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Database: PDB
Entry: 3PDN
LinkDB: 3PDN
Original site: 3PDN 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       23-OCT-10   3PDN              
TITLE     CRYSTAL STRUCTURE OF SMYD3 IN COMPLEX WITH METHYLTRANSFERASE INHIBITOR
TITLE    2 SINEFUNGIN                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SET AND MYND DOMAIN-CONTAINING PROTEIN 3;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ZINC FINGER MYND DOMAIN-CONTAINING PROTEIN 1;               
COMPND   5 EC: 2.1.1.43;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SMYD3, ZMYND1, ZNFN3A1;                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ROSSMANN FOLD, ZINC FINGER, METHYLTRANSFERASE, TRANSFERASE,           
KEYWDS   2 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.SIRINUPONG,J.BRUNZELLE,Z.YANG                                       
REVDAT   4   09-FEB-11 3PDN    1       JRNL                                     
REVDAT   3   19-JAN-11 3PDN    1       JRNL                                     
REVDAT   2   15-DEC-10 3PDN    1       JRNL                                     
REVDAT   1   17-NOV-10 3PDN    0                                                
JRNL        AUTH   N.SIRINUPONG,J.BRUNZELLE,E.DOKO,Z.YANG                       
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE AUTOINHIBITION AND              
JRNL        TITL 2 POSTTRANSLATIONAL ACTIVATION OF HISTONE METHYLTRANSFERASE    
JRNL        TITL 3 SMYD3.                                                       
JRNL        REF    J.MOL.BIOL.                   V. 406   149 2011              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   21167177                                                     
JRNL        DOI    10.1016/J.JMB.2010.12.014                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.8.0                                         
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,              
REMARK   3               : MATTHEWS,TEN EYCK,TRONRUD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.45                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 48667                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.157                          
REMARK   3   R VALUE            (WORKING SET)  : 0.155                          
REMARK   3   FREE R VALUE                      : 0.189                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.070                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2467                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.70                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.74                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 3527                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.1919                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 3352                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.1899                   
REMARK   3   BIN FREE R VALUE                        : 0.2312                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.96                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 175                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3390                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 68                                      
REMARK   3   SOLVENT ATOMS            : 645                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.12                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.67170                                             
REMARK   3    B22 (A**2) : 3.34170                                              
REMARK   3    B33 (A**2) : 1.33000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.17                
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.946                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3606   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 4871   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1737   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 98     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 517    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3606   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : NULL   ; NULL   ; NULL                
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : NULL   ; NULL   ; NULL                
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.93                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : NULL                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : NULL                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 2:21)                               
REMARK   3    ORIGIN FOR THE GROUP (A):   28.1299   23.0479   25.8451           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0602 T22:   -0.0099                                    
