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Database: PDB
Entry: 5WCG
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Original site: 5WCG 
HEADER    TRANSFERASE                             30-JUN-17   5WCG              
TITLE     SET AND MYND DOMAIN CONTAINING PROTEIN 2                              
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: UNIDENTIFIED BACULOVIRUS;                         
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10469;                                      
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFBOH-MHL                                 
KEYWDS    ZINC FINGER, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM,     
KEYWDS   2 SGC, TRANSFERASE                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.DONG,H.ZENG,J.R.WALKER,A.HUTCH,A.SEITOVA,J.TATLOCK,R.KUMPF,A.OWEN,  
AUTHOR   2 A.TAYLOR,A.CASIMIRO-GARCIA,C.BOUNTRA,C.H.ARROWSMITH,A.M.EDWARDS,     
AUTHOR   3 P.J.BROWN,H.WU,STRUCTURAL GENOMICS CONSORTIUM (SGC)                  
REVDAT   1   02-AUG-17 5WCG    0                                                
JRNL        AUTH   H.ZENG,A.DONG,J.R.WALKER,A.HUTCH,A.SEITOVA,J.TATLOCK,        
JRNL        AUTH 2 R.KUMPF,A.OWEN,A.TAYLOR,A.CASIMIRO-GARCIA,C.BOUNTRA,         
JRNL        AUTH 3 C.H.ARROWSMITH,A.M.EDWARDS,P.J.BROWN,H.WU                    
JRNL        TITL   THE CRYSTAL STRUCTURE OF SMYD2 IN COMPLEX WITH COMPOUND      
JRNL        TITL 2 MTF003                                                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.02 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.02                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 32306                          
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) : 0.171                           
REMARK   3   R VALUE            (WORKING SET) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.213                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 995                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.02                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.08                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2144                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.10                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2380                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 67                           
REMARK   3   BIN FREE R VALUE                    : 0.2670                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3393                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 57                                      
REMARK   3   SOLVENT ATOMS            : 185                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.49                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.63000                                              
REMARK   3    B22 (A**2) : 0.24000                                              
REMARK   3    B33 (A**2) : -1.10000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.76000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.159         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.148         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.112         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.205         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.928                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3591 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3253 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4873 ; 1.402 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7572 ; 0.963 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   448 ; 5.769 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   161 ;33.979 ;24.286       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   619 ;12.728 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    19 ;15.416 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   525 ; 0.088 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4081 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   717 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 5WCG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUL-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000228582.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-JUN-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.4                                
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                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33305                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.020                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : 0.14500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.02                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.98400                            
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: PHASER 2.5.7, HKL-3000                                
REMARK 200 STARTING MODEL: 3S7B                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.08                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.04M CITRIC ACID, 0.06M   
REMARK 280  BIS-TRIS PROPANE PH6.4, VAPOR DIFFUSION, HANGING DROP,              
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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   X+1/2,Y+1/2,Z                                           
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        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  1.000000  0.000000  0.000000       46.17150            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       49.15600            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       46.17150            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       49.15600            
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 TOTAL BURIED SURFACE AREA: 480 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 20420 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 5.0 KCAL/MOL                          
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 771  LIES ON A SPECIAL POSITION.                          
