GenomeNet

Database: PDB
Entry: 4ER3
LinkDB: 4ER3
Original site: 4ER3 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       19-APR-12   4ER3              
TITLE     CRYSTAL STRUCTURE OF HUMAN DOT1L IN COMPLEX WITH INHIBITOR 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: 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,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 4ER3    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 INHIBITOR   
JRNL        TITL 2 EPZ004777                                                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 26518                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.252                           
REMARK   3   R VALUE            (WORKING SET) : 0.250                           
REMARK   3   FREE R VALUE                     : 0.282                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1310                            
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) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1825                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.90                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3760                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 101                          
REMARK   3   BIN FREE R VALUE                    : 0.4160                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2424                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 78                                      
REMARK   3   SOLVENT ATOMS            : 18                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 54.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.59000                                             
REMARK   3    B22 (A**2) : -1.59000                                             
REMARK   3    B33 (A**2) : 2.38000                                              
REMARK   3    B12 (A**2) : -0.79000                                             
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): 0.253         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.220         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.181         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.761         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.925                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.900                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2598 ; 0.010 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  1690 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3543 ; 1.154 ; 1.945       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4123 ; 0.882 ; 2.994       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   318 ; 6.083 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   115 ;31.913 ;24.174       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   406 ;14.121 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;10.490 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   388 ; 0.070 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2880 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   525 ; 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):  1582 ; 0.686 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   631 ; 0.093 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2551 ; 1.281 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1016 ; 1.448 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   992 ; 2.468 ; 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  : NULL                                       
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 4ER3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-APR-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB071965.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-NOV-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
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   : 26567                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.859                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 11.000                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.60                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.71500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.71500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
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   (%): 70.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M (NH4)2SO4, 0.01M MGCL2, 0.1M        
REMARK 280  NACACO, PH 5.5, 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       32.32400            
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       16.16200            
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       24.24300            
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        8.08100            
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       40.40500            
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     TYR A   128                                                      
REMARK 465     GLU A   129                                                      
REMARK 465     PRO A   130                                                      
REMARK 465     PHE A   131                                                      
REMARK 465     SER A   132                                                      
REMARK 465     PRO A   133                                                      
REMARK 465     GLU A   134                                                      
REMARK 465     VAL A   135                                                      
REMARK 465     TYR A   136                                                      
REMARK 465     GLY A   137                                                      
REMARK 465     VAL A   303                                                      
REMARK 465     SER A   304                                                      
REMARK 465     TRP A   305                                                      
REMARK 465     THR A   306                                                      
REMARK 465     GLY A   307                                                      
REMARK 465     LYS A   308                                                      
REMARK 465     PRO A   309                                                      
REMARK 465     PRO A   332                                                      
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 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    CD   CE   NZ                                        
REMARK 470     GLU A  56    CG   CD   OE1  OE2                                  
REMARK 470     TYR A  58    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG A  73    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A  77    CE   NZ                                             
REMARK 470     GLN A  94    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    CG   CD   CE   NZ                                   
REMARK 470     ASN A 127    CG   OD1  ND2                                       
REMARK 470     GLU A 138    CG   CD   OE1  OE2                                  
REMARK 470     THR A 139    OG1  CG2                                            
REMARK 470     SER A 140    OG                                                  
REMARK 470     LYS A 152    CD   CE   NZ                                        
REMARK 470     ASP A 156    CG   OD1  OD2                                       
REMARK 470     LYS A 180    CD   CE   NZ                                        
REMARK 470     LYS A 193    CD   CE   NZ                                        
REMARK 470     LYS A 212    CE   NZ                                             
