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Database: PDB
Entry: 5KJK
LinkDB: 5KJK
Original site: 5KJK 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       20-JUN-16   5KJK              
TITLE     SMYD2 IN COMPLEX WITH AZ370                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: N-LYSINE METHYLTRANSFERASE SMYD2;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP;                                                       
COMPND   5 SYNONYM: HSKM-B,HISTONE METHYLTRANSFERASE SMYD2,LYSINE N-            
COMPND   6 METHYLTRANSFERASE 3C,SET AND MYND DOMAIN-CONTAINING PROTEIN 2;       
COMPND   7 EC: 2.1.1.-,2.1.1.43;                                                
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 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: SMYD2, KMT3C;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    SMYD2, HISTONE METHYLTRANSFERASE, INHIBITOR, TRANSFERASE,             
KEYWDS   2 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.FERGUSON                                                            
REVDAT   2   04-JAN-17 5KJK    1       JRNL                                     
REVDAT   1   07-DEC-16 5KJK    0                                                
JRNL        AUTH   S.D.COWEN,D.RUSSELL,L.A.DAKIN,H.CHEN,N.A.LARSEN,R.GODIN,     
JRNL        AUTH 2 S.THRONER,X.ZHENG,A.MOLINA,J.WU,T.CHEUNG,T.HOWARD,           
JRNL        AUTH 3 R.GARCIA-ARENAS,N.KEEN,C.S.PENDLETON,J.A.PIETENPOL,          
JRNL        AUTH 4 A.D.FERGUSON                                                 
JRNL        TITL   DESIGN, SYNTHESIS, AND BIOLOGICAL ACTIVITY OF SUBSTRATE      
JRNL        TITL 2 COMPETITIVE SMYD2 INHIBITORS.                                
JRNL        REF    J. MED. CHEM.                 V.  59 11079 2016              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   28002961                                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.93 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.7                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.93                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 110.21                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 45560                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.179                          
REMARK   3   R VALUE            (WORKING SET)  : 0.178                          
REMARK   3   FREE R VALUE                      : 0.203                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.040                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2296                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : 0.000                          
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.93                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.98                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 76.68                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2672                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2150                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2529                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2140                   
REMARK   3   BIN FREE R VALUE                        : 0.2340                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.35                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 143                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3453                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 92                                      
REMARK   3   SOLVENT ATOMS            : 340                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 35.95                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.28                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.97500                                              
REMARK   3    B22 (A**2) : 1.97500                                              
REMARK   3    B33 (A**2) : -3.95010                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.230               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.130               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.118               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.125               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.116               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.942                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3627   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 4891   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1306   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 92     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 550    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3627   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 2      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 454    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 4447   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.05                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.41                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 18.91                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -20.7642  -51.4861  -27.0105           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0683 T22:   -0.1335                                    
