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Database: PDB
Entry: 3UWP
LinkDB: 3UWP
Original site: 3UWP 
HEADER    TRANSFERASE                             02-DEC-11   3UWP              
TITLE     CRYSTAL STRUCTURE OF DOT1L IN COMPLEX WITH 5-IODOTUBERCIDIN           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-79 SPECIFIC; 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 1-420;                                        
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: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-V2R-PRARE2;                           
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28-MHL                                 
KEYWDS    HISTONE, METHYLTRANSFERASE, EPIGENETICS, TUBERCIDIN, STRUCTURAL       
KEYWDS   2 GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC, TRANSFERASE           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.YU,W.TEMPEL,D.SMIL,M.SCHAPIRA,Y.LI,M.VEDADI,K.T.NGUYEN,             
AUTHOR   2 A.K.WERNIMONT,C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,J.WEIGELT,        
AUTHOR   3 P.J.BROWN,STRUCTURAL GENOMICS CONSORTIUM (SGC)                       
REVDAT   1   14-MAR-12 3UWP    0                                                
JRNL        AUTH   W.YU,W.TEMPEL,D.SMIL,M.SCHAPIRA,Y.LI,M.VEDADI,K.T.NGUYEN,    
JRNL        AUTH 2 A.K.WERNIMONT,C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,          
JRNL        AUTH 3 J.WEIGELT,P.J.BROWN                                          
JRNL        TITL   CRYSTAL STRUCTURE OF DOT1L IN COMPLEX WITH 5-IODOTUBERCIDIN  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 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) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 43105                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : FROM PDB ENTRY 3QOW             
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.853                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2092                            
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) : 2.05                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.10                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2785                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.24                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2960                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 135                          
REMARK   3   BIN FREE R VALUE                    : 0.3080                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2669                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 29                                      
REMARK   3   SOLVENT ATOMS            : 66                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.82                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.95900                                             
REMARK   3    B22 (A**2) : -1.95900                                             
REMARK   3    B33 (A**2) : 2.93900                                              
REMARK   3    B12 (A**2) : -0.98000                                             
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): 0.125         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.122         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.091         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.927         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.950                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2808 ; 0.013 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  1851 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3839 ; 1.327 ; 1.952       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4498 ; 0.879 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   352 ; 5.435 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   130 ;32.233 ;23.769       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   439 ;13.411 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;17.800 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   423 ; 0.077 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3161 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   588 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     4        A   344                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.1790  58.3140   3.2350              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0182 T22:   0.0205                                     
REMARK   3      T33:   0.0396 T12:   0.0071                                     
REMARK   3      T13:   0.0015 T23:  -0.0022                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6851 L22:   1.2583                                     
REMARK   3      L33:   0.4925 L12:  -1.4903                                     
REMARK   3      L13:   0.0403 L23:  -0.1079                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0168 S12:   0.0761 S13:  -0.0151                       
REMARK   3      S21:  -0.0469 S22:  -0.0137 S23:   0.0620                       
REMARK   3      S31:   0.0572 S32:  -0.0295 S33:   0.0305                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK BULK SOLVENT                                    
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 ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 3UWP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-DEC-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB069303.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-JUN-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
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-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91963                            
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 : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43269                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 5.900                              
REMARK 200  R MERGE                    (I) : 0.09800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.12                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.97300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.43                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.5M SODIUM FORMATE, 0.1M SODIUM         
REMARK 280  ACETATE, PH 4.6, VAPOR DIFFUSION, TEMPERATURE 291K                  
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       35.68067            
