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Database: PDB
Entry: 3RIB
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HEADER    TRANSFERASE                             13-APR-11   3RIB              
TITLE     HUMAN LYSINE METHYLTRANSFERASE SMYD2 IN COMPLEX WITH ADOHCY           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: N-LYSINE METHYLTRANSFERASE SMYD2;                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: HSKM-B, HISTONE METHYLTRANSFERASE SMYD2, LYSINE N-          
COMPND   5 METHYLTRANSFERASE 3C, SET AND MYND DOMAIN-CONTAINING PROTEIN 2;      
COMPND   6 EC: 2.1.1.-, 2.1.1.43;                                               
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SMYD2, KMT3C;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS;                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28B                                    
KEYWDS    SMYD PROTEINS, MYND, SET DOMAIN, HISTONE LYSINE METHYLTRANSFERASE,    
KEYWDS   2 HISTONE METHYLATION, H3K36, H3K4, TRANSFERASE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.XU,T.ZHANG,C.ZHONG,J.DING                                           
REVDAT   3   08-NOV-17 3RIB    1       REMARK                                   
REVDAT   2   26-JUN-13 3RIB    1       JRNL                                     
REVDAT   1   20-JUL-11 3RIB    0                                                
JRNL        AUTH   S.XU,C.ZHONG,T.ZHANG,J.DING                                  
JRNL        TITL   STRUCTURE OF HUMAN LYSINE METHYLTRANSFERASE SMYD2 REVEALS    
JRNL        TITL 2 INSIGHTS INTO THE SUBSTRATE DIVERGENCE IN SMYD PROTEINS      
JRNL        REF    J MOL CELL BIOL               V.   3   293 2011              
JRNL        REFN                   ISSN 1674-2788                               
JRNL        PMID   21724641                                                     
JRNL        DOI    10.1093/JMCB/MJR015                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.79 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.79                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 25192                          
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) : 0.249                           
REMARK   3   R VALUE            (WORKING SET) : 0.246                           
REMARK   3   FREE R VALUE                     : 0.300                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1256                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.79                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.86                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1311                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 72.18                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3340                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 77                           
REMARK   3   BIN FREE R VALUE                    : 0.3530                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6830                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 103                                     
REMARK   3   SOLVENT ATOMS            : 49                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.94                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.15000                                              
REMARK   3    B22 (A**2) : -0.53000                                             
REMARK   3    B33 (A**2) : -2.32000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.61000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
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): 0.465         
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 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.890                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.825                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7077 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9546 ; 0.946 ; 1.977       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   844 ; 4.460 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   335 ;35.904 ;24.179       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1280 ;17.002 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    40 ;15.599 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1011 ; 0.063 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5305 ; 0.003 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4238 ; 0.701 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6822 ; 1.003 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2839 ; 0.418 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2724 ; 0.753 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3RIB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-APR-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000064965.