REMARK   3     T33:    0.0117 T12:    0.0102                                    
REMARK   3     T13:   -0.0230 T23:   -0.0191                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.3674 L22:    1.9883                                    
REMARK   3     L33:    2.1325 L12:    0.0799                                    
REMARK   3     L13:   -0.4018 L23:    1.5736                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0300 S12:   -0.1867 S13:    0.1810                     
REMARK   3     S21:   -0.0024 S22:    0.1350 S23:   -0.4563                     
REMARK   3     S31:   -0.0689 S32:    0.2213 S33:   -0.1049                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 22:68)                              
REMARK   3    ORIGIN FOR THE GROUP (A):   18.3844   33.7693    3.3938           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0146 T22:   -0.0344                                    
REMARK   3     T33:   -0.0170 T12:    0.0129                                    
REMARK   3     T13:    0.0422 T23:    0.0080                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.2633 L22:    0.5482                                    
REMARK   3     L33:    1.5282 L12:    0.2554                                    
REMARK   3     L13:   -0.2524 L23:    0.5867                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0265 S12:    0.0692 S13:    0.0982                     
REMARK   3     S21:   -0.1764 S22:    0.0784 S23:   -0.0689                     
REMARK   3     S31:   -0.2833 S32:   -0.0658 S33:   -0.1050                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 69:96)                              
REMARK   3    ORIGIN FOR THE GROUP (A):   18.3233   27.6623   -9.2425           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0082 T22:    0.0204                                    
REMARK   3     T33:   -0.0373 T12:   -0.0113                                    
REMARK   3     T13:    0.0252 T23:    0.0257                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.6937 L22:    7.0625                                    
REMARK   3     L33:    4.2959 L12:    2.1517                                    
REMARK   3     L13:   -0.3066 L23:   -2.8098                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0216 S12:    0.0933 S13:    0.0519                     
REMARK   3     S21:   -0.3449 S22:    0.2759 S23:    0.0225                     
REMARK   3     S31:    0.0386 S32:   -0.2666 S33:   -0.2543                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 97:175)                             
REMARK   3    ORIGIN FOR THE GROUP (A):   16.4333   14.5196    4.8679           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0325 T22:   -0.0305                                    
REMARK   3     T33:   -0.0471 T12:    0.0012                                    
REMARK   3     T13:    0.0110 T23:   -0.0020                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.6727 L22:    0.8565                                    
REMARK   3     L33:    1.2120 L12:    0.4255                                    
REMARK   3     L13:   -0.3152 L23:   -0.3263                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0438 S12:    0.0538 S13:    0.0224                     
REMARK   3     S21:   -0.1262 S22:    0.0565 S23:   -0.0229                     
REMARK   3     S31:    0.1096 S32:    0.0129 S33:   -0.0126                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 176:278)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   12.9479   29.3928   21.8237           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0234 T22:   -0.0176                                    
REMARK   3     T33:   -0.0130 T12:   -0.0022                                    
REMARK   3     T13:    0.0025 T23:   -0.0075                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.1503 L22:    0.5972                                    
REMARK   3     L33:    0.6702 L12:   -0.1738                                    
REMARK   3     L13:   -0.3284 L23:    0.3071                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0362 S12:   -0.0129 S13:    0.0342                     
REMARK   3     S21:   -0.0025 S22:   -0.0013 S23:   -0.0462                     
REMARK   3     S31:   -0.0378 S32:    0.0332 S33:   -0.0349                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 279:303)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   -5.7832   36.5863   12.6950           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0058 T22:    0.0069                                    
REMARK   3     T33:   -0.0088 T12:    0.0226                                    
