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Database: PDB
Entry: 5HQ8
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HEADER    TRANSFERASE                             21-JAN-16   5HQ8              
TITLE     CO-CRYSTAL STRUCTURE OF HUMAN SMYD3 WITH A MEKK2 PEPTIDE AT 2.13A     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SMYD3;                  
COMPND   3 CHAIN: A, B;                                                         
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;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: MEKK2 PEPTIDE;                                             
COMPND  10 CHAIN: I, J;                                                         
COMPND  11 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;                                       
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 SYNTHETIC: YES;                                                      
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_TAXID: 9606                                                 
KEYWDS    SMYD3, METHYLTRANSFERASE, ONCOLOGY, TRANSFERASE                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.A.ELKINS,W.G.BONNETTE                                               
REVDAT   3   18-MAY-16 5HQ8    1       JRNL                                     
REVDAT   2   27-APR-16 5HQ8    1       JRNL                                     
REVDAT   1   30-MAR-16 5HQ8    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.    1.72 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) : 1.72                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.43                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 110414                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.201                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5551                            
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 25.4326 -  5.3286    0.98     3489   187  0.1531 0.1840        
REMARK   3     2  5.3286 -  4.2358    0.99     3530   185  0.1361 0.1481        
REMARK   3     3  4.2358 -  3.7022    1.00     3501   177  0.1409 0.1588        
REMARK   3     4  3.7022 -  3.3645    1.00     3525   173  0.1641 0.1780        
REMARK   3     5  3.3645 -  3.1238    1.00     3493   182  0.1765 0.2217        
REMARK   3     6  3.1238 -  2.9399    1.00     3503   193  0.1857 0.2144        
REMARK   3     7  2.9399 -  2.7929    1.00     3480   184  0.1827 0.2084        
REMARK   3     8  2.7929 -  2.6715    1.00     3545   170  0.1816 0.2104        
REMARK   3     9  2.6715 -  2.5687    1.00     3507   171  0.1862 0.2071        
REMARK   3    10  2.5687 -  2.4802    1.00     3518   188  0.1822 0.2103        
REMARK   3    11  2.4802 -  2.4027    1.00     3484   177  0.1819 0.2078        
REMARK   3    12  2.4027 -  2.3340    1.00     3490   183  0.1783 0.2108        
REMARK   3    13  2.3340 -  2.2726    1.00     3459   203  0.1744 0.2141        
REMARK   3    14  2.2726 -  2.2172    1.00     3490   193  0.1738 0.1986        
REMARK   3    15  2.2172 -  2.1668    1.00     3510   195  0.1776 0.2068        
REMARK   3    16  2.1668 -  2.1208    1.00     3445   179  0.1843 0.2305        
REMARK   3    17  2.1208 -  2.0783    1.00     3539   179  0.1827 0.2191        
REMARK   3    18  2.0783 -  2.0391    1.00     3495   179  0.1818 0.2192        
REMARK   3    19  2.0391 -  2.0027    1.00     3496   206  0.2019 0.2084        
REMARK   3    20  2.0027 -  1.9688    1.00     3442   184  0.1959 0.2241        
REMARK   3    21  1.9688 -  1.9371    1.00     3542   183  0.1937 0.2426        
REMARK   3    22  1.9371 -  1.9073    1.00     3466   180  0.1941 0.2279        
REMARK   3    23  1.9073 -  1.8792    1.00     3488   188  0.2061 0.2258        
REMARK   3    24  1.8792 -  1.8528    1.00     3505   193  0.2055 0.2338        
REMARK   3    25  1.8528 -  1.8277    1.00     3469   180  0.2072 0.2445        
REMARK   3    26  1.8277 -  1.8040    1.00     3500   182  0.2125 0.2397        
REMARK   3    27  1.8040 -  1.7815    1.00     3493   193  0.2167 0.2599        
REMARK   3    28  1.7815 -  1.7600    1.00     3462   186  0.2228 0.2374        
REMARK   3    29  1.7600 -  1.7395    1.00     3524   186  0.2267 0.3000        
REMARK   3    30  1.7395 -  1.7200    1.00     3473   192  0.2493 0.2818        
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)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.690           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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      :  0.018           7104                                  
