GenomeNet

Database: PDB
Entry: 4WUY
LinkDB: 4WUY
Original site: 4WUY 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       04-NOV-14   4WUY              
TITLE     CRYSTAL STRUCTURE OF PROTEIN LYSINE METHYLTRANSFERASE SMYD2 IN COMPLEX
TITLE    2 WITH LLY-507, A CELL-ACTIVE, POTENT AND SELECTIVE INHIBITOR          
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: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    SMYD2 - LLY-507, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.NGUYEN,A.ALLALI-HASSANI,S.ANTONYSAMY,S.CHANG,L.H.CHEN,C.CURTIS,     
AUTHOR   2 S.EMTAGE,L.FAN,T.GHEYI,F.LI,S.LIU,J.R.MARTIN,D.MENDEL,J.B.OLSEN,     
AUTHOR   3 L.PELLETIER,T.SHATSEVA,S.WU,F.F.ZHANG,C.H.ARROWSMITH,P.J.BROWN,      
AUTHOR   4 R.M.CAMPBELL,B.A.GARCIA,D.BARSYTE-LOVEJOY,M.MADER,M.VEDADI           
REVDAT   3   10-JUN-15 4WUY    1       JRNL                                     
REVDAT   2   15-APR-15 4WUY    1       JRNL                                     
REVDAT   1   08-APR-15 4WUY    0                                                
JRNL        AUTH   H.NGUYEN,A.ALLALI-HASSANI,S.ANTONYSAMY,S.CHANG,L.H.CHEN,     
JRNL        AUTH 2 C.CURTIS,S.EMTAGE,L.FAN,T.GHEYI,F.LI,S.LIU,J.R.MARTIN,       
JRNL        AUTH 3 D.MENDEL,J.B.OLSEN,L.PELLETIER,T.SHATSEVA,S.WU,F.F.ZHANG,    
JRNL        AUTH 4 C.H.ARROWSMITH,P.J.BROWN,R.M.CAMPBELL,B.A.GARCIA,            
JRNL        AUTH 5 D.BARSYTE-LOVEJOY,M.MADER,M.VEDADI                           
JRNL        TITL   LLY-507, A CELL-ACTIVE, POTENT, AND SELECTIVE INHIBITOR OF   
JRNL        TITL 2 PROTEIN-LYSINE METHYLTRANSFERASE SMYD2.                      
JRNL        REF    J.BIOL.CHEM.                  V. 290 13641 2015              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   25825497                                                     
JRNL        DOI    10.1074/JBC.M114.626861                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.63 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
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) : 1.63                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.70                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 62742                          
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) : 0.154                           
REMARK   3   R VALUE            (WORKING SET) : 0.151                           
REMARK   3   FREE R VALUE                     : 0.200                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3340                            
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) : 1.63                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4496                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.08                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2440                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 214                          
REMARK   3   BIN FREE R VALUE                    : 0.2720                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3218                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 91                                      
REMARK   3   SOLVENT ATOMS            : 430                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.62000                                              
REMARK   3    B22 (A**2) : -0.08000                                             
REMARK   3    B33 (A**2) : -0.54000                                             
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): 0.092         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.082         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.050         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.253         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.967                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3437 ; 0.005 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4655 ; 1.004 ; 1.989       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   427 ; 4.856 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   145 ;35.013 ;24.138       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   572 ;11.212 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;16.663 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   499 ; 0.070 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2604 ; 0.004 ; 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):  1696 ; 6.501 ;34.650       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2127 ; 7.336 ;54.376       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1741 ; 6.598 ;38.118       
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):  5754 ; 7.477 ;  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):  3437 ; 0.727 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   112 ;24.155 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  3682 ;21.416 ; 5.000       
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   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4WUY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-NOV-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000204547.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-JUN-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 31-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-225                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66084                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.630                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS HCL PH 8.6, 14% PEG 20K      