REMARK   3     T13:   -0.0245 T23:   -0.0343                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.5885 L22:    1.6883                                    
REMARK   3     L33:    3.1235 L12:   -0.1412                                    
REMARK   3     L13:   -1.5822 L23:   -0.5570                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0406 S12:    0.1469 S13:   -0.1335                     
REMARK   3     S21:   -0.2301 S22:   -0.1417 S23:    0.0340                     
REMARK   3     S31:    0.1635 S32:   -0.0723 S33:    0.1011                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 304:380)                            
REMARK   3    ORIGIN FOR THE GROUP (A):    0.8880   46.8557   17.2920           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0048 T22:   -0.0630                                    
REMARK   3     T33:   -0.0560 T12:    0.0170                                    
REMARK   3     T13:    0.0323 T23:   -0.0002                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.2777 L22:    1.0991                                    
REMARK   3     L33:    0.7193 L12:   -0.3370                                    
REMARK   3     L13:   -0.1973 L23:    0.1005                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1394 S12:    0.0596 S13:    0.0491                     
REMARK   3     S21:   -0.1918 S22:   -0.0268 S23:   -0.0293                     
REMARK   3     S31:   -0.1275 S32:   -0.0442 S33:   -0.1127                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 381:428)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   18.5473   55.7122   17.1912           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0090 T22:   -0.0773                                    
REMARK   3     T33:    0.1305 T12:   -0.0304                                    
REMARK   3     T13:    0.1099 T23:   -0.0261                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.4675 L22:    3.4512                                    
REMARK   3     L33:    0.4185 L12:   -0.9445                                    
REMARK   3     L13:   -0.0167 L23:   -0.2161                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1551 S12:   -0.0371 S13:    0.4156                     
REMARK   3     S21:   -0.1890 S22:   -0.0065 S23:   -0.4331                     
REMARK   3     S31:   -0.1732 S32:    0.0042 S33:   -0.1486                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3PDN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-OCT-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB062250.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-OCT-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
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) : 1.27823, 1.28268                   
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
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          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48766                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 6.900                              
REMARK 200  R MERGE                    (I) : 0.08900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.46                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 13% PEG 3350, 50 MM NA FORMATE, 100 MM   
REMARK 280  TRIS, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K       
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       30.62000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.69200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.12300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       53.69200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.62000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.12300            
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     MET A     1                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A   2    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  57    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  58    CG   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     ARG A 426    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  13       18.38   -144.09                                   
REMARK 500    LYS A 271       -6.92     78.54                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 487        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH A 588        DISTANCE =  6.77 ANGSTROMS                       
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                              MG A 440  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 869   O                                                      
REMARK 620 2 HOH A1006   O    96.7                                              
REMARK 620 3 HOH A1005   O    86.2 177.0                                        