REMARK   3   ANGLE     :  1.419           9587                                  
REMARK   3   CHIRALITY :  0.091           1063                                  
REMARK   3   PLANARITY :  0.011           1234                                  
REMARK   3   DIHEDRAL  : 13.623           2692                                  
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):  36.7776  -5.9930  40.0590              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1011 T22:   0.1912                                     
REMARK   3      T33:   0.2413 T12:  -0.0011                                     
REMARK   3      T13:  -0.0006 T23:  -0.0301                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4384 L22:   2.0541                                     
REMARK   3      L33:   2.5629 L12:   0.6538                                     
REMARK   3      L13:   0.5889 L23:   1.2407                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0013 S12:  -0.0652 S13:   0.1977                       
REMARK   3      S21:   0.0277 S22:   0.1750 S23:  -0.2142                       
REMARK   3      S31:   0.0213 S32:   0.2445 S33:  -0.1370                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 94:186)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.5971  -0.0999  43.6186              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0906 T22:   0.1695                                     
REMARK   3      T33:   0.2792 T12:  -0.0065                                     
REMARK   3      T13:   0.0055 T23:  -0.0516                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8928 L22:   2.5419                                     
REMARK   3      L33:   3.0048 L12:  -0.4682                                     
REMARK   3      L13:   0.3008 L23:   0.8578                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0552 S12:  -0.0939 S13:   0.0123                       
REMARK   3      S21:   0.0635 S22:   0.0276 S23:   0.1253                       
REMARK   3      S31:  -0.1333 S32:  -0.0052 S33:  -0.0955                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 187:427)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  33.8138 -27.6944  38.1049              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1038 T22:   0.1568                                     
REMARK   3      T33:   0.1571 T12:   0.0001                                     
REMARK   3      T13:   0.0175 T23:  -0.0070                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3054 L22:   1.3680                                     
REMARK   3      L33:   0.4990 L12:   0.1691                                     
REMARK   3      L13:   0.0365 L23:  -0.1689                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1020 S12:  -0.1027 S13:  -0.1675                       
REMARK   3      S21:   0.0394 S22:   0.0407 S23:  -0.1643                       
REMARK   3      S31:  -0.0096 S32:   0.0470 S33:   0.0502                       
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 5HQ8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JAN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000217172.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-NOV-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
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) : 1.07808                            
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   : 138107                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.592                              
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     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.1100                            
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   (%): 53.28                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: HUMAN SMYD3 (1-428) WITH SAM IN THE      
REMARK 280  SAM-BINDING SITE WAS CONCENTRATED TO 11.7 MG/ML IN 25 MM TRIS-      
REMARK 280  HCL PH 8 AND 150 MM NACL. PEPTIDE (21ST CENTURY BIOCHEMICAL) WAS    
REMARK 280  SOLUBILIZED IN 100MM WATER. TWO UL PEPTIDE WAS ADDED TO 200 UL      
REMARK 280  OF PROTEIN (FIVE FOLD MOLAR EXCESS OF PEPTIDE) AND ALLOWED TO       
REMARK 280  COMPLEX WITH THE PROTEIN OVERNIGHT AT 4C. CRYSTALS WERE OBTAINED    
REMARK 280  FROM A HAMPTON INDEX HT BROAD SCREEN IN SITTING DROPS AT 22C        
REMARK 280  WITH CONDITION H7 (0.15 DL-MALIC ACID PH 7.0, 20% W/V PEG 3,350)    
REMARK 280  . CRYSTALS WERE FLASH FROZEN IN 20 PERCENT ETHYLENE GLYCOL IN       
