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Database: PDB
Entry: 3QWW
LinkDB: 3QWW
Original site: 3QWW 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       28-FEB-11   3QWW              
TITLE     CRYSTAL STRUCTURE OF HISTONE LYSINE METHYLTRANSFERASE SMYD2 IN COMPLEX
TITLE    2 WITH THE METHYLTRANSFERASE INHIBITOR SINEFUNGIN                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SET AND MYND DOMAIN-CONTAINING PROTEIN 2;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: SMYD2;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PSUMO                                     
KEYWDS    METHYLTRANSFERASE, HSP90, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.JIANG,N.SIRINUPONG,J.BRUNZELLE,Z.YANG                               
REVDAT   2   21-MAR-12 3QWW    1       JRNL   VERSN                             
REVDAT   1   06-JUL-11 3QWW    0                                                
JRNL        AUTH   Y.JIANG,N.SIRINUPONG,J.BRUNZELLE,Z.YANG                      
JRNL        TITL   CRYSTAL STRUCTURES OF HISTONE AND P53 METHYLTRANSFERASE      
JRNL        TITL 2 SMYD2 REVEAL A CONFORMATIONAL FLEXIBILITY OF THE             
JRNL        TITL 3 AUTOINHIBITORY C-TERMINAL DOMAIN.                            
JRNL        REF    PLOS ONE                      V.   6 21640 2011              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   21738746                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0021640                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.8.0                                         
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.13                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 45783                          
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)  : 0.187                          
REMARK   3   R VALUE            (WORKING SET)  : 0.186                          
REMARK   3   FREE R VALUE                      : 0.207                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.050                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2311                           
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               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.80                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.85                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 3279                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2265                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 3103                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2238                   
REMARK   3   BIN FREE R VALUE                        : 0.2750                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.37                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 176                      
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            : 3441                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 429                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.93                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.51                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.20630                                             
REMARK   3    B22 (A**2) : 2.50990                                              
REMARK   3    B33 (A**2) : -2.30360                                             
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) : 0.20                
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      : 0.946                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.921                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3573   ; 2.000  ; NULL                
REMARK   3    BOND ANGLES               : 4824   ; 2.000  ; NULL                
REMARK   3    TORSION ANGLES            : 1275   ; 2.000  ; NULL                
REMARK   3    TRIGONAL CARBON PLANES    : 92     ; 2.000  ; NULL                
REMARK   3    GENERAL PLANES            : 518    ; 5.000  ; NULL                
REMARK   3    ISOTROPIC THERMAL FACTORS : 3573   ; 20.000 ; NULL                
REMARK   3    BAD NON-BONDED CONTACTS   : 1      ; 5.000  ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 449    ; 5.000  ; NULL                
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   : 4480   ; 4.000  ; NULL                
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.04                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.24                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 18.24                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3QWW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAR-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB064205.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-DEC-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97872                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45863                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : 0.08300                            
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) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.50300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: BUSTER 2.8.0                                          
REMARK 200 STARTING MODEL: PDB ENTRY 3QWW                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.78                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% POLYETHYLENE GLYCOL 8000, 50 MM      
REMARK 280  NACL, 100 MM TRIS, PH 8.5, 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       28.76000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       56.26000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.57500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       56.26000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.76000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.57500            
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     ARG A     2                                                      
REMARK 465     HIS A   433                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   542     O    HOH A   569              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    VAL A 277       50.03   -101.93                                   
REMARK 500    SER A 284      -77.02    -52.76                                   
REMARK 500    ASN A 397       77.81   -115.25                                   
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    ARG A 280        23.7      L          L   OUTSIDE RANGE           
REMARK 500    SER A 284        23.8      L          L   OUTSIDE RANGE           
REMARK 500    MET A 353        23.4      L          L   OUTSIDE RANGE           
REMARK 500    ILE A 367        23.9      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 682        DISTANCE =  5.64 ANGSTROMS                       
