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Database: PDB
Entry: 3RU0
LinkDB: 3RU0
Original site: 3RU0 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       04-MAY-11   3RU0              
TITLE     COCRYSTAL STRUCTURE OF HUMAN SMYD3 WITH INHIBITOR SINEFUNGIN BOUND    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SET AND MYND DOMAIN-CONTAINING PROTEIN 3;                  
COMPND   3 CHAIN: A, B;                                                         
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: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    METHYLTRANSFERASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.W.FOREMAN,M.BROWN,F.PARK,S.EMTAGE,J.HARRISS,C.DAS,L.ZHU,A.CREW,     
AUTHOR   2 L.ARNOLD,S.SHAABAN,P.TUCKER                                          
REVDAT   2   24-AUG-11 3RU0    1       JRNL   VERSN                             
REVDAT   1   18-MAY-11 3RU0    0                                                
JRNL        AUTH   K.W.FOREMAN,M.BROWN,F.PARK,S.EMTAGE,J.HARRISS,C.DAS,L.ZHU,   
JRNL        AUTH 2 A.CREW,L.ARNOLD,S.SHAABAN,P.TUCKER                           
JRNL        TITL   STRUCTURAL AND FUNCTIONAL PROFILING OF THE HUMAN HISTONE     
JRNL        TITL 2 METHYLTRANSFERASE SMYD3.                                     
JRNL        REF    PLOS ONE                      V.   6 22290 2011              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   21779408                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0022290                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.83                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 94957                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.216                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6521                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 60                                      
REMARK   3   SOLVENT ATOMS            : 482                                     
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  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3RU0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAY-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB065375.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-JUL-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 31-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.28146, 1.24294                   
REMARK 200  MONOCHROMATOR                  : DIAMOND                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 94957                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.849                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 21.832                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.06300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.48                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.75UL OF PROTEIN 10MG/ML AND 1MM        
REMARK 280  SINEFUNGIN IN 25MM TRISHCL PH7.6, 150MM NACL, 1MM TCEP AND 0.75UL   
REMARK 280  RESERVOIR SOLUTION: 100MM HEPES PH 7.5, 16% PEG 3350, 200MM         
REMARK 280  MAGNESIUM CHLORIDE , VAPOR DIFFUSION, HANGING DROP, TEMPERATURE     
REMARK 280  294K                                                                
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       59.03650            
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: 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     LEU A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     GLU A   429                                                      
REMARK 465     GLY A   430                                                      
REMARK 465     HIS A   431                                                      
REMARK 465     HIS A   432                                                      
REMARK 465     HIS A   433                                                      
REMARK 465     HIS A   434                                                      
REMARK 465     HIS A   435                                                      
REMARK 465     HIS A   436                                                      
REMARK 465     MET B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 465     LEU B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     PRO B     3                                                      
