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Entry: 5F5E
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HEADER    TRANSFERASE                             04-DEC-15   5F5E              
TITLE     THE CRYSTAL STRUCTURE OF MLL1 SET DOMAIN WITH N3816I/Q3867L MUTATION  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE 2A;                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: MLL1 SET DOMAIN (UNP RESIDUES 3813-3969);                  
COMPND   5 SYNONYM: LYSINE N-METHYLTRANSFERASE 2A,ALL-1,CXXC-TYPE ZINC FINGER   
COMPND   6 PROTEIN 7,MYELOID/LYMPHOID OR MIXED-LINEAGE LEUKEMIA,MYELOID/LYMPHOID
COMPND   7 OR MIXED-LINEAGE LEUKEMIA PROTEIN 1,TRITHORAX-LIKE PROTEIN,ZINC      
COMPND   8 FINGER PROTEIN HRX;                                                  
COMPND   9 EC: 2.1.1.43;                                                        
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: KMT2A, ALL1, CXXC7, HRX, HTRX, MLL, MLL1, TRX1;                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA;                                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28B-SUMO                               
KEYWDS    HISTONE METHYLTRANSFERASE, HISTONE METHYLATION, SET DOMAIN,           
KEYWDS   2 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.LI,M.LEI,Y.CHEN                                                     
REVDAT   2   20-APR-16 5F5E    1       JRNL                                     
REVDAT   1   24-FEB-16 5F5E    0                                                
JRNL        AUTH   Y.LI,J.HAN,Y.ZHANG,F.CAO,Z.LIU,S.LI,J.WU,C.HU,Y.WANG,        
JRNL        AUTH 2 J.SHUAI,J.CHEN,L.CAO,D.LI,P.SHI,C.TIAN,J.ZHANG,Y.DOU,G.LI,   
JRNL        AUTH 3 Y.CHEN,M.LEI                                                 
JRNL        TITL   STRUCTURAL BASIS FOR ACTIVITY REGULATION OF MLL FAMILY       
JRNL        TITL 2 METHYLTRANSFERASES.                                          
JRNL        REF    NATURE                        V. 530   447 2016              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   26886794                                                     
JRNL        DOI    10.1038/NATURE16952                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.07                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 17284                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 875                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 28.0709 -  3.2726    1.00     2881   151  0.1750 0.2154        
REMARK   3     2  3.2726 -  2.5982    1.00     2768   127  0.2180 0.2272        
REMARK   3     3  2.5982 -  2.2699    1.00     2700   163  0.2259 0.2748        
REMARK   3     4  2.2699 -  2.0625    1.00     2703   142  0.2209 0.2543        
REMARK   3     5  2.0625 -  1.9147    1.00     2698   141  0.2275 0.2649        
REMARK   3     6  1.9147 -  1.8018    1.00     2659   151  0.2539 0.2781        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.330           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.14                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.011           1211                                  
REMARK   3   ANGLE     :  1.105           1624                                  
REMARK   3   CHIRALITY :  0.051            174                                  
REMARK   3   PLANARITY :  0.004            206                                  
REMARK   3   DIHEDRAL  : 15.228            452                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 3814 THROUGH 3822 )               
REMARK   3    ORIGIN FOR THE GROUP (A): -15.3151 328.7671 212.2872              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2840 T22:   0.5649                                     
REMARK   3      T33:   1.1565 T12:   0.0080                                     
REMARK   3      T13:  -0.5869 T23:   0.0885                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6434 L22:   1.3364                                     
REMARK   3      L33:   6.4793 L12:  -1.3597                                     
REMARK   3      L13:   1.5188 L23:  -2.2907                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3180 S12:   0.6715 S13:   0.3783                       
REMARK   3      S21:  -1.8989 S22:   0.2644 S23:   2.2333                       
REMARK   3      S31:  -0.8614 S32:  -0.7614 S33:  -0.0993                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 3823 THROUGH 3835 )               
REMARK   3    ORIGIN FOR THE GROUP (A): -17.8005 313.2893 219.1648              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3347 T22:   0.3442                                     
REMARK   3      T33:   0.3200 T12:  -0.0845                                     
