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Database: PDB
Entry: 3QWP
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Original site: 3QWP 
HEADER    TRANSFERASE                             28-FEB-11   3QWP              
TITLE     CRYSTAL STRUCTURE OF SET AND MYND DOMAIN CONTAINING 3; ZINC FINGER    
TITLE    2 MYND DOMAIN-CONTAINING PROTEIN 1                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SET AND MYND DOMAIN-CONTAINING PROTEIN 3;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ZINC FINGER MYND DOMAIN-CONTAINING PROTEIN 1;               
COMPND   5 EC: 2.1.1.43;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SMYD3, ZMYND1, ZNFN3A1;                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) V2RPRARE;                        
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28-MHL                                 
KEYWDS    SMYD3,SET AND MYND DOMAIN, ZINC FINGER MYND DOMAIN-CONTAINING PROTEIN 
KEYWDS   2 1, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC,         
KEYWDS   3 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.DONG,L.DOMBROVSKI,Y.LI,A.WERNIMONT,J.WEIGELT,C.BOUNTRA,             
AUTHOR   2 C.H.ARROWSMITH,A.M.EDWARDS,J.MIN,H.WU,STRUCTURAL GENOMICS CONSORTIUM 
AUTHOR   3 (SGC)                                                                
REVDAT   1   06-APR-11 3QWP    0                                                
JRNL        AUTH   L.DOMBROVSKI,A.DONG,H.WU,J.MIN                               
JRNL        TITL   THE CRYSTAL STRUCTURE OF HUMAN HISTONE-LYSINE                
JRNL        TITL 2 N-METHYLTRANSFERASE SMYD3                                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.53 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102, COOT 0.6                            
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.53                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.39                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 62914                          
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) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.217                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3372                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.53                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.57                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4245                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.40                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2610                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 220                          
REMARK   3   BIN FREE R VALUE                    : 0.2970                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3348                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 78                                      
REMARK   3   SOLVENT ATOMS            : 485                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.25                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.61000                                              
REMARK   3    B22 (A**2) : -0.31000                                             
REMARK   3    B33 (A**2) : -0.31000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.085         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.051         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.378         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.941                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3598 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4862 ; 1.507 ; 1.986       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   447 ; 6.473 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   165 ;34.494 ;24.182       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   636 ;13.134 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;16.669 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   530 ; 0.121 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2707 ; 0.017 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2202 ; 1.599 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3557 ; 2.532 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1396 ; 3.899 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1305 ; 6.013 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3QWP COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAR-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB064198.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-DEC-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97929                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66393                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.530                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 8.100                              