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-MAR-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.2825                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25466                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.790                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : 0.14300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.66900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.66900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHENIX-AUTOSOL                                        
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 0.2M LITHIUM SULFATE,      
REMARK 280  0.1M BIS-TRIS, PH 6.5, HANGING DROP, TEMPERATURE 277K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       97.28000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       28.59250            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       97.28000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       28.59250            
REMARK 290   SMTRY3   4  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     ARG A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     LEU A     6                                                      
REMARK 465     HIS A   437                                                      
REMARK 465     HIS A   438                                                      
REMARK 465     HIS A   439                                                      
REMARK 465     HIS A   440                                                      
REMARK 465     HIS A   441                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ARG B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     GLY B     5                                                      
REMARK 465     LEU B     6                                                      
REMARK 465     LYS B   281                                                      
REMARK 465     LEU B   282                                                      
REMARK 465     SER B   283                                                      
REMARK 465     ASP B   284                                                      
REMARK 465     PRO B   285                                                      
REMARK 465     PRO B   286                                                      
REMARK 465     LYS B   287                                                      
REMARK 465     PHE B   332                                                      
REMARK 465     GLU B   333                                                      
REMARK 465     ASP B   334                                                      
REMARK 465     SER B   335                                                      
REMARK 465     ASN B   336                                                      
REMARK 465     HIS B   437                                                      
REMARK 465     HIS B   438                                                      
REMARK 465     HIS B   439                                                      
REMARK 465     HIS B   440                                                      
REMARK 465     HIS B   441                                                      
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    PHE A  34      157.85    179.88                                   
REMARK 500    ARG A  67      -61.25   -125.73                                   
REMARK 500    ASN A 101       50.94   -140.32                                   
REMARK 500    HIS A 119       72.33   -157.04                                   
REMARK 500    PRO A 124       12.18    -68.93                                   
REMARK 500    GLU A 190       31.25    -90.50                                   
REMARK 500    ASP A 284       77.75     58.93                                   
REMARK 500    LYS A 309        6.86    -67.43                                   
REMARK 500    TYR A 311      -28.59   -144.44                                   