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     GLY A     5                                                      
REMARK 465     HIS A   433                                                      
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   2    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  80    CE   NZ                                             
REMARK 470     LYS A 127    CE   NZ                                             
REMARK 470     LYS A 132    NZ                                                  
REMARK 470     GLU A 144    CD   OE1  OE2                                       
REMARK 470     LYS A 162    CD   CE   NZ                                        
REMARK 470     LYS A 231    NZ                                                  
REMARK 470     ARG A 253    NH1  NH2                                            
REMARK 470     GLN A 265    CD   OE1  NE2                                       
REMARK 470     LYS A 274    CD   CE   NZ                                        
REMARK 470     LYS A 281    CG   CD   CE   NZ                                   
REMARK 470     SER A 283    OG                                                  
REMARK 470     ASP A 284    CG   OD1  OD2                                       
REMARK 470     LYS A 287    CG   CD   CE   NZ                                   
REMARK 470     GLU A 304    CD   OE1  OE2                                       
REMARK 470     ARG A 306    NE   CZ   NH1  NH2                                  
REMARK 470     GLU A 326    CD   OE1  OE2                                       
REMARK 470     LYS A 327    CD   CE   NZ                                        
REMARK 470     LYS A 365    CE   NZ                                             
REMARK 470     LYS A 372    CD   CE   NZ                                        
REMARK 470     LEU A 376    CG   CD1  CD2                                       
REMARK 470     LYS A 398    CD   CE   NZ                                        
REMARK 470     LYS A 407    CE   NZ                                             
REMARK 470     LYS A 418    CD   CE   NZ                                        
REMARK 470     GLN A 428    CD   OE1  NE2                                       
REMARK 470     SER A 432    OG                                                  
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 101       48.70   -154.15                                   
REMARK 500    PRO A 167     -178.17    -69.73                                   
REMARK 500    TYR A 311        9.85   -154.71                                   
REMARK 500    HIS A 397       75.84   -104.67                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  52   SG                                                     
REMARK 620 2 CYS A  55   SG  106.6                                              
REMARK 620 3 CYS A  74   SG  105.3  99.3                                        
REMARK 620 4 CYS A  78   SG  107.7 120.1 116.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 503  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  65   SG                                                     
REMARK 620 2 CYS A  68   SG  111.0                                              
REMARK 620 3 HIS A  86   NE2 106.5 105.1                                        
REMARK 620 4 CYS A  90   SG  110.9 115.9 106.6                                  
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 209   SG                                                     
REMARK 620 2 CYS A 262   SG  113.3                                              
REMARK 620 3 CYS A 264   SG  110.3 104.5                                        
REMARK 620 4 CYS A 267   SG   96.6 115.9 116.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue A4M A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS A 506                 
DBREF  5WCG A    1   433  UNP    Q9NRG4   SMYD2_HUMAN      1    433             
SEQADV 5WCG 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     ZN  A 501       1                                                       
HET     ZN  A 502       1                                                       
HET     ZN  A 503       1                                                       
HET    A4M  A 504      37                                                       
HET    DMS  A 505       4                                                       
HET    TRS  A 506       8                                                       
HET    UNX  A 507       1                                                       
HET    UNX  A 508       1                                                       
HET    UNX  A 509       1                                                       
HET    UNX  A 510       1                                                       
HET    UNX  A 511       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     A4M [3-(6-AMINO-2-METHYL-9H-PURIN-9-YL)AZETIDIN-1-YL]{5-             
HETNAM   2 A4M  [(4-CYCLOHEPTYLPIPERAZIN-1-YL)METHYL]-1-METHYL-1H-              
HETNAM   3 A4M  PYRAZOL-3-YL}METHANONE                                          
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETNAM     UNX UNKNOWN ATOM OR ION                                              
HETSYN     TRS TRIS BUFFER                                                      
FORMUL   2   ZN    3(ZN 2+)                                                     