REMARK 470     ARG A 220    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A 227    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 230    CD   OE1  OE2                                       
REMARK 470     GLU A 248    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 255    CG   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     SER A 302    OG                                                  
REMARK 470     VAL A 310    CG1  CG2                                            
REMARK 470     SER A 327    OG                                                  
REMARK 470     LYS A 330    CD   CE   NZ                                        
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    TYR A  58      -32.41   -133.73                                   
REMARK 500    LEU A  60       61.02   -105.09                                   
REMARK 500    PRO A  95     -166.99    -69.21                                   
REMARK 500    CYS A 179      149.08    -37.32                                   
REMARK 500    PHE A 277      105.25    -33.89                                   
REMARK 500    ILE A 317      108.91    -59.63                                   
REMARK 500    LYS A 330       17.21    -67.07                                   
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 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 408                 
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: 4ER5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ER6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ER7   RELATED DB: PDB                                   
DBREF  4ER3 A    1   351  UNP    Q8TEK3   DOT1L_HUMAN      1    351             
SEQADV 4ER3 GLY A    0  UNP  Q8TEK3              EXPRESSION TAG                 
SEQRES   1 A  352  GLY MET GLY GLU LYS LEU GLU LEU ARG LEU LYS SER PRO          
SEQRES   2 A  352  VAL GLY ALA GLU PRO ALA VAL TYR PRO TRP PRO LEU PRO          
SEQRES   3 A  352  VAL TYR ASP LYS HIS HIS ASP ALA ALA HIS GLU ILE ILE          
SEQRES   4 A  352  GLU THR ILE ARG TRP VAL CYS GLU GLU ILE PRO ASP LEU          
SEQRES   5 A  352  LYS LEU ALA MET GLU ASN TYR VAL LEU ILE ASP TYR ASP          
SEQRES   6 A  352  THR LYS SER PHE GLU SER MET GLN ARG LEU CYS ASP LYS          
SEQRES   7 A  352  TYR ASN ARG ALA ILE ASP SER ILE HIS GLN LEU TRP LYS          
SEQRES   8 A  352  GLY THR THR GLN PRO MET LYS LEU ASN THR ARG PRO SER          
SEQRES   9 A  352  THR GLY LEU LEU ARG HIS ILE LEU GLN GLN VAL TYR ASN          
SEQRES  10 A  352  HIS SER VAL THR ASP PRO GLU LYS LEU ASN ASN TYR GLU          
SEQRES  11 A  352  PRO PHE SER PRO GLU VAL TYR GLY GLU THR SER PHE ASP          
SEQRES  12 A  352  LEU VAL ALA GLN MET ILE ASP GLU ILE LYS MET THR ASP          
SEQRES  13 A  352  ASP ASP LEU PHE VAL ASP LEU GLY SER GLY VAL GLY GLN          
SEQRES  14 A  352  VAL VAL LEU GLN VAL ALA ALA ALA THR ASN CYS LYS HIS          
SEQRES  15 A  352  HIS TYR GLY VAL GLU LYS ALA ASP ILE PRO ALA LYS TYR          
SEQRES  16 A  352  ALA GLU THR MET ASP ARG GLU PHE ARG LYS TRP MET LYS          
SEQRES  17 A  352  TRP TYR GLY LYS LYS HIS ALA GLU TYR THR LEU GLU ARG          
SEQRES  18 A  352  GLY ASP PHE LEU SER GLU GLU TRP ARG GLU ARG ILE ALA          
SEQRES  19 A  352  ASN THR SER VAL ILE PHE VAL ASN ASN PHE ALA PHE GLY          
SEQRES  20 A  352  PRO GLU VAL ASP HIS GLN LEU LYS GLU ARG PHE ALA ASN          
SEQRES  21 A  352  MET LYS GLU GLY GLY ARG ILE VAL SER SER LYS PRO PHE          
SEQRES  22 A  352  ALA PRO LEU ASN PHE ARG ILE ASN SER ARG ASN LEU SER          
SEQRES  23 A  352  ASP ILE GLY THR ILE MET ARG VAL VAL GLU LEU SER PRO          
SEQRES  24 A  352  LEU LYS GLY SER VAL SER TRP THR GLY LYS PRO VAL SER          
SEQRES  25 A  352  TYR TYR LEU HIS THR ILE ASP ARG THR ILE LEU GLU ASN          
SEQRES  26 A  352  TYR PHE SER SER LEU LYS ASN PRO LYS LEU ARG GLU GLU          
SEQRES  27 A  352  GLN GLU ALA ALA ARG ARG ARG GLN GLN ARG GLU SER LYS          
SEQRES  28 A  352  SER                                                          
HET    0QK  A 401      39                                                       
HET    SO4  A 402       5                                                       
HET    SO4  A 403       5                                                       
HET    SO4  A 404       5                                                       
HET    SO4  A 405       5                                                       
HET    SO4  A 406       5                                                       
HET    EDO  A 407       4                                                       
HET    EDO  A 408       4                                                       
HET    UNX  A 409       1                                                       
HET    UNX  A 410       1                                                       
HET    UNX  A 411       1                                                       
HET    UNX  A 412       1                                                       
HET    UNX  A 413       1                                                       
HET    UNX  A 414       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     SO4 SULFATE ION                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     UNX UNKNOWN ATOM OR ION                                              
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  0QK    C28 H41 N7 O4                                                
FORMUL   3  SO4    5(O4 S 2-)                                                   
FORMUL   8  EDO    2(C2 H6 O2)                                                  
FORMUL  10  UNX    6(X)                                                         
FORMUL  16  HOH   *18(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 MET A   55  LEU A   60  1                                   6    
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 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  ASN A  259  1                                  14    
HELIX   11  11 ASP A  286  THR A  289  5                                   4    
HELIX   12  12 ARG A  319  LYS A  330  1                                  12    
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  PHE A 159   O  HIS A 181           
SHEET    4   C 7 VAL A 237  VAL A 240  1  O  VAL A 237   N  LEU A 158           
SHEET    5   C 7 ARG A 265  SER A 268  1  O  ARG A 265   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           
CISPEP   1 TRP A   22    PRO A   23          0        -7.93                     
SITE     1 AC1 14 MET A 147  ASP A 161  GLY A 163  SER A 164                    
SITE     2 AC1 14 VAL A 169  GLU A 186  LYS A 187  GLY A 221                    
SITE     3 AC1 14 ASP A 222  PHE A 223  ASN A 241  PHE A 245                    
SITE     4 AC1 14 SER A 268  TYR A 312                                          
SITE     1 AC2  2 ASN A  99  ARG A 101                                          
SITE     1 AC3  1 THR A 104                                                     
SITE     1 AC4  3 SER A  67  PHE A  68  GLU A  69                               
SITE     1 AC5  4 HIS A 117  GLU A 201  LYS A 204  LYS A 300                    
SITE     1 AC6  3 ARG A 203  LYS A 207  HIS A 213                               
SITE     1 AC7  3 VAL A 160  TYR A 183  THR A 235                               
SITE     1 AC8  2 ARG A 229  ARG A 256                                          
CRYST1  155.705  155.705   48.486  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      0.006422  0.003708  0.000000        0.00000                         
SCALE2      0.000000  0.007416  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020625        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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