REMARK   3      T13:   0.0078 T23:   0.0103                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8684 L22:   8.8325                                     
REMARK   3      L33:   4.5199 L12:  -3.5307                                     
REMARK   3      L13:   1.4197 L23:  -0.4670                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2329 S12:  -0.2525 S13:   0.1360                       
REMARK   3      S21:   0.2900 S22:   0.0752 S23:   0.3980                       
REMARK   3      S31:  -0.2499 S32:  -0.3760 S33:   0.1493                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 3836 THROUGH 3860 )               
REMARK   3    ORIGIN FOR THE GROUP (A): -11.9610 311.9052 215.1910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4077 T22:   0.2729                                     
REMARK   3      T33:   0.2132 T12:  -0.1365                                     
REMARK   3      T13:  -0.0118 T23:   0.0056                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9695 L22:   1.2829                                     
REMARK   3      L33:   2.9928 L12:   1.5698                                     
REMARK   3      L13:   0.3650 L23:   0.2424                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5514 S12:   0.3715 S13:  -0.1375                       
REMARK   3      S21:  -0.6242 S22:   0.6017 S23:  -0.0558                       
REMARK   3      S31:  -0.1638 S32:  -0.0845 S33:   0.0063                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 3861 THROUGH 3878 )               
REMARK   3    ORIGIN FOR THE GROUP (A):   4.9034 317.5244 232.8142              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3556 T22:   0.2545                                     
REMARK   3      T33:   0.2328 T12:   0.0296                                     
REMARK   3      T13:  -0.0619 T23:  -0.0749                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.7322 L22:   8.0034                                     
REMARK   3      L33:   8.7927 L12:  -2.4319                                     
REMARK   3      L13:   0.9306 L23:  -4.4220                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3596 S12:  -0.2560 S13:   0.0234                       
REMARK   3      S21:   0.3775 S22:   0.1002 S23:  -0.4897                       
REMARK   3      S31:  -0.0297 S32:   0.6427 S33:   0.2138                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 3879 THROUGH 3912 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.9263 314.9281 222.4577              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2697 T22:   0.1903                                     
REMARK   3      T33:   0.2284 T12:  -0.0541                                     
REMARK   3      T13:   0.0619 T23:  -0.0214                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6786 L22:   3.2142                                     
REMARK   3      L33:   4.2884 L12:   0.2741                                     
REMARK   3      L13:   1.3352 L23:   0.2282                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3923 S12:   0.3829 S13:  -0.2541                       
REMARK   3      S21:  -0.2417 S22:   0.3238 S23:  -0.4369                       
REMARK   3      S31:   0.0428 S32:   0.2201 S33:   0.0551                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 3913 THROUGH 3958 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.1576 315.9488 212.7101              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5693 T22:   0.3602                                     
REMARK   3      T33:   0.2561 T12:  -0.2745                                     
REMARK   3      T13:   0.0496 T23:  -0.0552                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5899 L22:   2.6944                                     
REMARK   3      L33:   3.0401 L12:   1.1229                                     
REMARK   3      L13:   0.5683 L23:   0.5165                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6958 S12:   0.4861 S13:  -0.2308                       
REMARK   3      S21:  -0.8020 S22:   0.7023 S23:  -0.3564                       
REMARK   3      S31:  -0.2649 S32:   0.4023 S33:  -0.0757                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 3959 THROUGH 3969 )               
REMARK   3    ORIGIN FOR THE GROUP (A):   4.8827 302.7535 210.2720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6366 T22:   0.7787                                     
REMARK   3      T33:   0.8337 T12:  -0.1199                                     
REMARK   3      T13:   0.3087 T23:  -0.5085                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8110 L22:   2.6291                                     