REMARK 280  WELL SOLUTION PRIOR TO DATA COLLECTION, VAPOR DIFFUSION, SITTING    
REMARK 280  DROP, TEMPERATURE 295K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       59.07750            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2610 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19320 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, I                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2680 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18640 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, J                                  
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 465     GLY B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     PHE B    -1                                                      
REMARK 465     THR B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     SER B   428                                                      
REMARK 465     ASP I   251                                                      
REMARK 465     ASN I   252                                                      
REMARK 465     PRO I   253                                                      
REMARK 465     ILE I   254                                                      
REMARK 465     PHE I   255                                                      
REMARK 465     NH2 I   265                                                      
REMARK 465     TYR J   250                                                      
REMARK 465     ASP J   251                                                      
REMARK 465     ASN J   252                                                      
REMARK 465     PRO J   253                                                      
REMARK 465     ILE J   254                                                      
REMARK 465     PHE J   255                                                      
REMARK 465     NH2 J   265                                                      
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     LYS A  42    CG   CD   CE   NZ                                   
REMARK 470     LYS A  56    CD   CE   NZ                                        
REMARK 470     GLU A  57    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  58    CG   CD   CE   NZ                                   
REMARK 470     LYS A  69    NZ                                                  
REMARK 470     LYS A  74    CD   CE   NZ                                        
REMARK 470     LYS A  77    CD   CE   NZ                                        
REMARK 470     LYS A  78    CE   NZ                                             
REMARK 470     LYS A  88    NZ                                                  
REMARK 470     LYS A  94    CE   NZ                                             
REMARK 470     ARG A  96    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 111    NZ                                                  
REMARK 470     ASP A 139    CG   OD1  OD2                                       
REMARK 470     LYS A 140    CG   CD   CE   NZ                                   
REMARK 470     GLU A 157    CD   OE1  OE2                                       
REMARK 470     GLN A 281    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 284    CD   CE   NZ                                        
REMARK 470     LYS A 297    CE   NZ                                             
REMARK 470     ARG A 319    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 391    NZ                                                  
REMARK 470     GLU A 412    CD   OE1  OE2                                       
REMARK 470     PRO B   3    CG   CD                                             
REMARK 470     LEU B   4    CG   CD1  CD2                                       
REMARK 470     LYS B   5    CD   CE   NZ                                        
REMARK 470     ARG B  25    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  42    CD   CE   NZ                                        
REMARK 470     GLU B  57    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  58    CG   CD   CE   NZ                                   
REMARK 470     LYS B  74    CE   NZ                                             
REMARK 470     LYS B  77    CG   CD   CE   NZ                                   
REMARK 470     LYS B  78    NZ                                                  
REMARK 470     LYS B  84    CE   NZ                                             
REMARK 470     ARG B  96    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS B 122    CE   NZ                                             
