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Database: PDB
Entry: 1PEG
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Original site: 1PEG 
HEADER    TRANSFERASE                             21-MAY-03   1PEG              
TITLE     STRUCTURAL BASIS FOR THE PRODUCT SPECIFICITY OF HISTONE               
TITLE    2 LYSINE METHYLTRANSFERASES                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE H3 METHYLTRANSFERASE DIM-5;                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 17-318;                                           
COMPND   5 EC: 2.1.1.43;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: HISTONE H3;                                                
COMPND   9 CHAIN: P, Q;                                                         
COMPND  10 FRAGMENT: RESIDUES 1-15;                                             
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: NEUROSPORA CRASSA;                              
SOURCE   3 ORGANISM_TAXID: 5141;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS RIL                   
SOURCE   7 (STRATAGENE);                                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PGEX2T;                               
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PXC379;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 OTHER_DETAILS: THE HISTONE H3 PEPTIDE (N-TERMINAL RESIDUES           
SOURCE  13 1-15) IS SYNTHESIZED.                                                
KEYWDS    TERNARY STRUCTURE OF DIM-5, A SUV39-TYPE HISTONE-H3 LYS-9             
KEYWDS   2 METHYLTRANSFERASE, SET DOMAIN PROTEIN FORMS A KNOT-LIKE              
KEYWDS   3 SUBSTRUCTURE, PRE-SET TRIANGULAR ZN3CYS9 ZINC CLUSTER, POST-         
KEYWDS   4 SET ZINC-BINDING SITE, A HYBRID BETA SHEET FORMED BY DIM-5           
KEYWDS   5 AND H3 TAIL                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.ZHANG,Z.YANG,S.I.KHAN,J.R.HORTON,H.TAMARU,E.U.SELKER,               
AUTHOR   2 X.CHENG                                                              
REVDAT   2   24-FEB-09 1PEG    1       VERSN                                    
REVDAT   1   05-AUG-03 1PEG    0                                                
JRNL        AUTH   X.ZHANG,Z.YANG,S.I.KHAN,J.R.HORTON,H.TAMARU,                 
JRNL        AUTH 2 E.U.SELKER,X.CHENG                                           
JRNL        TITL   STRUCTURAL BASIS FOR THE PRODUCT SPECIFICITY OF              
JRNL        TITL 2 HISTONE LYSINE METHYLTRANSFERASES                            
JRNL        REF    MOL.CELL                      V.  12   177 2003              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   12887903                                                     
JRNL        DOI    10.1016/S1097-2765(03)00224-7                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.59 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.59                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.90                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 81.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 19510                          
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 SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.320                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 943                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.012                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.59                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.74                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 49.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1825                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3000                       
REMARK   3   BIN FREE R VALUE                    : 0.3800                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 94                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.064                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3558                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 60                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 59.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 58.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.97000                                             
REMARK   3    B22 (A**2) : 2.33000                                              
REMARK   3    B33 (A**2) : -0.36000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.45                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.55                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 30.90                           
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.64                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.86                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.80                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 28.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.77                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
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  NCS MODEL : CONSTR                                                  
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THE NON-CRYSTALLOGRAPHIC SYMMETRY         
REMARK   3  RESTRAINS WERE IMPOSED ON THE TWO COMPLEXES DURING THE              
REMARK   3  REFINEMENT, EXCEPT THE POST-SET REGION RESIDUES 53 TO 100.          
REMARK   3  MOLECULE B IS VERY FLEXIBLE IN THIS REGION (ONLY THE CA ATOMS       
REMARK   3  ARE GIVEN FOR THE RESIDUES 53 TO 87), WHILE THE CORRESPONDING       
REMARK   3  REGION IN MOLECULE A IS ORDERED.                                    
