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Database: PDB
Entry: 4EQZ
LinkDB: 4EQZ
Original site: 4EQZ 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       19-APR-12   4EQZ              
TITLE     CRYSTAL STRUCTURE OF HUMAN DOT1L IN COMPLEX WITH INHIBITOR FED2       
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,Y.LI,K.T.NGUYEN,A.FEDERATION,J.MARINEAU,  
AUTHOR   2 J.QI,M.VEDADI,J.E.BRADNER,M.SCHAPIRA,C.H.ARROWSMITH,A.M.EDWARDS,     
AUTHOR   3 C.BOUNTRA,P.J.BROWN,STRUCTURAL GENOMICS CONSORTIUM (SGC)             
REVDAT   1   02-MAY-12 4EQZ    0                                                
JRNL        AUTH   A.K.WERNIMONT,W.TEMPEL,W.YU,Y.LI,K.T.NGUYEN,A.FEDERATION,    
JRNL        AUTH 2 J.MARINEAU,J.QI,M.VEDADI,J.E.BRADNER,M.SCHAPIRA,             
JRNL        AUTH 3 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 FED2                                                         
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
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) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 37503                          
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) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.221                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1850                            
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) : 2.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.21                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2589                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2630                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 142                          
REMARK   3   BIN FREE R VALUE                    : 0.3020                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2618                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 42                                      
REMARK   3   SOLVENT ATOMS            : 108                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.89                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.75000                                             
REMARK   3    B22 (A**2) : -0.75000                                             
REMARK   3    B33 (A**2) : 1.13000                                              
REMARK   3    B12 (A**2) : -0.38000                                             
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): 0.150         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.137         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.094         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.608         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.937                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2851 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1898 ; 0.004 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3903 ; 1.387 ; 1.958       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4630 ; 1.014 ; 3.005       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   359 ; 5.496 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   139 ;32.437 ;24.245       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   455 ;14.331 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;19.796 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   421 ; 0.086 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3241 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   590 ; 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):  1728 ; 0.880 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   684 ; 0.167 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2813 ; 1.663 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1123 ; 2.221 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1083 ; 3.591 ; 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 4EQZ 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 RCSB071963.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-NOV-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97944                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XSCALE                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37551                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 132.679                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 11.200                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.27                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.00                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.81500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.81500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.900                              
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   (%): 65.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.60                     
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       35.49600            
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       17.74800            
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       26.62200            
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        8.87400            
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       44.37000            
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     LYS A     4                                                      
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     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 465     MET A   417                                                      
REMARK 465     ASN A   418                                                      
REMARK 465     THR A   419                                                      
REMARK 465     ALA A   420                                                      
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  29    CD   CE   NZ                                        
REMARK 470     GLU A  56    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  69    CD   OE1  OE2                                       
REMARK 470     LYS A  77    CD   CE   NZ                                        
REMARK 470     GLN A  94    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  97    CD   CE   NZ                                        
REMARK 470     GLU A 123    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 124    CG   CD   CE   NZ                                   
REMARK 470     TYR A 136    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A 138    CG   CD   OE1  OE2                                  
REMARK 470     MET A 147    SD   CE                                             
REMARK 470     LYS A 152    CG   CD   CE   NZ                                   
REMARK 470     LYS A 180    CD   CE   NZ                                        
REMARK 470     LYS A 193    CD   CE   NZ                                        
REMARK 470     LYS A 204    CE   NZ                                             