REMARK 465     ALA B   423                                                      
REMARK 465     ASN B   424                                                      
REMARK 465     ILE B   425                                                      
REMARK 465     ARG B   426                                                      
REMARK 465     ALA B   427                                                      
REMARK 465     SER B   428                                                      
REMARK 465     GLU B   429                                                      
REMARK 465     GLY B   430                                                      
REMARK 465     HIS B   431                                                      
REMARK 465     HIS B   432                                                      
REMARK 465     HIS B   433                                                      
REMARK 465     HIS B   434                                                      
REMARK 465     HIS B   435                                                      
REMARK 465     HIS B   436                                                      
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     LEU A   4    CG   CD1  CD2                                       
REMARK 470     ARG A  25    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  42    CG   CD   CE   NZ                                   
REMARK 470     LYS A  56    CG   CD   CE   NZ                                   
REMARK 470     GLU A  57    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  58    CG   CD   CE   NZ                                   
REMARK 470     ARG A  61    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  74    CG   CD   CE   NZ                                   
REMARK 470     LYS A  77    CG   CD   CE   NZ                                   
REMARK 470     LYS A  78    CG   CD   CE   NZ                                   
REMARK 470     LYS A  84    CD   CE   NZ                                        
REMARK 470     ARG A  96    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 114    CG   OD1  OD2                                       
REMARK 470     GLU A 119    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 134    CG   OD1  ND2                                       
REMARK 470     GLU A 138    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 139    CG   OD1  OD2                                       
REMARK 470     GLU A 142    CD   OE1  OE2                                       
REMARK 470     GLU A 247    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 281    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 292    CD   CE   NZ                                        
REMARK 470     GLU A 295    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 303    CD   OE1  OE2                                       
REMARK 470     GLU A 412    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 426    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 428    OG                                                  
REMARK 470     LEU B   4    CG   CD1  CD2                                       
REMARK 470     ASN B  13    CG   OD1  ND2                                       
REMARK 470     THR B  22    OG1  CG2                                            
REMARK 470     ARG B  25    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  42    CG   CD   CE   NZ                                   
REMARK 470     GLU B  57    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  77    CG   CD   CE   NZ                                   
REMARK 470     ARG B  96    CD   NE   CZ   NH1  NH2                             
REMARK 470     ASP B 114    CG   OD1  OD2                                       
REMARK 470     GLU B 119    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 134    CG   OD1  ND2                                       
REMARK 470     GLU B 138    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 139    CG   OD1  OD2                                       
REMARK 470     GLU B 142    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 145    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU B 173    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 230    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 247    CD   OE1  OE2                                       