REMARK 470     LYS B 140    CD   CE   NZ                                        
REMARK 470     GLN B 146    CD   OE1  NE2                                       
REMARK 470     ARG B 156    NH1  NH2                                            
REMARK 470     GLU B 247    CD   OE1  OE2                                       
REMARK 470     ARG B 250    NE   CZ   NH1  NH2                                  
REMARK 470     LYS B 251    NZ                                                  
REMARK 470     LYS B 284    CD   CE   NZ                                        
REMARK 470     GLU B 285    CD   OE1  OE2                                       
REMARK 470     LYS B 291    NZ                                                  
REMARK 470     LYS B 292    NZ                                                  
REMARK 470     LYS B 301    CE   NZ                                             
REMARK 470     GLU B 303    CD   OE1  OE2                                       
REMARK 470     ARG B 319    CZ   NH1  NH2                                       
REMARK 470     LYS B 391    CD   CE   NZ                                        
REMARK 470     ARG B 401    CZ   NH1  NH2                                       
REMARK 470     ARG B 406    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU B 412    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 415    CG1  CG2  CD1                                       
REMARK 470     GLU B 419    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 420    CD   OE1  OE2                                       
REMARK 470     ASP B 422    CG   OD1  OD2                                       
REMARK 470     ARG B 426    NE   CZ   NH1  NH2                                  
REMARK 470     GLU I 256    CG   CD   OE1  OE2                                  
REMARK 470     LYS I 257    CG   CD   CE   NZ                                   
REMARK 470     GLU J 256    CG   CD   OE1  OE2                                  
REMARK 470     LYS J 257    CD   CE   NZ                                        
REMARK 470     THR J 263    CG2                                                 
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   607     O    HOH A   632              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS A  41   CB    CYS A  41   SG     -0.100                       
REMARK 500    CYS B 261   CB    CYS B 261   SG     -0.103                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS A 180   CA  -  CB  -  SG  ANGL. DEV. =   7.9 DEGREES          
REMARK 500    ASP B  50   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    MET B 308   CG  -  SD  -  CE  ANGL. DEV. = -10.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A 271       -0.63     75.67                                   
REMARK 500    ARG B  51      -60.28    -90.37                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ARG A 319         10.25                                           
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  107.8                                              
REMARK 620 3 CYS A  71   SG  113.9 113.0                                        
REMARK 620 4 CYS A  75   SG  106.7 112.5 102.9                                  
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  111.5                                              
REMARK 620 3 HIS A  83   NE2 110.2 103.7                                        
REMARK 620 4 CYS A  87   SG  110.8 112.6 107.7                                  
REMARK 620 N                    1     2     3                                   
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 PRO A 167   O                                                      
REMARK 620 2 PHE A 169   O    91.7                                              
REMARK 620 3 HOH A 873   O    80.0 101.3                                        
REMARK 620 4 HOH A 924   O    94.8  88.5 169.0                                  
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  114.5                                              
REMARK 620 3 CYS A 263   SG  105.7 106.8                                        
REMARK 620 4 CYS A 266   SG  101.5 114.6 113.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 503  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  49   SG                                                     
REMARK 620 2 CYS B  52   SG  107.2                                              
REMARK 620 3 CYS B  71   SG  111.3 111.0                                        
