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Database: PDB
Entry: 5CCM
LinkDB: 5CCM
Original site: 5CCM 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       02-JUL-15   5CCM              
TITLE     CRYSTAL STRUCTURE OF SMYD3 WITH SAM AND EPZ030456                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SMYD3;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: SET AND MYND DOMAIN-CONTAINING PROTEIN 3,ZINC FINGER MYND   
COMPND   5 DOMAIN-CONTAINING PROTEIN 1;                                         
COMPND   6 EC: 2.1.1.43;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SMYD3, ZMYND1, ZNFN3A1;                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PROTEIN-INHIBITOR COMPLEX, METHYLTRANSFERASE, EPIGENETICS, DRUG       
KEYWDS   2 DISCOVERY, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.A.BORIACK-SJODIN                                                    
REVDAT   2   30-MAR-16 5CCM    1       JRNL                                     
REVDAT   1   09-SEP-15 5CCM    0                                                
JRNL        AUTH   L.H.MITCHELL,P.A.BORIACK-SJODIN,S.SMITH,M.THOMENIUS,N.RIOUX, 
JRNL        AUTH 2 M.MUNCHHOF,J.E.MILLS,C.KLAUS,J.TOTMAN,T.V.RIERA,A.RAIMONDI,  
JRNL        AUTH 3 S.L.JACQUES,K.WEST,M.FOLEY,N.J.WATERS,K.W.KUNTZ,T.J.WIGLE,   
JRNL        AUTH 4 M.P.SCOTT,R.A.COPELAND,J.J.SMITH,R.CHESWORTH                 
JRNL        TITL   NOVEL OXINDOLE SULFONAMIDES AND SULFAMIDES: EPZ031686, THE   
JRNL        TITL 2 FIRST ORALLY BIOAVAILABLE SMALL MOLECULE SMYD3 INHIBITOR.    
JRNL        REF    ACS MED.CHEM.LETT.            V.   7   134 2016              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   26985287                                                     
JRNL        DOI    10.1021/ACSMEDCHEMLETT.5B00272                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0073                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 18577                          
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) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 948                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.29                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.35                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1182                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.82                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2970                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 50                           
REMARK   3   BIN FREE R VALUE                    : 0.3530                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3384                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 69                                      
REMARK   3   SOLVENT ATOMS            : 123                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.06                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 6.20000                                              
REMARK   3    B22 (A**2) : -1.46000                                             
REMARK   3    B33 (A**2) : -4.74000                                             
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.432         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.263         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.210         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.939         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.908                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3540 ; 0.006 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3419 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4769 ; 1.211 ; 2.001       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7883 ; 0.772 ; 3.003       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   424 ; 5.781 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   162 ;34.538 ;24.074       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   658 ;14.376 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    27 ;15.938 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   519 ; 0.066 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3903 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   794 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1696 ; 1.442 ; 3.279       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1696 ; 1.442 ; 3.279       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2117 ; 2.454 ; 4.910       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 5CCM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUL-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000211373.