REMARK 470     ARG B 250    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 267    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 281    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 284    CG   CD   CE   NZ                                   
REMARK 470     GLU B 295    CD   OE1  OE2                                       
REMARK 470     ARG B 319    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 383    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 391    CG   CD   CE   NZ                                   
REMARK 470     ARG B 394    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 406    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 412    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 416    CG   CD1  CD2                                       
REMARK 470     GLU B 419    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 420    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 422    CG   OD1  OD2                                       
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   461     O    HOH A   658              1.94            
REMARK 500   O    HOH B   577     O    HOH B   615              2.00            
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    ARG B 107   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ASP B 241   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 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    ARG A  51      -64.30    -90.36                                   
REMARK 500    PHE A 362       68.83   -117.80                                   
REMARK 500    PHE B  31      147.20   -172.28                                   
REMARK 500    ASN B 132       29.36     45.32                                   
REMARK 500    PHE B 362       71.65   -119.18                                   
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 B 614        DISTANCE =  5.60 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                              ZN B 439  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  83   NE2                                                    
REMARK 620 2 CYS B  65   SG  108.4                                              
REMARK 620 3 CYS B  62   SG  108.8 111.7                                        
REMARK 620 4 CYS B  87   SG  106.9 112.2 108.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 439  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  83   NE2                                                    
REMARK 620 2 CYS A  65   SG  105.3                                              
REMARK 620 3 CYS A  62   SG  110.9 109.1                                        
REMARK 620 4 CYS A  87   SG  106.0 114.6 110.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 440  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  75   SG                                                     
REMARK 620 2 CYS A  52   SG  114.0                                              
REMARK 620 3 CYS A  49   SG  111.5 108.7                                        
REMARK 620 4 CYS A  71   SG  103.8 108.3 110.4                                  
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 263   SG                                                     
REMARK 620 2 CYS A 266   SG  113.9                                              
REMARK 620 3 CYS A 261   SG  109.3 113.9                                        
REMARK 620 4 CYS A 208   SG  104.0  99.3 115.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 440  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 263   SG                                                     
REMARK 620 2 CYS B 266   SG  123.7                                              
REMARK 620 3 CYS B 261   SG  105.4 109.0                                        
REMARK 620 4 CYS B 208   SG  108.9  98.0 111.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 438  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  71   SG                                                     
REMARK 620 2 CYS B  52   SG  110.8                                              
REMARK 620 3 CYS B  49   SG  109.0 108.1                                        
REMARK 620 4 CYS B  75   SG  102.4 116.5 109.8                                  