REMARK 620 4 CYS B  75   SG  109.6 116.4 101.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  62   SG                                                     
REMARK 620 2 CYS B  65   SG  109.4                                              
REMARK 620 3 HIS B  83   NE2 112.7 103.1                                        
REMARK 620 4 CYS B  87   SG  111.9 111.9 107.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 504  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PRO B 167   O                                                      
REMARK 620 2 PHE B 169   O    90.0                                              
REMARK 620 3 HOH B 766   O   174.5  94.4                                        
REMARK 620 4 HOH B 848   O    85.8 175.0  90.0                                  
REMARK 620 5 HOH B 852   O    89.7  99.7  86.2  83.0                            
REMARK 620 6 HOH B 853   O    93.4  88.2  90.1  89.4 171.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 208   SG                                                     
REMARK 620 2 CYS B 261   SG  115.0                                              
REMARK 620 3 CYS B 263   SG  108.8 104.0                                        
REMARK 620 4 CYS B 266   SG   94.7 116.3 118.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH A 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH B 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO I 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO J 301                 
DBREF  5HQ8 A    1   428  UNP    Q9H7B4   SMYD3_HUMAN      1    428             
DBREF  5HQ8 B    1   428  UNP    Q9H7B4   SMYD3_HUMAN      1    428             
DBREF  5HQ8 I  250   265  PDB    5HQ8     5HQ8           250    265             
DBREF  5HQ8 J  250   265  PDB    5HQ8     5HQ8           250    265             
SEQADV 5HQ8 GLY A   -3  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 5HQ8 SER A   -2  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 5HQ8 PHE A   -1  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 5HQ8 THR A    0  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 5HQ8 ASN A   13  UNP  Q9H7B4    LYS    13 CONFLICT                       
SEQADV 5HQ8 GLY B   -3  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 5HQ8 SER B   -2  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 5HQ8 PHE B   -1  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 5HQ8 THR B    0  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 5HQ8 ASN B   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                                                  
SEQRES   1 B  432  GLY SER PHE THR MET GLU PRO LEU LYS VAL GLU LYS PHE          
SEQRES   2 B  432  ALA THR ALA ASN ARG GLY ASN GLY LEU ARG ALA VAL THR          
SEQRES   3 B  432  PRO LEU ARG PRO GLY GLU LEU LEU PHE ARG SER ASP PRO          
SEQRES   4 B  432  LEU ALA TYR THR VAL CYS LYS GLY SER ARG GLY VAL VAL          
SEQRES   5 B  432  CYS ASP ARG CYS LEU LEU GLY LYS GLU LYS LEU MET ARG          
SEQRES   6 B  432  CYS SER GLN CYS ARG VAL ALA LYS TYR CYS SER ALA LYS          
SEQRES   7 B  432  CYS GLN LYS LYS ALA TRP PRO ASP HIS LYS ARG GLU CYS          
SEQRES   8 B  432  LYS CYS LEU LYS SER CYS LYS PRO ARG TYR PRO PRO ASP          
SEQRES   9 B  432  SER VAL ARG LEU LEU GLY ARG VAL VAL PHE LYS LEU MET          
SEQRES  10 B  432  ASP GLY ALA PRO SER GLU SER GLU LYS LEU TYR SER PHE          
SEQRES  11 B  432  TYR ASP LEU GLU SER ASN ILE ASN LYS LEU THR GLU ASP          
SEQRES  12 B  432  LYS LYS GLU GLY LEU ARG GLN LEU VAL MET THR PHE GLN          
SEQRES  13 B  432  HIS PHE MET ARG GLU GLU ILE GLN ASP ALA SER GLN LEU          
SEQRES  14 B  432  PRO PRO ALA PHE ASP LEU PHE GLU ALA PHE ALA LYS VAL          
SEQRES  15 B  432  ILE CYS ASN SER PHE THR ILE CYS ASN ALA GLU MET GLN          
SEQRES  16 B  432  GLU VAL GLY VAL GLY LEU TYR PRO SER ILE SER LEU LEU          
SEQRES  17 B  432  ASN HIS SER CYS ASP PRO ASN CYS SER ILE VAL PHE ASN          
SEQRES  18 B  432  GLY PRO HIS LEU LEU LEU ARG ALA VAL ARG ASP ILE GLU          
SEQRES  19 B  432  VAL GLY GLU GLU LEU THR ILE CYS TYR LEU ASP MET LEU          
SEQRES  20 B  432  MET THR SER GLU GLU ARG ARG LYS GLN LEU ARG ASP GLN          
SEQRES  21 B  432  TYR CYS PHE GLU CYS ASP CYS PHE ARG CYS GLN THR GLN          
SEQRES  22 B  432  ASP LYS ASP ALA ASP MET LEU THR GLY ASP GLU GLN VAL          
SEQRES  23 B  432  TRP LYS GLU VAL GLN GLU SER LEU LYS LYS ILE GLU GLU          
SEQRES  24 B  432  LEU LYS ALA HIS TRP LYS TRP GLU GLN VAL LEU ALA MET          
