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Database: PDB
Entry: 4EKI
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Original site: 4EKI 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       09-APR-12   4EKI              
TITLE     CRYSTAL STRUCTURE OF DOT1L IN COMPLEX WITH EPZ004777                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-79 SPECIFIC; 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 1-416;                                        
COMPND   5 SYNONYM: DOT1-LIKE PROTEIN, HISTONE H3-K79 METHYLTRANSFERASE, H3-K79-
COMPND   6 HMTASE, LYSINE N-METHYLTRANSFERASE 4;                                
COMPND   7 EC: 2.1.1.43;                                                        
COMPND   8 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                                         
KEYWDS    METHYLTRANSFERASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.JIN                                                                 
REVDAT   2   09-JAN-13 4EKI    1       JRNL                                     
REVDAT   1   17-OCT-12 4EKI    0                                                
JRNL        AUTH   A.BASAVAPATHRUNI,L.JIN,S.R.DAIGLE,C.R.MAJER,C.A.THERKELSEN,  
JRNL        AUTH 2 T.J.WIGLE,K.W.KUNTZ,R.CHESWORTH,R.M.POLLOCK,M.P.SCOTT,       
JRNL        AUTH 3 M.P.MOYER,V.M.RICHON,R.A.COPELAND,E.J.OLHAVA                 
JRNL        TITL   CONFORMATIONAL ADAPTATION DRIVES POTENT, SELECTIVE AND       
JRNL        TITL 2 DURABLE INHIBITION OF THE HUMAN PROTEIN METHYLTRANSFERASE    
JRNL        TITL 3 DOT1L.                                                       
JRNL        REF    CHEM.BIOL.DRUG DES.           V.  80   971 2012              
JRNL        REFN                   ISSN 1747-0277                               
JRNL        PMID   22978415                                                     
JRNL        DOI    10.1111/CBDD.12050                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.85 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) : 2.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.09                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 15029                          
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) : 0.212                           
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.262                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 785                             
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) : 2.85                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.92                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 974                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.10                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2700                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 61                           
REMARK   3   BIN FREE R VALUE                    : 0.4060                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2591                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 54                                      
REMARK   3   SOLVENT ATOMS            : 10                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 90.38                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.37000                                              
REMARK   3    B22 (A**2) : 0.37000                                              
REMARK   3    B33 (A**2) : -0.56000                                             
REMARK   3    B12 (A**2) : 0.19000                                              
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): 0.471         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.319         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.244         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.475        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.925                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2709 ; 0.009 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3674 ; 1.456 ; 1.972       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   316 ; 6.427 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   129 ;37.649 ;23.953       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   465 ;19.466 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;15.673 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   396 ; 0.104 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2042 ; 0.008 ; 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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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 4EKI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-APR-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB071732.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-AUG-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15834                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.53900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: PHASER                       
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3QOW                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.47                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM ACETATE, 1.8-2.0 M         
REMARK 280  AMMONIUM SULFATE, 5 MM TCEP, PH 5.2, COMPOUND SOAKED INTO CROSS-    
REMARK 280  LINKED DOT1L-SAM CRYSTAL, TEMPERATURE 293K, VAPOR DIFFUSION,        
REMARK 280  HANGING DROP                                                        
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       32.30133            
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       16.15067            
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       24.22600            
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        8.07533            
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       40.37667            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 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     HIS A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     VAL A    59                                                      
REMARK 465     LEU A    60                                                      
REMARK 465     ILE A    61                                                      
REMARK 465     ASN A   127                                                      
REMARK 465     TYR A   128                                                      
REMARK 465     GLU A   129                                                      
REMARK 465     PRO A   130                                                      
