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Database: PDB
Entry: 5HI7
LinkDB: 5HI7
Original site: 5HI7 
HEADER    TRANSFERASE/INHIBITOR                   11-JAN-16   5HI7              
TITLE     CO-CRYSTAL STRUCTURE OF HUMAN SMYD3 WITH AN AZA-SAH COMPOUND          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SMYD3;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: SET AND MYND DOMAIN-CONTAINING PROTEIN 3,ZINC FINGER MYND   
COMPND   5 DOMAIN-CONTAINING PROTEIN 1;                                         
COMPND   6 EC: 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: SMYD3, ZMYND1, ZNFN3A1;                                        
SOURCE   6 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;                         
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10469;                                      
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SF9                                        
KEYWDS    SMYD3, METHYLTRANSFERASE, ONCOLOGY, INHIBITOR, TRANSFERASE-INHIBITOR  
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.A.ELKINS,W.G.BONNETTE                                               
REVDAT   3   18-MAY-16 5HI7    1       JRNL                                     
REVDAT   2   27-APR-16 5HI7    1       JRNL                                     
REVDAT   1   30-MAR-16 5HI7    0                                                
JRNL        AUTH   G.S.VAN ALLER,A.P.GRAVES,P.A.ELKINS,W.G.BONNETTE,            
JRNL        AUTH 2 P.J.MCDEVITT,F.ZAPPACOSTA,R.S.ANNAN,T.W.DEAN,D.S.SU,         
JRNL        AUTH 3 C.L.CARPENTER,H.P.MOHAMMAD,R.G.KRUGER                        
JRNL        TITL   STRUCTURE-BASED DESIGN OF A NOVEL SMYD3 INHIBITOR THAT       
JRNL        TITL 2 BRIDGES THE SAM-AND MEKK2-BINDING POCKETS.                   
JRNL        REF    STRUCTURE                     V.  24   774 2016              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   27066749                                                     
JRNL        DOI    10.1016/J.STR.2016.03.010                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX DEV_1801                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.71                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 23433                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.170                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1211                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 44.7185 -  4.4710    0.96     2542   130  0.1954 0.2027        
REMARK   3     2  4.4710 -  3.5492    0.98     2468   130  0.1663 0.1957        
REMARK   3     3  3.5492 -  3.1007    0.99     2464   141  0.1907 0.2015        
REMARK   3     4  3.1007 -  2.8172    1.00     2467   140  0.2068 0.2312        
REMARK   3     5  2.8172 -  2.6153    1.00     2460   150  0.2147 0.2841        
REMARK   3     6  2.6153 -  2.4612    1.00     2448   143  0.2184 0.2357        
REMARK   3     7  2.4612 -  2.3379    1.00     2458   118  0.2269 0.2754        
REMARK   3     8  2.3379 -  2.2361    1.00     2461   124  0.2226 0.2836        
REMARK   3     9  2.2361 -  2.1501    1.00     2454   135  0.2303 0.2717        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.200            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.040           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           3395                                  
REMARK   3   ANGLE     :  0.626           4612                                  
REMARK   3   CHIRALITY :  0.037            521                                  
REMARK   3   PLANARITY :  0.004            592                                  
REMARK   3   DIHEDRAL  : 11.897           1246                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 3:93)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   8.7044  -3.4687  -5.0462              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1978 T22:   0.2701                                     
REMARK   3      T33:   0.2804 T12:  -0.0032                                     
REMARK   3      T13:   0.0409 T23:  -0.0304                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9412 L22:   1.0427                                     
REMARK   3      L33:   6.2003 L12:   0.5447                                     
REMARK   3      L13:   0.9712 L23:   0.4625                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0258 S12:  -0.1029 S13:   0.0942                       
REMARK   3      S21:   0.2667 S22:  -0.0153 S23:   0.0821                       
REMARK   3      S31:  -0.0572 S32:   0.1333 S33:  -0.0250                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 94:186)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.5955 -17.7629  -5.2762              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1937 T22:   0.1521                                     
REMARK   3      T33:   0.1899 T12:  -0.0384                                     
REMARK   3      T13:  -0.0035 T23:  -0.0099                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9711 L22:   2.4863                                     