REMARK 200  R MERGE                    (I) : 0.07400                            
REMARK 200  R SYM                      (I) : 0.07400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 30.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.53                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.56                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.56400                            
REMARK 200  R SYM FOR SHELL            (I) : 0.56400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3MEK                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2M CACL2, VAPOR          
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 297K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       30.65150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.69350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.10300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       53.69350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.65150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.10300            
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     GLY A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     SER A   428                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  25    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  56    CG   CD   CE   NZ                                   
REMARK 470     GLU A  57    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  58    CG   CD   CE   NZ                                   
REMARK 470     GLN A  64    CD   OE1  NE2                                       
REMARK 470     LYS A  74    CE   NZ                                             
REMARK 470     LYS A  77    CD   CE   NZ                                        
REMARK 470     LYS A  78    CD   CE   NZ                                        
REMARK 470     LYS A  88    CG   CD   CE   NZ                                   
REMARK 470     LYS A  91    CE   NZ                                             
REMARK 470     LYS A  94    CG   CD   CE   NZ                                   
REMARK 470     ARG A  96    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 111    NZ                                                  
REMARK 470     GLU A 119    CD   OE1  OE2                                       
REMARK 470     LYS A 301    CE   NZ                                             
REMARK 470     ARG A 406    CZ   NH1  NH2                                       
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   OD1  ASP A   262     O    HOH A   879              1.44            
REMARK 500   OD2  ASP A   262     O    HOH A   860              2.11            
REMARK 500   O    HOH A   651     O    HOH A   669              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS A  71   CB    CYS A  71   SG     -0.162                       
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    ASN A  13       11.77   -144.20                                   
REMARK 500    LYS A 271       -8.65     76.45                                   
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 500  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  83   NE2                                                    
REMARK 620 2 CYS A  62   SG  114.1                                              
REMARK 620 3 CYS A  87   SG  106.1 110.7                                        
REMARK 620 4 CYS A  65   SG  101.5 110.6 113.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 263   SG                                                     
REMARK 620 2 CYS A 261   SG  113.7                                              
REMARK 620 3 CYS A 266   SG  119.0 119.4                                        
REMARK 620 4 CYS A 208   SG   98.3 100.6  99.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  52   SG                                                     
REMARK 620 2 CYS A  71   SG  109.5                                              
REMARK 620 3 CYS A  75   SG  118.0 101.8                                        
REMARK 620 4 CYS A  49   SG  106.6 114.0 107.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM A 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3010                
DBREF  3QWP A    1   428  UNP    Q9H7B4   SMYD3_HUMAN      1    428             
SEQADV 3QWP GLY A    0  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3QWP ASN A   13  UNP  Q9H7B4    LYS    13 CONFLICT                       
SEQADV 3QWP ARG A  140  UNP  Q9H7B4    LYS   140 CONFLICT                       
SEQRES   1 A  429  GLY MET GLU PRO LEU LYS VAL GLU LYS PHE ALA THR ALA          
SEQRES   2 A  429  ASN ARG GLY ASN GLY LEU ARG ALA VAL THR PRO LEU ARG          
SEQRES   3 A  429  PRO GLY GLU LEU LEU PHE ARG SER ASP PRO LEU ALA TYR          
SEQRES   4 A  429  THR VAL CYS LYS GLY SER ARG GLY VAL VAL CYS ASP ARG          
SEQRES   5 A  429  CYS LEU LEU GLY LYS GLU LYS LEU MET ARG CYS SER GLN          