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 437                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 438                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 439                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 440                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SFG B 437                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 438                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 439                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 440                  
DBREF  3RU0 A    2   428  UNP    Q9H7B4   SMYD3_HUMAN      2    428             
DBREF  3RU0 B    2   428  UNP    Q9H7B4   SMYD3_HUMAN      2    428             
SEQADV 3RU0 MET A   -1  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3RU0 ALA A    0  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3RU0 LEU A    1  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3RU0 ASN A   13  UNP  Q9H7B4    LYS    13 CONFLICT                       
SEQADV 3RU0 GLU A  429  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3RU0 GLY A  430  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3RU0 HIS A  431  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3RU0 HIS A  432  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3RU0 HIS A  433  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3RU0 HIS A  434  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3RU0 HIS A  435  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3RU0 HIS A  436  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3RU0 MET B   -1  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3RU0 ALA B    0  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3RU0 LEU B    1  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3RU0 ASN B   13  UNP  Q9H7B4    LYS    13 CONFLICT                       
SEQADV 3RU0 GLU B  429  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3RU0 GLY B  430  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3RU0 HIS B  431  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3RU0 HIS B  432  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3RU0 HIS B  433  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3RU0 HIS B  434  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3RU0 HIS B  435  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3RU0 HIS B  436  UNP  Q9H7B4              EXPRESSION TAG                 
SEQRES   1 A  438  MET ALA LEU GLU PRO LEU LYS VAL GLU LYS PHE ALA THR          
SEQRES   2 A  438  ALA ASN ARG GLY ASN GLY LEU ARG ALA VAL THR PRO LEU          
SEQRES   3 A  438  ARG PRO GLY GLU LEU LEU PHE ARG SER ASP PRO LEU ALA          
SEQRES   4 A  438  TYR THR VAL CYS LYS GLY SER ARG GLY VAL VAL CYS ASP          
SEQRES   5 A  438  ARG CYS LEU LEU GLY LYS GLU LYS LEU MET ARG CYS SER          
SEQRES   6 A  438  GLN CYS ARG VAL ALA LYS TYR CYS SER ALA LYS CYS GLN          
SEQRES   7 A  438  LYS LYS ALA TRP PRO ASP HIS LYS ARG GLU CYS LYS CYS          
SEQRES   8 A  438  LEU LYS SER CYS LYS PRO ARG TYR PRO PRO ASP SER VAL          
SEQRES   9 A  438  ARG LEU LEU GLY ARG VAL VAL PHE LYS LEU MET ASP GLY          
SEQRES  10 A  438  ALA PRO SER GLU SER GLU LYS LEU TYR SER PHE TYR ASP          
SEQRES  11 A  438  LEU GLU SER ASN ILE ASN LYS LEU THR GLU ASP LYS LYS          
SEQRES  12 A  438  GLU GLY LEU ARG GLN LEU VAL MET THR PHE GLN HIS PHE          
SEQRES  13 A  438  MET ARG GLU GLU ILE GLN ASP ALA SER GLN LEU PRO PRO          
SEQRES  14 A  438  ALA PHE ASP LEU PHE GLU ALA PHE ALA LYS VAL ILE CYS          
SEQRES  15 A  438  ASN SER PHE THR ILE CYS ASN ALA GLU MET GLN GLU VAL          
SEQRES  16 A  438  GLY VAL GLY LEU TYR PRO SER ILE SER LEU LEU ASN HIS          
SEQRES  17 A  438  SER CYS ASP PRO ASN CYS SER ILE VAL PHE ASN GLY PRO          
SEQRES  18 A  438  HIS LEU LEU LEU ARG ALA VAL ARG ASP ILE GLU VAL GLY          
SEQRES  19 A  438  GLU GLU LEU THR ILE CYS TYR LEU ASP MET LEU MET THR          
SEQRES  20 A  438  SER GLU GLU ARG ARG LYS GLN LEU ARG ASP GLN TYR CYS          
SEQRES  21 A  438  PHE GLU CYS ASP CYS PHE ARG CYS GLN THR GLN ASP LYS          
SEQRES  22 A  438  ASP ALA ASP MET LEU THR GLY ASP GLU GLN VAL TRP LYS          
SEQRES  23 A  438  GLU VAL GLN GLU SER LEU LYS LYS ILE GLU GLU LEU LYS          
SEQRES  24 A  438  ALA HIS TRP LYS TRP GLU GLN VAL LEU ALA MET CYS GLN          