REMARK 500    GLN A 354       16.49     52.62                                   
REMARK 500    HIS A 397       72.25   -111.24                                   
REMARK 500    ASN B 101       48.42   -153.06                                   
REMARK 500    ASP B 188     -158.22    -90.67                                   
REMARK 500    PRO B 232      114.00    -36.27                                   
REMARK 500    ASP B 271        5.98    -67.78                                   
REMARK 500    TYR B 311      -34.54   -138.56                                   
REMARK 500    SER B 330       -3.43    -47.21                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 443  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  68   SG                                                     
REMARK 620 2 HIS B  86   NE2 104.6                                              
REMARK 620 3 CYS B  65   SG  116.3 104.1                                        
REMARK 620 4 CYS B  90   SG  118.0 104.1 108.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 442  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  55   SG                                                     
REMARK 620 2 CYS B  52   SG  114.8                                              
REMARK 620 3 CYS B  74   SG  102.3 102.1                                        
REMARK 620 4 CYS B  78   SG  114.8 110.3 111.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 442  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  78   SG                                                     
REMARK 620 2 CYS A  55   SG  115.1                                              
REMARK 620 3 CYS A  52   SG  111.1 106.6                                        
REMARK 620 4 CYS A  74   SG  121.4  96.4 104.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 443  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  90   SG                                                     
REMARK 620 2 CYS A  65   SG  130.7                                              
REMARK 620 3 CYS A  68   SG  115.9 112.7                                        
REMARK 620 4 HIS A  86   NE2 107.6  85.3  84.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 444  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 267   SG                                                     
REMARK 620 2 CYS B 262   SG  112.0                                              
REMARK 620 3 CYS B 209   SG   89.9 147.5                                        
REMARK 620 4 CYS B 264   SG  102.8  87.1 112.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 444  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 264   SG                                                     
REMARK 620 2 CYS A 262   SG   97.4                                              
REMARK 620 3 CYS A 209   SG  119.9 107.7                                        
REMARK 620 4 CYS A 267   SG  119.9 112.0  99.8                                  
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 ZN A 442                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 443                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 444                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 445                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 446                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 447                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 448                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 449                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 450                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 451                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 452                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 442                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 443                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 444                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH B 445                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 446                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 447                 
DBREF  3RIB A    1   433  UNP    Q9NRG4   SMYD2_HUMAN      1    433             
DBREF  3RIB B    1   433  UNP    Q9NRG4   SMYD2_HUMAN      1    433             