SEQRES   6 A  429  CYS ARG VAL ALA LYS TYR CYS SER ALA LYS CYS GLN LYS          
SEQRES   7 A  429  LYS ALA TRP PRO ASP HIS LYS ARG GLU CYS LYS CYS LEU          
SEQRES   8 A  429  LYS SER CYS LYS PRO ARG TYR PRO PRO ASP SER VAL ARG          
SEQRES   9 A  429  LEU LEU GLY ARG VAL VAL PHE LYS LEU MET ASP GLY ALA          
SEQRES  10 A  429  PRO SER GLU SER GLU LYS LEU TYR SER PHE TYR ASP LEU          
SEQRES  11 A  429  GLU SER ASN ILE ASN LYS LEU THR GLU ASP ARG LYS GLU          
SEQRES  12 A  429  GLY LEU ARG GLN LEU VAL MET THR PHE GLN HIS PHE MET          
SEQRES  13 A  429  ARG GLU GLU ILE GLN ASP ALA SER GLN LEU PRO PRO ALA          
SEQRES  14 A  429  PHE ASP LEU PHE GLU ALA PHE ALA LYS VAL ILE CYS ASN          
SEQRES  15 A  429  SER PHE THR ILE CYS ASN ALA GLU MET GLN GLU VAL GLY          
SEQRES  16 A  429  VAL GLY LEU TYR PRO SER ILE SER LEU LEU ASN HIS SER          
SEQRES  17 A  429  CYS ASP PRO ASN CYS SER ILE VAL PHE ASN GLY PRO HIS          
SEQRES  18 A  429  LEU LEU LEU ARG ALA VAL ARG ASP ILE GLU VAL GLY GLU          
SEQRES  19 A  429  GLU LEU THR ILE CYS TYR LEU ASP MET LEU MET THR SER          
SEQRES  20 A  429  GLU GLU ARG ARG LYS GLN LEU ARG ASP GLN TYR CYS PHE          
SEQRES  21 A  429  GLU CYS ASP CYS PHE ARG CYS GLN THR GLN ASP LYS ASP          
SEQRES  22 A  429  ALA ASP MET LEU THR GLY ASP GLU GLN VAL TRP LYS GLU          
SEQRES  23 A  429  VAL GLN GLU SER LEU LYS LYS ILE GLU GLU LEU LYS ALA          
SEQRES  24 A  429  HIS TRP LYS TRP GLU GLN VAL LEU ALA MET CYS GLN ALA          
SEQRES  25 A  429  ILE ILE SER SER ASN SER GLU ARG LEU PRO ASP ILE ASN          
SEQRES  26 A  429  ILE TYR GLN LEU LYS VAL LEU ASP CYS ALA MET ASP ALA          
SEQRES  27 A  429  CYS ILE ASN LEU GLY LEU LEU GLU GLU ALA LEU PHE TYR          
SEQRES  28 A  429  GLY THR ARG THR MET GLU PRO TYR ARG ILE PHE PHE PRO          
SEQRES  29 A  429  GLY SER HIS PRO VAL ARG GLY VAL GLN VAL MET LYS VAL          
SEQRES  30 A  429  GLY LYS LEU GLN LEU HIS GLN GLY MET PHE PRO GLN ALA          
SEQRES  31 A  429  MET LYS ASN LEU ARG LEU ALA PHE ASP ILE MET ARG VAL          
SEQRES  32 A  429  THR HIS GLY ARG GLU HIS SER LEU ILE GLU ASP LEU ILE          
SEQRES  33 A  429  LEU LEU LEU GLU GLU CYS ASP ALA ASN ILE ARG ALA SER          
HET     ZN  A 500       1                                                       
HET     ZN  A 501       1                                                       
HET     ZN  A 502       1                                                       
HET    SAM  A 510      27                                                       
HET    GOL  A3001       6                                                       
HET    GOL  A3004       6                                                       
HET    GOL  A3005       6                                                       
HET    GOL  A3006       6                                                       
HET    GOL  A3007       6                                                       
HET    GOL  A3008       6                                                       
HET    GOL  A3009       6                                                       
HET    GOL  A3010       6                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2   ZN    3(ZN 2+)                                                     
FORMUL   5  SAM    C15 H22 N6 O5 S                                              
FORMUL   6  GOL    8(C3 H8 O3)                                                  
FORMUL  14  HOH   *485(H2 O)                                                    
HELIX    1   1 LYS A   42  ARG A   45  5                                   4    
HELIX    2   2 SER A   72  ALA A   79  1                                   8    
HELIX    3   3 ALA A   79  CYS A   93  1                                  15    
HELIX    4   4 PRO A   99  GLY A  115  1                                  17    
HELIX    5   5 SER A  118  LYS A  122  5                                   5    
HELIX    6   6 SER A  125  LEU A  129  5                                   5    
HELIX    7   7 ASN A  132  LEU A  136  5                                   5    
HELIX    8   8 THR A  137  MET A  155  1                                  19    
HELIX    9   9 ASP A  161  LEU A  165  5                                   5    
HELIX   10  10 ASP A  170  SER A  182  1                                  13    
HELIX   11  11 SER A  200  LEU A  204  5                                   5    
HELIX   12  12 THR A  245  CYS A  258  1                                  14    
HELIX   13  13 CYS A  263  GLN A  269  1                                   7    
HELIX   14  14 LYS A  271  LEU A  276  1                                   6    
HELIX   15  15 ASP A  279  HIS A  299  1                                  21    
HELIX   16  16 LYS A  301  SER A  314  1                                  14    
HELIX   17  17 ASN A  324  GLY A  342  1                                  19    