REMARK   3     T33:   -0.0936 T12:    0.0450                                    
REMARK   3     T13:    0.0946 T23:    0.0119                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.6662 L22:    0.9953                                    
REMARK   3     L33:    0.8475 L12:   -0.0925                                    
REMARK   3     L13:    0.1402 L23:    0.0131                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1262 S12:   -0.0449 S13:   -0.2592                     
REMARK   3     S21:   -0.0861 S22:    0.0421 S23:   -0.0356                     
REMARK   3     S31:   -0.0735 S32:   -0.0952 S33:    0.0840                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5KJK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000222358.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-DEC-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.976327                           
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 : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45560                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.930                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 77.930                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY                : 2.800                              
REMARK 200  R MERGE                    (I) : 0.04900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.93                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.03                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 3S7B                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.1 M TRIS-HCL, 5%         
REMARK 280  ETHANOL, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       8555   Y+1/2,-X+1/2,Z+1/2                                      
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 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  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       77.93250            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       77.93250            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       26.23850            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       77.93250            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       77.93250            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       26.23850            
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       77.93250            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       77.93250            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       26.23850            
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000       77.93250            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       77.93250            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       26.23850            
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 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    CYS A  90      -72.20    -54.04                                   
REMARK 500    ASN A 101       43.10   -143.69                                   
REMARK 500    VAL A 277       50.08   -107.66                                   
REMARK 500    TYR A 311      -15.28   -143.87                                   
REMARK 500    HIS A 397       68.78   -100.44                                   
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 A 507  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  52   SG                                                     
REMARK 620 2 CYS A  55   SG  108.1                                              
REMARK 620 3 CYS A  74   SG  104.1  97.6                                        
REMARK 620 4 CYS A  78   SG  111.0 118.5 116.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 508  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  65   SG                                                     
REMARK 620 2 CYS A  68   SG  111.5                                              
REMARK 620 3 HIS A  86   NE2 110.8 101.6                                        
REMARK 620 4 CYS A  90   SG  108.0 119.6 104.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 509  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 209   SG                                                     
REMARK 620 2 CYS A 262   SG  115.2                                              
REMARK 620 3 CYS A 264   SG  108.9 103.7                                        
