            
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) : 2.57                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.64                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1564                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2800                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 79                           
REMARK   3   BIN FREE R VALUE                    : 0.2820                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2535                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 83                                      
REMARK   3   SOLVENT ATOMS            : 20                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.73                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.52000                                             
REMARK   3    B22 (A**2) : -0.52000                                             
REMARK   3    B33 (A**2) : 0.78000                                              
REMARK   3    B12 (A**2) : -0.26000                                             
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): 0.256         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.201         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.140         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.508        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.943                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2702 ; 0.011 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  1772 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3692 ; 1.307 ; 1.930       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4314 ; 0.871 ; 2.988       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   332 ; 5.683 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   113 ;33.011 ;23.540       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   406 ;13.989 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;15.913 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   408 ; 0.074 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2987 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   558 ; 0.001 ; 0.020       
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):  1654 ; 0.659 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   657 ; 0.092 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2662 ; 1.253 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1048 ; 1.624 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1027 ; 2.757 ; 4.500       
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):  26.6645  57.9165   2.9241              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0257 T22:   0.0980                                     
REMARK   3      T33:   0.0321 T12:   0.0069                                     
REMARK   3      T13:  -0.0094 T23:  -0.0123                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5240 L22:   2.3269                                     
REMARK   3      L33:   0.5068 L12:  -2.9837                                     
REMARK   3      L13:  -0.2355 L23:  -0.0850                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0803 S12:   0.3092 S13:   0.1284                       
REMARK   3      S21:  -0.0418 S22:  -0.0308 S23:  -0.0793                       
REMARK   3      S31:   0.0043 S32:  -0.0525 S33:   0.1111                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4ER5 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 RCSB071966.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-OCT-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 : XSCALE                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22277                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.570                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.243                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 11.000                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.57                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.71                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.30                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.93900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.93900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.700                              
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   (%): 66.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.70                     
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       35.45267            
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       17.72633            
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       26.58950            
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        8.86317            
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       44.31583            
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    57                                                      
REMARK 465     TYR A    58                                                      
REMARK 465     VAL A    59                                                      
REMARK 465     LEU A    60                                                      
REMARK 465     ILE A    61                                                      
REMARK 465     ASP A    62                                                      
REMARK 465     TRP A   305                                                      
REMARK 465     THR A   306                                                      
REMARK 465     GLY A   307                                                      
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    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  29    CG   CD   CE   NZ                                   
REMARK 470     ARG A  42    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A  52    CE   NZ                                             
REMARK 470     GLU A  56    CG   CD   OE1  OE2                                  
REMARK 470     TYR A  63    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A  69    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  73    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLN A  94    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  97    CG   CD   CE   NZ                                   