REMARK   3      L33:   3.5349 L12:  -0.8717                                     
REMARK   3      L13:  -2.9611 L23:  -1.1750                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5201 S12:   0.0358 S13:   0.1106                       
REMARK   3      S21:  -0.3971 S22:  -0.0753 S23:  -0.3122                       
REMARK   3      S31:  -0.6828 S32:   0.6073 S33:  -2.1253                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5F5E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-DEC-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000216052.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-JUN-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL19U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9785                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17325                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 9.600                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.83                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42100                            
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.5.1                                          
REMARK 200 STARTING MODEL: 2W5Y                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 35% TACSIMATE, PH 7.0, VAPOR             
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
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   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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       69.77067            
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       34.88533            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       34.88533            
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       69.77067            
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 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     SER A  3812                                                      
REMARK 465     ASP A  3813                                                      
REMARK 465     PHE A  3946                                                      
REMARK 465     PRO A  3947                                                      
REMARK 465     ILE A  3948                                                      
REMARK 465     GLU A  3949                                                      
REMARK 465     ASP A  3950                                                      
REMARK 465     ALA A  3951                                                      
REMARK 465     SER A  3952                                                      
REMARK 465     ASN A  3953                                                      
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     MET A3818    SD   CE                                             
REMARK 470     ARG A3821    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A3828    CG   CD   CE   NZ                                   
REMARK 470     ASP A3889    CG   OD1  OD2                                       
REMARK 470     GLU A3910    CG   CD   OE1  OE2                                  
REMARK 470     ASP A3921    CG   OD1  OD2                                       
REMARK 470     LYS A3945    CG   CD   CE   NZ                                   
REMARK 470     LYS A3954    CG   CD   CE   NZ                                   
REMARK 470     LEU A3955    CG   CD1  CD2                                       
REMARK 470     LYS A3963    CG   CD   CE   NZ                                   
REMARK 470     LYS A3966    CG   CD   CE   NZ                                   
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   O    HOH A  4199     O    HOH A  4237              1.89            
REMARK 500   O    HOH A  4102     O    HOH A  4108              1.93            
REMARK 500   OD2  ASP A  3869     O    HOH A  4101              2.12            
REMARK 500   O    HOH A  4197     O    HOH A  4221              2.13            
REMARK 500   NH2  ARG A  3871     O    HOH A  4102              2.14            
REMARK 500   O    HOH A  4174     O    HOH A  4218              2.17            
REMARK 500   O    ILE A  3838     O    HOH A  4103              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 A3888     -156.97   -160.73                                   
REMARK 500    LYS A3966      -16.85     67.30                                   
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                              ZN A4001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A3909   SG                                                     
REMARK 620 2 CYS A3957   SG   99.4                                              