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-FEB-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX300HS                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19568                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
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     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 5.100                              
REMARK 200  R MERGE                    (I) : 0.14600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.10 M MAGNESIUM FORMATE, 0.1M TRIS      
REMARK 280  8.0, 14% W/V PEG 3350, PH 8.0, VAPOR DIFFUSION, HANGING DROP,       
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
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       30.24200            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.67900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.92600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       53.67900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.24200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       32.92600            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     ARG A   426                                                      
REMARK 465     ALA A   427                                                      
REMARK 465     SER A   428                                                      
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    ASN A  13       21.43   -143.77                                   
REMARK 500    ARG A  14       44.01   -144.83                                   
REMARK 500    LYS A 271       -5.97     73.48                                   
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 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  49   SG                                                     
REMARK 620 2 CYS A  52   SG  103.0                                              
REMARK 620 3 CYS A  71   SG  117.0 108.8                                        
REMARK 620 4 CYS A  75   SG  112.8 112.7 102.7                                  
REMARK 620 N                    1     2     3                                   
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  62   SG                                                     
REMARK 620 2 CYS A  65   SG  106.7                                              
REMARK 620 3 HIS A  83   NE2 110.0 110.4                                        
REMARK 620 4 CYS A  87   SG  114.4 108.0 107.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 208   SG                                                     
REMARK 620 2 CYS A 261   SG  118.9                                              
REMARK 620 3 CYS A 263   SG  106.6 108.9                                        
REMARK 620 4 CYS A 266   SG   98.0 111.8 112.2                                  
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 ZN A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN 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 SAM A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 4ZX A 505                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5CCL   RELATED DB: PDB                                   
DBREF  5CCM A    1   428  UNP    Q9H7B4   SMYD3_HUMAN      1    428             
SEQADV 5CCM ASN A   13  UNP  Q9H7B4    LYS    13 CONFLICT                       
SEQRES   1 A  428  MET GLU PRO LEU LYS VAL GLU LYS PHE ALA THR ALA ASN          
SEQRES   2 A  428  ARG GLY ASN GLY LEU ARG ALA VAL THR PRO LEU ARG PRO          
SEQRES   3 A  428  GLY GLU LEU LEU PHE ARG SER ASP PRO LEU ALA TYR THR          
SEQRES   4 A  428  VAL CYS LYS GLY SER ARG GLY VAL VAL CYS ASP ARG CYS          
SEQRES   5 A  428  LEU LEU GLY LYS GLU LYS LEU MET ARG CYS SER GLN CYS          
SEQRES   6 A  428  ARG VAL ALA LYS TYR CYS SER ALA LYS CYS GLN LYS LYS          