REMARK 280  AND 200 MM SODIUM CHLORIDE, PH 9.0, VAPOR DIFFUSION, SITTING        
REMARK 280  DROP, TEMPERATURE 281K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
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       44.51250            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       49.96000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       44.51250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       49.96000            
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: 810 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 18930 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     LYS A   281                                                      
REMARK 465     LEU A   282                                                      
REMARK 465     SER A   283                                                      
REMARK 465     ASP A   284                                                      
REMARK 465     PRO A   285                                                      
REMARK 465     PRO A   286                                                      
REMARK 465     ARG A   307                                                      
REMARK 465     ALA A   308                                                      
REMARK 465     LYS A   309                                                      
REMARK 465     HIS A   310                                                      
REMARK 465     TYR A   311                                                      
REMARK 465     LYS A   312                                                      
REMARK 465     SER A   313                                                      
REMARK 465     PRO A   314                                                      
REMARK 465     SER A   315                                                      
REMARK 465     GLU A   434                                                      
REMARK 465     GLY A   435                                                      
REMARK 465     HIS A   436                                                      
REMARK 465     HIS A   437                                                      
REMARK 465     HIS A   438                                                      
REMARK 465     HIS A   439                                                      
REMARK 465     HIS A   440                                                      
REMARK 465     HIS A   441                                                      
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     GLU A  60    CD   OE1  OE2                                       
REMARK 470     GLU A 121    CD   OE1  OE2                                       
REMARK 470     ARG A 253    CZ   NH1  NH2                                       
REMARK 470     GLN A 265    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 274    CG   CD   CE   NZ                                   
REMARK 470     LYS A 287    CG   CD   CE   NZ                                   
REMARK 470     GLU A 289    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 296    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 300    CG   OD1  ND2                                       
REMARK 470     VAL A 301    CG1  CG2                                            
REMARK 470     GLU A 303    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 304    CG   CD   OE1  OE2                                  
REMARK 470     PHE A 305    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG A 306    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 316    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 317    CG   CD1  CD2                                       
REMARK 470     GLU A 319    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 320    CG1  CG2  CD1                                       
REMARK 470     GLU A 322    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 323    CG   CD1  CD2                                       
REMARK 470     SER A 324    OG                                                  
REMARK 470     GLU A 326    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 327    CG   CD   CE   NZ                                   
REMARK 470     SER A 329    OG                                                  
REMARK 470     SER A 330    OG                                                  
REMARK 470     VAL A 331    CG1  CG2                                            
REMARK 470     GLU A 333    CG   CD   OE1  OE2                                  
REMARK 470     VAL A 349    CG1  CG2                                            
REMARK 470     GLN A 428    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 431    CG   CD   OE1  OE2                                  
REMARK 470     SER A 432    OG                                                  
REMARK 470     HIS A 433    CG   ND1  CD2  CE1  NE2                             
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       39.26   -145.26                                   
REMARK 500    CYS A 210       70.12   -117.54                                   
REMARK 500    VAL A 277       54.95   -103.82                                   
