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Database: PDB
Entry: 3S7J
LinkDB: 3S7J
Original site: 3S7J 
HEADER    TRANSFERASE                             26-MAY-11   3S7J              
TITLE     STRUCTURAL BASIS OF SUBSTRATE METHYLATION AND INHIBITION OF SMYD2     
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                                                      
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    METHYLTRANSFERASE, P53, TRANSFERASE                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.D.FERGUSON                                                          
REVDAT   2   21-SEP-11 3S7J    1       JRNL                                     
REVDAT   1   10-AUG-11 3S7J    0                                                
JRNL        AUTH   A.D.FERGUSON,N.A.LARSEN,T.HOWARD,H.POLLARD,I.GREEN,C.GRANDE, 
JRNL        AUTH 2 T.CHEUNG,R.GARCIA-ARENAS,S.COWEN,J.WU,R.GODIN,H.CHEN,N.KEEN  
JRNL        TITL   STRUCTURAL BASIS OF SUBSTRATE METHYLATION AND INHIBITION OF  
JRNL        TITL 2 SMYD2.                                                       
JRNL        REF    STRUCTURE                     V.  19  1262 2011              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   21782458                                                     
JRNL        DOI    10.1016/J.STR.2011.06.011                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.04 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.9.3                                         
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) : 3.04                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.88                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 10997                          
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)  : 0.194                          
REMARK   3   R VALUE            (WORKING SET)  : 0.194                          
REMARK   3   FREE R VALUE                      : 0.210                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.820                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 584                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 6                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.04                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.33                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 98.15                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2683                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2340                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2551                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2329                   
REMARK   3   BIN FREE R VALUE                        : 0.2553                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.92                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 132                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3449                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 90.38                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 82.67                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.73370                                             
REMARK   3    B22 (A**2) : -2.73370                                             
REMARK   3    B33 (A**2) : 5.46730                                              
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) : 0.64                
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
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      : 0.921                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.915                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3557   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 4798   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1277   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 97     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 506    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3557   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 446    ; 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   : 3896   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.25                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.96                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 21.97                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION:   A    6    A  433                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   50.6261   20.5606   54.1704           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1747 T22:   -0.0184                                    
REMARK   3     T33:   -0.3120 T12:    0.2101                                    
REMARK   3     T13:    0.0350 T23:    0.1120                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.5641 L22:    3.3413                                    
REMARK   3     L33:    3.5957 L12:   -0.2207                                    
REMARK   3     L13:   -0.2967 L23:   -0.6199                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0590 S12:   -0.1316 S13:   -0.0285                     
REMARK   3     S21:    0.1548 S22:   -0.1499 S23:   -0.2708                     
REMARK   3     S31:   -0.6924 S32:   -0.4066 S33:    0.0909                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3S7J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUN-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB065859.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-DEC-08                          
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                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.2805                             
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12111                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.040                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 109.390                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 16.500                             