REMARK   4                                                                      
REMARK   4 1PEG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAY-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB019272.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-NOV-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.40                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X25                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
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 : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21803                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.590                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.6                               
REMARK 200  DATA REDUNDANCY                : 4.500                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : 0.08800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.59                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.68                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 67.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.22800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.22800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1ML9                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 2000 MONOMETHYL ETHER,               
REMARK 280  TRIMETHYLAMINE, PH 8.4, VAPOR DIFFUSION, HANGING DROP,              
REMARK 280  TEMPERATURE 289K, PH 8.40                                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       34.13000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       57.34500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.08500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       57.34500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       34.13000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.08500            
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, P                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1480 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -124.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, Q                                  
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     ILE A    17                                                      
REMARK 465     ARG A    18                                                      
REMARK 465     SER A    19                                                      
REMARK 465     PHE A    20                                                      
REMARK 465     ALA A    21                                                      
REMARK 465     THR A    22                                                      
REMARK 465     HIS A    23                                                      
REMARK 465     ALA A    24                                                      
REMARK 465     GLN A    25                                                      
REMARK 465     ASP A    88                                                      
REMARK 465     SER A    89                                                      
REMARK 465     ASP A    90                                                      
REMARK 465     GLU A    91                                                      
REMARK 465     GLU A    92                                                      
REMARK 465     ALA A    93                                                      
REMARK 465     GLN A   224                                                      
REMARK 465     GLY A   286                                                      
REMARK 465     LEU A   287                                                      
REMARK 465     THR A   288                                                      
REMARK 465     GLY A   289                                                      
REMARK 465     LEU A   290                                                      
REMARK 465     GLU A   291                                                      
REMARK 465     SER A   292                                                      
REMARK 465     ASP A   293                                                      
REMARK 465     ALA A   294                                                      
REMARK 465     HIS A   295                                                      
REMARK 465     ASP A   296                                                      
REMARK 465     PRO A   297                                                      
REMARK 465     SER A   298                                                      
REMARK 465     LYS A   299                                                      
REMARK 465     ILE A   300                                                      
REMARK 465     SER A   301                                                      
REMARK 465     GLU A   302                                                      
REMARK 465     MET A   303                                                      
REMARK 465     THR A   304                                                      
REMARK 465     LYS A   305                                                      
REMARK 465     ALA P     1                                                      
REMARK 465     ARG P     2                                                      
REMARK 465     THR P     3                                                      
REMARK 465     LYS P     4                                                      
REMARK 465     GLN P     5                                                      
REMARK 465     THR P     6                                                      
REMARK 465     LYS P    14                                                      
REMARK 465     ALA P    15                                                      
REMARK 465     ILE B    17                                                      
REMARK 465     ARG B    18                                                      
REMARK 465     SER B    19                                                      
REMARK 465     PHE B    20                                                      
REMARK 465     ALA B    21                                                      
REMARK 465     THR B    22                                                      