REMARK 465     PHE A   131                                                      
REMARK 465     ASN A   331                                                      
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 465     ASN A   352                                                      
REMARK 465     ALA A   353                                                      
REMARK 465     ALA A   354                                                      
REMARK 465     THR A   355                                                      
REMARK 465     PRO A   356                                                      
REMARK 465     THR A   357                                                      
REMARK 465     LYS A   358                                                      
REMARK 465     GLY A   359                                                      
REMARK 465     PRO A   360                                                      
REMARK 465     GLU A   361                                                      
REMARK 465     GLY A   362                                                      
REMARK 465     LYS A   363                                                      
REMARK 465     VAL A   364                                                      
REMARK 465     ALA A   365                                                      
REMARK 465     GLY A   366                                                      
REMARK 465     PRO A   367                                                      
REMARK 465     ALA A   368                                                      
REMARK 465     ASP A   369                                                      
REMARK 465     ALA A   370                                                      
REMARK 465     PRO A   371                                                      
REMARK 465     MET A   372                                                      
REMARK 465     ASP A   373                                                      
REMARK 465     SER A   374                                                      
REMARK 465     GLY A   375                                                      
REMARK 465     ALA A   376                                                      
REMARK 465     GLU A   377                                                      
REMARK 465     GLU A   378                                                      
REMARK 465     GLU A   379                                                      
REMARK 465     LYS A   380                                                      
REMARK 465     ALA A   381                                                      
REMARK 465     GLY A   382                                                      
REMARK 465     ALA A   383                                                      
REMARK 465     ALA A   384                                                      
REMARK 465     THR A   385                                                      
REMARK 465     VAL A   386                                                      
REMARK 465     LYS A   387                                                      
REMARK 465     LYS A   388                                                      
REMARK 465     PRO A   389                                                      
REMARK 465     SER A   390                                                      
REMARK 465     PRO A   391                                                      
REMARK 465     SER A   392                                                      
REMARK 465     LYS A   393                                                      
REMARK 465     ALA A   394                                                      
REMARK 465     ARG A   395                                                      
REMARK 465     LYS A   396                                                      
REMARK 465     LYS A   397                                                      
REMARK 465     LYS A   398                                                      
REMARK 465     LEU A   399                                                      
REMARK 465     ASN A   400                                                      
REMARK 465     LYS A   401                                                      
REMARK 465     LYS A   402                                                      
REMARK 465     GLY A   403                                                      
REMARK 465     ARG A   404                                                      
REMARK 465     LYS A   405                                                      
REMARK 465     MET A   406                                                      
REMARK 465     ALA A   407                                                      
REMARK 465     GLY A   408                                                      
REMARK 465     ARG A   409                                                      
REMARK 465     LYS A   410                                                      
REMARK 465     ARG A   411                                                      
REMARK 465     GLY A   412                                                      
REMARK 465     ARG A   413                                                      
REMARK 465     PRO A   414                                                      
REMARK 465     LYS A   415                                                      
REMARK 465     LYS A   416                                                      
REMARK 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 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    GLU A  56       28.17    -60.95                                   
REMARK 500    LEU A  88      -36.84    -36.69                                   
REMARK 500    LYS A  97      117.02    -38.24                                   
REMARK 500    LEU A  98      -89.83    -49.72                                   
REMARK 500    PRO A 122       18.30    -64.14                                   
REMARK 500    LYS A 124       42.81    -66.22                                   
REMARK 500    GLU A 134       69.75    -67.25                                   
REMARK 500    HIS A 181      149.96   -175.20                                   
REMARK 500    LYS A 187      -63.01    -92.62                                   
REMARK 500    SER A 304       64.73     60.23                                   
REMARK 500    ILE A 317      108.80    -57.21                                   
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 SO4 A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 504                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3QOW   RELATED DB: PDB                                   