REMARK 620 4 HOH A1004   O    83.4  89.8  91.1                                  
REMARK 620 5 HOH A 896   O    94.9  86.6  92.6 175.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 436  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  83   NE2                                                    
REMARK 620 2 CYS A  87   SG  107.4                                              
REMARK 620 3 CYS A  62   SG  113.9 109.2                                        
REMARK 620 4 CYS A  65   SG  103.0 113.0 110.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 439  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 875   O                                                      
REMARK 620 2 HOH A1002   O    91.2                                              
REMARK 620 3 HOH A 932   O    89.5  88.2                                        
REMARK 620 4 HOH A 751   O    86.5 175.9  95.1                                  
REMARK 620 5 HOH A 791   O    93.1  89.9 176.8  86.9                            
REMARK 620 6 HOH A1003   O   170.6  91.9  81.8  90.9  95.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 437  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  75   SG                                                     
REMARK 620 2 CYS A  52   SG  118.7                                              
REMARK 620 3 CYS A  71   SG  103.6 107.9                                        
REMARK 620 4 CYS A  49   SG  108.4 106.1 112.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 438  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 208   SG                                                     
REMARK 620 2 CYS A 261   SG  117.0                                              
REMARK 620 3 CYS A 266   SG  101.4 113.3                                        
REMARK 620 4 CYS A 263   SG  110.9 103.7 110.6                                  
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 SFG A 429                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 430                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 431                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 432                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 433                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 434                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 435                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 436                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 437                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 438                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 439                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 440                  
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THIS SEQUENCE CORRESPONDS TO GENBANK ENTRY BC031010.                 
DBREF  3PDN A    1   428  UNP    Q9H7B4   SMYD3_HUMAN      1    428             
SEQADV 3PDN ASN A   13  UNP  Q9H7B4    LYS    13 SEE REMARK 999                 
SEQADV 3PDN ARG A  140  UNP  Q9H7B4    LYS   140 SEE REMARK 999                 
SEQRES   1 A  428  MET GLU PRO LEU LYS VAL GLU LYS PHE ALA THR ALA ASN          
SEQRES   2 A  428  ARG GLY ASN GLY LEU ARG ALA VAL THR PRO LEU ARG PRO          
SEQRES   3 A  428  GLY GLU LEU LEU PHE ARG SER ASP PRO LEU ALA TYR THR          
SEQRES   4 A  428  VAL CYS LYS GLY SER ARG GLY VAL VAL CYS ASP ARG CYS          
SEQRES   5 A  428  LEU LEU GLY LYS GLU LYS LEU MET ARG CYS SER GLN CYS          
SEQRES   6 A  428  ARG VAL ALA LYS TYR CYS SER ALA LYS CYS GLN LYS LYS          
SEQRES   7 A  428  ALA TRP PRO ASP HIS LYS ARG GLU CYS LYS CYS LEU LYS          
SEQRES   8 A  428  SER CYS LYS PRO ARG TYR PRO PRO ASP SER VAL ARG LEU          
SEQRES   9 A  428  LEU GLY ARG VAL VAL PHE LYS LEU MET ASP GLY ALA PRO          
SEQRES  10 A  428  SER GLU SER GLU LYS LEU TYR SER PHE TYR ASP LEU GLU          
SEQRES  11 A  428  SER ASN ILE ASN LYS LEU THR GLU ASP ARG LYS GLU GLY          
SEQRES  12 A  428  LEU ARG GLN LEU VAL MET THR PHE GLN HIS PHE MET ARG          
SEQRES  13 A  428  GLU GLU ILE GLN ASP ALA SER GLN LEU PRO PRO ALA PHE          
SEQRES  14 A  428  ASP LEU PHE GLU ALA PHE ALA LYS VAL ILE CYS ASN SER          
SEQRES  15 A  428  PHE THR ILE CYS ASN ALA GLU MET GLN GLU VAL GLY VAL          
SEQRES  16 A  428  GLY LEU TYR PRO SER ILE SER LEU LEU ASN HIS SER CYS          
SEQRES  17 A  428  ASP PRO ASN CYS SER ILE VAL PHE ASN GLY PRO HIS LEU          
SEQRES  18 A  428  LEU LEU ARG ALA VAL ARG ASP ILE GLU VAL GLY GLU GLU          
SEQRES  19 A  428  LEU THR ILE CYS TYR LEU ASP MET LEU MET THR SER GLU          
SEQRES  20 A  428  GLU ARG ARG LYS GLN LEU ARG ASP GLN TYR CYS PHE GLU          
SEQRES  21 A  428  CYS ASP CYS PHE ARG CYS GLN THR GLN ASP LYS ASP ALA          
SEQRES  22 A  428  ASP MET LEU THR GLY ASP GLU GLN VAL TRP LYS GLU VAL          