REMARK 200  R MERGE                    (I) : 0.10400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 25.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.04                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.34                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.30                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.50200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.19                     
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       77.28250            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       77.28250            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       26.59000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       77.28250            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       77.28250            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       26.59000            
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       77.28250            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       77.28250            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       26.59000            
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000       77.28250            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       77.28250            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       26.59000            
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     ARG A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     GLY A     5                                                      
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    LYS A  17       11.44   -146.05                                   
REMARK 500    CYS A  68      -20.97   -144.35                                   
REMARK 500    ASN A  75     -157.31   -153.70                                   
REMARK 500    ASN A 101       50.84   -144.85                                   
REMARK 500    HIS A 119       78.89   -118.03                                   
REMARK 500    ASP A 168     -140.05      8.52                                   
REMARK 500    ASN A 169     -128.81    -73.52                                   
REMARK 500    ASP A 170       66.52   -101.28                                   
REMARK 500    LYS A 218       79.78   -117.37                                   
REMARK 500    VAL A 277       58.12   -109.26                                   
REMARK 500    ASP A 284      106.28     79.17                                   
REMARK 500    LYS A 287      148.63    111.14                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    VAL A  94        24.8      L          L   OUTSIDE RANGE           
REMARK 500    VAL A 236        24.7      L          L   OUTSIDE RANGE           
REMARK 500    VAL A 337        24.8      L          L   OUTSIDE RANGE           
REMARK 500    ILE A 367        23.5      L          L   OUTSIDE RANGE           
REMARK 500    VAL A 381        23.5      L          L   OUTSIDE RANGE           
REMARK 500    GLU A 396        24.5      L          L   OUTSIDE RANGE           
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 434  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  52   SG                                                     
REMARK 620 2 CYS A  78   SG  106.5                                              
REMARK 620 3 CYS A  55   SG  109.8 124.6                                        
REMARK 620 4 CYS A  74   SG   96.1 125.5  90.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 435  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  86   NE2                                                    
REMARK 620 2 CYS A  90   SG  103.4                                              
REMARK 620 3 CYS A  68   SG   94.4 117.9                                        
REMARK 620 4 CYS A  65   SG  110.2 109.5 118.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 436  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 267   SG                                                     
REMARK 620 2 CYS A 209   SG   96.2                                              
REMARK 620 3 CYS A 264   SG  123.2 108.1                                        
REMARK 620 4 CYS A 262   SG  119.7 116.1  94.4                                  
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 1000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 434                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 435                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 436                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3S7B   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3S7D   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3S7F   RELATED DB: PDB                                   
DBREF  3S7J A    1   433  UNP    Q9NRG4   SMYD2_HUMAN      1    433             
SEQADV 3S7J GLU A  165  UNP  Q9NRG4    GLY   165 CONFLICT                       
SEQRES   1 A  433  MET ARG ALA GLU GLY LEU GLY GLY LEU GLU ARG PHE CYS          
SEQRES   2 A  433  SER PRO GLY LYS GLY ARG GLY LEU ARG ALA LEU GLN PRO          
SEQRES   3 A  433  PHE GLN VAL GLY ASP LEU LEU PHE SER CYS PRO ALA TYR          
SEQRES   4 A  433  ALA TYR VAL LEU THR VAL ASN GLU ARG GLY ASN HIS CYS          
SEQRES   5 A  433  GLU TYR CYS PHE THR ARG LYS GLU GLY LEU SER LYS CYS          
SEQRES   6 A  433  GLY ARG CYS LYS GLN ALA PHE TYR CYS ASN VAL GLU CYS          
SEQRES   7 A  433  GLN LYS GLU ASP TRP PRO MET HIS LYS LEU GLU CYS SER          
SEQRES   8 A  433  PRO MET VAL VAL PHE GLY GLU ASN TRP ASN PRO SER GLU          
SEQRES   9 A  433  THR VAL ARG LEU THR ALA ARG ILE LEU ALA LYS GLN LYS          
SEQRES  10 A  433  ILE HIS PRO GLU ARG THR PRO SER GLU LYS LEU LEU ALA          
SEQRES  11 A  433  VAL LYS GLU PHE GLU SER HIS LEU ASP LYS LEU ASP ASN          
SEQRES  12 A  433  GLU LYS LYS ASP LEU ILE GLN SER ASP ILE ALA ALA LEU          
SEQRES  13 A  433  HIS HIS PHE TYR SER LYS HIS LEU GLU PHE PRO ASP ASN          
SEQRES  14 A  433  ASP SER LEU VAL VAL LEU PHE ALA GLN VAL ASN CYS ASN          
SEQRES  15 A  433  GLY PHE THR ILE GLU ASP GLU GLU LEU SER HIS LEU GLY          
SEQRES  16 A  433  SER ALA ILE PHE PRO ASP VAL ALA LEU MET ASN HIS SER          
SEQRES  17 A  433  CYS CYS PRO ASN VAL ILE VAL THR TYR LYS GLY THR LEU          
SEQRES  18 A  433  ALA GLU VAL ARG ALA VAL GLN GLU ILE LYS PRO GLY GLU          