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 508  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  52   SG                                                     
REMARK 620 2 CYS A  55   SG  107.7                                              
REMARK 620 3 CYS A  74   SG  104.7  99.6                                        
REMARK 620 4 CYS A  78   SG  107.7 121.6 114.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 506  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  65   SG                                                     
REMARK 620 2 CYS A  68   SG  111.1                                              
REMARK 620 3 HIS A  86   NE2 113.7 100.9                                        
REMARK 620 4 CYS A  90   SG  110.0 115.1 105.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 507  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 209   SG                                                     
REMARK 620 2 CYS A 262   SG  113.4                                              
REMARK 620 3 CYS A 264   SG  109.1 104.7                                        
REMARK 620 4 CYS A 267   SG   98.9 115.6 115.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 3UJ A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 506                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 507                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 508                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 509                  
DBREF  4WUY A    1   433  UNP    Q9NRG4   SMYD2_HUMAN      1    433             
SEQADV 4WUY GLU A  434  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4WUY GLY A  435  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4WUY HIS A  436  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4WUY HIS A  437  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4WUY HIS A  438  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4WUY HIS A  439  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4WUY HIS A  440  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4WUY HIS A  441  UNP  Q9NRG4              EXPRESSION TAG                 
SEQRES   1 A  441  MET ARG ALA GLU GLY LEU GLY GLY LEU GLU ARG PHE CYS          
SEQRES   2 A  441  SER PRO GLY LYS GLY ARG GLY LEU ARG ALA LEU GLN PRO          
SEQRES   3 A  441  PHE GLN VAL GLY ASP LEU LEU PHE SER CYS PRO ALA TYR          
SEQRES   4 A  441  ALA TYR VAL LEU THR VAL ASN GLU ARG GLY ASN HIS CYS          
SEQRES   5 A  441  GLU TYR CYS PHE THR ARG LYS GLU GLY LEU SER LYS CYS          
SEQRES   6 A  441  GLY ARG CYS LYS GLN ALA PHE TYR CYS ASN VAL GLU CYS          
SEQRES   7 A  441  GLN LYS GLU ASP TRP PRO MET HIS LYS LEU GLU CYS SER          
SEQRES   8 A  441  PRO MET VAL VAL PHE GLY GLU ASN TRP ASN PRO SER GLU          
SEQRES   9 A  441  THR VAL ARG LEU THR ALA ARG ILE LEU ALA LYS GLN LYS          
SEQRES  10 A  441  ILE HIS PRO GLU ARG THR PRO SER GLU LYS LEU LEU ALA          
SEQRES  11 A  441  VAL LYS GLU PHE GLU SER HIS LEU ASP LYS LEU ASP ASN          
SEQRES  12 A  441  GLU LYS LYS ASP LEU ILE GLN SER ASP ILE ALA ALA LEU          
SEQRES  13 A  441  HIS HIS PHE TYR SER LYS HIS LEU GLY PHE PRO ASP ASN          
SEQRES  14 A  441  ASP SER LEU VAL VAL LEU PHE ALA GLN VAL ASN CYS ASN          
SEQRES  15 A  441  GLY PHE THR ILE GLU ASP GLU GLU LEU SER HIS LEU GLY          
SEQRES  16 A  441  SER ALA ILE PHE PRO ASP VAL ALA LEU MET ASN HIS SER          
SEQRES  17 A  441  CYS CYS PRO ASN VAL ILE VAL THR TYR LYS GLY THR LEU          
SEQRES  18 A  441  ALA GLU VAL ARG ALA VAL GLN GLU ILE LYS PRO GLY GLU          
SEQRES  19 A  441  GLU VAL PHE THR SER TYR ILE ASP LEU LEU TYR PRO THR          
SEQRES  20 A  441  GLU ASP ARG ASN ASP ARG LEU ARG ASP SER TYR PHE PHE          
SEQRES  21 A  441  THR CYS GLU CYS GLN GLU CYS THR THR LYS ASP LYS ASP          
SEQRES  22 A  441  LYS ALA LYS VAL GLU ILE ARG LYS LEU SER ASP PRO PRO          
SEQRES  23 A  441  LYS ALA GLU ALA ILE ARG ASP MET VAL ARG TYR ALA ARG          
SEQRES  24 A  441  ASN VAL ILE GLU GLU PHE ARG ARG ALA LYS HIS TYR LYS          
SEQRES  25 A  441  SER PRO SER GLU LEU LEU GLU ILE CYS GLU LEU SER GLN          
SEQRES  26 A  441  GLU LYS MET SER SER VAL PHE GLU ASP SER ASN VAL TYR          
SEQRES  27 A  441  MET LEU HIS MET MET TYR GLN ALA MET GLY VAL CYS LEU          
SEQRES  28 A  441  TYR MET GLN ASP TRP GLU GLY ALA LEU GLN TYR GLY GLN          
SEQRES  29 A  441  LYS ILE ILE LYS PRO TYR SER LYS HIS TYR PRO LEU TYR          
SEQRES  30 A  441  SER LEU ASN VAL ALA SER MET TRP LEU LYS LEU GLY ARG          
SEQRES  31 A  441  LEU TYR MET GLY LEU GLU HIS LYS ALA ALA GLY GLU LYS          
SEQRES  32 A  441  ALA LEU LYS LYS ALA ILE ALA ILE MET GLU VAL ALA HIS          
SEQRES  33 A  441  GLY LYS ASP HIS PRO TYR ILE SER GLU ILE LYS GLN GLU          
SEQRES  34 A  441  ILE GLU SER HIS GLU GLY HIS HIS HIS HIS HIS HIS              
HET    3UJ  A 501      43                                                       
HET    SAH  A 502      26                                                       
HET    GOL  A 503       6                                                       
HET    GOL  A 504       6                                                       
HET    GOL  A 505       6                                                       