REMARK 620 4 CYS A 267   SG   95.2 116.5 117.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BU3 A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BU3 A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BU3 A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BU3 A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6T1 A 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 507                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 508                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 509                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5KJL   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5KJM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5KJN   RELATED DB: PDB                                   
DBREF  5KJK A    5   433  UNP    Q9NRG4   SMYD2_HUMAN      5    433             
SEQADV 5KJK GLU A  165  UNP  Q9NRG4    GLY   165 ENGINEERED MUTATION            
SEQRES   1 A  429  GLY LEU GLY GLY LEU GLU ARG PHE CYS SER PRO GLY LYS          
SEQRES   2 A  429  GLY ARG GLY LEU ARG ALA LEU GLN PRO PHE GLN VAL GLY          
SEQRES   3 A  429  ASP LEU LEU PHE SER CYS PRO ALA TYR ALA TYR VAL LEU          
SEQRES   4 A  429  THR VAL ASN GLU ARG GLY ASN HIS CYS GLU TYR CYS PHE          
SEQRES   5 A  429  THR ARG LYS GLU GLY LEU SER LYS CYS GLY ARG CYS LYS          
SEQRES   6 A  429  GLN ALA PHE TYR CYS ASN VAL GLU CYS GLN LYS GLU ASP          
SEQRES   7 A  429  TRP PRO MET HIS LYS LEU GLU CYS SER PRO MET VAL VAL          
SEQRES   8 A  429  PHE GLY GLU ASN TRP ASN PRO SER GLU THR VAL ARG LEU          
SEQRES   9 A  429  THR ALA ARG ILE LEU ALA LYS GLN LYS ILE HIS PRO GLU          
SEQRES  10 A  429  ARG THR PRO SER GLU LYS LEU LEU ALA VAL LYS GLU PHE          
SEQRES  11 A  429  GLU SER HIS LEU ASP LYS LEU ASP ASN GLU LYS LYS ASP          
SEQRES  12 A  429  LEU ILE GLN SER ASP ILE ALA ALA LEU HIS HIS PHE TYR          
SEQRES  13 A  429  SER LYS HIS LEU GLU PHE PRO ASP ASN ASP SER LEU VAL          
SEQRES  14 A  429  VAL LEU PHE ALA GLN VAL ASN CYS ASN GLY PHE THR ILE          
SEQRES  15 A  429  GLU ASP GLU GLU LEU SER HIS LEU GLY SER ALA ILE PHE          
SEQRES  16 A  429  PRO ASP VAL ALA LEU MET ASN HIS SER CYS CYS PRO ASN          
SEQRES  17 A  429  VAL ILE VAL THR TYR LYS GLY THR LEU ALA GLU VAL ARG          
SEQRES  18 A  429  ALA VAL GLN GLU ILE LYS PRO GLY GLU GLU VAL PHE THR          
SEQRES  19 A  429  SER TYR ILE ASP LEU LEU TYR PRO THR GLU ASP ARG ASN          
SEQRES  20 A  429  ASP ARG LEU ARG ASP SER TYR PHE PHE THR CYS GLU CYS          
SEQRES  21 A  429  GLN GLU CYS THR THR LYS ASP LYS ASP LYS ALA LYS VAL          
SEQRES  22 A  429  GLU ILE ARG LYS LEU SER ASP PRO PRO LYS ALA GLU ALA          
SEQRES  23 A  429  ILE ARG ASP MET VAL ARG TYR ALA ARG ASN VAL ILE GLU          
SEQRES  24 A  429  GLU PHE ARG ARG ALA LYS HIS TYR LYS SER PRO SER GLU          
SEQRES  25 A  429  LEU LEU GLU ILE CYS GLU LEU SER GLN GLU LYS MET SER          
SEQRES  26 A  429  SER VAL PHE GLU ASP SER ASN VAL TYR MET LEU HIS MET          
SEQRES  27 A  429  MET TYR GLN ALA MET GLY VAL CYS LEU TYR MET GLN ASP          
SEQRES  28 A  429  TRP GLU GLY ALA LEU GLN TYR GLY GLN LYS ILE ILE LYS          
SEQRES  29 A  429  PRO TYR SER LYS HIS TYR PRO LEU TYR SER LEU ASN VAL          
SEQRES  30 A  429  ALA SER MET TRP LEU LYS LEU GLY ARG LEU TYR MET GLY          
SEQRES  31 A  429  LEU GLU HIS LYS ALA ALA GLY GLU LYS ALA LEU LYS LYS          
SEQRES  32 A  429  ALA ILE ALA ILE MET GLU VAL ALA HIS GLY LYS ASP HIS          
SEQRES  33 A  429  PRO TYR ILE SER GLU ILE LYS GLN GLU ILE GLU SER HIS          
HET    SAM  A 501      27                                                       
HET    BU3  A 502       6                                                       
HET    BU3  A 503       6                                                       
HET    BU3  A 504       6                                                       
HET    BU3  A 505       6                                                       
HET    6T1  A 506      38                                                       
HET     ZN  A 507       1                                                       
HET     ZN  A 508       1                                                       
HET     ZN  A 509       1                                                       
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
HETNAM     BU3 (R,R)-2,3-BUTANEDIOL                                             
HETNAM     6T1 2-[2-[1-[2-(3,4-DICHLOROPHENYL)ETHYL]AZETIDIN-3-                 
HETNAM   2 6T1  YL]OXYPHENYL]-~{N}-(3-PYRROLIDIN-1-YLPROPYL)PYRIDINE-           
HETNAM   3 6T1  4-CARBOXAMIDE                                                   
HETNAM      ZN ZINC ION                                                         
HETSYN     6T1 AZ13450370                                                       
FORMUL   2  SAM    C15 H22 N6 O5 S                                              
FORMUL   3  BU3    4(C4 H10 O2)                                                 
FORMUL   7  6T1    C30 H34 CL2 N4 O2                                            
FORMUL   8   ZN    3(ZN 2+)                                                     
FORMUL  11  HOH   *340(H2 O)                                                    
HELIX    1 AA1 VAL A   45  ARG A   48  5                                   4    
HELIX    2 AA2 ASN A   75  LYS A   87  1                                  13    