REMARK 525    HOH A 791        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH A 824        DISTANCE =  6.03 ANGSTROMS                       
REMARK 525    HOH A 844        DISTANCE =  5.58 ANGSTROMS                       
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 436  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  86   NE2                                                    
REMARK 620 2 CYS A  68   SG  106.1                                              
REMARK 620 3 CYS A  65   SG  105.3 112.2                                        
REMARK 620 4 CYS A  90   SG  106.1 114.0 112.4                                  
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 CYS A  78   SG                                                     
REMARK 620 2 CYS A  55   SG  113.7                                              
REMARK 620 3 CYS A  52   SG  107.7 108.8                                        
REMARK 620 4 CYS A  74   SG  127.1  94.1 103.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 437  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 264   SG                                                     
REMARK 620 2 CYS A 262   SG  106.6                                              
REMARK 620 3 CYS A 267   SG  113.5 116.3                                        
REMARK 620 4 CYS A 209   SG  109.4 113.9  97.0                                  
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 SFG A 434                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 435                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 436                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 437                  
DBREF  3QWW A    1   433  UNP    Q8R5A0   SMYD2_MOUSE      1    433             
SEQRES   1 A  433  MET ARG ALA GLU ALA ARG GLY GLY LEU GLU ARG PHE CYS          
SEQRES   2 A  433  SER ALA GLY LYS GLY ARG GLY LEU ARG ALA LEU ARG PRO          
SEQRES   3 A  433  PHE HIS VAL GLY ASP LEU LEU PHE SER CYS PRO ALA TYR          
SEQRES   4 A  433  ALA CYS VAL LEU THR VAL GLY GLU ARG GLY HIS HIS CYS          
SEQRES   5 A  433  GLU CYS CYS PHE ALA ARG LYS GLU GLY LEU SER LYS CYS          
SEQRES   6 A  433  GLY ARG CYS LYS GLN ALA PHE TYR CYS ASP VAL GLU CYS          
SEQRES   7 A  433  GLN LYS GLU ASP TRP PRO LEU HIS LYS LEU GLU CYS SER          
SEQRES   8 A  433  SER MET VAL VAL LEU 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 ARG 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 GLN PHE TYR SER LYS TYR LEU GLU PHE PRO ASP HIS          
SEQRES  14 A  433  SER 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 HIS PRO GLY ASP          
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 ARG GLU CYS THR THR LYS ASP LYS ASP          
SEQRES  22 A  433  LYS ALA LYS VAL GLU VAL ARG LYS LEU SER SER PRO PRO          
SEQRES  23 A  433  GLN 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 LYS TYR GLY GLN          
SEQRES  29 A  433  LYS ILE ILE LYS PRO TYR SER LYS HIS TYR PRO VAL 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 ASN 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    SFG  A 434      27                                                       
HET     ZN  A 435       1                                                       
HET     ZN  A 436       1                                                       
HET     ZN  A 437       1                                                       
HETNAM     SFG SINEFUNGIN                                                       
HETNAM      ZN ZINC ION                                                         
HETSYN     SFG ADENOSYL-ORNITHINE                                               
FORMUL   2  SFG    C15 H23 N7 O5                                                
FORMUL   3   ZN    3(ZN 2+)                                                     
FORMUL   6  HOH   *429(H2 O)                                                    
HELIX    1   1 VAL A   45  ARG A   48  5                                   4    
HELIX    2   2 ASP A   75  LYS A   87  1                                  13    
HELIX    3   3 GLU A   89  LEU A   96  1                                   8    
HELIX    4   4 SER A  103  HIS A  119  1                                  17    
HELIX    5   5 THR A  123  LYS A  127  5                                   5    
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 ASP A  201  MET A  205  5                                   5    
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 GLN 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 ASN A  397  HIS A  416  1                                  20    
HELIX   20  20 HIS A  420  SER A  432  1                                  13    
SHEET    1   A 4 LEU A   9  CYS A  13  0                                        
SHEET    2   A 4 ARG A  19  ALA A  23 -1  O  GLY A  20   N  PHE A  12           
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  SER A 196   N  VAL A  42           
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         NE2 HIS A  86                ZN    ZN A 436     1555   1555  2.04  
LINK         SG  CYS A  68                ZN    ZN A 436     1555   1555  2.11  
LINK         SG  CYS A  78                ZN    ZN A 435     1555   1555  2.20  
LINK         SG  CYS A 264                ZN    ZN A 437     1555   1555  2.27  
LINK         SG  CYS A 262                ZN    ZN A 437     1555   1555  2.28  
LINK         SG  CYS A 267                ZN    ZN A 437     1555   1555  2.30  
LINK         SG  CYS A  55                ZN    ZN A 435     1555   1555  2.36  
LINK         SG  CYS A  52                ZN    ZN A 435     1555   1555  2.38  
LINK         SG  CYS A 209                ZN    ZN A 437     1555   1555  2.40  
LINK         SG  CYS A  65                ZN    ZN A 436     1555   1555  2.40  
LINK         SG  CYS A  90                ZN    ZN A 436     1555   1555  2.40  
LINK         SG  CYS A  74                ZN    ZN A 435     1555   1555  2.49  
CISPEP   1 SER A  284    PRO A  285          0        -3.68                     
SITE     1 AC1 21 GLY A  16  LYS A  17  ARG A  19  GLU A 135                    
SITE     2 AC1 21 HIS A 137  CYS A 181  ASN A 182  ALA A 203                    
SITE     3 AC1 21 LEU A 204  ASN A 206  HIS A 207  TYR A 240                    
SITE     4 AC1 21 TYR A 258  PHE A 260  HOH A 452  HOH A 454                    
SITE     5 AC1 21 HOH A 473  HOH A 493  HOH A 544  HOH A 557                    
SITE     6 AC1 21 HOH A 866                                                     
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   57.520   75.150  112.520  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      0.017385  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013307  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008887        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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