REMARK 620 3 CYS A3959   SG   82.7  97.6                                        
REMARK 620 4 CYS A3964   SG   82.8 174.2  87.9                                  
REMARK 620 5 HOH A4109   O   126.7 119.8 121.9  55.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 4001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH A 4002                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5F59   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5F6L   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5F6K   RELATED DB: PDB                                   
DBREF  5F5E A 3813  3969  UNP    Q03164   KMT2A_HUMAN   3813   3969             
SEQADV 5F5E SER A 3812  UNP  Q03164              EXPRESSION TAG                 
SEQADV 5F5E ILE A 3861  UNP  Q03164    ASN  3861 ENGINEERED MUTATION            
SEQADV 5F5E LEU A 3867  UNP  Q03164    GLN  3867 ENGINEERED MUTATION            
SEQRES   1 A  158  SER ASP LEU PRO MET PRO MET ARG PHE ARG HIS LEU LYS          
SEQRES   2 A  158  LYS THR SER LYS GLU ALA VAL GLY VAL TYR ARG SER PRO          
SEQRES   3 A  158  ILE HIS GLY ARG GLY LEU PHE CYS LYS ARG ASN ILE ASP          
SEQRES   4 A  158  ALA GLY GLU MET VAL ILE GLU TYR ALA GLY ILE VAL ILE          
SEQRES   5 A  158  ARG SER ILE LEU THR ASP LYS ARG GLU LYS TYR TYR ASP          
SEQRES   6 A  158  SER LYS GLY ILE GLY CYS TYR MET PHE ARG ILE ASP ASP          
SEQRES   7 A  158  SER GLU VAL VAL ASP ALA THR MET HIS GLY ASN ALA ALA          
SEQRES   8 A  158  ARG PHE ILE ASN HIS SER CYS GLU PRO ASN CYS TYR SER          
SEQRES   9 A  158  ARG VAL ILE ASN ILE ASP GLY GLN LYS HIS ILE VAL ILE          
SEQRES  10 A  158  PHE ALA MET ARG LYS ILE TYR ARG GLY GLU GLU LEU THR          
SEQRES  11 A  158  TYR ASP TYR LYS PHE PRO ILE GLU ASP ALA SER ASN LYS          
SEQRES  12 A  158  LEU PRO CYS ASN CYS GLY ALA LYS LYS CYS ARG LYS PHE          
SEQRES  13 A  158  LEU ASN                                                      
HET     ZN  A4001       1                                                       
HET    SAH  A4002      26                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  SAH    C14 H20 N6 O5 S                                              
FORMUL   4  HOH   *142(H2 O)                                                    
HELIX    1 AA1 PRO A 3815  ARG A 3821  1                                   7    
HELIX    2 AA2 HIS A 3822  ALA A 3830  1                                   9    
HELIX    3 AA3 LEU A 3867  LYS A 3878  1                                  12    
HELIX    4 AA4 ASN A 3900  ILE A 3905  5                                   6    
SHEET    1 AA1 4 VAL A3831  ARG A3835  0                                        
SHEET    2 AA1 4 ARG A3841  CYS A3845 -1  O  PHE A3844   N  GLY A3832           
SHEET    3 AA1 4 GLU A3939  TYR A3942 -1  O  LEU A3940   N  LEU A3843           
SHEET    4 AA1 4 ASN A3906  HIS A3907  1  N  ASN A3906   O  TYR A3942           
SHEET    1 AA2 3 MET A3854  GLU A3857  0                                        
SHEET    2 AA2 3 GLN A3923  ALA A3930 -1  O  ILE A3928   N  VAL A3855           
SHEET    3 AA2 3 CYS A3913  ILE A3920 -1  N  ILE A3918   O  HIS A3925           
SHEET    1 AA3 3 ILE A3861  ARG A3864  0                                        
SHEET    2 AA3 3 GLU A3891  ASP A3894 -1  O  VAL A3892   N  ILE A3863           
SHEET    3 AA3 3 MET A3884  ARG A3886 -1  N  PHE A3885   O  VAL A3893           
LINK         SG  CYS A3909                ZN    ZN A4001     1555   1555  2.39  
LINK         SG  CYS A3957                ZN    ZN A4001     1555   1555  2.12  
LINK         SG  CYS A3959                ZN    ZN A4001     1555   1555  2.50  
LINK         SG  CYS A3964                ZN    ZN A4001     1555   1555  2.26  
LINK        ZN    ZN A4001                 O   HOH A4109     1555   1555  2.68  
SITE     1 AC1  5 CYS A3909  CYS A3957  CYS A3959  CYS A3964                    
SITE     2 AC1  5 HOH A4109                                                     
SITE     1 AC2 18 ILE A3838  HIS A3839  GLY A3840  ARG A3841                    
SITE     2 AC2 18 TYR A3883  ARG A3903  PHE A3904  ASN A3906                    
SITE     3 AC2 18 HIS A3907  TYR A3944  PRO A3956  CYS A3957                    
SITE     4 AC2 18 ASN A3958  HOH A4122  HOH A4135  HOH A4149                    
SITE     5 AC2 18 HOH A4169  HOH A4187                                          
CRYST1   54.574   54.574  104.656  90.00  90.00 120.00 P 32 2 1      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      0.018324  0.010579  0.000000        0.00000                         
SCALE2      0.000000  0.021158  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009555        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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