SEQRES  25 A  438  ALA ILE ILE SER SER ASN SER GLU ARG LEU PRO ASP ILE          
SEQRES  26 A  438  ASN ILE TYR GLN LEU LYS VAL LEU ASP CYS ALA MET ASP          
SEQRES  27 A  438  ALA CYS ILE ASN LEU GLY LEU LEU GLU GLU ALA LEU PHE          
SEQRES  28 A  438  TYR GLY THR ARG THR MET GLU PRO TYR ARG ILE PHE PHE          
SEQRES  29 A  438  PRO GLY SER HIS PRO VAL ARG GLY VAL GLN VAL MET LYS          
SEQRES  30 A  438  VAL GLY LYS LEU GLN LEU HIS GLN GLY MET PHE PRO GLN          
SEQRES  31 A  438  ALA MET LYS ASN LEU ARG LEU ALA PHE ASP ILE MET ARG          
SEQRES  32 A  438  VAL THR HIS GLY ARG GLU HIS SER LEU ILE GLU ASP LEU          
SEQRES  33 A  438  ILE LEU LEU LEU GLU GLU CYS ASP ALA ASN ILE ARG ALA          
SEQRES  34 A  438  SER GLU GLY HIS HIS HIS HIS HIS HIS                          
SEQRES   1 B  438  MET ALA LEU GLU PRO LEU LYS VAL GLU LYS PHE ALA THR          
SEQRES   2 B  438  ALA ASN ARG GLY ASN GLY LEU ARG ALA VAL THR PRO LEU          
SEQRES   3 B  438  ARG PRO GLY GLU LEU LEU PHE ARG SER ASP PRO LEU ALA          
SEQRES   4 B  438  TYR THR VAL CYS LYS GLY SER ARG GLY VAL VAL CYS ASP          
SEQRES   5 B  438  ARG CYS LEU LEU GLY LYS GLU LYS LEU MET ARG CYS SER          
SEQRES   6 B  438  GLN CYS ARG VAL ALA LYS TYR CYS SER ALA LYS CYS GLN          
SEQRES   7 B  438  LYS LYS ALA TRP PRO ASP HIS LYS ARG GLU CYS LYS CYS          
SEQRES   8 B  438  LEU LYS SER CYS LYS PRO ARG TYR PRO PRO ASP SER VAL          
SEQRES   9 B  438  ARG LEU LEU GLY ARG VAL VAL PHE LYS LEU MET ASP GLY          
SEQRES  10 B  438  ALA PRO SER GLU SER GLU LYS LEU TYR SER PHE TYR ASP          
SEQRES  11 B  438  LEU GLU SER ASN ILE ASN LYS LEU THR GLU ASP LYS LYS          
SEQRES  12 B  438  GLU GLY LEU ARG GLN LEU VAL MET THR PHE GLN HIS PHE          
SEQRES  13 B  438  MET ARG GLU GLU ILE GLN ASP ALA SER GLN LEU PRO PRO          
SEQRES  14 B  438  ALA PHE ASP LEU PHE GLU ALA PHE ALA LYS VAL ILE CYS          
SEQRES  15 B  438  ASN SER PHE THR ILE CYS ASN ALA GLU MET GLN GLU VAL          
SEQRES  16 B  438  GLY VAL GLY LEU TYR PRO SER ILE SER LEU LEU ASN HIS          
SEQRES  17 B  438  SER CYS ASP PRO ASN CYS SER ILE VAL PHE ASN GLY PRO          
SEQRES  18 B  438  HIS LEU LEU LEU ARG ALA VAL ARG ASP ILE GLU VAL GLY          
SEQRES  19 B  438  GLU GLU LEU THR ILE CYS TYR LEU ASP MET LEU MET THR          
SEQRES  20 B  438  SER GLU GLU ARG ARG LYS GLN LEU ARG ASP GLN TYR CYS          
SEQRES  21 B  438  PHE GLU CYS ASP CYS PHE ARG CYS GLN THR GLN ASP LYS          
SEQRES  22 B  438  ASP ALA ASP MET LEU THR GLY ASP GLU GLN VAL TRP LYS          
SEQRES  23 B  438  GLU VAL GLN GLU SER LEU LYS LYS ILE GLU GLU LEU LYS          
SEQRES  24 B  438  ALA HIS TRP LYS TRP GLU GLN VAL LEU ALA MET CYS GLN          
SEQRES  25 B  438  ALA ILE ILE SER SER ASN SER GLU ARG LEU PRO ASP ILE          
SEQRES  26 B  438  ASN ILE TYR GLN LEU LYS VAL LEU ASP CYS ALA MET ASP          
SEQRES  27 B  438  ALA CYS ILE ASN LEU GLY LEU LEU GLU GLU ALA LEU PHE          
SEQRES  28 B  438  TYR GLY THR ARG THR MET GLU PRO TYR ARG ILE PHE PHE          
SEQRES  29 B  438  PRO GLY SER HIS PRO VAL ARG GLY VAL GLN VAL MET LYS          
SEQRES  30 B  438  VAL GLY LYS LEU GLN LEU HIS GLN GLY MET PHE PRO GLN          
SEQRES  31 B  438  ALA MET LYS ASN LEU ARG LEU ALA PHE ASP ILE MET ARG          
SEQRES  32 B  438  VAL THR HIS GLY ARG GLU HIS SER LEU ILE GLU ASP LEU          
SEQRES  33 B  438  ILE LEU LEU LEU GLU GLU CYS ASP ALA ASN ILE ARG ALA          
SEQRES  34 B  438  SER GLU GLY HIS HIS HIS HIS HIS HIS                          
HET    SFG  A 437      27                                                       
HET     ZN  A 438       1                                                       
HET     ZN  A 439       1                                                       
HET     ZN  A 440       1                                                       
HET    SFG  B 437      27                                                       
HET     ZN  B 438       1                                                       
HET     ZN  B 439       1                                                       
HET     ZN  B 440       1                                                       
HETNAM     SFG SINEFUNGIN                                                       
HETNAM      ZN ZINC ION                                                         