REMARK 465     HIS B    23                                                      
REMARK 465     ALA B    24                                                      
REMARK 465     GLN B    25                                                      
REMARK 465     ASP B    88                                                      
REMARK 465     SER B    89                                                      
REMARK 465     ASP B    90                                                      
REMARK 465     GLU B    91                                                      
REMARK 465     GLU B    92                                                      
REMARK 465     ALA B    93                                                      
REMARK 465     ASP B    94                                                      
REMARK 465     PRO B    95                                                      
REMARK 465     TYR B    96                                                      
REMARK 465     THR B    97                                                      
REMARK 465     ARG B    98                                                      
REMARK 465     LYS B    99                                                      
REMARK 465     ASP B   218                                                      
REMARK 465     PRO B   219                                                      
REMARK 465     LEU B   220                                                      
REMARK 465     LEU B   221                                                      
REMARK 465     ALA B   222                                                      
REMARK 465     GLY B   223                                                      
REMARK 465     GLN B   224                                                      
REMARK 465     PRO B   225                                                      
REMARK 465     LEU B   287                                                      
REMARK 465     THR B   288                                                      
REMARK 465     GLY B   289                                                      
REMARK 465     LEU B   290                                                      
REMARK 465     GLU B   291                                                      
REMARK 465     SER B   292                                                      
REMARK 465     ASP B   293                                                      
REMARK 465     ALA B   294                                                      
REMARK 465     HIS B   295                                                      
REMARK 465     ASP B   296                                                      
REMARK 465     PRO B   297                                                      
REMARK 465     SER B   298                                                      
REMARK 465     LYS B   299                                                      
REMARK 465     ILE B   300                                                      
REMARK 465     SER B   301                                                      
REMARK 465     GLU B   302                                                      
REMARK 465     MET B   303                                                      
REMARK 465     ALA Q     1                                                      
REMARK 465     ARG Q     2                                                      
REMARK 465     THR Q     3                                                      
REMARK 465     LYS Q     4                                                      
REMARK 465     GLN Q     5                                                      
REMARK 465     THR Q     6                                                      
REMARK 465     GLY Q    12                                                      
REMARK 465     GLY Q    13                                                      
REMARK 465     LYS Q    14                                                      
REMARK 465     ALA Q    15                                                      
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     ARG A  33    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  34    CG   CD   OE1  OE2                                  
REMARK 470     ASN A  54    CG   OD1  ND2                                       
REMARK 470     ASP A  59    CG   OD1  OD2                                       
REMARK 470     GLN A  60    CG   CD   OE1  NE2                                  
REMARK 470     SER A  61    OG                                                  
REMARK 470     SER A  70    N    C    O    CB   OG                              
REMARK 470     ASP A  71    N    C    O    CB   CG   OD1  OD2                   
REMARK 470     GLU A  72    N    C    O    CB   CG   CD   OE1                   
REMARK 470     GLU A  72    OE2                                                 
REMARK 470     GLU A  73    CG   CD   OE1  OE2                                  
REMARK 470     GLN A  80    CG   CD   OE1  NE2                                  
REMARK 470     ASP A  94    N    C    O    CB   CG   OD1  OD2                   
REMARK 470     PRO A  95    N    C    O    CB   CG   CD                         
REMARK 470     TYR A  96    N    C    O    CB   CG   CD1  CD2                   
REMARK 470     TYR A  96    CE1  CE2  CZ   OH                                   
REMARK 470     THR A  97    N    C    O    CB   OG1  CG2                        
REMARK 470     ARG A  98    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 101    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 120    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 141    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A 184    OG1  CG2                                            
REMARK 470     GLU A 186    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 189    CG   OD1  OD2                                       
REMARK 470     ARG A 192    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 194    CG   CD   OE1  OE2                                  
REMARK 470     SER A 195    OG                                                  
REMARK 470     THR A 196    OG1  CG2                                            
REMARK 470     ILE A 197    CB   CG1  CG2  CD1                                  