REMARK   3      L33:   3.2539 L12:  -0.9539                                     
REMARK   3      L13:  -0.5301 L23:  -0.0727                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0363 S12:  -0.2268 S13:  -0.1225                       
REMARK   3      S21:   0.2131 S22:   0.0007 S23:  -0.0020                       
REMARK   3      S31:   0.1869 S32:   0.0477 S33:   0.0516                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 187:427)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  21.7708   7.5702 -18.5853              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2282 T22:   0.1860                                     
REMARK   3      T33:   0.1955 T12:  -0.0021                                     
REMARK   3      T13:   0.0211 T23:  -0.0075                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7397 L22:   1.3545                                     
REMARK   3      L33:   0.2434 L12:   0.4704                                     
REMARK   3      L13:  -0.0474 L23:  -0.2544                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0023 S12:   0.0116 S13:   0.0416                       
REMARK   3      S21:   0.0640 S22:   0.0030 S23:  -0.0522                       
REMARK   3      S31:  -0.0069 S32:   0.0089 S33:  -0.0026                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5HI7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JAN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000216976.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-JAN-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 295                                
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                       : 21-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.07820                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46288                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
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     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 2.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.4000                            
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SMYD3 CRYSTALLIZATION AND SOAKING OF     
REMARK 280  GSK2807: SMYD3 (1-428) EXPRESSED IN BACULOVIRUS AND WITH SAH IN     
REMARK 280  THE SAM-BINDING SITE WAS CRYSTALLIZED IN SITTING DROPS AT 22C       
REMARK 280  USING 1UL FRESH PROTEIN AT 8.9MG/ML WITH THE ADDITION OF 1UL        
REMARK 280  MOTHER LIQUOR (200MM MGOAC TETRAHYDRATE, 20% PEG 3350). CRYSTALS    
REMARK 280  GREW TO A LARGE SIZE BUT VARIED IN QUANTITY WHEN SET UP IN          
REMARK 280  REPLICATES. A SEED STOCK WAS FORMED FROM THESE CRYSTALS AND         
REMARK 280  ADDED AT 20% TO THE MOTHER LIQUOR SOLUTION PRIOR TO PLATE SETUP.    
REMARK 280  CRYSTALS OF LARGE SIZE WERE THEN CREATED WITH 1.3UL PROTEIN AND     
REMARK 280  1.3UL OF MOTHER LIQUOR CONTAINING SEEDS IN A SITTING DROP MRC-2     
REMARK 280  PLATE (HAMPTON RESEARCH). CRYSTAL NUCLEATION OCCURRED OVERNIGHT     
REMARK 280  AND REACHED MAXIMUM SIZE IN 4 DAYS, VAPOR DIFFUSION, SITTING        
REMARK 280  DROP, TEMPERATURE 295K                                              
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       30.23500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       52.42550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.20050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       52.42550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.23500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.20050            
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    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     PHE A    -1                                                      
REMARK 465     THR A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLU A     2                                                      
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     PRO A   3    CG   CD                                             
REMARK 470     LYS A   5    CD   CE   NZ                                        
REMARK 470     ARG A  25    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  42    CG   CD   CE   NZ                                   
REMARK 470     LYS A  56    NZ                                                  
REMARK 470     GLU A  57    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  58    CG   CD   CE   NZ                                   
REMARK 470     ARG A  61    NH1  NH2                                            
REMARK 470     GLN A  64    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  69    CG   CD   CE   NZ                                   
REMARK 470     LYS A  74    CD   CE   NZ                                        
REMARK 470     LYS A  77    CG   CD   CE   NZ                                   
REMARK 470     LYS A  78    CG   CD   CE   NZ                                   
REMARK 470     LYS A  84    CE   NZ                                             
REMARK 470     LYS A  88    CG   CD   CE   NZ                                   
