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Database: PDB
Entry: 5KJM
LinkDB: 5KJM
Original site: 5KJM 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       20-JUN-16   5KJM              
TITLE     SMYD2 IN COMPLEX WITH AZ931                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: N-LYSINE METHYLTRANSFERASE SMYD2;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HSKM-B,HISTONE METHYLTRANSFERASE SMYD2,LYSINE N-            
COMPND   5 METHYLTRANSFERASE 3C,SET AND MYND DOMAIN-CONTAINING PROTEIN 2;       
COMPND   6 EC: 2.1.1.-,2.1.1.43;                                                
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 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    TRANFERASE, HISTONE METHYLTRANSFERASE, INHIBITOR, TRANSFERASE-        
KEYWDS   2 TRANSFERASE INHIBITOR COMPLEX                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.FERGUSON                                                            
REVDAT   2   04-JAN-17 5KJM    1       JRNL                                     
REVDAT   1   07-DEC-16 5KJM    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.    2.19 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) : 2.19                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 78.02                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 32734                          
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)  : 0.178                          
REMARK   3   R VALUE            (WORKING SET)  : 0.176                          
REMARK   3   FREE R VALUE                      : 0.214                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.170                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1691                           
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               : 16                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.19                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.26                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 94.01                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2820                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2140                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2667                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2130                   
REMARK   3   BIN FREE R VALUE                        : 0.2360                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.43                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 153                      
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          : 72                                      
REMARK   3   SOLVENT ATOMS            : 276                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 43.59                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.27                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.54320                                              
REMARK   3    B22 (A**2) : 1.54320                                              
REMARK   3    B33 (A**2) : -3.08650                                             
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) : 0.250               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.186               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.161               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.179               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.159               
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      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.932                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3608   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 4868   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1288   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 92     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 525    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3608   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 1      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 445    ; 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   : 4331   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.10                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.25                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 19.51                    
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):  -51.4844   20.7418   -0.8980           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1710 T22:   -0.0794                                    
REMARK   3     T33:   -0.1372 T12:   -0.0656                                    
REMARK   3     T13:   -0.0121 T23:   -0.0798                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.0339 L22:    1.5432                                    
REMARK   3     L33:    1.0827 L12:    0.0073                                    
REMARK   3     L13:   -0.0757 L23:   -0.0609                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0410 S12:    0.0886 S13:   -0.0301                     
REMARK   3     S21:    0.0131 S22:   -0.1443 S23:    0.2003                     
REMARK   3     S31:   -0.1537 S32:    0.1108 S33:    0.1033                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5KJM 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_1000222360.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-SEP-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) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32761                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.190                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 78.020                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.06000                            
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) : 2.19                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
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   (%): 62.18                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.25                     
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       78.01650            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       78.01650            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       26.36750            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       78.01650            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       78.01650            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       26.36750            
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       78.01650            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       78.01650            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       26.36750            
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000       78.01650            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       78.01650            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       26.36750            
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      -74.99    -49.23                                   
REMARK 500    ASN A 101       41.96   -146.38                                   
REMARK 500    ASP A 284       81.04     66.51                                   
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 503  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  52   SG                                                     
REMARK 620 2 CYS A  55   SG  108.9                                              
REMARK 620 3 CYS A  74   SG  105.6  98.8                                        
REMARK 620 4 CYS A  78   SG  108.6 115.8 118.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 504  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  65   SG                                                     
REMARK 620 2 CYS A  68   SG  109.4                                              
REMARK 620 3 HIS A  86   NE2 111.6  98.6                                        
REMARK 620 4 CYS A  90   SG  109.9 120.1 106.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 505  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 209   SG                                                     
REMARK 620 2 CYS A 262   SG  114.5                                              
REMARK 620 3 CYS A 264   SG  110.4 102.2                                        
REMARK 620 4 CYS A 267   SG   96.8 118.2 115.1                                  
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 6TM A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 505                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5KJK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5KJL   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5KJN   RELATED DB: PDB                                   
DBREF  5KJM A    5   433  UNP    Q9NRG4   SMYD2_HUMAN      5    433             
SEQADV 5KJM 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    6TM  A 502      42                                                       
HET     ZN  A 503       1                                                       
HET     ZN  A 504       1                                                       
HET     ZN  A 505       1                                                       
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
HETNAM     6TM 6-[2-[4-[2-(3,4-DICHLOROPHENYL)ETHYL]PIPERAZIN-1-                
HETNAM   2 6TM  YL]PHENYL]-~{N}-(3-PYRROLIDIN-1-YLPROPYL)-2~{H}-                
HETNAM   3 6TM  PYRAZOLO[3,4-B]PYRIDINE-4-CARBOXAMIDE                           
HETNAM      ZN ZINC ION                                                         
HETSYN     6TM AZ931                                                            
FORMUL   2  SAM    C15 H22 N6 O5 S                                              
FORMUL   3  6TM    C32 H37 CL2 N7 O                                             
FORMUL   4   ZN    3(ZN 2+)                                                     
FORMUL   7  HOH   *276(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 ASP A  201  MET A  205  5                                   5    
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 503     1555   1555  2.35  
LINK         SG  CYS A  55                ZN    ZN A 503     1555   1555  2.39  
LINK         SG  CYS A  65                ZN    ZN A 504     1555   1555  2.45  
LINK         SG  CYS A  68                ZN    ZN A 504     1555   1555  2.16  
LINK         SG  CYS A  74                ZN    ZN A 503     1555   1555  2.44  
LINK         SG  CYS A  78                ZN    ZN A 503     1555   1555  2.26  
LINK         NE2 HIS A  86                ZN    ZN A 504     1555   1555  2.16  
LINK         SG  CYS A  90                ZN    ZN A 504     1555   1555  2.36  
LINK         SG  CYS A 209                ZN    ZN A 505     1555   1555  2.45  
LINK         SG  CYS A 262                ZN    ZN A 505     1555   1555  2.35  
LINK         SG  CYS A 264                ZN    ZN A 505     1555   1555  2.48  
LINK         SG  CYS A 267                ZN    ZN A 505     1555   1555  2.20  
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  6TM A 502                    
SITE     5 AC1 20 HOH A 616  HOH A 654  HOH A 659  HOH A 709                    
SITE     1 AC2 16 THR A 105  ILE A 149  VAL A 179  ASN A 180                    
SITE     2 AC2 16 CYS A 181  ASN A 182  GLY A 183  PHE A 184                    
SITE     3 AC2 16 THR A 185  TYR A 240  TYR A 258  SAM A 501                    
SITE     4 AC2 16 HOH A 617  HOH A 715  HOH A 737  HOH A 751                    
SITE     1 AC3  4 CYS A  52  CYS A  55  CYS A  74  CYS A  78                    
SITE     1 AC4  4 CYS A  65  CYS A  68  HIS A  86  CYS A  90                    
SITE     1 AC5  4 CYS A 209  CYS A 262  CYS A 264  CYS A 267                    
CRYST1  156.033  156.033   52.735  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      0.006409  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006409  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018963        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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