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Database: PDB
Entry: 3S7B
LinkDB: 3S7B
Original site: 3S7B 
HEADER    TRANSFERASE                             26-MAY-11   3S7B              
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, TRANSFERASE                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.D.FERGUSON                                                          
REVDAT   2   21-SEP-11 3S7B    1       JRNL                                     
REVDAT   1   10-AUG-11 3S7B    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.    2.42 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.9.7                                         
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) : 2.42                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 55.10                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 24402                          
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)  : 0.175                          
REMARK   3   R VALUE            (WORKING SET)  : 0.174                          
REMARK   3   FREE R VALUE                      : 0.198                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.090                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1243                           
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               : 12                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.42                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.53                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.58                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2932                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2012                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2778                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.1995                   
REMARK   3   BIN FREE R VALUE                        : 0.2326                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.25                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 154                      
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            : 3454                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 99                                      
REMARK   3   SOLVENT ATOMS            : 160                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 49.71                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.81                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.26970                                              
REMARK   3    B22 (A**2) : 2.26970                                              
REMARK   3    B33 (A**2) : -4.53940                                             
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) : 0.32                
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) : 0.26                
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      : 0.947                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.935                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3629   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 4891   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1291   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 93     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 511    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3629   ; 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   : 450    ; 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   : 4174   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.12                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.20                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 19.13                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION:   A    5    A  433                                     
REMARK   3    ORIGIN FOR THE GROUP (A):  -20.9207  -51.5192   -0.7973           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0805 T22:   -0.1711                                    
REMARK   3     T33:   -0.1573 T12:    0.0512                                    
REMARK   3     T13:    0.1124 T23:    0.0056                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.3038 L22:    1.4068                                    
REMARK   3     L33:    1.2801 L12:    0.1006                                    
REMARK   3     L13:   -0.0481 L23:   -0.1453                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1634 S12:   -0.0104 S13:   -0.3388                     
REMARK   3     S21:   -0.0698 S22:    0.0181 S23:   -0.0542                     
REMARK   3     S31:   -0.0187 S32:   -0.1237 S33:    0.1453                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3S7B 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 RCSB065851.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-APR-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                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0723                             
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   : 24403                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.420                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 55.100                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.42                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.55                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.79                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.22                     
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       77.93000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       77.93000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       26.41500            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       77.93000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       77.93000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       26.41500            
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       77.93000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       77.93000            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       26.41500            
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000       77.93000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       77.93000            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       26.41500            
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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    CYS A  90      -72.89    -49.16                                   
REMARK 500    ASN A 101       44.57   -144.15                                   
REMARK 500    VAL A 277       49.35   -107.87                                   
REMARK 500    TYR A 311      -17.46   -142.06                                   
REMARK 500    HIS A 397       68.20   -100.28                                   
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        23.0      L          L   OUTSIDE RANGE           
REMARK 500    VAL A 337        24.9      L          L   OUTSIDE RANGE           
REMARK 500    ILE A 367        23.3      L          L   OUTSIDE RANGE           
REMARK 500    LYS A 398        24.9      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 441  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  86   NE2                                                    
REMARK 620 2 CYS A  68   SG  100.4                                              
REMARK 620 3 CYS A  90   SG  106.0 117.1                                        
REMARK 620 4 CYS A  65   SG  113.4 110.6 109.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 442  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 262   SG                                                     
REMARK 620 2 CYS A 267   SG  116.2                                              
REMARK 620 3 CYS A 264   SG  107.4 113.3                                        