HET     ZN  A 506       1                                                       
HET     ZN  A 507       1                                                       
HET     ZN  A 508       1                                                       
HET     ZN  A 509       1                                                       
HETNAM     3UJ 5-CYANO-2'-{4-[2-(3-METHYL-1H-INDOL-1-YL)                        
HETNAM   2 3UJ  ETHYL]PIPERAZIN-1-YL}-N-[3-(PYRROLIDIN-1-YL)                    
HETNAM   3 3UJ  PROPYL]BIPHENYL-3-CARBOXAMIDE                                   
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
HETNAM     GOL GLYCEROL                                                         
HETNAM      ZN ZINC ION                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  3UJ    C36 H42 N6 O                                                 
FORMUL   3  SAH    C14 H20 N6 O5 S                                              
FORMUL   4  GOL    3(C3 H8 O3)                                                  
FORMUL   7   ZN    4(ZN 2+)                                                     
FORMUL  11  HOH   *430(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 ALA A  130  PHE A  134  5                                   5    
HELIX    7 AA7 HIS A  137  LEU A  141  5                                   5    
HELIX    8 AA8 ASP A  142  GLY A  165  1                                  24    
HELIX    9 AA9 ASP A  168  GLY A  183  1                                  16    
HELIX   10 AB1 PHE A  199  LEU A  204  1                                   6    
HELIX   11 AB2 PRO A  246  PHE A  259  1                                  14    
HELIX   12 AB3 CYS A  264  LYS A  270  1                                   7    
HELIX   13 AB4 LYS A  272  VAL A  277  1                                   6    
HELIX   14 AB5 ALA A  288  ARG A  306  1                                  19    
HELIX   15 AB6 LEU A  317  SER A  330  1                                  14    
HELIX   16 AB7 ASN A  336  GLN A  354  1                                  19    
HELIX   17 AB8 ASP A  355  TYR A  374  1                                  20    
HELIX   18 AB9 SER A  378  LEU A  395  1                                  18    
HELIX   19 AC1 HIS A  397  HIS A  416  1                                  20    
HELIX   20 AC2 HIS A  420  HIS A  433  1                                  14    
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  ILE A 186   O  LEU A 194           
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 508     1555   1555  2.36  
LINK         SG  CYS A  55                ZN    ZN A 508     1555   1555  2.30  
LINK         SG  CYS A  65                ZN    ZN A 506     1555   1555  2.32  
LINK         SG  CYS A  68                ZN    ZN A 506     1555   1555  2.30  
LINK         SG  CYS A  74                ZN    ZN A 508     1555   1555  2.35  
LINK         SG  CYS A  78                ZN    ZN A 508     1555   1555  2.33  
LINK         NE2 HIS A  86                ZN    ZN A 506     1555   1555  2.05  
LINK         SG  CYS A  90                ZN    ZN A 506     1555   1555  2.32  
LINK         SG  CYS A 209                ZN    ZN A 507     1555   1555  2.38  
LINK         SG ACYS A 210                ZN    ZN A 509     1555   1555  2.15  
LINK         SG  CYS A 262                ZN    ZN A 507     1555   1555  2.32  
LINK         SG  CYS A 264                ZN    ZN A 507     1555   1555  2.34  
LINK         SG  CYS A 267                ZN    ZN A 507     1555   1555  2.29  
SITE     1 AC1 16 LEU A 141  LYS A 145  ALA A 177  ASN A 180                    
SITE     2 AC1 16 CYS A 181  ASN A 182  GLY A 183  PHE A 184                    
SITE     3 AC1 16 THR A 185  TYR A 240  SER A 257  TYR A 258                    
SITE     4 AC1 16 PHE A 259  HOH A 698  HOH A 751  HOH A 778                    
SITE     1 AC2 18 GLY A  16  LYS A  17  ARG A  19  HIS A 137                    
SITE     2 AC2 18 CYS A 181  ALA A 203  LEU A 204  ASN A 206                    
SITE     3 AC2 18 HIS A 207  TYR A 240  TYR A 258  PHE A 260                    
SITE     4 AC2 18 HOH A 700  HOH A 737  HOH A 777  HOH A 799                    
SITE     5 AC2 18 HOH A 874  HOH A 892                                          
SITE     1 AC3  7 VAL A  76  GLU A  77  LYS A 140  PHE A 259                    
SITE     2 AC3  7 HOH A 602  HOH A 626  HOH A 660                               
SITE     1 AC4  8 ALA A  38  TYR A  39  TYR A  41  LYS A 115                    
SITE     2 AC4  8 HOH A 742  HOH A 750  HOH A 762  HOH A 828                    
SITE     1 AC5  7 LEU A 243  ARG A 250  LYS A 272  LYS A 276                    
SITE     2 AC5  7 HIS A 373  TYR A 374  PRO A 375                               
SITE     1 AC6  4 CYS A  65  CYS A  68  HIS A  86  CYS A  90                    
SITE     1 AC7  4 CYS A 209  CYS A 262  CYS A 264  CYS A 267                    
SITE     1 AC8  4 CYS A  52  CYS A  55  CYS A  74  CYS A  78                    
SITE     1 AC9  2 CYS A 210  GLU A 266                                          
CRYST1   89.025   99.920   60.297  90.00  90.00  90.00 P 21 21 2     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      0.011233  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010008  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016584        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system