HELIX    3 AA3 GLU A   89  GLY A   97  1                                   9    
HELIX    4 AA4 GLU A   98  TRP A  100  5                                   3    
HELIX    5 AA5 SER A  103  HIS A  119  1                                  17    
HELIX    6 AA6 ALA A  130  PHE A  134  5                                   5    
HELIX    7 AA7 HIS A  137  LEU A  141  5                                   5    
HELIX    8 AA8 ASP A  142  SER A  161  1                                  20    
HELIX    9 AA9 ASP A  168  GLY A  183  1                                  16    
HELIX   10 AB1 PHE A  199  LEU A  204  1                                   6    
HELIX   11 AB2 PRO A  246  PHE A  259  1                                  14    
HELIX   12 AB3 CYS A  264  LYS A  270  1                                   7    
HELIX   13 AB4 LYS A  272  VAL A  277  1                                   6    
HELIX   14 AB5 LYS A  287  LYS A  309  1                                  23    
HELIX   15 AB6 SER A  313  SER A  329  1                                  17    
HELIX   16 AB7 ASN A  336  MET A  353  1                                  18    
HELIX   17 AB8 ASP A  355  TYR A  374  1                                  20    
HELIX   18 AB9 SER A  378  LEU A  395  1                                  18    
HELIX   19 AC1 HIS A  397  HIS A  416  1                                  20    
HELIX   20 AC2 HIS A  420  HIS A  433  1                                  14    
SHEET    1 AA1 2 LEU A   9  CYS A  13  0                                        
SHEET    2 AA1 2 ARG A  19  ALA A  23 -1  O  ARG A  22   N  GLU A  10           
SHEET    1 AA2 3 LEU A  32  PRO A  37  0                                        
SHEET    2 AA2 3 LEU A 221  ALA A 226 -1  O  VAL A 224   N  LEU A  33           
SHEET    3 AA2 3 VAL A 213  LYS A 218 -1  N  THR A 216   O  GLU A 223           
SHEET    1 AA3 3 ALA A  40  LEU A  43  0                                        
SHEET    2 AA3 3 HIS A 193  ILE A 198 -1  O  ILE A 198   N  ALA A  40           
SHEET    3 AA3 3 PHE A 184  GLU A 187 -1  N  ILE A 186   O  LEU A 194           
SHEET    1 AA4 2 SER A  63  LYS A  64  0                                        
SHEET    2 AA4 2 PHE A  72  TYR A  73 -1  O  TYR A  73   N  SER A  63           
SHEET    1 AA5 2 ASN A 206  HIS A 207  0                                        
SHEET    2 AA5 2 PHE A 237  THR A 238  1  O  THR A 238   N  ASN A 206           
LINK         SG  CYS A  52                ZN    ZN A 507     1555   1555  2.34  
LINK         SG  CYS A  55                ZN    ZN A 507     1555   1555  2.36  
LINK         SG  CYS A  65                ZN    ZN A 508     1555   1555  2.40  
LINK         SG  CYS A  68                ZN    ZN A 508     1555   1555  2.17  
LINK         SG  CYS A  74                ZN    ZN A 507     1555   1555  2.49  
LINK         SG  CYS A  78                ZN    ZN A 507     1555   1555  2.22  
LINK         NE2 HIS A  86                ZN    ZN A 508     1555   1555  2.18  
LINK         SG  CYS A  90                ZN    ZN A 508     1555   1555  2.36  
LINK         SG  CYS A 209                ZN    ZN A 509     1555   1555  2.44  
LINK         SG  CYS A 262                ZN    ZN A 509     1555   1555  2.35  
LINK         SG  CYS A 264                ZN    ZN A 509     1555   1555  2.39  
LINK         SG  CYS A 267                ZN    ZN A 509     1555   1555  2.17  
SITE     1 AC1 20 GLY A  16  LYS A  17  ARG A  19  GLU A 135                    
SITE     2 AC1 20 HIS A 137  LYS A 162  CYS A 181  ASN A 182                    
SITE     3 AC1 20 ALA A 203  LEU A 204  ASN A 206  HIS A 207                    
SITE     4 AC1 20 TYR A 240  TYR A 258  PHE A 260  6T1 A 506                    
SITE     5 AC1 20 HOH A 631  HOH A 644  HOH A 654  HOH A 814                    
SITE     1 AC2  8 ARG A  67  THR A 247  GLU A 248  ASN A 251                    
SITE     2 AC2  8 ARG A 255  THR A 261  LYS A 270  HOH A 618                    
SITE     1 AC3  2 TRP A 356  GLY A 394                                          
SITE     1 AC4  3 GLY A   5  ARG A 122  LYS A 127                               
SITE     1 AC5  3 ARG A  67  GLN A  79  TRP A  83                               
SITE     1 AC6 16 THR A 105  LYS A 145  ILE A 149  ASN A 180                    
SITE     2 AC6 16 CYS A 181  ASN A 182  GLY A 183  PHE A 184                    
SITE     3 AC6 16 THR A 185  TYR A 240  SER A 257  TYR A 258                    
SITE     4 AC6 16 SAM A 501  HOH A 727  HOH A 740  HOH A 773                    
SITE     1 AC7  4 CYS A  52  CYS A  55  CYS A  74  CYS A  78                    
SITE     1 AC8  4 CYS A  65  CYS A  68  HIS A  86  CYS A  90                    
SITE     1 AC9  4 CYS A 209  CYS A 262  CYS A 264  CYS A 267                    
CRYST1  155.865  155.865   52.477  90.00  90.00  90.00 I 4           8          
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      0.006416  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006416  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019056        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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