REMARK 470     LYS A  91    CD   CE   NZ                                        
REMARK 470     LYS A  94    CG   CD   CE   NZ                                   
REMARK 470     ARG A  96    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 119    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 122    CD   CE   NZ                                        
REMARK 470     ASP A 139    OD1                                                 
REMARK 470     LYS A 141    NZ                                                  
REMARK 470     GLU A 157    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 164    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 192    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 214    CD1                                                 
REMARK 470     GLU A 230    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 280    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 281    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 284    CD   CE   NZ                                        
REMARK 470     GLU A 285    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 291    CG   CD   CE   NZ                                   
REMARK 470     LYS A 292    CD   CE   NZ                                        
REMARK 470     LYS A 301    CE   NZ                                             
REMARK 470     GLU A 303    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 316    CG   OD1  ND2                                       
REMARK 470     SER A 317    OG                                                  
REMARK 470     GLU A 318    CD   OE1  OE2                                       
REMARK 470     LYS A 391    CD   CE   NZ                                        
REMARK 470     ARG A 394    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A 401    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A 406    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A 412    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL A  67      -63.21   -108.43                                   
REMARK 500    MET A 190       -3.59     71.31                                   
REMARK 500    LYS A 271       -5.19     77.07                                   
REMARK 500    ILE A 312      -61.88    -95.28                                   
REMARK 500    PRO A 363     -177.39    -64.05                                   
REMARK 500    HIS A 404      -62.78   -106.44                                   
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 503  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  49   SG                                                     
REMARK 620 2 CYS A  52   SG  104.5                                              
REMARK 620 3 CYS A  71   SG  110.5 115.9                                        
REMARK 620 4 CYS A  75   SG  107.1 117.8 100.9                                  
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  62   SG                                                     
REMARK 620 2 CYS A  65   SG  104.8                                              
REMARK 620 3 HIS A  83   NE2 110.3 101.1                                        
REMARK 620 4 CYS A  87   SG  109.2 112.8 117.8                                  
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 208   SG                                                     
REMARK 620 2 CYS A 261   SG  114.6                                              
REMARK 620 3 CYS A 263   SG  105.8 104.0                                        
REMARK 620 4 CYS A 266   SG  100.0 118.0 114.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 505  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 332   OD1                                                    
REMARK 620 2 GLN A 372   OE1  75.9                                              
REMARK 620 3 HOH A 621   O   160.0  84.3                                        
REMARK 620 4 HOH A 605   O   106.6 163.9  93.1                                  
REMARK 620 5 HOH A 713   O    92.3 105.0  90.3  90.9                            
REMARK 620 6 HOH A 606   O    86.6  74.0  90.5  90.1 178.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 504  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 626   O                                                      
REMARK 620 2 HOH A 604   O    90.3                                              
REMARK 620 3 HOH A 612   O   179.7  89.6                                        
REMARK 620 4 HOH A 695   O    90.2  89.9  90.0                                  
REMARK 620 5 HOH A 677   O    89.6 179.8  90.5  89.9                            
REMARK 620 6 HOH A 701   O    89.8  89.9  89.9 179.9  90.2                      
REMARK 620 N                    1     2     3     4     5                       
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 MG A 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 505                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 62X A 507                 
DBREF  5HI7 A    1   428  UNP    Q9H7B4   SMYD3_HUMAN      1    428             