SEQADV 3RIB LEU A  434  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 3RIB GLU A  435  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 3RIB HIS A  436  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 3RIB HIS A  437  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 3RIB HIS A  438  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 3RIB HIS A  439  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 3RIB HIS A  440  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 3RIB HIS A  441  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 3RIB LEU B  434  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 3RIB GLU B  435  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 3RIB HIS B  436  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 3RIB HIS B  437  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 3RIB HIS B  438  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 3RIB HIS B  439  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 3RIB HIS B  440  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 3RIB HIS B  441  UNP  Q9NRG4              EXPRESSION TAG                 
SEQRES   1 A  441  MET ARG ALA GLU GLY LEU GLY GLY LEU GLU ARG PHE CYS          
SEQRES   2 A  441  SER PRO GLY LYS GLY ARG GLY LEU ARG ALA LEU GLN PRO          
SEQRES   3 A  441  PHE GLN VAL GLY ASP LEU LEU PHE SER CYS PRO ALA TYR          
SEQRES   4 A  441  ALA TYR VAL LEU THR VAL ASN GLU ARG GLY ASN HIS CYS          
SEQRES   5 A  441  GLU TYR CYS PHE THR ARG LYS GLU GLY LEU SER LYS CYS          
SEQRES   6 A  441  GLY ARG CYS LYS GLN ALA PHE TYR CYS ASN VAL GLU CYS          
SEQRES   7 A  441  GLN LYS GLU ASP TRP PRO MET HIS LYS LEU GLU CYS SER          
SEQRES   8 A  441  PRO MET VAL VAL PHE GLY GLU ASN TRP ASN PRO SER GLU          
SEQRES   9 A  441  THR VAL ARG LEU THR ALA ARG ILE LEU ALA LYS GLN LYS          
SEQRES  10 A  441  ILE HIS PRO GLU ARG THR PRO SER GLU LYS LEU LEU ALA          
SEQRES  11 A  441  VAL LYS GLU PHE GLU SER HIS LEU ASP LYS LEU ASP ASN          
SEQRES  12 A  441  GLU LYS LYS ASP LEU ILE GLN SER ASP ILE ALA ALA LEU          
SEQRES  13 A  441  HIS HIS PHE TYR SER LYS HIS LEU GLY PHE PRO ASP ASN          
SEQRES  14 A  441  ASP SER LEU VAL VAL LEU PHE ALA GLN VAL ASN CYS ASN          
SEQRES  15 A  441  GLY PHE THR ILE GLU ASP GLU GLU LEU SER HIS LEU GLY          
SEQRES  16 A  441  SER ALA ILE PHE PRO ASP VAL ALA LEU MET ASN HIS SER          
SEQRES  17 A  441  CYS CYS PRO ASN VAL ILE VAL THR TYR LYS GLY THR LEU          
SEQRES  18 A  441  ALA GLU VAL ARG ALA VAL GLN GLU ILE LYS PRO GLY GLU          
SEQRES  19 A  441  GLU VAL PHE THR SER TYR ILE ASP LEU LEU TYR PRO THR          
SEQRES  20 A  441  GLU ASP ARG ASN ASP ARG LEU ARG ASP SER TYR PHE PHE          
SEQRES  21 A  441  THR CYS GLU CYS GLN GLU CYS THR THR LYS ASP LYS ASP          
SEQRES  22 A  441  LYS ALA LYS VAL GLU ILE ARG LYS LEU SER ASP PRO PRO          
SEQRES  23 A  441  LYS ALA GLU ALA ILE ARG ASP MET VAL ARG TYR ALA ARG          
SEQRES  24 A  441  ASN VAL ILE GLU GLU PHE ARG ARG ALA LYS HIS TYR LYS          
SEQRES  25 A  441  SER PRO SER GLU LEU LEU GLU ILE CYS GLU LEU SER GLN          
SEQRES  26 A  441  GLU LYS MET SER SER VAL PHE GLU ASP SER ASN VAL TYR          
SEQRES  27 A  441  MET LEU HIS MET MET TYR GLN ALA MET GLY VAL CYS LEU          
SEQRES  28 A  441  TYR MET GLN ASP TRP GLU GLY ALA LEU GLN TYR GLY GLN          
SEQRES  29 A  441  LYS ILE ILE LYS PRO TYR SER LYS HIS TYR PRO LEU TYR          
SEQRES  30 A  441  SER LEU ASN VAL ALA SER MET TRP LEU LYS LEU GLY ARG          
SEQRES  31 A  441  LEU TYR MET GLY LEU GLU HIS LYS ALA ALA GLY GLU LYS          
SEQRES  32 A  441  ALA LEU LYS LYS ALA ILE ALA ILE MET GLU VAL ALA HIS          
SEQRES  33 A  441  GLY LYS ASP HIS PRO TYR ILE SER GLU ILE LYS GLN GLU          
SEQRES  34 A  441  ILE GLU SER HIS LEU GLU HIS HIS HIS HIS HIS HIS              
SEQRES   1 B  441  MET ARG ALA GLU GLY LEU GLY GLY LEU GLU ARG PHE CYS          
SEQRES   2 B  441  SER PRO GLY LYS GLY ARG GLY LEU ARG ALA LEU GLN PRO          
SEQRES   3 B  441  PHE GLN VAL GLY ASP LEU LEU PHE SER CYS PRO ALA TYR          
SEQRES   4 B  441  ALA TYR VAL LEU THR VAL ASN GLU ARG GLY ASN HIS CYS          
SEQRES   5 B  441  GLU TYR CYS PHE THR ARG LYS GLU GLY LEU SER LYS CYS          
SEQRES   6 B  441  GLY ARG CYS LYS GLN ALA PHE TYR CYS ASN VAL GLU CYS          
SEQRES   7 B  441  GLN LYS GLU ASP TRP PRO MET HIS LYS LEU GLU CYS SER          