REMARK 470     ARG A 199    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 201    CG   CD   CE   NZ                                   
REMARK 470     ASP A 213    N    C    O    CB   CG   OD1  OD2                   
REMARK 470     PRO A 214    N    C    O    CB   CG   CD                         
REMARK 470     ASP A 215    N    C    O    CB   CG   OD1  OD2                   
REMARK 470     SER A 216    N    C    O    CB   OG                              
REMARK 470     LEU A 217    N    C    O    CB   CG   CD1  CD2                   
REMARK 470     ASP A 218    N    C    O    CB   CG   OD1  OD2                   
REMARK 470     PRO A 219    N    C    O    CB   CG   CD                         
REMARK 470     LEU A 220    N    C    O    CB   CG   CD1  CD2                   
REMARK 470     LEU A 221    N    C    O    CB   CG   CD1  CD2                   
REMARK 470     ALA A 222    N    C    O    CB                                   
REMARK 470     GLY A 223    N    C    O                                         
REMARK 470     ASP A 245    CG   OD1  OD2                                       
REMARK 470     ASP A 256    CG   OD1  OD2                                       
REMARK 470     THR A 280    OG1  CG2                                            
REMARK 470     ASP A 282    CG   OD1  OD2                                       
REMARK 470     THR A 310    OG1  CG2                                            
REMARK 470     LYS A 312    CG   CD   CE   NZ                                   
REMARK 470     ARG A 314    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR A 316    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASN B  42    CG   OD1  ND2                                       
REMARK 470     LYS B  53    N    C    O    CB   CG   CD   CE                    
REMARK 470     LYS B  53    NZ                                                  
REMARK 470     ASN B  54    N    C    O    CB   CG   OD1  ND2                   
REMARK 470     VAL B  55    N    C    O    CB   CG1  CG2                        
REMARK 470     PRO B  56    N    C    O    CB   CG   CD                         
REMARK 470     VAL B  57    N    C    O    CB   CG1  CG2                        
REMARK 470     ALA B  58    N    C    O    CB                                   
REMARK 470     ASP B  59    N    C    O    CB   CG   OD1  OD2                   
REMARK 470     GLN B  60    N    C    O    CB   CG   CD   OE1                   
REMARK 470     GLN B  60    NE2                                                 
REMARK 470     SER B  61    N    C    O    CB   OG                              
REMARK 470     PHE B  62    N    C    O    CB   CG   CD1  CD2                   
REMARK 470     PHE B  62    CE1  CE2  CZ                                        
REMARK 470     ARG B  63    N    C    O    CB   CG   CD   NE                    
REMARK 470     ARG B  63    CZ   NH1  NH2                                       
REMARK 470     VAL B  64    N    C    O    CB   CG1  CG2                        
REMARK 470     GLY B  65    N    C    O                                         
REMARK 470     CYS B  66    N    C    O    CB   SG                              
REMARK 470     SER B  67    N    C    O    CB   OG                              
REMARK 470     CYS B  68    N    C    O    CB   SG                              
REMARK 470     ALA B  69    N    C    O    CB                                   
REMARK 470     SER B  70    N    C    O    CB   OG                              
REMARK 470     ASP B  71    N    C    O    CB   CG   OD1  OD2                   
REMARK 470     GLU B  72    N    C    O    CB   CG   CD   OE1                   
REMARK 470     GLU B  72    OE2                                                 
REMARK 470     GLU B  73    N    C    O    CB   CG   CD   OE1                   
REMARK 470     GLU B  73    OE2                                                 
REMARK 470     CYS B  74    N    C    O    CB   SG                              
REMARK 470     MET B  75    N    C    O    CB   CG   SD   CE                    
REMARK 470     TYR B  76    N    C    O    CB   CG   CD1  CD2                   
REMARK 470     TYR B  76    CE1  CE2  CZ   OH                                   
REMARK 470     SER B  77    N    C    O    CB   OG                              
REMARK 470     THR B  78    N    C    O    CB   OG1  CG2                        
REMARK 470     CYS B  79    N    C    O    CB   SG                              
REMARK 470     GLN B  80    N    C    O    CB   CG   CD   OE1                   
REMARK 470     GLN B  80    NE2                                                 
REMARK 470     CYS B  81    N    C    O    CB   SG                              
REMARK 470     LEU B  82    N    C    O    CB   CG   CD1  CD2                   
REMARK 470     ASP B  83    N    C    O    CB   CG   OD1  OD2                   
REMARK 470     GLU B  84    N    C    O    CB   CG   CD   OE1                   
REMARK 470     GLU B  84    OE2                                                 
REMARK 470     MET B  85    N    C    O    CB   CG   SD   CE                    
REMARK 470     ALA B  86    N    C    O    CB                                   
REMARK 470     PRO B  87    N    C    O    CB   CG   CD                         
REMARK 470     ARG B 101    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 107    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 110    CG   CD   CE   NZ                                   
REMARK 470     LEU B 113    CG   CD1  CD2                                       
REMARK 470     ARG B 115    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 117    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 120    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 123    CG   CD   OE1  OE2                                  
REMARK 470     CYS B 128    N    C    O    CB   SG                              
REMARK 470     HIS B 129    N    C    O    CB   CG   ND1  CD2                   
REMARK 470     HIS B 129    CE1  NE2                                            
REMARK 470     GLN B 130    N    C    O    CB   CG   CD   OE1                   
REMARK 470     GLN B 130    NE2                                                 
REMARK 470     GLY B 131    N    C    O                                         