SEQRES  25 B  432  CYS GLN ALA ILE ILE SER SER ASN SER GLU ARG LEU PRO          
SEQRES  26 B  432  ASP ILE ASN ILE TYR GLN LEU LYS VAL LEU ASP CYS ALA          
SEQRES  27 B  432  MET ASP ALA CYS ILE ASN LEU GLY LEU LEU GLU GLU ALA          
SEQRES  28 B  432  LEU PHE TYR GLY THR ARG THR MET GLU PRO TYR ARG ILE          
SEQRES  29 B  432  PHE PHE PRO GLY SER HIS PRO VAL ARG GLY VAL GLN VAL          
SEQRES  30 B  432  MET LYS VAL GLY LYS LEU GLN LEU HIS GLN GLY MET PHE          
SEQRES  31 B  432  PRO GLN ALA MET LYS ASN LEU ARG LEU ALA PHE ASP ILE          
SEQRES  32 B  432  MET ARG VAL THR HIS GLY ARG GLU HIS SER LEU ILE GLU          
SEQRES  33 B  432  ASP LEU ILE LEU LEU LEU GLU GLU CYS ASP ALA ASN ILE          
SEQRES  34 B  432  ARG ALA SER                                                  
SEQRES   1 I   16  TYR ASP ASN PRO ILE PHE GLU LYS PHE GLY LYS GLY GLY          
SEQRES   2 I   16  THR TYR NH2                                                  
SEQRES   1 J   16  TYR ASP ASN PRO ILE PHE GLU LYS PHE GLY LYS GLY GLY          
SEQRES   2 J   16  THR TYR NH2                                                  
HET     ZN  A 501       1                                                       
HET     ZN  A 502       1                                                       
HET     ZN  A 503       1                                                       
HET     MG  A 504       1                                                       
HET    EDO  A 505       4                                                       
HET    EDO  A 506       4                                                       
HET    SAH  A 507      26                                                       
HET     ZN  B 501       1                                                       
HET     ZN  B 502       1                                                       
HET     ZN  B 503       1                                                       
HET     MG  B 504       1                                                       
HET    EDO  B 505       4                                                       
HET    GOL  B 506       6                                                       
HET    EDO  B 507       4                                                       
HET    SAH  B 508      26                                                       
HET    EDO  I 301       4                                                       
HET    EDO  J 301       4                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
HETNAM     GOL GLYCEROL                                                         
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5   ZN    6(ZN 2+)                                                     
FORMUL   8   MG    2(MG 2+)                                                     
FORMUL   9  EDO    6(C2 H6 O2)                                                  
FORMUL  11  SAH    2(C14 H20 N6 O5 S)                                           
FORMUL  17  GOL    C3 H8 O3                                                     
FORMUL  22  HOH   *717(H2 O)                                                    
HELIX    1 AA1 LYS A   42  ARG A   45  5                                   4    
HELIX    2 AA2 SER A   72  LYS A   94  1                                  23    
HELIX    3 AA3 PRO A   99  LEU A  112  1                                  14    
HELIX    4 AA4 SER A  118  LYS A  122  5                                   5    
HELIX    5 AA5 SER A  125  LEU A  129  5                                   5    
HELIX    6 AA6 ASN A  132  LEU A  136  5                                   5    
HELIX    7 AA7 THR A  137  MET A  155  1                                  19    
HELIX    8 AA8 ASP A  161  LEU A  165  5                                   5    
HELIX    9 AA9 ASP A  170  SER A  182  1                                  13    
HELIX   10 AB1 SER A  200  LEU A  204  5                                   5    
HELIX   11 AB2 THR A  245  CYS A  258  1                                  14    
HELIX   12 AB3 CYS A  263  GLN A  269  1                                   7    
HELIX   13 AB4 LYS A  271  LEU A  276  1                                   6    
HELIX   14 AB5 ASP A  279  HIS A  299  1                                  21    
HELIX   15 AB6 LYS A  301  ASN A  316  1                                  16    
HELIX   16 AB7 ASN A  324  GLY A  342  1                                  19    
HELIX   17 AB8 LEU A  343  THR A  354  1                                  12    
HELIX   18 AB9 THR A  354  PHE A  362  1                                   9    