HELIX   18  18 LEU A  343  PHE A  362  1                                  20    
HELIX   19  19 HIS A  366  GLN A  383  1                                  18    
HELIX   20  20 MET A  385  HIS A  404  1                                  20    
HELIX   21  21 HIS A  408  ALA A  427  1                                  20    
SHEET    1   A 4 VAL A   6  ALA A  10  0                                        
SHEET    2   A 4 ASN A  16  ALA A  20 -1  O  GLY A  17   N  PHE A   9           
SHEET    3   A 4 GLU A 234  ILE A 237 -1  O  LEU A 235   N  LEU A  18           
SHEET    4   A 4 ASN A 205  HIS A 206  1  N  ASN A 205   O  ILE A 237           
SHEET    1   B 3 LEU A  29  SER A  33  0                                        
SHEET    2   B 3 HIS A 220  ALA A 225 -1  O  LEU A 223   N  LEU A  30           
SHEET    3   B 3 CYS A 212  ASN A 217 -1  N  ASN A 217   O  HIS A 220           
SHEET    1   C 3 ALA A  37  VAL A  40  0                                        
SHEET    2   C 3 GLU A 192  LEU A 197 -1  O  LEU A 197   N  ALA A  37           
SHEET    3   C 3 PHE A 183  CYS A 186 -1  N  ILE A 185   O  VAL A 193           
SHEET    1   D 2 MET A  60  ARG A  61  0                                        
SHEET    2   D 2 LYS A  69  TYR A  70 -1  O  TYR A  70   N  MET A  60           
LINK         NE2 HIS A  83                ZN    ZN A 500     1555   1555  2.08  
LINK         SG ACYS A 263                ZN    ZN A 502     1555   1555  2.16  
LINK         SG  CYS A  52                ZN    ZN A 501     1555   1555  2.23  
LINK         SG  CYS A  62                ZN    ZN A 500     1555   1555  2.26  
LINK         SG  CYS A  71                ZN    ZN A 501     1555   1555  2.27  
LINK         SG ACYS A 261                ZN    ZN A 502     1555   1555  2.30  
LINK         SG  CYS A  75                ZN    ZN A 501     1555   1555  2.32  
LINK         SG  CYS A 266                ZN    ZN A 502     1555   1555  2.33  
LINK         SG BCYS A 261                ZN    ZN A 502     1555   1555  2.34  
LINK         SG  CYS A  87                ZN    ZN A 500     1555   1555  2.38  
LINK         SG  CYS A  65                ZN    ZN A 500     1555   1555  2.38  
LINK         SG  CYS A  49                ZN    ZN A 501     1555   1555  2.39  
LINK         SG  CYS A 208                ZN    ZN A 502     1555   1555  2.46  
LINK         SG BCYS A 263                ZN    ZN A 502     1555   1555  2.49  
CISPEP   1 LYS A   94    PRO A   95          0        12.79                     
SITE     1 AC1  4 CYS A  62  CYS A  65  HIS A  83  CYS A  87                    
SITE     1 AC2  4 CYS A  49  CYS A  52  CYS A  71  CYS A  75                    
SITE     1 AC3  4 CYS A 208  CYS A 261  CYS A 263  CYS A 266                    
SITE     1 AC4 22 ARG A  14  ASN A  16  TYR A 124  GLU A 130                    
SITE     2 AC4 22 ASN A 132  ASN A 181  SER A 202  LEU A 203                    
SITE     3 AC4 22 LEU A 204  ASN A 205  HIS A 206  TYR A 239                    
SITE     4 AC4 22 TYR A 257  PHE A 259  HOH A 491  HOH A 497                    
SITE     5 AC4 22 HOH A 512  HOH A 564  HOH A 567  HOH A 629                    
SITE     6 AC4 22 HOH A 679  GOL A3001                                          
SITE     1 AC5 11 ASN A 181  SER A 182  PHE A 183  SER A 202                    
SITE     2 AC5 11 ILE A 237  TYR A 239  TYR A 257  SAM A 510                    
SITE     3 AC5 11 HOH A 518  HOH A 751  GOL A3004                               
SITE     1 AC6  6 SER A 182  PHE A 183  THR A 184  HOH A 553                    
SITE     2 AC6  6 HOH A 591  GOL A3001                                          
SITE     1 AC7  7 GLN A 191  LYS A 297  ASP A 332  ASP A 336                    
SITE     2 AC7  7 TYR A 358  GLN A 372  LYS A 375                               
SITE     1 AC8  5 PHE A 151  GLN A 152  ILE A 159  GLN A 160                    
SITE     2 AC8  5 HOH A 724                                                     
SITE     1 AC9  4 ARG A 140  ILE A 179  GLN A 256  HOH A 640                    
SITE     1 BC1  7 ASP A  82  PHE A 110  ASP A 114  GLU A 142                    
SITE     2 BC1  7 HOH A 582  HOH A 685  HOH A 876                               
SITE     1 BC2  7 CYS A 238  LEU A 240  MET A 242  HIS A 366                    
SITE     2 BC2  7 HOH A 494  HOH A 591  GOL A3010                               
SITE     1 BC3  9 ILE A 214  VAL A 215  HIS A 366  PRO A 367                    
SITE     2 BC3  9 VAL A 368  HOH A 520  HOH A 535  HOH A 553                    
SITE     3 BC3  9 GOL A3009                                                     
CRYST1   61.303   66.206  107.387  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      0.016312  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015104  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009312        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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