REMARK 470     CYS B 132    SG                                                  
REMARK 470     ALA B 133    CB                                                  
REMARK 470     LYS B 136    CG   CD   CE   NZ                                   
REMARK 470     ARG B 141    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 158    CG   OD1  OD2                                       
REMARK 470     LYS B 170    CG   CD   CE   NZ                                   
REMARK 470     ARG B 171    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR B 184    OG1  CG2                                            
REMARK 470     GLU B 187    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 189    CG   OD1  OD2                                       
REMARK 470     ARG B 192    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 194    CG   CD   OE1  OE2                                  
REMARK 470     SER B 195    OG                                                  
REMARK 470     THR B 196    OG1  CG2                                            
REMARK 470     ILE B 197    CB   CG1  CG2  CD1                                  
REMARK 470     ALA B 198    N    C    O    CB                                   
REMARK 470     ARG B 199    N    C    O    CB   CG   CD   NE                    
REMARK 470     ARG B 199    CZ   NH1  NH2                                       
REMARK 470     ARG B 200    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B 212    N    C    O    CB   OG                              
REMARK 470     ASP B 213    N    C    O    CB   CG   OD1  OD2                   
REMARK 470     PRO B 214    N    C    O    CB   CG   CD                         
REMARK 470     ASP B 215    N    C    O    CB   CG   OD1  OD2                   
REMARK 470     SER B 216    N    C    O    CB   OG                              
REMARK 470     LEU B 217    N    C    O    CB   CG   CD1  CD2                   
REMARK 470     ASP B 245    CG   OD1  OD2                                       
REMARK 470     VAL B 254    CG1  CG2                                            
REMARK 470     ASP B 256    CG   OD1  OD2                                       
REMARK 470     HIS B 257    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP B 259    CG   OD1  OD2                                       
REMARK 470     THR B 280    OG1  CG2                                            
REMARK 470     ASP B 282    CG   OD1  OD2                                       
REMARK 470     THR B 304    CG2                                                 
REMARK 470     LYS B 305    CG   CD   CE   NZ                                   
REMARK 470     THR B 310    OG1  CG2                                            
REMARK 470     LYS B 312    CG   CD   CE   NZ                                   
REMARK 470     ARG B 314    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR B 316    CG   CD1  CD2  CE1  CE2  CZ   OH                    
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    PRO A 274   CA  -  N   -  CD  ANGL. DEV. =  -8.9 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    GLU A  34       -3.74     85.87                                   
REMARK 500    GLN A  60        3.58    -66.67                                   
REMARK 500    CYS A  68      146.16    -27.98                                   
REMARK 500    ARG A 101       -4.27   -152.20                                   
REMARK 500    PHE A 102       10.29    -68.69                                   
REMARK 500    GLN A 107       -4.18   -162.71                                   
REMARK 500    HIS A 129     -153.87   -161.26                                   
REMARK 500    GLN A 130       34.03    -89.97                                   
REMARK 500    ALA A 133       44.01    -81.07                                   
REMARK 500    LYS A 136      -55.13    -15.29                                   
REMARK 500    CYS A 138      112.13    -38.76                                   
REMARK 500    THR A 156     -172.62    -69.98                                   
REMARK 500    VAL A 175      -71.72    -83.73                                   
REMARK 500    SER A 195      -67.30    -90.92                                   
REMARK 500    THR A 196      -17.56    -43.60                                   
REMARK 500    ILE A 197      -72.40    -89.67                                   
REMARK 500    ARG A 199     -120.16   -153.67                                   
REMARK 500    ASP A 202      102.76    -29.67                                   
REMARK 500    LEU A 226      160.00    -45.40                                   
REMARK 500    SER A 234     -165.61    176.24                                   
REMARK 500    THR A 237       -9.61    -53.90                                   
REMARK 500    PRO A 246      162.00    -49.60                                   
REMARK 500    ASP A 256      -43.37    -28.73                                   
REMARK 500    HIS A 257        7.37     89.58                                   
REMARK 500    PHE A 281      148.07   -170.58                                   
REMARK 500    THR A 310      109.74    -21.95                                   
REMARK 500    CYS A 313      114.75    -37.67                                   
REMARK 500    ARG A 314       24.49    -71.03                                   
REMARK 500    ARG B 101       12.82   -160.28                                   
REMARK 500    GLN B 107      -58.70   -135.56                                   
REMARK 500    ASP B 116      -18.31    -45.96                                   
REMARK 500    LEU B 119      -71.05    -58.72                                   
REMARK 500    ASP B 137       31.51    -78.56                                   
REMARK 500    THR B 156     -158.39    -79.26                                   
REMARK 500    VAL B 175      -71.57    -83.22                                   
REMARK 500    SER B 185       -7.65    -49.86                                   
REMARK 500    GLU B 186      -73.28    -71.75                                   
REMARK 500    SER B 195      -67.00    -91.02                                   
REMARK 500    THR B 196      -17.58    -43.89                                   