HELIX   19 AC1 HIS A  366  GLN A  383  1                                  18    
HELIX   20 AC2 MET A  385  HIS A  404  1                                  20    
HELIX   21 AC3 SER A  409  SER A  428  1                                  20    
HELIX   22 AC4 LYS B   42  ARG B   45  5                                   4    
HELIX   23 AC5 SER B   72  LYS B   84  1                                  13    
HELIX   24 AC6 GLU B   86  LYS B   94  1                                   9    
HELIX   25 AC7 PRO B   99  LEU B  112  1                                  14    
HELIX   26 AC8 SER B  118  LYS B  122  5                                   5    
HELIX   27 AC9 SER B  125  LEU B  129  5                                   5    
HELIX   28 AD1 ASN B  132  LEU B  136  5                                   5    
HELIX   29 AD2 THR B  137  MET B  155  1                                  19    
HELIX   30 AD3 ASP B  161  LEU B  165  5                                   5    
HELIX   31 AD4 ASP B  170  SER B  182  1                                  13    
HELIX   32 AD5 SER B  200  LEU B  204  5                                   5    
HELIX   33 AD6 THR B  245  CYS B  258  1                                  14    
HELIX   34 AD7 CYS B  263  GLN B  269  1                                   7    
HELIX   35 AD8 LYS B  271  LEU B  276  1                                   6    
HELIX   36 AD9 ASP B  279  HIS B  299  1                                  21    
HELIX   37 AE1 LYS B  301  ASN B  316  1                                  16    
HELIX   38 AE2 ASN B  324  GLY B  342  1                                  19    
HELIX   39 AE3 LEU B  343  ARG B  353  1                                  11    
HELIX   40 AE4 THR B  354  PHE B  362  1                                   9    
HELIX   41 AE5 HIS B  366  GLN B  383  1                                  18    
HELIX   42 AE6 MET B  385  HIS B  404  1                                  20    
HELIX   43 AE7 HIS B  408  ALA B  427  1                                  20    
SHEET    1 AA1 4 VAL A   6  ALA A  10  0                                        
SHEET    2 AA1 4 ASN A  16  ALA A  20 -1  O  ARG A  19   N  GLU A   7           
SHEET    3 AA1 4 GLU A 234  ILE A 237 -1  O  LEU A 235   N  LEU A  18           
SHEET    4 AA1 4 ASN A 205  HIS A 206  1  N  ASN A 205   O  ILE A 237           
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 221   N  SER A  33           
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  VAL A 193           
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 VAL B   6  ALA B  10  0                                        
SHEET    2 AA5 2 ASN B  16  ALA B  20 -1  O  GLY B  17   N  PHE B   9           
SHEET    1 AA6 3 LEU B  29  SER B  33  0                                        
SHEET    2 AA6 3 HIS B 220  ALA B 225 -1  O  LEU B 221   N  SER B  33           
SHEET    3 AA6 3 CYS B 212  ASN B 217 -1  N  ASN B 217   O  HIS B 220           
SHEET    1 AA7 3 ALA B  37  VAL B  40  0                                        
SHEET    2 AA7 3 GLU B 192  LEU B 197 -1  O  LEU B 197   N  ALA B  37           
SHEET    3 AA7 3 PHE B 183  CYS B 186 -1  N  PHE B 183   O  GLY B 196           
SHEET    1 AA8 2 MET B  60  ARG B  61  0                                        
SHEET    2 AA8 2 LYS B  69  TYR B  70 -1  O  TYR B  70   N  MET B  60           
SHEET    1 AA9 2 ASN B 205  HIS B 206  0                                        
SHEET    2 AA9 2 THR B 236  ILE B 237  1  O  ILE B 237   N  ASN B 205           
LINK         SG  CYS A  49                ZN    ZN A 503     1555   1555  2.38  
LINK         SG  CYS A  52                ZN    ZN A 503     1555   1555  2.29  
LINK         SG  CYS A  62                ZN    ZN A 502     1555   1555  2.32  
LINK         SG  CYS A  65                ZN    ZN A 502     1555   1555  2.28  
LINK         SG  CYS A  71                ZN    ZN A 503     1555   1555  2.32  
LINK         SG  CYS A  75                ZN    ZN A 503     1555   1555  2.09  
LINK         NE2 HIS A  83                ZN    ZN A 502     1555   1555  2.08  
LINK         SG  CYS A  87                ZN    ZN A 502     1555   1555  2.37  
LINK         O   PRO A 167                MG    MG A 504     1555   1555  2.43  
LINK         O   PHE A 169                MG    MG A 504     1555   1555  2.42  
LINK         SG  CYS A 208                ZN    ZN A 501     1555   1555  2.38  
LINK         SG  CYS A 261                ZN    ZN A 501     1555   1555  2.34  
LINK         SG  CYS A 263                ZN    ZN A 501     1555   1555  2.32  
LINK         SG  CYS A 266                ZN    ZN A 501     1555   1555  2.33  