SEQRES   8 B  441  PRO MET VAL VAL PHE GLY GLU ASN TRP ASN PRO SER GLU          
SEQRES   9 B  441  THR VAL ARG LEU THR ALA ARG ILE LEU ALA LYS GLN LYS          
SEQRES  10 B  441  ILE HIS PRO GLU ARG THR PRO SER GLU LYS LEU LEU ALA          
SEQRES  11 B  441  VAL LYS GLU PHE GLU SER HIS LEU ASP LYS LEU ASP ASN          
SEQRES  12 B  441  GLU LYS LYS ASP LEU ILE GLN SER ASP ILE ALA ALA LEU          
SEQRES  13 B  441  HIS HIS PHE TYR SER LYS HIS LEU GLY PHE PRO ASP ASN          
SEQRES  14 B  441  ASP SER LEU VAL VAL LEU PHE ALA GLN VAL ASN CYS ASN          
SEQRES  15 B  441  GLY PHE THR ILE GLU ASP GLU GLU LEU SER HIS LEU GLY          
SEQRES  16 B  441  SER ALA ILE PHE PRO ASP VAL ALA LEU MET ASN HIS SER          
SEQRES  17 B  441  CYS CYS PRO ASN VAL ILE VAL THR TYR LYS GLY THR LEU          
SEQRES  18 B  441  ALA GLU VAL ARG ALA VAL GLN GLU ILE LYS PRO GLY GLU          
SEQRES  19 B  441  GLU VAL PHE THR SER TYR ILE ASP LEU LEU TYR PRO THR          
SEQRES  20 B  441  GLU ASP ARG ASN ASP ARG LEU ARG ASP SER TYR PHE PHE          
SEQRES  21 B  441  THR CYS GLU CYS GLN GLU CYS THR THR LYS ASP LYS ASP          
SEQRES  22 B  441  LYS ALA LYS VAL GLU ILE ARG LYS LEU SER ASP PRO PRO          
SEQRES  23 B  441  LYS ALA GLU ALA ILE ARG ASP MET VAL ARG TYR ALA ARG          
SEQRES  24 B  441  ASN VAL ILE GLU GLU PHE ARG ARG ALA LYS HIS TYR LYS          
SEQRES  25 B  441  SER PRO SER GLU LEU LEU GLU ILE CYS GLU LEU SER GLN          
SEQRES  26 B  441  GLU LYS MET SER SER VAL PHE GLU ASP SER ASN VAL TYR          
SEQRES  27 B  441  MET LEU HIS MET MET TYR GLN ALA MET GLY VAL CYS LEU          
SEQRES  28 B  441  TYR MET GLN ASP TRP GLU GLY ALA LEU GLN TYR GLY GLN          
SEQRES  29 B  441  LYS ILE ILE LYS PRO TYR SER LYS HIS TYR PRO LEU TYR          
SEQRES  30 B  441  SER LEU ASN VAL ALA SER MET TRP LEU LYS LEU GLY ARG          
SEQRES  31 B  441  LEU TYR MET GLY LEU GLU HIS LYS ALA ALA GLY GLU LYS          
SEQRES  32 B  441  ALA LEU LYS LYS ALA ILE ALA ILE MET GLU VAL ALA HIS          
SEQRES  33 B  441  GLY LYS ASP HIS PRO TYR ILE SER GLU ILE LYS GLN GLU          
SEQRES  34 B  441  ILE GLU SER HIS LEU GLU HIS HIS HIS HIS HIS HIS              
HET     ZN  A 442       1                                                       
HET     ZN  A 443       1                                                       
HET     ZN  A 444       1                                                       
HET    SAH  A 445      26                                                       
HET    SO4  A 446       5                                                       
HET    SO4  A 447       5                                                       
HET    SO4  A 448       5                                                       
HET    SO4  A 449       5                                                       
HET    SO4  A 450       5                                                       
HET    SO4  A 451       5                                                       
HET    SO4  A 452       5                                                       
HET     ZN  B 442       1                                                       
HET     ZN  B 443       1                                                       
HET     ZN  B 444       1                                                       
HET    SAH  B 445      26                                                       
HET    SO4  B 446       5                                                       
HET    SO4  B 447       5                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3   ZN    6(ZN 2+)                                                     
FORMUL   6  SAH    2(C14 H20 N6 O5 S)                                           
FORMUL   7  SO4    9(O4 S 2-)                                                   
FORMUL  20  HOH   *49(H2 O)                                                     
HELIX    1   1 VAL A   45  ARG A   48  5                                   4    
HELIX    2   2 ASN A   75  PHE A   96  1                                  22    
HELIX    3   3 GLY A   97  TRP A  100  5                                   4    
HELIX    4   4 SER A  103  HIS A  119  1                                  17    
HELIX    5   5 ALA A  130  PHE A  134  5                                   5    
HELIX    6   6 HIS A  137  LEU A  141  5                                   5    
HELIX    7   7 ASP A  142  SER A  161  1                                  20    