SEQADV 5HI7 GLY A   -3  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 5HI7 SER A   -2  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 5HI7 PHE A   -1  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 5HI7 THR A    0  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 5HI7 ASN A   13  UNP  Q9H7B4    LYS    13 CONFLICT                       
SEQRES   1 A  432  GLY SER PHE THR MET GLU PRO LEU LYS VAL GLU LYS PHE          
SEQRES   2 A  432  ALA THR ALA ASN ARG GLY ASN GLY LEU ARG ALA VAL THR          
SEQRES   3 A  432  PRO LEU ARG PRO GLY GLU LEU LEU PHE ARG SER ASP PRO          
SEQRES   4 A  432  LEU ALA TYR THR VAL CYS LYS GLY SER ARG GLY VAL VAL          
SEQRES   5 A  432  CYS ASP ARG CYS LEU LEU GLY LYS GLU LYS LEU MET ARG          
SEQRES   6 A  432  CYS SER GLN CYS ARG VAL ALA LYS TYR CYS SER ALA LYS          
SEQRES   7 A  432  CYS GLN LYS LYS ALA TRP PRO ASP HIS LYS ARG GLU CYS          
SEQRES   8 A  432  LYS CYS LEU LYS SER CYS LYS PRO ARG TYR PRO PRO ASP          
SEQRES   9 A  432  SER VAL ARG LEU LEU GLY ARG VAL VAL PHE LYS LEU MET          
SEQRES  10 A  432  ASP GLY ALA PRO SER GLU SER GLU LYS LEU TYR SER PHE          
SEQRES  11 A  432  TYR ASP LEU GLU SER ASN ILE ASN LYS LEU THR GLU ASP          
SEQRES  12 A  432  LYS LYS GLU GLY LEU ARG GLN LEU VAL MET THR PHE GLN          
SEQRES  13 A  432  HIS PHE MET ARG GLU GLU ILE GLN ASP ALA SER GLN LEU          
SEQRES  14 A  432  PRO PRO ALA PHE ASP LEU PHE GLU ALA PHE ALA LYS VAL          
SEQRES  15 A  432  ILE CYS ASN SER PHE THR ILE CYS ASN ALA GLU MET GLN          
SEQRES  16 A  432  GLU VAL GLY VAL GLY LEU TYR PRO SER ILE SER LEU LEU          
SEQRES  17 A  432  ASN HIS SER CYS ASP PRO ASN CYS SER ILE VAL PHE ASN          
SEQRES  18 A  432  GLY PRO HIS LEU LEU LEU ARG ALA VAL ARG ASP ILE GLU          
SEQRES  19 A  432  VAL GLY GLU GLU LEU THR ILE CYS TYR LEU ASP MET LEU          
SEQRES  20 A  432  MET THR SER GLU GLU ARG ARG LYS GLN LEU ARG ASP GLN          
SEQRES  21 A  432  TYR CYS PHE GLU CYS ASP CYS PHE ARG CYS GLN THR GLN          
SEQRES  22 A  432  ASP LYS ASP ALA ASP MET LEU THR GLY ASP GLU GLN VAL          
SEQRES  23 A  432  TRP LYS GLU VAL GLN GLU SER LEU LYS LYS ILE GLU GLU          
SEQRES  24 A  432  LEU LYS ALA HIS TRP LYS TRP GLU GLN VAL LEU ALA MET          
SEQRES  25 A  432  CYS GLN ALA ILE ILE SER SER ASN SER GLU ARG LEU PRO          
SEQRES  26 A  432  ASP ILE ASN ILE TYR GLN LEU LYS VAL LEU ASP CYS ALA          
SEQRES  27 A  432  MET ASP ALA CYS ILE ASN LEU GLY LEU LEU GLU GLU ALA          
SEQRES  28 A  432  LEU PHE TYR GLY THR ARG THR MET GLU PRO TYR ARG ILE          
SEQRES  29 A  432  PHE PHE PRO GLY SER HIS PRO VAL ARG GLY VAL GLN VAL          
SEQRES  30 A  432  MET LYS VAL GLY LYS LEU GLN LEU HIS GLN GLY MET PHE          
SEQRES  31 A  432  PRO GLN ALA MET LYS ASN LEU ARG LEU ALA PHE ASP ILE          
SEQRES  32 A  432  MET ARG VAL THR HIS GLY ARG GLU HIS SER LEU ILE GLU          
SEQRES  33 A  432  ASP LEU ILE LEU LEU LEU GLU GLU CYS ASP ALA ASN ILE          
SEQRES  34 A  432  ARG ALA SER                                                  
HET     ZN  A 501       1                                                       
HET     ZN  A 502       1                                                       
HET     ZN  A 503       1                                                       
HET     MG  A 504       1                                                       
HET     MG  A 505       1                                                       
HET    DMS  A 506      10                                                       
HET    62X  A 507      32                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     62X 5'-{[(3S)-3-AMINO-3-CARBOXYPROPYL][3-(DIMETHYLAMINO)             
HETNAM   2 62X  PROPYL]AMINO}-5'-DEOXYADENOSINE                                 
FORMUL   2   ZN    3(ZN 2+)                                                     
FORMUL   5   MG    2(MG 2+)                                                     
FORMUL   7  DMS    C2 H6 O S                                                    
FORMUL   8  62X    C19 H32 N8 O5                                                
FORMUL   9  HOH   *119(H2 O)                                                    
HELIX    1 AA1 SER A   72  LYS A   94  1                                  23    
HELIX    2 AA2 PRO A   99  GLY A  115  1                                  17    
HELIX    3 AA3 SER A  118  LYS A  122  5                                   5    
HELIX    4 AA4 ASN A  132  LEU A  136  5                                   5    
HELIX    5 AA5 THR A  137  MET A  155  1                                  19    
HELIX    6 AA6 ASP A  161  LEU A  165  5                                   5    
HELIX    7 AA7 ASP A  170  SER A  182  1                                  13    
HELIX    8 AA8 SER A  200  LEU A  204  5                                   5    
HELIX    9 AA9 THR A  245  GLN A  256  1                                  12    
HELIX   10 AB1 CYS A  263  GLN A  269  1                                   7    
HELIX   11 AB2 LYS A  271  LEU A  276  1                                   6    
HELIX   12 AB3 ASP A  279  HIS A  299  1                                  21    