LINK         SG  CYS B  49                ZN    ZN B 503     1555   1555  2.35  
LINK         SG  CYS B  52                ZN    ZN B 503     1555   1555  2.31  
LINK         SG  CYS B  62                ZN    ZN B 502     1555   1555  2.34  
LINK         SG  CYS B  65                ZN    ZN B 502     1555   1555  2.30  
LINK         SG  CYS B  71                ZN    ZN B 503     1555   1555  2.37  
LINK         SG  CYS B  75                ZN    ZN B 503     1555   1555  2.26  
LINK         NE2 HIS B  83                ZN    ZN B 502     1555   1555  2.08  
LINK         SG  CYS B  87                ZN    ZN B 502     1555   1555  2.32  
LINK         O   PRO B 167                MG    MG B 504     1555   1555  2.41  
LINK         O   PHE B 169                MG    MG B 504     1555   1555  2.49  
LINK         SG  CYS B 208                ZN    ZN B 501     1555   1555  2.37  
LINK         SG  CYS B 261                ZN    ZN B 501     1555   1555  2.32  
LINK         SG  CYS B 263                ZN    ZN B 501     1555   1555  2.39  
LINK         SG  CYS B 266                ZN    ZN B 501     1555   1555  2.34  
LINK        MG    MG A 504                 O   HOH A 873     1555   1555  2.21  
LINK        MG    MG A 504                 O   HOH A 924     1555   1555  2.21  
LINK        MG    MG B 504                 O   HOH B 766     1555   1555  2.13  
LINK        MG    MG B 504                 O   HOH B 848     1555   1555  2.22  
LINK        MG    MG B 504                 O   HOH B 852     1555   1555  2.16  
LINK        MG    MG B 504                 O   HOH B 853     1555   1555  2.26  
CISPEP   1 LYS A   94    PRO A   95          0        -0.13                     
CISPEP   2 LYS B   94    PRO B   95          0         1.38                     
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  4 PRO A 167  PHE A 169  HOH A 873  HOH A 924                    
SITE     1 AC5  3 LEU A 344  HIS A 382  GLN A 383                               
SITE     1 AC6  7 CYS A 238  LEU A 240  MET A 242  HIS A 366                    
SITE     2 AC6  7 HOH A 710  GLY I 262  TYR I 264                               
SITE     1 AC7 23 ARG A  14  GLY A  15  ASN A  16  TYR A 124                    
SITE     2 AC7 23 GLU A 130  ASN A 132  CYS A 180  ASN A 181                    
SITE     3 AC7 23 SER A 202  LEU A 204  ASN A 205  HIS A 206                    
SITE     4 AC7 23 TYR A 239  TYR A 257  PHE A 259  HOH A 671                    
SITE     5 AC7 23 HOH A 698  HOH A 753  HOH A 789  HOH A 804                    
SITE     6 AC7 23 HOH A 865  HOH A 878  LYS I 260                               
SITE     1 AC8  4 CYS B 208  CYS B 261  CYS B 263  CYS B 266                    
SITE     1 AC9  4 CYS B  62  CYS B  65  HIS B  83  CYS B  87                    
SITE     1 AD1  4 CYS B  49  CYS B  52  CYS B  71  CYS B  75                    
SITE     1 AD2  6 PRO B 167  PHE B 169  HOH B 766  HOH B 848                    
SITE     2 AD2  6 HOH B 852  HOH B 853                                          
SITE     1 AD3  8 THR B 184  CYS B 186  ILE B 214  PHE B 216                    
SITE     2 AD3  8 HOH B 649  GLY J 261  GLY J 262  HOH J 401                    
SITE     1 AD4  7 GLN B 152  ILE B 159  ALA B 162  LEU B 171                    
SITE     2 AD4  7 HOH B 607  HOH B 616  HOH B 786                               
SITE     1 AD5  7 CYS B 238  LEU B 240  MET B 242  HIS B 366                    
SITE     2 AD5  7 HOH B 762  GLY J 262  TYR J 264                               
SITE     1 AD6 20 ARG B  14  ASN B  16  TYR B 124  ASN B 132                    
SITE     2 AD6 20 CYS B 180  ASN B 181  SER B 202  LEU B 204                    
SITE     3 AD6 20 ASN B 205  HIS B 206  TYR B 239  TYR B 257                    
SITE     4 AD6 20 PHE B 259  HOH B 611  HOH B 638  HOH B 642                    
SITE     5 AD6 20 HOH B 716  HOH B 721  HOH B 763  LYS J 260                    
SITE     1 AD7  5 GLU A 192  GLY I 261  HOH I 405  HOH I 406                    
SITE     2 AD7  5 HOH I 407                                                     
SITE     1 AD8  3 GLU B 192  GLY J 261  HOH J 405                               
CRYST1   53.109  118.155   84.782  90.00  90.61  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018829  0.000000  0.000200        0.00000                         
SCALE2      0.000000  0.008463  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011796        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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