HELIX    8   8 ASP A  168  GLY A  183  1                                  16    
HELIX    9   9 ASP A  201  MET A  205  5                                   5    
HELIX   10  10 PRO A  246  TYR A  258  1                                  13    
HELIX   11  11 CYS A  264  LYS A  270  1                                   7    
HELIX   12  12 LYS A  272  VAL A  277  1                                   6    
HELIX   13  13 LYS A  287  LYS A  309  1                                  23    
HELIX   14  14 SER A  313  SER A  330  1                                  18    
HELIX   15  15 ASN A  336  MET A  353  1                                  18    
HELIX   16  16 ASP A  355  TYR A  374  1                                  20    
HELIX   17  17 SER A  378  LEU A  395  1                                  18    
HELIX   18  18 HIS A  397  GLY A  417  1                                  21    
HELIX   19  19 HIS A  420  SER A  432  1                                  13    
HELIX   20  20 ASN B   75  PHE B   96  1                                  22    
HELIX   21  21 GLY B   97  TRP B  100  5                                   4    
HELIX   22  22 SER B  103  HIS B  119  1                                  17    
HELIX   23  23 ALA B  130  PHE B  134  5                                   5    
HELIX   24  24 HIS B  137  LEU B  141  5                                   5    
HELIX   25  25 ASP B  142  SER B  161  1                                  20    
HELIX   26  26 ASP B  168  GLY B  183  1                                  16    
HELIX   27  27 ASP B  201  MET B  205  5                                   5    
HELIX   28  28 PRO B  246  TYR B  258  1                                  13    
HELIX   29  29 GLN B  265  LYS B  270  1                                   6    
HELIX   30  30 LYS B  272  VAL B  277  1                                   6    
HELIX   31  31 GLU B  289  LYS B  309  1                                  21    
HELIX   32  32 SER B  313  SER B  330  1                                  18    
HELIX   33  33 VAL B  337  GLN B  354  1                                  18    
HELIX   34  34 ASP B  355  TYR B  374  1                                  20    
HELIX   35  35 SER B  378  LEU B  395  1                                  18    
HELIX   36  36 HIS B  397  HIS B  416  1                                  20    
HELIX   37  37 HIS B  420  SER B  432  1                                  13    
SHEET    1   A 2 LEU A   9  SER A  14  0                                        
SHEET    2   A 2 GLY A  18  ALA A  23 -1  O  ARG A  22   N  GLU A  10           
SHEET    1   B 3 LEU A  32  PRO A  37  0                                        
SHEET    2   B 3 LEU A 221  ALA A 226 -1  O  VAL A 224   N  LEU A  33           
SHEET    3   B 3 VAL A 213  LYS A 218 -1  N  LYS A 218   O  LEU A 221           
SHEET    1   C 3 ALA A  40  LEU A  43  0                                        
SHEET    2   C 3 HIS A 193  ILE A 198 -1  O  ILE A 198   N  ALA A  40           
SHEET    3   C 3 PHE A 184  GLU A 187 -1  N  ILE A 186   O  GLY A 195           
SHEET    1   D 2 SER A  63  LYS A  64  0                                        
SHEET    2   D 2 PHE A  72  TYR A  73 -1  O  TYR A  73   N  SER A  63           
SHEET    1   E 2 ASN A 206  HIS A 207  0                                        
SHEET    2   E 2 PHE A 237  THR A 238  1  O  THR A 238   N  ASN A 206           
SHEET    1   F 2 LEU B   9  CYS B  13  0                                        
SHEET    2   F 2 ARG B  19  ALA B  23 -1  O  GLY B  20   N  PHE B  12           
SHEET    1   G 3 LEU B  32  PRO B  37  0                                        
SHEET    2   G 3 LEU B 221  ALA B 226 -1  O  ALA B 222   N  CYS B  36           
SHEET    3   G 3 VAL B 213  LYS B 218 -1  N  THR B 216   O  GLU B 223           
SHEET    1   H 3 ALA B  40  LEU B  43  0                                        
SHEET    2   H 3 HIS B 193  ILE B 198 -1  O  ILE B 198   N  ALA B  40           
SHEET    3   H 3 PHE B 184  GLU B 187 -1  N  ILE B 186   O  GLY B 195           
SHEET    1   I 2 SER B  63  LYS B  64  0                                        
SHEET    2   I 2 PHE B  72  TYR B  73 -1  O  TYR B  73   N  SER B  63           
SHEET    1   J 2 ASN B 206  HIS B 207  0                                        
SHEET    2   J 2 PHE B 237  THR B 238  1  O  THR B 238   N  ASN B 206           