SEQRES  19 A  433  GLU VAL PHE THR SER TYR ILE ASP LEU LEU TYR PRO THR          
SEQRES  20 A  433  GLU ASP ARG ASN ASP ARG LEU ARG ASP SER TYR PHE PHE          
SEQRES  21 A  433  THR CYS GLU CYS GLN GLU CYS THR THR LYS ASP LYS ASP          
SEQRES  22 A  433  LYS ALA LYS VAL GLU ILE ARG LYS LEU SER ASP PRO PRO          
SEQRES  23 A  433  LYS ALA GLU ALA ILE ARG ASP MET VAL ARG TYR ALA ARG          
SEQRES  24 A  433  ASN VAL ILE GLU GLU PHE ARG ARG ALA LYS HIS TYR LYS          
SEQRES  25 A  433  SER PRO SER GLU LEU LEU GLU ILE CYS GLU LEU SER GLN          
SEQRES  26 A  433  GLU LYS MET SER SER VAL PHE GLU ASP SER ASN VAL TYR          
SEQRES  27 A  433  MET LEU HIS MET MET TYR GLN ALA MET GLY VAL CYS LEU          
SEQRES  28 A  433  TYR MET GLN ASP TRP GLU GLY ALA LEU GLN TYR GLY GLN          
SEQRES  29 A  433  LYS ILE ILE LYS PRO TYR SER LYS HIS TYR PRO LEU TYR          
SEQRES  30 A  433  SER LEU ASN VAL ALA SER MET TRP LEU LYS LEU GLY ARG          
SEQRES  31 A  433  LEU TYR MET GLY LEU GLU HIS LYS ALA ALA GLY GLU LYS          
SEQRES  32 A  433  ALA LEU LYS LYS ALA ILE ALA ILE MET GLU VAL ALA HIS          
SEQRES  33 A  433  GLY LYS ASP HIS PRO TYR ILE SER GLU ILE LYS GLN GLU          
SEQRES  34 A  433  ILE GLU SER HIS                                              
HET    SAM  A1000      27                                                       
HET     ZN  A 434       1                                                       
HET     ZN  A 435       1                                                       
HET     ZN  A 436       1                                                       
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
HETNAM      ZN ZINC ION                                                         
FORMUL   2  SAM    C15 H22 N6 O5 S                                              
FORMUL   3   ZN    3(ZN 2+)                                                     
HELIX    1   1 VAL A   45  ARG A   48  5                                   4    
HELIX    2   2 ASN A   75  GLY A   97  1                                  23    
HELIX    3   3 GLU A   98  TRP A  100  5                                   3    
HELIX    4   4 SER A  103  HIS A  119  1                                  17    
HELIX    5   5 HIS A  137  LEU A  141  5                                   5    
HELIX    6   6 ASP A  142  SER A  161  1                                  20    
HELIX    7   7 SER A  171  GLY A  183  1                                  13    
HELIX    8   8 ASP A  201  MET A  205  5                                   5    
HELIX    9   9 PRO A  246  PHE A  259  1                                  14    
HELIX   10  10 CYS A  264  LYS A  270  1                                   7    
HELIX   11  11 LYS A  272  VAL A  277  1                                   6    
HELIX   12  12 LYS A  287  LYS A  309  1                                  23    
HELIX   13  13 SER A  313  SER A  330  1                                  18    
HELIX   14  14 ASN A  336  MET A  353  1                                  18    
HELIX   15  15 ASP A  355  TYR A  374  1                                  20    
HELIX   16  16 SER A  378  LEU A  395  1                                  18    
HELIX   17  17 HIS A  397  HIS A  416  1                                  20    
HELIX   18  18 HIS A  420  HIS A  433  1                                  14    
SHEET    1   A 4 LEU A   9  CYS A  13  0                                        
SHEET    2   A 4 ARG A  19  ALA A  23 -1  O  ARG A  22   N  GLU A  10           
SHEET    3   A 4 GLU A 235  THR A 238 -1  O  VAL A 236   N  LEU A  21           
SHEET    4   A 4 ASN A 206  HIS A 207  1  N  ASN A 206   O  THR A 238           
SHEET    1   B 3 LEU A  32  PRO A  37  0                                        
SHEET    2   B 3 LEU A 221  ALA A 226 -1  O  VAL A 224   N  LEU A  33           
SHEET    3   B 3 VAL A 213  LYS A 218 -1  N  THR A 216   O  GLU A 223           
SHEET    1   C 3 ALA A  40  LEU A  43  0                                        
SHEET    2   C 3 HIS A 193  ILE A 198 -1  O  ILE A 198   N  ALA A  40           
SHEET    3   C 3 PHE A 184  GLU A 187 -1  N  ILE A 186   O  LEU A 194           
SHEET    1   D 2 SER A  63  LYS A  64  0                                        
SHEET    2   D 2 PHE A  72  TYR A  73 -1  O  TYR A  73   N  SER A  63           
LINK         SG  CYS A  52                ZN    ZN A 434     1555   1555  2.26  
LINK         NE2 HIS A  86                ZN    ZN A 435     1555   1555  2.30  
LINK         SG  CYS A  90                ZN    ZN A 435     1555   1555  2.32  
LINK         SG  CYS A 267                ZN    ZN A 436     1555   1555  2.33  
LINK         SG  CYS A  68                ZN    ZN A 435     1555   1555  2.33  
LINK         SG  CYS A  78                ZN    ZN A 434     1555   1555  2.35  
LINK         SG  CYS A 209                ZN    ZN A 436     1555   1555  2.35  
LINK         SG  CYS A  55                ZN    ZN A 434     1555   1555  2.40  
LINK         SG  CYS A 264                ZN    ZN A 436     1555   1555  2.41  
LINK         SG  CYS A 262                ZN    ZN A 436     1555   1555  2.54  
LINK         SG  CYS A  65                ZN    ZN A 435     1555   1555  2.59  
LINK         SG  CYS A  74                ZN    ZN A 434     1555   1555  2.63  
SITE     1 AC1 16 GLY A  16  LYS A  17  ARG A  19  GLU A 135                    
SITE     2 AC1 16 HIS A 137  LYS A 162  CYS A 181  ASN A 182                    
SITE     3 AC1 16 ALA A 203  LEU A 204  MET A 205  ASN A 206                    
SITE     4 AC1 16 HIS A 207  TYR A 240  TYR A 258  PHE A 260                    
SITE     1 AC2  4 CYS A  52  CYS A  55  CYS A  74  CYS A  78                    
SITE     1 AC3  4 CYS A  65  CYS A  68  HIS A  86  CYS A  90                    
SITE     1 AC4  4 CYS A 209  CYS A 262  CYS A 264  CYS A 267                    
CRYST1  154.565  154.565   53.180  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      0.006470  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006470  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018804        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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