REMARK 620 4 CYS A 209   SG  117.5  92.2 109.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 440  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  78   SG                                                     
REMARK 620 2 CYS A  52   SG  109.0                                              
REMARK 620 3 CYS A  55   SG  118.0 106.7                                        
REMARK 620 4 CYS A  74   SG  118.9 104.5  98.3                                  
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 BU3 A 434                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BU3 A 435                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BU3 A 436                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BU3 A 437                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BU3 A 438                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH5 A 439                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 440                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 441                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 442                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3S7D   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3S7F   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3S7J   RELATED DB: PDB                                   
DBREF  3S7B A    1   433  UNP    Q9NRG4   SMYD2_HUMAN      1    433             
SEQADV 3S7B 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    BU3  A 434       6                                                       
HET    BU3  A 435       6                                                       
HET    BU3  A 436       6                                                       
HET    BU3  A 437       6                                                       
HET    BU3  A 438       6                                                       
HET    NH5  A 439      39                                                       
HET     ZN  A 440       1                                                       
HET     ZN  A 441       1                                                       
HET     ZN  A 442       1                                                       
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
HETNAM     BU3 (R,R)-2,3-BUTANEDIOL                                             
HETNAM     NH5 N-CYCLOHEXYL-N~3~-[2-(3,4-DICHLOROPHENYL)ETHYL]-N-(2-            
HETNAM   2 NH5  {[2-(5-HYDROXY-3-OXO-3,4-DIHYDRO-2H-1,4-BENZOXAZIN-8-           
HETNAM   3 NH5  YL)ETHYL]AMINO}ETHYL)-BETA-ALANINAMIDE                          
HETNAM      ZN ZINC ION                                                         
FORMUL   2  SAM    C15 H22 N6 O5 S                                              
FORMUL   3  BU3    5(C4 H10 O2)                                                 
FORMUL   8  NH5    C29 H38 CL2 N4 O4                                            
FORMUL   9   ZN    3(ZN 2+)                                                     
FORMUL  12  HOH   *160(H2 O)                                                    
HELIX    1   1 VAL A   45  ARG A   48  5                                   4    
HELIX    2   2 ASN A   75  LYS A   87  1                                  13    
HELIX    3   3 GLU A   89  GLY A   97  1                                   9    
HELIX    4   4 GLU A   98  TRP A  100  5                                   3    
HELIX    5   5 SER A  103  HIS A  119  1                                  17    
HELIX    6   6 ALA A  130  PHE A  134  5                                   5    
HELIX    7   7 HIS A  137  LEU A  141  5                                   5    
HELIX    8   8 ASP A  142  SER A  161  1                                  20    
HELIX    9   9 ASP A  168  GLY A  183  1                                  16    
HELIX   10  10 PHE A  199  LEU A  204  1                                   6    
HELIX   11  11 PRO A  246  PHE A  259  1                                  14    
HELIX   12  12 CYS A  264  LYS A  270  1                                   7    
HELIX   13  13 LYS A  272  VAL A  277  1                                   6    
HELIX   14  14 LYS A  287  LYS A  309  1                                  23    
HELIX   15  15 SER A  313  SER A  329  1                                  17    
HELIX   16  16 ASN A  336  MET A  353  1                                  18    
HELIX   17  17 ASP A  355  TYR A  374  1                                  20    
HELIX   18  18 SER A  378  LEU A  395  1                                  18    
HELIX   19  19 HIS A  397  HIS A  416  1                                  20    
HELIX   20  20 HIS A  420  HIS A  433  1                                  14    
SHEET    1   A 2 LEU A   9  CYS A  13  0                                        
SHEET    2   A 2 ARG A  19  ALA A  23 -1  O  ARG A  22   N  GLU A  10           
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           
SHEET    1   E 2 ASN A 206  HIS A 207  0                                        
SHEET    2   E 2 PHE A 237  THR A 238  1  O  THR A 238   N  ASN A 206           
LINK         NE2 HIS A  86                ZN    ZN A 441     1555   1555  2.15  
LINK         SG  CYS A  68                ZN    ZN A 441     1555   1555  2.19  
LINK         SG  CYS A 262                ZN    ZN A 442     1555   1555  2.21  
LINK         SG  CYS A  78                ZN    ZN A 440     1555   1555  2.24  
LINK         SG  CYS A 267                ZN    ZN A 442     1555   1555  2.29  
LINK         SG  CYS A  90                ZN    ZN A 441     1555   1555  2.30  
LINK         SG  CYS A  52                ZN    ZN A 440     1555   1555  2.37  
LINK         SG  CYS A  65                ZN    ZN A 441     1555   1555  2.42  
LINK         SG  CYS A  55                ZN    ZN A 440     1555   1555  2.43  
LINK         SG  CYS A  74                ZN    ZN A 440     1555   1555  2.43  
LINK         SG  CYS A 264                ZN    ZN A 442     1555   1555  2.44  
LINK         SG  CYS A 209                ZN    ZN A 442     1555   1555  2.51  
SITE     1 AC1 21 GLY A  16  LYS A  17  ARG A  19  GLU A 135                    
SITE     2 AC1 21 HIS A 137  LYS A 162  CYS A 181  ASN A 182                    
SITE     3 AC1 21 ALA A 203  LEU A 204  MET A 205  ASN A 206                    
SITE     4 AC1 21 HIS A 207  TYR A 240  TYR A 258  PHE A 260                    
SITE     5 AC1 21 BU3 A 438  NH5 A 439  HOH A 468  HOH A 471                    
SITE     6 AC1 21 HOH A 495                                                     
SITE     1 AC2  3 PRO A 314  VAL A 349  TYR A 352                               
SITE     1 AC3  3 TRP A 356  ARG A 390  GLY A 394                               
SITE     1 AC4  5 TYR A  41  TYR A  54  CYS A  55  THR A 220                    
SITE     2 AC4  5 HOH A 533                                                     
SITE     1 AC5  1 ARG A  67                                                     
SITE     1 AC6  4 GLY A  18  ARG A  19  GLU A 135  SAM A1000                    
SITE     1 AC7 16 THR A 105  ILE A 149  ASN A 180  CYS A 181                    
SITE     2 AC7 16 ASN A 182  GLY A 183  PHE A 184  THR A 185                    
SITE     3 AC7 16 ALA A 203  THR A 238  SER A 239  TYR A 240                    
SITE     4 AC7 16 SER A 257  TYR A 258  HOH A 523  SAM A1000                    
SITE     1 AC8  4 CYS A  52  CYS A  55  CYS A  74  CYS A  78                    
SITE     1 AC9  4 CYS A  65  CYS A  68  HIS A  86  CYS A  90                    
SITE     1 BC1  4 CYS A 209  CYS A 262  CYS A 264  CYS A 267                    
CRYST1  155.860  155.860   52.830  90.00  90.00  90.00 I 4           8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006416  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006416  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018929        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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