LINK         SG  CYS B  68                ZN    ZN B 443     1555   1555  2.13  
LINK         NE2 HIS B  86                ZN    ZN B 443     1555   1555  2.20  
LINK         SG  CYS B  55                ZN    ZN B 442     1555   1555  2.21  
LINK         SG  CYS A  78                ZN    ZN A 442     1555   1555  2.22  
LINK         SG  CYS A  90                ZN    ZN A 443     1555   1555  2.25  
LINK         SG  CYS A  55                ZN    ZN A 442     1555   1555  2.26  
LINK         SG  CYS B  52                ZN    ZN B 442     1555   1555  2.26  
LINK         SG  CYS B  65                ZN    ZN B 443     1555   1555  2.29  
LINK         SG  CYS B  90                ZN    ZN B 443     1555   1555  2.32  
LINK         SG  CYS B 267                ZN    ZN B 444     1555   1555  2.32  
LINK         SG  CYS B  74                ZN    ZN B 442     1555   1555  2.40  
LINK         SG  CYS A 264                ZN    ZN A 444     1555   1555  2.41  
LINK         SG  CYS B  78                ZN    ZN B 442     1555   1555  2.41  
LINK         SG  CYS A 262                ZN    ZN A 444     1555   1555  2.42  
LINK         SG  CYS A  52                ZN    ZN A 442     1555   1555  2.43  
LINK         SG  CYS A 209                ZN    ZN A 444     1555   1555  2.43  
LINK         SG  CYS A 267                ZN    ZN A 444     1555   1555  2.45  
LINK         SG  CYS A  65                ZN    ZN A 443     1555   1555  2.48  
LINK         SG  CYS A  68                ZN    ZN A 443     1555   1555  2.49  
LINK         SG  CYS B 262                ZN    ZN B 444     1555   1555  2.49  
LINK         NE2 HIS A  86                ZN    ZN A 443     1555   1555  2.49  
LINK         SG  CYS B 209                ZN    ZN B 444     1555   1555  2.49  
LINK         SG  CYS A  74                ZN    ZN A 442     1555   1555  2.60  
LINK         SG  CYS B 264                ZN    ZN B 444     1555   1555  2.85  
SITE     1 AC1  4 CYS A  52  CYS A  55  CYS A  74  CYS A  78                    
SITE     1 AC2  4 CYS A  65  CYS A  68  HIS A  86  CYS A  90                    
SITE     1 AC3  4 CYS A 209  CYS A 262  CYS A 264  CYS A 267                    
SITE     1 AC4 16 GLY A  16  LYS A  17  ARG A  19  GLU A 135                    
SITE     2 AC4 16 HIS A 137  CYS A 181  ASN A 182  ALA A 203                    
SITE     3 AC4 16 LEU A 204  ASN A 206  HIS A 207  TYR A 240                    
SITE     4 AC4 16 TYR A 258  PHE A 260  SO4 A 452  HOH A 489                    
SITE     1 AC5  3 HIS A 397  ALA A 399  ALA A 400                               
SITE     1 AC6  6 CYS A 181  GLY A 183  PHE A 184  TYR A 240                    
SITE     2 AC6  6 TYR A 258  SO4 A 449                                          
SITE     1 AC7  5 THR A 105  VAL A 179  GLY A 183  PHE A 184                    
SITE     2 AC7  5 THR A 185                                                     
SITE     1 AC8  4 GLY A 183  THR A 185  TYR A 240  SO4 A 447                    
SITE     1 AC9  2 ASP A 252  ARG A 253                                          
SITE     1 BC1  8 CYS A 209  LEU A 243  GLU A 266  LYS A 272                    
SITE     2 BC1  8 LYS A 276  HIS A 373  TYR A 374  PRO A 375                    
SITE     1 BC2  5 PRO A  15  GLY A  16  LYS A  17  GLU A 263                    
SITE     2 BC2  5 SAH A 445                                                     
SITE     1 BC3  4 CYS B  52  CYS B  55  CYS B  74  CYS B  78                    
SITE     1 BC4  4 CYS B  65  CYS B  68  HIS B  86  CYS B  90                    
SITE     1 BC5  4 CYS B 209  CYS B 262  CYS B 264  CYS B 267                    
SITE     1 BC6 12 GLY B  16  LYS B  17  ARG B  19  GLU B 135                    
SITE     2 BC6 12 HIS B 137  CYS B 181  ALA B 203  ASN B 206                    
SITE     3 BC6 12 HIS B 207  TYR B 240  TYR B 258  PHE B 260                    
SITE     1 BC7  4 GLY B  30  LEU B  32  ARG B 225  GLY B 417                    
SITE     1 BC8  4 HIS B 397  LYS B 398  ALA B 399  ALA B 400                    
CRYST1  194.560   57.185   96.607  90.00 103.95  90.00 C 1 2 1       8          
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      0.005140  0.000000  0.001277        0.00000                         
SCALE2      0.000000  0.017487  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010666        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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