SEQRES   7 A  428  ALA TRP PRO ASP HIS LYS ARG GLU CYS LYS CYS LEU LYS          
SEQRES   8 A  428  SER CYS LYS PRO ARG TYR PRO PRO ASP SER VAL ARG LEU          
SEQRES   9 A  428  LEU GLY ARG VAL VAL PHE LYS LEU MET ASP GLY ALA PRO          
SEQRES  10 A  428  SER GLU SER GLU LYS LEU TYR SER PHE TYR ASP LEU GLU          
SEQRES  11 A  428  SER ASN ILE ASN LYS LEU THR GLU ASP LYS LYS GLU GLY          
SEQRES  12 A  428  LEU ARG GLN LEU VAL MET THR PHE GLN HIS PHE MET ARG          
SEQRES  13 A  428  GLU GLU ILE GLN ASP ALA SER GLN LEU PRO PRO ALA PHE          
SEQRES  14 A  428  ASP LEU PHE GLU ALA PHE ALA LYS VAL ILE CYS ASN SER          
SEQRES  15 A  428  PHE THR ILE CYS ASN ALA GLU MET GLN GLU VAL GLY VAL          
SEQRES  16 A  428  GLY LEU TYR PRO SER ILE SER LEU LEU ASN HIS SER CYS          
SEQRES  17 A  428  ASP PRO ASN CYS SER ILE VAL PHE ASN GLY PRO HIS LEU          
SEQRES  18 A  428  LEU LEU ARG ALA VAL ARG ASP ILE GLU VAL GLY GLU GLU          
SEQRES  19 A  428  LEU THR ILE CYS TYR LEU ASP MET LEU MET THR SER GLU          
SEQRES  20 A  428  GLU ARG ARG LYS GLN LEU ARG ASP GLN TYR CYS PHE GLU          
SEQRES  21 A  428  CYS ASP CYS PHE ARG CYS GLN THR GLN ASP LYS ASP ALA          
SEQRES  22 A  428  ASP MET LEU THR GLY ASP GLU GLN VAL TRP LYS GLU VAL          
SEQRES  23 A  428  GLN GLU SER LEU LYS LYS ILE GLU GLU LEU LYS ALA HIS          
SEQRES  24 A  428  TRP LYS TRP GLU GLN VAL LEU ALA MET CYS GLN ALA ILE          
SEQRES  25 A  428  ILE SER SER ASN SER GLU ARG LEU PRO ASP ILE ASN ILE          
SEQRES  26 A  428  TYR GLN LEU LYS VAL LEU ASP CYS ALA MET ASP ALA CYS          
SEQRES  27 A  428  ILE ASN LEU GLY LEU LEU GLU GLU ALA LEU PHE TYR GLY          
SEQRES  28 A  428  THR ARG THR MET GLU PRO TYR ARG ILE PHE PHE PRO GLY          
SEQRES  29 A  428  SER HIS PRO VAL ARG GLY VAL GLN VAL MET LYS VAL GLY          
SEQRES  30 A  428  LYS LEU GLN LEU HIS GLN GLY MET PHE PRO GLN ALA MET          
SEQRES  31 A  428  LYS ASN LEU ARG LEU ALA PHE ASP ILE MET ARG VAL THR          
SEQRES  32 A  428  HIS GLY ARG GLU HIS SER LEU ILE GLU ASP LEU ILE LEU          
SEQRES  33 A  428  LEU LEU GLU GLU CYS ASP ALA ASN ILE ARG ALA SER              
HET     ZN  A 501       1                                                       
HET     ZN  A 502       1                                                       
HET     ZN  A 503       1                                                       
HET    SAM  A 504      27                                                       
HET    4ZX  A 505      39                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
HETNAM     4ZX 6-CHLORANYL-2-OXIDANYLIDENE-N-[(1S,5R)-8-[4-                     
HETNAM   2 4ZX  [(PHENYLMETHYL)AMINO]PIPERIDIN-1-YL]SULFONYL-8-                 
HETNAM   3 4ZX  AZABICYCLO[3.2.1]OCTAN-3-YL]-1,3-DIHYDROINDOLE-5-               
HETNAM   4 4ZX  CARBOXAMIDE                                                     
FORMUL   2   ZN    3(ZN 2+)                                                     
FORMUL   5  SAM    C15 H22 N6 O5 S                                              
FORMUL   6  4ZX    C28 H34 CL N5 O4 S                                           
FORMUL   7  HOH   *123(H2 O)                                                    
HELIX    1 AA1 SER A   72  LYS A   94  1                                  23    
HELIX    2 AA2 PRO A   99  GLY A  115  1                                  17    
HELIX    3 AA3 SER A  118  LYS A  122  5                                   5    
HELIX    4 AA4 SER A  125  LEU A  129  5                                   5    
HELIX    5 AA5 ASN A  132  LEU A  136  5                                   5    
HELIX    6 AA6 THR A  137  MET A  155  1                                  19    
HELIX    7 AA7 ASP A  161  LEU A  165  5                                   5    
HELIX    8 AA8 ASP A  170  ASN A  181  1                                  12    
HELIX    9 AA9 SER A  200  LEU A  204  5                                   5    
HELIX   10 AB1 THR A  245  CYS A  258  1                                  14    
HELIX   11 AB2 CYS A  263  GLN A  269  1                                   7    
HELIX   12 AB3 LYS A  271  LEU A  276  1                                   6    