SEQRES  23 A  428  GLN GLU SER LEU LYS LYS ILE GLU GLU LEU LYS ALA HIS          
SEQRES  24 A  428  TRP LYS TRP GLU GLN VAL LEU ALA MET CYS GLN ALA ILE          
SEQRES  25 A  428  ILE SER SER ASN SER GLU ARG LEU PRO ASP ILE ASN ILE          
SEQRES  26 A  428  TYR GLN LEU LYS VAL LEU ASP CYS ALA MET ASP ALA CYS          
SEQRES  27 A  428  ILE ASN LEU GLY LEU LEU GLU GLU ALA LEU PHE TYR GLY          
SEQRES  28 A  428  THR ARG THR MET GLU PRO TYR ARG ILE PHE PHE PRO GLY          
SEQRES  29 A  428  SER HIS PRO VAL ARG GLY VAL GLN VAL MET LYS VAL GLY          
SEQRES  30 A  428  LYS LEU GLN LEU HIS GLN GLY MET PHE PRO GLN ALA MET          
SEQRES  31 A  428  LYS ASN LEU ARG LEU ALA PHE ASP ILE MET ARG VAL THR          
SEQRES  32 A  428  HIS GLY ARG GLU HIS SER LEU ILE GLU ASP LEU ILE LEU          
SEQRES  33 A  428  LEU LEU GLU GLU CYS ASP ALA ASN ILE ARG ALA SER              
HET    SFG  A 429      27                                                       
HET    GOL  A 430       6                                                       
HET    GOL  A 431       6                                                       
HET    GOL  A 432       6                                                       
HET    GOL  A 433       6                                                       
HET    GOL  A 434       6                                                       
HET    GOL  A 435       6                                                       
HET     ZN  A 436       1                                                       
HET     ZN  A 437       1                                                       
HET     ZN  A 438       1                                                       
HET     MG  A 439       1                                                       
HET     MG  A 440       1                                                       
HETNAM     SFG ADENOSYL-ORNITHINE                                               
HETNAM     GOL GLYCEROL                                                         
HETNAM      ZN ZINC ION                                                         
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  SFG    C15 H23 N7 O5                                                
FORMUL   3  GOL    6(C3 H8 O3)                                                  
FORMUL   9   ZN    3(ZN 2+)                                                     
FORMUL  12   MG    2(MG 2+)                                                     
FORMUL  14  HOH   *645(H2 O)                                                    
HELIX    1   1 SER A   72  CYS A   93  1                                  22    
HELIX    2   2 PRO A   99  GLY A  115  1                                  17    
HELIX    3   3 SER A  118  LYS A  122  5                                   5    
HELIX    4   4 SER A  125  LEU A  129  5                                   5    
HELIX    5   5 ASN A  132  LEU A  136  5                                   5    
HELIX    6   6 THR A  137  MET A  155  1                                  19    
HELIX    7   7 ASP A  161  LEU A  165  5                                   5    
HELIX    8   8 ASP A  170  SER A  182  1                                  13    
HELIX    9   9 SER A  200  LEU A  204  5                                   5    
HELIX   10  10 THR A  245  CYS A  258  1                                  14    
HELIX   11  11 CYS A  263  GLN A  269  1                                   7    
HELIX   12  12 LYS A  271  LEU A  276  1                                   6    
HELIX   13  13 ASP A  279  HIS A  299  1                                  21    
HELIX   14  14 LYS A  301  SER A  314  1                                  14    
HELIX   15  15 ASN A  324  GLY A  342  1                                  19    
HELIX   16  16 LEU A  343  PHE A  362  1                                  20    
HELIX   17  17 HIS A  366  GLN A  383  1                                  18    
HELIX   18  18 MET A  385  HIS A  404  1                                  20    
HELIX   19  19 HIS A  408  ALA A  427  1                                  20    
SHEET    1   A 4 VAL A   6  ALA A  10  0                                        
SHEET    2   A 4 ASN A  16  ALA A  20 -1  O  GLY A  17   N  PHE A   9           
SHEET    3   A 4 GLU A 234  ILE A 237 -1  O  LEU A 235   N  LEU A  18           
SHEET    4   A 4 ASN A 205  HIS A 206  1  N  ASN A 205   O  ILE A 237           
SHEET    1   B 3 LEU A  29  SER A  33  0                                        
SHEET    2   B 3 HIS A 220  ALA A 225 -1  O  LEU A 223   N  PHE A  31           
SHEET    3   B 3 CYS A 212  ASN A 217 -1  N  VAL A 215   O  LEU A 222           
SHEET    1   C 3 ALA A  37  VAL A  40  0                                        
SHEET    2   C 3 GLU A 192  LEU A 197 -1  O  VAL A 195   N  THR A  39           