REMARK 470     LYS A 207    CD   CE   NZ                                        
REMARK 470     LYS A 212    CD   CE   NZ                                        
REMARK 470     ARG A 220    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A 255    CD   OE1  OE2                                       
REMARK 470     LYS A 261    CE   NZ                                             
REMARK 470     ARG A 278    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A 282    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 308    CE   NZ                                             
REMARK 470     ARG A 342    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER A   328     OE1  GLN A   338              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 247   C   -  N   -  CA  ANGL. DEV. =   9.4 DEGREES          
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 AW0 A 501                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4ER0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ER3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ER5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ER6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ER7   RELATED DB: PDB                                   
DBREF  4EQZ A    1   420  UNP    Q8TEK3   DOT1L_HUMAN      1    420             
SEQADV 4EQZ GLY A    0  UNP  Q8TEK3              EXPRESSION TAG                 
SEQRES   1 A  421  GLY MET GLY GLU LYS LEU GLU LEU ARG LEU LYS SER PRO          
SEQRES   2 A  421  VAL GLY ALA GLU PRO ALA VAL TYR PRO TRP PRO LEU PRO          
SEQRES   3 A  421  VAL TYR ASP LYS HIS HIS ASP ALA ALA HIS GLU ILE ILE          
SEQRES   4 A  421  GLU THR ILE ARG TRP VAL CYS GLU GLU ILE PRO ASP LEU          
SEQRES   5 A  421  LYS LEU ALA MET GLU ASN TYR VAL LEU ILE ASP TYR ASP          
SEQRES   6 A  421  THR LYS SER PHE GLU SER MET GLN ARG LEU CYS ASP LYS          
SEQRES   7 A  421  TYR ASN ARG ALA ILE ASP SER ILE HIS GLN LEU TRP LYS          
SEQRES   8 A  421  GLY THR THR GLN PRO MET LYS LEU ASN THR ARG PRO SER          
SEQRES   9 A  421  THR GLY LEU LEU ARG HIS ILE LEU GLN GLN VAL TYR ASN          
SEQRES  10 A  421  HIS SER VAL THR ASP PRO GLU LYS LEU ASN ASN TYR GLU          
SEQRES  11 A  421  PRO PHE SER PRO GLU VAL TYR GLY GLU THR SER PHE ASP          
SEQRES  12 A  421  LEU VAL ALA GLN MET ILE ASP GLU ILE LYS MET THR ASP          
SEQRES  13 A  421  ASP ASP LEU PHE VAL ASP LEU GLY SER GLY VAL GLY GLN          
SEQRES  14 A  421  VAL VAL LEU GLN VAL ALA ALA ALA THR ASN CYS LYS HIS          
SEQRES  15 A  421  HIS TYR GLY VAL GLU LYS ALA ASP ILE PRO ALA LYS TYR          
SEQRES  16 A  421  ALA GLU THR MET ASP ARG GLU PHE ARG LYS TRP MET LYS          
SEQRES  17 A  421  TRP TYR GLY LYS LYS HIS ALA GLU TYR THR LEU GLU ARG          
SEQRES  18 A  421  GLY ASP PHE LEU SER GLU GLU TRP ARG GLU ARG ILE ALA          
SEQRES  19 A  421  ASN THR SER VAL ILE PHE VAL ASN ASN PHE ALA PHE GLY          
SEQRES  20 A  421  PRO GLU VAL ASP HIS GLN LEU LYS GLU ARG PHE ALA ASN          
SEQRES  21 A  421  MET LYS GLU GLY GLY ARG ILE VAL SER SER LYS PRO PHE          
SEQRES  22 A  421  ALA PRO LEU ASN PHE ARG ILE ASN SER ARG ASN LEU SER          
SEQRES  23 A  421  ASP ILE GLY THR ILE MET ARG VAL VAL GLU LEU SER PRO          
SEQRES  24 A  421  LEU LYS GLY SER VAL SER TRP THR GLY LYS PRO VAL SER          
SEQRES  25 A  421  TYR TYR LEU HIS THR ILE ASP ARG THR ILE LEU GLU ASN          
SEQRES  26 A  421  TYR PHE SER SER LEU LYS ASN PRO LYS LEU ARG GLU GLU          
SEQRES  27 A  421  GLN GLU ALA ALA ARG ARG ARG GLN GLN ARG GLU SER LYS          
SEQRES  28 A  421  SER ASN ALA ALA THR PRO THR LYS GLY PRO GLU GLY LYS          
SEQRES  29 A  421  VAL ALA GLY PRO ALA ASP ALA PRO MET ASP SER GLY ALA          
SEQRES  30 A  421  GLU GLU GLU LYS ALA GLY ALA ALA THR VAL LYS LYS PRO          
SEQRES  31 A  421  SER PRO SER LYS ALA ARG LYS LYS LYS LEU ASN LYS LYS          
SEQRES  32 A  421  GLY ARG LYS MET ALA GLY ARG LYS ARG GLY ARG PRO LYS          
SEQRES  33 A  421  LYS MET ASN THR ALA                                          
HET    AW0  A 501      36                                                       
HET    UNX  A 502       1                                                       
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     AW0 5'-DEOXY-5'-[(3-{[(4-METHYLPHENYL)                               
HETNAM   2 AW0  CARBAMOYL]AMINO}PROPYL)(PROPAN-2-YL)AMINO]ADENOSINE             
HETNAM     UNX UNKNOWN ATOM OR ION                                              
FORMUL   2  AW0    C24 H34 N8 O4                                                
FORMUL   3  UNX    6(X)                                                         
FORMUL   9  HOH   *108(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  GLY A   91  1                                  25    
HELIX    4   4 SER A  103  VAL A  119  1                                  17    
HELIX    5   5 ASP A  121  ASN A  126  1                                   6    
HELIX    6   6 ASN A  127  GLU A  129  5                                   3    
HELIX    7   7 SER A  140  ILE A  151  1                                  12    
HELIX    8   8 GLY A  167  THR A  177  1                                  11    
HELIX    9   9 ALA A  188  GLY A  210  1                                  23    
HELIX   10  10 SER A  225  ASN A  234  1                                  10    
HELIX   11  11 GLY A  246  ALA A  258  1                                  13    
HELIX   12  12 ASP A  286  THR A  289  5                                   4    
HELIX   13  13 ARG A  319  ASN A  331  1                                  13    
HELIX   14  14 ASN A  331  ARG A  342  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  PHE A 239   N  VAL A 160           
SHEET    5   C 7 ARG A 265  SER A 268  1  O  VAL A 267   N  ILE A 238           
SHEET    6   C 7 TYR A 313  ILE A 317 -1  O  HIS A 315   N  ILE A 266           
SHEET    7   C 7 MET A 291  GLU A 295 -1  N  VAL A 294   O  LEU A 314           
CISPEP   1 TRP A   22    PRO A   23          0        -5.64                     
CISPEP   2 GLU A  129    PRO A  130          0         1.59                     
SITE     1 AC1 18 PRO A 130  PHE A 131  ASP A 161  GLY A 163                    
SITE     2 AC1 18 SER A 164  GLY A 165  VAL A 169  GLU A 186                    
SITE     3 AC1 18 LYS A 187  GLY A 221  ASP A 222  PHE A 223                    
SITE     4 AC1 18 PHE A 239  VAL A 240  ASN A 241  PHE A 245                    
SITE     5 AC1 18 TYR A 312  HOH A 645                                          
CRYST1  150.009  150.009   53.244  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      0.006666  0.003849  0.000000        0.00000                         
SCALE2      0.000000  0.007698  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018781        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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