FORMUL   5  A4M    C26 H38 N10 O                                                
FORMUL   6  DMS    C2 H6 O S                                                    
FORMUL   7  TRS    C4 H12 N O3 1+                                               
FORMUL   8  UNX    5(X)                                                         
FORMUL  13  HOH   *185(H2 O)                                                    
HELIX    1 AA1 VAL A   45  ARG A   48  5                                   4    
HELIX    2 AA2 ASN A   75  LYS A   87  1                                  13    
HELIX    3 AA3 GLU A   89  GLY A   97  1                                   9    
HELIX    4 AA4 GLU A   98  TRP A  100  5                                   3    
HELIX    5 AA5 SER A  103  HIS A  119  1                                  17    
HELIX    6 AA6 THR A  123  LYS A  127  5                                   5    
HELIX    7 AA7 ALA A  130  PHE A  134  5                                   5    
HELIX    8 AA8 HIS A  137  LEU A  141  5                                   5    
HELIX    9 AA9 ASP A  142  SER A  161  1                                  20    
HELIX   10 AB1 ASP A  168  GLY A  183  1                                  16    
HELIX   11 AB2 ASP A  201  MET A  205  5                                   5    
HELIX   12 AB3 PRO A  246  PHE A  259  1                                  14    
HELIX   13 AB4 CYS A  264  LYS A  270  1                                   7    
HELIX   14 AB5 LYS A  272  VAL A  277  1                                   6    
HELIX   15 AB6 LYS A  287  LYS A  309  1                                  23    
HELIX   16 AB7 SER A  313  SER A  329  1                                  17    
HELIX   17 AB8 ASN A  336  MET A  353  1                                  18    
HELIX   18 AB9 ASP A  355  TYR A  374  1                                  20    
HELIX   19 AC1 SER A  378  LEU A  395  1                                  18    
HELIX   20 AC2 HIS A  397  GLY A  417  1                                  21    
HELIX   21 AC3 HIS A  420  SER A  432  1                                  13    
SHEET    1 AA1 2 LEU A   9  SER A  14  0                                        
SHEET    2 AA1 2 GLY A  18  ALA A  23 -1  O  ARG A  22   N  GLU A  10           
SHEET    1 AA2 3 LEU A  32  PRO A  37  0                                        
SHEET    2 AA2 3 LEU A 221  ALA A 226 -1  O  VAL A 224   N  LEU A  33           
SHEET    3 AA2 3 VAL A 213  LYS A 218 -1  N  THR A 216   O  GLU A 223           
SHEET    1 AA3 3 ALA A  40  LEU A  43  0                                        
SHEET    2 AA3 3 HIS A 193  ILE A 198 -1  O  ILE A 198   N  ALA A  40           
SHEET    3 AA3 3 PHE A 184  GLU A 187 -1  N  PHE A 184   O  ALA A 197           
SHEET    1 AA4 2 SER A  63  LYS A  64  0                                        
SHEET    2 AA4 2 PHE A  72  TYR A  73 -1  O  TYR A  73   N  SER A  63           
SHEET    1 AA5 2 ASN A 206  HIS A 207  0                                        
SHEET    2 AA5 2 PHE A 237  THR A 238  1  O  THR A 238   N  ASN A 206           
LINK         SG  CYS A  52                ZN    ZN A 501     1555   1555  2.35  
LINK         SG  CYS A  55                ZN    ZN A 501     1555   1555  2.35  
LINK         SG  CYS A  65                ZN    ZN A 503     1555   1555  2.45  
LINK         SG  CYS A  68                ZN    ZN A 503     1555   1555  2.19  
LINK         SG  CYS A  74                ZN    ZN A 501     1555   1555  2.37  
LINK         SG  CYS A  78                ZN    ZN A 501     1555   1555  2.34  
LINK         NE2 HIS A  86                ZN    ZN A 503     1555   1555  2.08  
LINK         SG  CYS A  90                ZN    ZN A 503     1555   1555  2.36  
LINK         SG  CYS A 209                ZN    ZN A 502     1555   1555  2.37  
LINK         SG  CYS A 262                ZN    ZN A 502     1555   1555  2.40  
LINK         SG  CYS A 264                ZN    ZN A 502     1555   1555  2.36  
LINK         SG  CYS A 267                ZN    ZN A 502     1555   1555  2.24  
SITE     1 AC1  4 CYS A  52  CYS A  55  CYS A  74  CYS A  78                    
SITE     1 AC2  4 CYS A 209  CYS A 262  CYS A 264  CYS A 267                    
SITE     1 AC3  4 CYS A  65  CYS A  68  HIS A  86  CYS A  90                    
SITE     1 AC4 18 GLY A  16  LYS A  17  HIS A 137  CYS A 181                    
SITE     2 AC4 18 ASN A 182  GLY A 183  PHE A 184  ALA A 203                    
SITE     3 AC4 18 ASN A 206  HIS A 207  TYR A 240  TYR A 258                    
SITE     4 AC4 18 PHE A 260  HOH A 636  HOH A 654  HOH A 695                    
SITE     5 AC4 18 HOH A 699  HOH A 745                                          
SITE     1 AC5  3 TYR A  41  TYR A  54  THR A 220                               
SITE     1 AC6  9 GLU A 104  THR A 105  VAL A 179  ASN A 180                    
SITE     2 AC6  9 GLY A 183  PHE A 184  SER A 196  HOH A 651                    
SITE     3 AC6  9 HOH A 714                                                     
CRYST1   92.343   98.312   58.833  90.00 101.95  90.00 C 1 2 1       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      0.010829  0.000000  0.002293        0.00000                         
SCALE2      0.000000  0.010172  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017374        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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