SHEET    3   C 3 PHE A 183  CYS A 186 -1  N  ILE A 185   O  VAL A 193           
SHEET    1   D 2 MET A  60  ARG A  61  0                                        
SHEET    2   D 2 LYS A  69  TYR A  70 -1  O  TYR A  70   N  MET A  60           
LINK        MG    MG A 440                 O   HOH A 869     1555   1555  1.96  
LINK        MG    MG A 440                 O   HOH A1006     1555   1555  1.98  
LINK        MG    MG A 440                 O   HOH A1005     1555   1555  2.05  
LINK         NE2 HIS A  83                ZN    ZN A 436     1555   1555  2.06  
LINK        MG    MG A 439                 O   HOH A 875     1555   1555  2.09  
LINK        MG    MG A 439                 O   HOH A1002     1555   1555  2.11  
LINK        MG    MG A 439                 O   HOH A 932     1555   1555  2.12  
LINK        MG    MG A 439                 O   HOH A 751     1555   1555  2.13  
LINK        MG    MG A 439                 O   HOH A 791     1555   1555  2.14  
LINK        MG    MG A 439                 O   HOH A1003     1555   1555  2.17  
LINK        MG    MG A 440                 O   HOH A1004     1555   1555  2.18  
LINK        MG    MG A 440                 O   HOH A 896     1555   1555  2.26  
LINK         SG  CYS A  75                ZN    ZN A 437     1555   1555  2.29  
LINK         SG  CYS A  87                ZN    ZN A 436     1555   1555  2.29  
LINK         SG  CYS A  52                ZN    ZN A 437     1555   1555  2.29  
LINK         SG  CYS A  62                ZN    ZN A 436     1555   1555  2.31  
LINK         SG  CYS A 208                ZN    ZN A 438     1555   1555  2.32  
LINK         SG  CYS A 261                ZN    ZN A 438     1555   1555  2.33  
LINK         SG  CYS A  71                ZN    ZN A 437     1555   1555  2.34  
LINK         SG  CYS A 266                ZN    ZN A 438     1555   1555  2.37  
LINK         SG  CYS A 263                ZN    ZN A 438     1555   1555  2.38  
LINK         SG  CYS A  65                ZN    ZN A 436     1555   1555  2.41  
LINK         SG  CYS A  49                ZN    ZN A 437     1555   1555  2.44  
CISPEP   1 LYS A   94    PRO A   95          0         8.42                     
SITE     1 AC1 23 ARG A  14  ASN A  16  TYR A 124  GLU A 130                    
SITE     2 AC1 23 ASN A 132  CYS A 180  ASN A 181  SER A 202                    
SITE     3 AC1 23 LEU A 203  LEU A 204  ASN A 205  HIS A 206                    
SITE     4 AC1 23 TYR A 239  TYR A 257  PHE A 259  GOL A 431                    
SITE     5 AC1 23 HOH A 655  HOH A 670  HOH A 674  HOH A 697                    
SITE     6 AC1 23 HOH A 725  HOH A 766  HOH A 827                               
SITE     1 AC2  8 CYS A 238  LEU A 240  MET A 242  HIS A 366                    
SITE     2 AC2  8 GOL A 432  HOH A 669  HOH A 678  HOH A 837                    
SITE     1 AC3 10 ASN A 181  SER A 182  PHE A 183  SER A 202                    
SITE     2 AC3 10 ILE A 237  TYR A 239  TYR A 257  SFG A 429                    
SITE     3 AC3 10 HOH A 702  HOH A 938                                          
SITE     1 AC4  9 ILE A 214  VAL A 215  HIS A 366  PRO A 367                    
SITE     2 AC4  9 VAL A 368  GOL A 430  HOH A 652  HOH A 693                    
SITE     3 AC4  9 HOH A 779                                                     
SITE     1 AC5  9 PRO A  81  ASP A  82  LYS A 111  GLY A 115                    
SITE     2 AC5  9 GLU A 142  GLN A 146  HOH A 536  HOH A 738                    
SITE     3 AC5  9 HOH A1015                                                     
SITE     1 AC6  6 PHE A 151  GLN A 152  ILE A 159  LEU A 171                    
SITE     2 AC6  6 HOH A 602  HOH A 817                                          
SITE     1 AC7 11 PHE A 126  ALA A 168  PHE A 169  ASP A 170                    
SITE     2 AC7 11 GLU A 173  ALA A 174  LYS A 177  HOH A 461                    
SITE     3 AC7 11 HOH A 528  HOH A 853  HOH A1036                               
SITE     1 AC8  4 CYS A  62  CYS A  65  HIS A  83  CYS A  87                    
SITE     1 AC9  4 CYS A  49  CYS A  52  CYS A  71  CYS A  75                    
SITE     1 BC1  4 CYS A 208  CYS A 261  CYS A 263  CYS A 266                    
SITE     1 BC2  6 HOH A 751  HOH A 791  HOH A 875  HOH A 932                    
SITE     2 BC2  6 HOH A1002  HOH A1003                                          
SITE     1 BC3  5 HOH A 869  HOH A 896  HOH A1004  HOH A1005                    
SITE     2 BC3  5 HOH A1006                                                     
CRYST1   61.240   66.246  107.384  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      0.016329  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015095  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009312        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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