HELIX   13 AB4 LYS A  301  SER A  314  1                                  14    
HELIX   14 AB5 ASN A  324  LEU A  341  1                                  18    
HELIX   15 AB6 LEU A  343  THR A  354  1                                  12    
HELIX   16 AB7 THR A  354  PHE A  362  1                                   9    
HELIX   17 AB8 HIS A  366  GLN A  383  1                                  18    
HELIX   18 AB9 MET A  385  HIS A  404  1                                  20    
HELIX   19 AC1 HIS A  408  ALA A  427  1                                  20    
SHEET    1 AA1 2 VAL A   6  ALA A  10  0                                        
SHEET    2 AA1 2 ASN A  16  ALA A  20 -1  O  GLY A  17   N  PHE A   9           
SHEET    1 AA2 3 LEU A  29  SER A  33  0                                        
SHEET    2 AA2 3 HIS A 220  ALA A 225 -1  O  LEU A 223   N  PHE A  31           
SHEET    3 AA2 3 CYS A 212  ASN A 217 -1  N  ASN A 217   O  HIS A 220           
SHEET    1 AA3 3 ALA A  37  VAL A  40  0                                        
SHEET    2 AA3 3 GLU A 192  LEU A 197 -1  O  LEU A 197   N  ALA A  37           
SHEET    3 AA3 3 PHE A 183  CYS A 186 -1  N  ILE A 185   O  GLY A 194           
SHEET    1 AA4 2 MET A  60  ARG A  61  0                                        
SHEET    2 AA4 2 LYS A  69  TYR A  70 -1  O  TYR A  70   N  MET A  60           
SHEET    1 AA5 2 ASN A 205  HIS A 206  0                                        
SHEET    2 AA5 2 THR A 236  ILE A 237  1  O  ILE A 237   N  ASN A 205           
LINK         SG  CYS A  49                ZN    ZN A 503     1555   1555  2.34  
LINK         SG  CYS A  52                ZN    ZN A 503     1555   1555  2.34  
LINK         SG  CYS A  62                ZN    ZN A 502     1555   1555  2.55  
LINK         SG  CYS A  65                ZN    ZN A 502     1555   1555  2.35  
LINK         SG  CYS A  71                ZN    ZN A 503     1555   1555  2.31  
LINK         SG  CYS A  75                ZN    ZN A 503     1555   1555  2.25  
LINK         NE2 HIS A  83                ZN    ZN A 502     1555   1555  2.04  
LINK         SG  CYS A  87                ZN    ZN A 502     1555   1555  2.30  
LINK         SG  CYS A 208                ZN    ZN A 501     1555   1555  2.41  
LINK         SG  CYS A 261                ZN    ZN A 501     1555   1555  2.25  
LINK         SG  CYS A 263                ZN    ZN A 501     1555   1555  2.29  
LINK         SG  CYS A 266                ZN    ZN A 501     1555   1555  2.35  
LINK         OD1 ASP A 332                MG    MG A 505     1555   1555  2.75  
LINK         OE1 GLN A 372                MG    MG A 505     1555   1555  2.76  
LINK        MG    MG A 504                 O   HOH A 626     1555   1555  2.18  
LINK        MG    MG A 504                 O   HOH A 604     1555   1555  2.18  
LINK        MG    MG A 504                 O   HOH A 612     1555   1555  2.18  
LINK        MG    MG A 504                 O   HOH A 695     1555   1555  2.18  
LINK        MG    MG A 505                 O   HOH A 621     1555   1555  2.18  
LINK        MG    MG A 505                 O   HOH A 605     1555   1555  2.18  
LINK        MG    MG A 505                 O   HOH A 713     1555   1555  2.18  
LINK        MG    MG A 505                 O   HOH A 606     1555   1555  2.18  
LINK        MG    MG A 504                 O   HOH A 677     1555   3644  2.18  
LINK        MG    MG A 504                 O   HOH A 701     1555   3644  2.18  
CISPEP   1 LYS A   94    PRO A   95          0         1.32                     
SITE     1 AC1  4 CYS A 208  CYS A 261  CYS A 263  CYS A 266                    
SITE     1 AC2  4 CYS A  62  CYS A  65  HIS A  83  CYS A  87                    
SITE     1 AC3  4 CYS A  49  CYS A  52  CYS A  71  CYS A  75                    
SITE     1 AC4  6 HOH A 604  HOH A 612  HOH A 626  HOH A 677                    
SITE     2 AC4  6 HOH A 695  HOH A 701                                          
SITE     1 AC5  6 ASP A 332  GLN A 372  HOH A 605  HOH A 606                    
SITE     2 AC5  6 HOH A 621  HOH A 713                                          
SITE     1 AC6  5 ASN A 187  MET A 190  PRO A 367  VAL A 368                    
SITE     2 AC6  5 HOH A 669                                                     
SITE     1 AC7 21 ARG A  14  ASN A  16  TYR A 124  GLU A 130                    
SITE     2 AC7 21 ASN A 132  LYS A 135  CYS A 180  ASN A 181                    
SITE     3 AC7 21 SER A 182  PHE A 183  SER A 202  ASN A 205                    
SITE     4 AC7 21 HIS A 206  TYR A 239  TYR A 257  PHE A 259                    
SITE     5 AC7 21 HOH A 609  HOH A 623  HOH A 644  HOH A 667                    
SITE     6 AC7 21 HOH A 670                                                     
CRYST1   60.470   66.401  104.851  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      0.016537  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015060  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009537        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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