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       17.84033            
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       26.76050            
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        8.92017            
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       44.60083            
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 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     MET A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     ARG A    -7                                                      
REMARK 465     GLU A    -6                                                      
REMARK 465     ASN A    -5                                                      
REMARK 465     LEU A    -4                                                      
REMARK 465     TYR A    -3                                                      
REMARK 465     PHE A    -2                                                      
REMARK 465     GLN A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     GLU A     3                                                      
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   4    CG   CD   CE   NZ                                   
REMARK 470     LYS A  29    CD   CE   NZ                                        
REMARK 470     GLU A  56    CG   CD   OE1  OE2                                  
REMARK 470     ILE A  61    CG1  CG2  CD1                                       
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     ASN A  99    CG   OD1  ND2                                       
REMARK 470     LYS A 124    CG   CD   CE   NZ                                   
REMARK 470     GLU A 134    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 138    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 152    CE   NZ                                             
REMARK 470     LYS A 180    CG   CD   CE   NZ                                   
REMARK 470     LYS A 187    CE   NZ                                             
REMARK 470     ASP A 189    CG   OD1  OD2                                       
REMARK 470     LYS A 193    CD   CE   NZ                                        
REMARK 470     LYS A 207    CD   CE   NZ                                        
REMARK 470     LYS A 212    CD   CE   NZ                                        
REMARK 470     GLU A 227    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 230    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 248    CD   OE1  OE2                                       
REMARK 470     LYS A 261    NZ                                                  
REMARK 470     ARG A 278    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 282    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 300    CG   CD   CE   NZ                                   
REMARK 470     LYS A 308    CE   NZ                                             
REMARK 470     LYS A 333    NZ                                                  
REMARK 470     GLU A 336    CD   OE1  OE2                                       
REMARK 470     GLU A 337    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 342    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 343    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 344    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  28     -167.93   -163.29                                   
REMARK 500    THR A 139      -85.47   -138.76                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 424  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MET A  55   O                                                      
REMARK 620 2 HOH A 481   O   173.7                                              
REMARK 620 3 ASN A  57   OD1  84.0  99.2                                        
REMARK 620 4 HOH A 480   O    88.6  85.7  96.2                                  
REMARK 620 5 LYS A  52   O    85.6 100.1  84.0 174.1                            
REMARK 620 6 LEU A  53   O    89.5  89.0 162.2 100.1  79.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5ID A 421                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 422                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 423                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 424                  
DBREF  3UWP A    1   420  UNP    Q8TEK3   DOT1L_HUMAN      1    420             
SEQADV 3UWP MET A  -17  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 3UWP HIS A  -16  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 3UWP HIS A  -15  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 3UWP HIS A  -14  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 3UWP HIS A  -13  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 3UWP HIS A  -12  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 3UWP HIS A  -11  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 3UWP SER A  -10  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 3UWP SER A   -9  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 3UWP GLY A   -8  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 3UWP ARG A   -7  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 3UWP GLU A   -6  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 3UWP ASN A   -5  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 3UWP LEU A   -4  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 3UWP TYR A   -3  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 3UWP PHE A   -2  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 3UWP GLN A   -1  UNP  Q8TEK3              EXPRESSION TAG                 
SEQADV 3UWP GLY A    0  UNP  Q8TEK3              EXPRESSION TAG                 
SEQRES   1 A  438  MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN          
SEQRES   2 A  438  LEU TYR PHE GLN GLY MET GLY GLU LYS LEU GLU LEU ARG          
SEQRES   3 A  438  LEU LYS SER PRO VAL GLY ALA GLU PRO ALA VAL TYR PRO          
SEQRES   4 A  438  TRP PRO LEU PRO VAL TYR ASP LYS HIS HIS ASP ALA ALA          
SEQRES   5 A  438  HIS GLU ILE ILE GLU THR ILE ARG TRP VAL CYS GLU GLU          
SEQRES   6 A  438  ILE PRO ASP LEU LYS LEU ALA MET GLU ASN TYR VAL LEU          
SEQRES   7 A  438  ILE ASP TYR ASP THR LYS SER PHE GLU SER MET GLN ARG          
SEQRES   8 A  438  LEU CYS ASP LYS TYR ASN ARG ALA ILE ASP SER ILE HIS          
SEQRES   9 A  438  GLN LEU TRP LYS GLY THR THR GLN PRO MET LYS LEU ASN          
SEQRES  10 A  438  THR ARG PRO SER THR GLY LEU LEU ARG HIS ILE LEU GLN          