HETSYN     SFG ADENOSYL-ORNITHINE                                               
FORMUL   3  SFG    2(C15 H23 N7 O5)                                             
FORMUL   4   ZN    6(ZN 2+)                                                     
FORMUL  11  HOH   *482(H2 O)                                                    
HELIX    1   1 SER A   72  LYS A   84  1                                  13    
HELIX    2   2 GLU A   86  LYS A   94  1                                   9    
HELIX    3   3 PRO A   99  LEU A  112  1                                  14    
HELIX    4   4 SER A  118  LYS A  122  5                                   5    
HELIX    5   5 SER A  125  LEU A  129  5                                   5    
HELIX    6   6 ASN A  132  LEU A  136  5                                   5    
HELIX    7   7 THR A  137  MET A  155  1                                  19    
HELIX    8   8 ASP A  161  LEU A  165  5                                   5    
HELIX    9   9 ASP A  170  SER A  182  1                                  13    
HELIX   10  10 SER A  200  LEU A  204  5                                   5    
HELIX   11  11 THR A  245  CYS A  258  1                                  14    
HELIX   12  12 CYS A  263  THR A  268  1                                   6    
HELIX   13  13 LYS A  271  LEU A  276  1                                   6    
HELIX   14  14 ASP A  279  HIS A  299  1                                  21    
HELIX   15  15 LYS A  301  SER A  317  1                                  17    
HELIX   16  16 ASN A  324  LEU A  341  1                                  18    
HELIX   17  17 LEU A  343  PHE A  362  1                                  20    
HELIX   18  18 HIS A  366  GLN A  383  1                                  18    
HELIX   19  19 MET A  385  HIS A  404  1                                  20    
HELIX   20  20 HIS A  408  SER A  428  1                                  21    
HELIX   21  21 LYS B   42  ARG B   45  5                                   4    
HELIX   22  22 SER B   72  LYS B   84  1                                  13    
HELIX   23  23 GLU B   86  LYS B   94  1                                   9    
HELIX   24  24 PRO B   99  LEU B  112  1                                  14    
HELIX   25  25 SER B  118  LYS B  122  5                                   5    
HELIX   26  26 ASN B  132  LEU B  136  5                                   5    
HELIX   27  27 THR B  137  MET B  155  1                                  19    
HELIX   28  28 ASP B  161  LEU B  165  5                                   5    
HELIX   29  29 ASP B  170  SER B  182  1                                  13    
HELIX   30  30 SER B  200  LEU B  204  5                                   5    
HELIX   31  31 THR B  245  CYS B  258  1                                  14    
HELIX   32  32 CYS B  263  GLN B  269  1                                   7    
HELIX   33  33 LYS B  271  LEU B  276  1                                   6    
HELIX   34  34 ASP B  279  HIS B  299  1                                  21    
HELIX   35  35 LYS B  301  ASN B  316  1                                  16    
HELIX   36  36 ASN B  324  GLY B  342  1                                  19    
HELIX   37  37 LEU B  343  THR B  354  1                                  12    
HELIX   38  38 THR B  354  PHE B  362  1                                   9    
HELIX   39  39 HIS B  366  GLN B  383  1                                  18    
HELIX   40  40 MET B  385  HIS B  404  1                                  20    
HELIX   41  41 HIS B  408  ASP B  422  1                                  15    
SHEET    1   A 4 VAL A   6  ALA A  10  0                                        
SHEET    2   A 4 ASN A  16  ALA A  20 -1  O  ARG A  19   N  GLU A   7           
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 221   N  SER A  33           
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           
SHEET    1   E 4 VAL B   6  ALA B  10  0                                        
SHEET    2   E 4 ASN B  16  ALA B  20 -1  O  GLY B  17   N  PHE B   9           
SHEET    3   E 4 GLU B 234  ILE B 237 -1  O  LEU B 235   N  LEU B  18           
SHEET    4   E 4 ASN B 205  HIS B 206  1  N  ASN B 205   O  ILE B 237           