HELIX   13 AB4 ASP A  279  HIS A  299  1                                  21    
HELIX   14 AB5 LYS A  301  SER A  314  1                                  14    
HELIX   15 AB6 ASN A  324  LEU A  341  1                                  18    
HELIX   16 AB7 LEU A  343  THR A  354  1                                  12    
HELIX   17 AB8 THR A  354  PHE A  362  1                                   9    
HELIX   18 AB9 HIS A  366  HIS A  382  1                                  17    
HELIX   19 AC1 MET A  385  HIS A  404  1                                  20    
HELIX   20 AC2 HIS A  408  ILE A  425  1                                  18    
SHEET    1 AA1 2 VAL A   6  ALA A  10  0                                        
SHEET    2 AA1 2 ASN A  16  ALA A  20 -1  O  GLY A  17   N  PHE A   9           
SHEET    1 AA2 3 LEU A  29  SER A  33  0                                        
SHEET    2 AA2 3 HIS A 220  ALA A 225 -1  O  LEU A 223   N  LEU A  30           
SHEET    3 AA2 3 CYS A 212  ASN A 217 -1  N  ASN A 217   O  HIS A 220           
SHEET    1 AA3 3 ALA A  37  VAL A  40  0                                        
SHEET    2 AA3 3 GLU A 192  LEU A 197 -1  O  VAL A 195   N  THR A  39           
SHEET    3 AA3 3 SER A 182  CYS A 186 -1  N  PHE A 183   O  GLY A 196           
SHEET    1 AA4 2 MET A  60  ARG A  61  0                                        
SHEET    2 AA4 2 LYS A  69  TYR A  70 -1  O  TYR A  70   N  MET A  60           
SHEET    1 AA5 2 ASN A 205  HIS A 206  0                                        
SHEET    2 AA5 2 THR A 236  ILE A 237  1  O  ILE A 237   N  ASN A 205           
LINK         SG  CYS A  49                ZN    ZN A 501     1555   1555  2.30  
LINK         SG  CYS A  52                ZN    ZN A 501     1555   1555  2.32  
LINK         SG  CYS A  62                ZN    ZN A 503     1555   1555  2.32  
LINK         SG  CYS A  65                ZN    ZN A 503     1555   1555  2.33  
LINK         SG  CYS A  71                ZN    ZN A 501     1555   1555  2.33  
LINK         SG  CYS A  75                ZN    ZN A 501     1555   1555  2.33  
LINK         NE2 HIS A  83                ZN    ZN A 503     1555   1555  2.08  
LINK         SG  CYS A  87                ZN    ZN A 503     1555   1555  2.32  
LINK         SG  CYS A 208                ZN    ZN A 502     1555   1555  2.34  
LINK         SG  CYS A 261                ZN    ZN A 502     1555   1555  2.33  
LINK         SG  CYS A 263                ZN    ZN A 502     1555   1555  2.31  
LINK         SG  CYS A 266                ZN    ZN A 502     1555   1555  2.33  
CISPEP   1 LYS A   94    PRO A   95          0         6.12                     
SITE     1 AC1  4 CYS A  49  CYS A  52  CYS A  71  CYS A  75                    
SITE     1 AC2  4 CYS A 208  CYS A 261  CYS A 263  CYS A 266                    
SITE     1 AC3  4 CYS A  62  CYS A  65  HIS A  83  CYS A  87                    
SITE     1 AC4 22 ARG A  14  GLY A  15  ASN A  16  TYR A 124                    
SITE     2 AC4 22 ASN A 132  ASN A 181  SER A 202  LEU A 203                    
SITE     3 AC4 22 LEU A 204  ASN A 205  HIS A 206  TYR A 239                    
SITE     4 AC4 22 TYR A 257  PHE A 259  4ZX A 505  HOH A 605                    
SITE     5 AC4 22 HOH A 644  HOH A 645  HOH A 659  HOH A 660                    
SITE     6 AC4 22 HOH A 669  HOH A 688                                          
SITE     1 AC5 23 CYS A 180  ASN A 181  SER A 182  PHE A 183                    
SITE     2 AC5 23 THR A 184  CYS A 186  MET A 190  GLU A 192                    
SITE     3 AC5 23 SER A 202  ILE A 214  ILE A 237  CYS A 238                    
SITE     4 AC5 23 TYR A 239  LEU A 240  ASP A 241  TYR A 257                    
SITE     5 AC5 23 GLU A 294  LYS A 329  ASP A 332  CYS A 333                    
SITE     6 AC5 23 VAL A 368  SAM A 504  HOH A 641                               
CRYST1   60.484   65.852  107.358  90.00  90.00  90.00 P 21 21 21    4          
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      0.016533  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015186  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009315        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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