SEQRES  11 A  438  GLN VAL TYR ASN HIS SER VAL THR ASP PRO GLU LYS LEU          
SEQRES  12 A  438  ASN ASN TYR GLU PRO PHE SER PRO GLU VAL TYR GLY GLU          
SEQRES  13 A  438  THR SER PHE ASP LEU VAL ALA GLN MET ILE ASP GLU ILE          
SEQRES  14 A  438  LYS MET THR ASP ASP ASP LEU PHE VAL ASP LEU GLY SER          
SEQRES  15 A  438  GLY VAL GLY GLN VAL VAL LEU GLN VAL ALA ALA ALA THR          
SEQRES  16 A  438  ASN CYS LYS HIS HIS TYR GLY VAL GLU LYS ALA ASP ILE          
SEQRES  17 A  438  PRO ALA LYS TYR ALA GLU THR MET ASP ARG GLU PHE ARG          
SEQRES  18 A  438  LYS TRP MET LYS TRP TYR GLY LYS LYS HIS ALA GLU TYR          
SEQRES  19 A  438  THR LEU GLU ARG GLY ASP PHE LEU SER GLU GLU TRP ARG          
SEQRES  20 A  438  GLU ARG ILE ALA ASN THR SER VAL ILE PHE VAL ASN ASN          
SEQRES  21 A  438  PHE ALA PHE GLY PRO GLU VAL ASP HIS GLN LEU LYS GLU          
SEQRES  22 A  438  ARG PHE ALA ASN MET LYS GLU GLY GLY ARG ILE VAL SER          
SEQRES  23 A  438  SER LYS PRO PHE ALA PRO LEU ASN PHE ARG ILE ASN SER          
SEQRES  24 A  438  ARG ASN LEU SER ASP ILE GLY THR ILE MET ARG VAL VAL          
SEQRES  25 A  438  GLU LEU SER PRO LEU LYS GLY SER VAL SER TRP THR GLY          
SEQRES  26 A  438  LYS PRO VAL SER TYR TYR LEU HIS THR ILE ASP ARG THR          
SEQRES  27 A  438  ILE LEU GLU ASN TYR PHE SER SER LEU LYS ASN PRO LYS          
SEQRES  28 A  438  LEU ARG GLU GLU GLN GLU ALA ALA ARG ARG ARG GLN GLN          
SEQRES  29 A  438  ARG GLU SER LYS SER ASN ALA ALA THR PRO THR LYS GLY          
SEQRES  30 A  438  PRO GLU GLY LYS VAL ALA GLY PRO ALA ASP ALA PRO MET          
SEQRES  31 A  438  ASP SER GLY ALA GLU GLU GLU LYS ALA GLY ALA ALA THR          
SEQRES  32 A  438  VAL LYS LYS PRO SER PRO SER LYS ALA ARG LYS LYS LYS          
SEQRES  33 A  438  LEU ASN LYS LYS GLY ARG LYS MET ALA GLY ARG LYS ARG          
SEQRES  34 A  438  GLY ARG PRO LYS LYS MET ASN THR ALA                          
HET    5ID  A 421      20                                                       
HET    IOD  A 422       1                                                       
HET    IOD  A 423       1                                                       
HET     NA  A 424       1                                                       
HET    UNX  A 425       1                                                       
HET    UNX  A 426       1                                                       
HET    UNX  A 427       1                                                       
HET    UNX  A 428       1                                                       
HET    UNX  A 429       1                                                       
HET    UNX  A 430       1                                                       
HETNAM     5ID (2R,3R,4S,5R)-2-(4-AMINO-5-IODO-7H-PYRROLO[2,3-                  
HETNAM   2 5ID  D]PYRIMIDIN-7-YL)-5-(HYDROXYMETHYL)TETRAHYDROFURAN-3,           
HETNAM   3 5ID  4-DIOL                                                          
HETNAM     IOD IODIDE ION                                                       
HETNAM      NA SODIUM ION                                                       
HETNAM     UNX UNKNOWN ATOM OR ION                                              
HETSYN     5ID 5-IODOTUBERCIDIN                                                 
FORMUL   2  5ID    C11 H13 I N4 O4                                              
FORMUL   3  IOD    2(I 1-)                                                      
FORMUL   5   NA    NA 1+                                                        
FORMUL   6  UNX    6(X)                                                         
FORMUL  12  HOH   *66(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 GLU A   56  TYR A   63  5                                   8    
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 ASP A  121  LEU A  125  5                                   5    
HELIX    7   7 SER A  132  GLU A  138  5                                   7    
HELIX    8   8 THR A  139  LYS A  152  1                                  14    
HELIX    9   9 GLY A  167  THR A  177  1                                  11    
HELIX   10  10 ALA A  188  GLY A  210  1                                  23    
HELIX   11  11 SER A  225  ASN A  234  1                                  10    
HELIX   12  12 GLY A  246  ALA A  258  1                                  13    
HELIX   13  13 ASP A  286  THR A  289  5                                   4    
HELIX   14  14 ARG A  319  ASN A  331  1                                  13    
HELIX   15  15 ASN A  331  ARG A  343  1                                  13    
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 GLU A 215  ARG A 220  0                                        
SHEET    2   C 7 HIS A 181  GLU A 186  1  N  GLY A 184   O  GLU A 219           
SHEET    3   C 7 LEU A 158  LEU A 162  1  N  ASP A 161   O  TYR A 183           
SHEET    4   C 7 VAL A 237  VAL A 240  1  O  PHE A 239   N  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           
LINK         O   MET A  55                NA    NA A 424     1555   1555  2.33  
LINK        NA    NA A 424                 O   HOH A 481     1555   1555  2.34  
LINK         OD1 ASN A  57                NA    NA A 424     1555   1555  2.35  
LINK        NA    NA A 424                 O   HOH A 480     1555   1555  2.37  
LINK         O   LYS A  52                NA    NA A 424     1555   1555  2.57  
LINK         O   LEU A  53                NA    NA A 424     1555   1555  2.74  
CISPEP   1 TRP A   22    PRO A   23          0        -0.12                     
SITE     1 AC1 10 TYR A  58  GLU A 129  GLY A 163  GLU A 186                    
SITE     2 AC1 10 LYS A 187  GLY A 221  ASP A 222  PHE A 223                    
SITE     3 AC1 10 ASN A 241  IOD A 422                                          
SITE     1 AC2  1 5ID A 421                                                     
SITE     1 AC3  2 GLY A 246  VAL A 249                                          
SITE     1 AC4  6 LYS A  52  LEU A  53  MET A  55  ASN A  57                    
SITE     2 AC4  6 HOH A 480  HOH A 481                                          
CRYST1  149.784  149.784   53.521  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      0.006676  0.003855  0.000000        0.00000                         
SCALE2      0.000000  0.007709  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018684        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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