REMARK 470     ASN A  99    CG   OD1  ND2                                       
REMARK 470     GLU A 123    CD   OE1  OE2                                       
REMARK 470     LYS A 124    CE   NZ                                             
REMARK 470     GLU A 129    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 134    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 152    CG   CD   CE   NZ                                   
REMARK 470     ASP A 156    CG   OD1  OD2                                       
REMARK 470     LYS A 180    CD   CE   NZ                                        
REMARK 470     LYS A 193    CG   CD   CE   NZ                                   
REMARK 470     GLU A 196    CD   OE1  OE2                                       
REMARK 470     LYS A 207    CD   CE   NZ                                        
REMARK 470     LYS A 212    CD   CE   NZ                                        
REMARK 470     GLU A 215    CD   OE1  OE2                                       
REMARK 470     GLU A 227    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 230    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 248    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 255    CD   OE1  OE2                                       
REMARK 470     LYS A 261    CD   CE   NZ                                        
REMARK 470     ARG A 278    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 282    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 300    CG   CD   CE   NZ                                   
REMARK 470     VAL A 303    CG1  CG2                                            
REMARK 470     SER A 304    OG                                                  
REMARK 470     LYS A 308    CG   CD   CE   NZ                                   
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    CD   OE1  OE2                                       
REMARK 470     GLN A 338    CG   CD   OE1  NE2                                  
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  28     -159.44   -163.58                                   
REMARK 500    GLU A 138        0.60    -59.34                                   
REMARK 500    THR A 139      -34.63   -134.55                                   
REMARK 500    SER A 302       90.12   -161.94                                   
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 0QK A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0QK A 502                 
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: 4ER6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ER7   RELATED DB: PDB                                   
DBREF  4ER5 A    1   412  UNP    Q8TEK3   DOT1L_HUMAN      1    412             
SEQADV 4ER5 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    0QK  A 501      39                                                       
HET    0QK  A 502      39                                                       
HET    UNX  A 503       1                                                       
HET    UNX  A 504       1                                                       
HET    UNX  A 505       1                                                       
HET    UNX  A 506       1                                                       
HET    UNX  A 507       1                                                       
HETNAM     0QK 7-{5-[(3-{[(4-TERT-BUTYLPHENYL)CARBAMOYL]AMINO}PROPYL)           
HETNAM   2 0QK  (PROPAN-2-YL)AMINO]-5-DEOXY-BETA-D-RIBOFURANOSYL}-7H-           
HETNAM   3 0QK  PYRROLO[2,3-D]PYRIMIDIN-4-AMINE                                 
HETNAM     UNX UNKNOWN ATOM OR ION                                              
FORMUL   2  0QK    2(C28 H41 N7 O4)                                             
FORMUL   4  UNX    5(X)                                                         
FORMUL   9  HOH   *20(H2 O)                                                     
HELIX    1   1 ASP A   32  ILE A   48  1                                  17    
HELIX    2   2 ILE A   48  MET A   55  1                                   8    
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  LEU A  125  5                                   5    
HELIX    6   6 THR A  139  ILE A  151  1                                  13    
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  ASN A  234  1                                  10    
HELIX   10  10 GLY A  246  ALA A  258  1                                  13    
HELIX   11  11 ASN A  280  LEU A  284  5                                   5    
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 LEU A   5  LEU A   9  0                                        
SHEET    2   A 2 ALA A  18  TRP A  22 -1  O  TYR A  20   N  LEU A   7           
SHEET    1   B 7 TYR A 216  ARG A 220  0                                        
SHEET    2   B 7 HIS A 181  GLU A 186  1  N  GLY A 184   O  GLU A 219           
SHEET    3   B 7 LEU A 158  LEU A 162  1  N  PHE A 159   O  TYR A 183           
SHEET    4   B 7 VAL A 237  VAL A 240  1  O  PHE A 239   N  VAL A 160           
SHEET    5   B 7 ARG A 265  SER A 268  1  O  VAL A 267   N  ILE A 238           
SHEET    6   B 7 TYR A 313  ILE A 317 -1  O  TYR A 313   N  SER A 268           
SHEET    7   B 7 MET A 291  GLU A 295 -1  N  VAL A 294   O  LEU A 314           
CISPEP   1 TRP A   22    PRO A   23          0        -1.88                     
CISPEP   2 GLU A  129    PRO A  130          0         7.21                     
SITE     1 AC1 16 TYR A 128  LEU A 143  ASP A 161  GLY A 163                    
SITE     2 AC1 16 SER A 164  GLY A 165  VAL A 169  GLU A 186                    
SITE     3 AC1 16 LYS A 187  GLY A 221  ASP A 222  PHE A 223                    
SITE     4 AC1 16 ASN A 241  PHE A 245  SER A 268  SER A 269                    
SITE     1 AC2 13 GLU A  46  LEU A 111  TYR A 115  PRO A 122                    
SITE     2 AC2 13 GLU A 123  LEU A 125  ASN A 126  ASN A 127                    
SITE     3 AC2 13 TYR A 128  PRO A 133  TYR A 136  GLY A 137                    
SITE     4 AC2 13 GLN A 168                                                     
CRYST1  150.605  150.605   53.179  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      0.006640  0.003834  0.000000        0.00000                         
SCALE2      0.000000  0.007667  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018804        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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