REMARK 900 DOT1L STRCUTURE WITH SAM                                             
REMARK 900 RELATED ID: 4EK9   RELATED DB: PDB                                   
REMARK 900 DOT1L STRUCTURE WITH EPZ000004                                       
REMARK 900 RELATED ID: 4EKG   RELATED DB: PDB                                   
REMARK 900 DOT1L STRUCTURE WITH EPZ003696                                       
DBREF  4EKI A    1   416  UNP    Q8TEK3   DOT1L_HUMAN      1    416             
SEQADV 4EKI HIS A   -8  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 4EKI HIS A   -7  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 4EKI HIS A   -6  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 4EKI HIS A   -5  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 4EKI HIS A   -4  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 4EKI HIS A   -3  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 4EKI SER A   -2  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 4EKI SER A   -1  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 4EKI GLY A    0  UNP  Q8TEK3              EXPRESSION TAG                 
SEQRES   1 A  425  HIS HIS HIS HIS HIS HIS SER SER GLY MET GLY GLU LYS          
SEQRES   2 A  425  LEU GLU LEU ARG LEU LYS SER PRO VAL GLY ALA GLU PRO          
SEQRES   3 A  425  ALA VAL TYR PRO TRP PRO LEU PRO VAL TYR ASP LYS HIS          
SEQRES   4 A  425  HIS ASP ALA ALA HIS GLU ILE ILE GLU THR ILE ARG TRP          
SEQRES   5 A  425  VAL CYS GLU GLU ILE PRO ASP LEU LYS LEU ALA MET GLU          
SEQRES   6 A  425  ASN TYR VAL LEU ILE ASP TYR ASP THR LYS SER PHE GLU          
SEQRES   7 A  425  SER MET GLN ARG LEU CYS ASP LYS TYR ASN ARG ALA ILE          
SEQRES   8 A  425  ASP SER ILE HIS GLN LEU TRP LYS GLY THR THR GLN PRO          
SEQRES   9 A  425  MET LYS LEU ASN THR ARG PRO SER THR GLY LEU LEU ARG          
SEQRES  10 A  425  HIS ILE LEU GLN GLN VAL TYR ASN HIS SER VAL THR ASP          
SEQRES  11 A  425  PRO GLU LYS LEU ASN ASN TYR GLU PRO PHE SER PRO GLU          
SEQRES  12 A  425  VAL TYR GLY GLU THR SER PHE ASP LEU VAL ALA GLN MET          
SEQRES  13 A  425  ILE ASP GLU ILE LYS MET THR ASP ASP ASP LEU PHE VAL          
SEQRES  14 A  425  ASP LEU GLY SER GLY VAL GLY GLN VAL VAL LEU GLN VAL          
SEQRES  15 A  425  ALA ALA ALA THR ASN CYS LYS HIS HIS TYR GLY VAL GLU          
SEQRES  16 A  425  LYS ALA ASP ILE PRO ALA LYS TYR ALA GLU THR MET ASP          
SEQRES  17 A  425  ARG GLU PHE ARG LYS TRP MET LYS TRP TYR GLY LYS LYS          
SEQRES  18 A  425  HIS ALA GLU TYR THR LEU GLU ARG GLY ASP PHE LEU SER          
SEQRES  19 A  425  GLU GLU TRP ARG GLU ARG ILE ALA ASN THR SER VAL ILE          
SEQRES  20 A  425  PHE VAL ASN ASN PHE ALA PHE GLY PRO GLU VAL ASP HIS          
SEQRES  21 A  425  GLN LEU LYS GLU ARG PHE ALA ASN MET LYS GLU GLY GLY          
SEQRES  22 A  425  ARG ILE VAL SER SER LYS PRO PHE ALA PRO LEU ASN PHE          
SEQRES  23 A  425  ARG ILE ASN SER ARG ASN LEU SER ASP ILE GLY THR ILE          
SEQRES  24 A  425  MET ARG VAL VAL GLU LEU SER PRO LEU LYS GLY SER VAL          
SEQRES  25 A  425  SER TRP THR GLY LYS PRO VAL SER TYR TYR LEU HIS THR          
SEQRES  26 A  425  ILE ASP ARG THR ILE LEU GLU ASN TYR PHE SER SER LEU          
SEQRES  27 A  425  LYS ASN PRO LYS LEU ARG GLU GLU GLN GLU ALA ALA ARG          
SEQRES  28 A  425  ARG ARG GLN GLN ARG GLU SER LYS SER ASN ALA ALA THR          
SEQRES  29 A  425  PRO THR LYS GLY PRO GLU GLY LYS VAL ALA GLY PRO ALA          
SEQRES  30 A  425  ASP ALA PRO MET ASP SER GLY ALA GLU GLU GLU LYS ALA          
SEQRES  31 A  425  GLY ALA ALA THR VAL LYS LYS PRO SER PRO SER LYS ALA          
SEQRES  32 A  425  ARG LYS LYS LYS LEU ASN LYS LYS GLY ARG LYS MET ALA          
SEQRES  33 A  425  GLY ARG LYS ARG GLY ARG PRO LYS LYS                          
HET    0QK  A 501      39                                                       
HET    SO4  A 502       5                                                       
HET    SO4  A 503       5                                                       
HET    SO4  A 504       5                                                       
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                                                      
FORMUL   2  0QK    C28 H41 N7 O4                                                
FORMUL   3  SO4    3(O4 S 2-)                                                   
FORMUL   6  HOH   *10(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 SER A   67  TRP A   89  1                                  23    
HELIX    4   4 SER A  103  VAL A  119  1                                  17    
HELIX    5   5 SER A  140  ILE A  151  1                                  12    
HELIX    6   6 GLY A  167  THR A  177  1                                  11    
HELIX    7   7 ALA A  188  TYR A  209  1                                  22    
HELIX    8   8 SER A  225  THR A  235  1                                  11    
HELIX    9   9 PHE A  245  ALA A  258  1                                  14    
HELIX   10  10 ASP A  286  THR A  289  5                                   4    
HELIX   11  11 SER A  304  LYS A  308  5                                   5    
HELIX   12  12 ARG A  319  SER A  328  1                                  10    
SHEET    1   A 2 GLU A   6  LEU A   9  0                                        
SHEET    2   A 2 ALA A  18  PRO A  21 -1  O  ALA A  18   N  LEU A   9           
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  THR A 217           
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  VAL A 160           
SHEET    5   C 7 ARG A 265  SER A 268  1  O  VAL A 267   N  ILE A 238           
SHEET    6   C 7 TYR A 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        -5.95                     
SITE     1 AC1 12 TYR A 136  ASP A 161  GLY A 163  SER A 164                    
SITE     2 AC1 12 VAL A 169  GLU A 186  LYS A 187  ALA A 188                    
SITE     3 AC1 12 GLY A 221  ASP A 222  PHE A 223  ASN A 241                    
SITE     1 AC2  3 ARG A 203  LYS A 207  HIS A 213                               
SITE     1 AC3  2 THR A 100  ARG A 101                                          
SITE     1 AC4  2 SER A 103  THR A 104                                          
CRYST1  155.053  155.053   48.452  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      0.006449  0.003724  0.000000        0.00000                         
SCALE2      0.000000  0.007447  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020639        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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