SHEET    1   F 3 LEU B  29  SER B  33  0                                        
SHEET    2   F 3 HIS B 220  ALA B 225 -1  O  LEU B 223   N  LEU B  30           
SHEET    3   F 3 CYS B 212  ASN B 217 -1  N  ASN B 217   O  HIS B 220           
SHEET    1   G 3 ALA B  37  VAL B  40  0                                        
SHEET    2   G 3 GLU B 192  LEU B 197 -1  O  VAL B 195   N  THR B  39           
SHEET    3   G 3 PHE B 183  CYS B 186 -1  N  ILE B 185   O  VAL B 193           
SHEET    1   H 2 MET B  60  ARG B  61  0                                        
SHEET    2   H 2 LYS B  69  TYR B  70 -1  O  TYR B  70   N  MET B  60           
LINK         NE2 HIS B  83                ZN    ZN B 439     1555   1555  2.06  
LINK         NE2 HIS A  83                ZN    ZN A 439     1555   1555  2.10  
LINK         SG  CYS A  75                ZN    ZN A 440     1555   1555  2.22  
LINK         SG  CYS B  65                ZN    ZN B 439     1555   1555  2.24  
LINK         SG  CYS A 263                ZN    ZN A 438     1555   1555  2.25  
LINK         SG  CYS A  65                ZN    ZN A 439     1555   1555  2.26  
LINK         SG  CYS B  62                ZN    ZN B 439     1555   1555  2.26  
LINK         SG  CYS B 263                ZN    ZN B 440     1555   1555  2.27  
LINK         SG  CYS B 266                ZN    ZN B 440     1555   1555  2.29  
LINK         SG  CYS B  71                ZN    ZN B 438     1555   1555  2.31  
LINK         SG  CYS B  52                ZN    ZN B 438     1555   1555  2.33  
LINK         SG  CYS A 266                ZN    ZN A 438     1555   1555  2.35  
LINK         SG  CYS A  52                ZN    ZN A 440     1555   1555  2.35  
LINK         SG  CYS B  49                ZN    ZN B 438     1555   1555  2.36  
LINK         SG  CYS B 261                ZN    ZN B 440     1555   1555  2.36  
LINK         SG  CYS A  49                ZN    ZN A 440     1555   1555  2.37  
LINK         SG  CYS A  62                ZN    ZN A 439     1555   1555  2.37  
LINK         SG  CYS B  75                ZN    ZN B 438     1555   1555  2.38  
LINK         SG  CYS B 208                ZN    ZN B 440     1555   1555  2.40  
LINK         SG  CYS B  87                ZN    ZN B 439     1555   1555  2.40  
LINK         SG  CYS A 261                ZN    ZN A 438     1555   1555  2.41  
LINK         SG  CYS A 208                ZN    ZN A 438     1555   1555  2.42  
LINK         SG  CYS A  87                ZN    ZN A 439     1555   1555  2.42  
LINK         SG  CYS A  71                ZN    ZN A 440     1555   1555  2.44  
CISPEP   1 LYS A   94    PRO A   95          0         8.29                     
CISPEP   2 LYS B   94    PRO B   95          0         4.08                     
SITE     1 AC1 19 ARG A  14  ASN A  16  TYR A 124  ASN A 132                    
SITE     2 AC1 19 CYS A 180  ASN A 181  SER A 202  LEU A 203                    
SITE     3 AC1 19 ASN A 205  HIS A 206  TYR A 239  TYR A 257                    
SITE     4 AC1 19 PHE A 259  HOH A 477  HOH A 504  HOH A 552                    
SITE     5 AC1 19 HOH A 582  HOH A 588  HOH A 606                               
SITE     1 AC2  4 CYS A 208  CYS A 261  CYS A 263  CYS A 266                    
SITE     1 AC3  4 CYS A  62  CYS A  65  HIS A  83  CYS A  87                    
SITE     1 AC4  4 CYS A  49  CYS A  52  CYS A  71  CYS A  75                    
SITE     1 AC5 19 ARG B  14  ASN B  16  TYR B 124  ASN B 132                    
SITE     2 AC5 19 CYS B 180  ASN B 181  SER B 202  LEU B 203                    
SITE     3 AC5 19 LEU B 204  ASN B 205  HIS B 206  TYR B 239                    
SITE     4 AC5 19 TYR B 257  PHE B 259  HOH B 447  HOH B 482                    
SITE     5 AC5 19 HOH B 529  HOH B 589  HOH B 604                               
SITE     1 AC6  4 CYS B  49  CYS B  52  CYS B  71  CYS B  75                    
SITE     1 AC7  4 CYS B  62  CYS B  65  HIS B  83  CYS B  87                    
SITE     1 AC8  4 CYS B 208  CYS B 261  CYS B 263  CYS B 266                    
CRYST1   58.175  118.073   82.901  90.00  91.58  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      0.017190  0.000000  0.000474        0.00000                         
SCALE2      0.000000  0.008469  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012067        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system