REMARK 500    SER B 234     -165.82    167.42                                   
REMARK 500    THR B 237       -9.67    -54.50                                   
REMARK 500    PRO B 246      163.00    -48.65                                   
REMARK 500    ASP B 256      -27.20    -38.22                                   
REMARK 500    ALA B 258      -60.91   -107.45                                   
REMARK 500    ASP B 259       98.47    -61.43                                   
REMARK 500    LYS B 260       -6.41   -153.74                                   
REMARK 500    LYS B 275      177.70    -55.17                                   
REMARK 500    PHE B 281      148.27   -170.42                                   
REMARK 500    ASN B 285      -26.76     88.49                                   
REMARK 500    THR B 310      110.31    -21.70                                   
REMARK 500    CYS B 313      113.65    -38.86                                   
REMARK 500    ARG B 314       25.82    -70.59                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    LYS B 275        -13.37                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A   1  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 128   SG                                                     
REMARK 620 2 CYS A 132   SG  114.2                                              
REMARK 620 3 CYS A  66   SG  101.8 106.9                                        
REMARK 620 4 CYS A  81   SG  108.1 114.3 110.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A   2  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 138   SG                                                     
REMARK 620 2 CYS A 128   SG  107.5                                              
REMARK 620 3 CYS A 134   SG  103.7 110.9                                        
REMARK 620 4 CYS A  74   SG  106.7 111.1 116.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A   3  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  66   SG                                                     
REMARK 620 2 CYS A  68   SG  115.0                                              
REMARK 620 3 CYS A  74   SG  103.8 108.4                                        
REMARK 620 4 CYS A  79   SG   96.3 108.8 124.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A   4  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 308   SG                                                     
REMARK 620 2 CYS A 313   SG  106.0                                              
REMARK 620 3 CYS A 306   SG  109.6 109.8                                        
REMARK 620 4 CYS A 244   SG  109.2 103.8 117.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B   8  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 306   SG                                                     
REMARK 620 2 CYS B 244   SG  114.4                                              
REMARK 620 3 CYS B 308   SG  110.0 113.3                                        
REMARK 620 4 CYS B 313   SG  103.4 110.8 103.9                                  
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 1                    
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2                    
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 3                    
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 4                    
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 5                    
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 6                    
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 7                    
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 8                    
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 319                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH B 2                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1ML9   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE NEUROSPOSA SET DOMAIN PROTEIN DIM-5, A              
REMARK 900 HISTONE H3 LYSINE METHYLTRASFERASE                                   
DBREF  1PEG A   17   318  UNP    Q8X225   DIM5_NEUCR      17    318             
DBREF  1PEG P    1    15  UNP    P02303   H3_YEAST         1     15             
DBREF  1PEG B   17   318  UNP    Q8X225   DIM5_NEUCR      17    318             
DBREF  1PEG Q    1    15  UNP    P02303   H3_YEAST         1     15             
SEQRES   1 A  302  ILE ARG SER PHE ALA THR HIS ALA GLN LEU PRO ILE SER          
SEQRES   2 A  302  ILE VAL ASN ARG GLU ASP ASP ALA PHE LEU ASN PRO ASN          
SEQRES   3 A  302  PHE ARG PHE ILE ASP HIS SER ILE ILE GLY LYS ASN VAL          
SEQRES   4 A  302  PRO VAL ALA ASP GLN SER PHE ARG VAL GLY CYS SER CYS          
SEQRES   5 A  302  ALA SER ASP GLU GLU CYS MET TYR SER THR CYS GLN CYS          
SEQRES   6 A  302  LEU ASP GLU MET ALA PRO ASP SER ASP GLU GLU ALA ASP          
SEQRES   7 A  302  PRO TYR THR ARG LYS LYS ARG PHE ALA TYR TYR SER GLN          
SEQRES   8 A  302  GLY ALA LYS LYS GLY LEU LEU ARG ASP ARG VAL LEU GLN          
SEQRES   9 A  302  SER GLN GLU PRO ILE TYR GLU CYS HIS GLN GLY CYS ALA          
SEQRES  10 A  302  CYS SER LYS ASP CYS PRO ASN ARG VAL VAL GLU ARG GLY          
SEQRES  11 A  302  ARG THR VAL PRO LEU GLN ILE PHE ARG THR LYS ASP ARG          
SEQRES  12 A  302  GLY TRP GLY VAL LYS CYS PRO VAL ASN ILE LYS ARG GLY          
SEQRES  13 A  302  GLN PHE VAL ASP ARG TYR LEU GLY GLU ILE ILE THR SER          
SEQRES  14 A  302  GLU GLU ALA ASP ARG ARG ARG ALA GLU SER THR ILE ALA          
SEQRES  15 A  302  ARG ARG LYS ASP VAL TYR LEU PHE ALA LEU ASP LYS PHE          
SEQRES  16 A  302  SER ASP PRO ASP SER LEU ASP PRO LEU LEU ALA GLY GLN          
SEQRES  17 A  302  PRO LEU GLU VAL ASP GLY GLU TYR MET SER GLY PRO THR          
SEQRES  18 A  302  ARG PHE ILE ASN HIS SER CYS ASP PRO ASN MET ALA ILE          
SEQRES  19 A  302  PHE ALA ARG VAL GLY ASP HIS ALA ASP LYS HIS ILE HIS          
SEQRES  20 A  302  ASP LEU ALA LEU PHE ALA ILE LYS ASP ILE PRO LYS GLY          
SEQRES  21 A  302  THR GLU LEU THR PHE ASP TYR VAL ASN GLY LEU THR GLY          
SEQRES  22 A  302  LEU GLU SER ASP ALA HIS ASP PRO SER LYS ILE SER GLU          
SEQRES  23 A  302  MET THR LYS CYS LEU CYS GLY THR ALA LYS CYS ARG GLY          
SEQRES  24 A  302  TYR LEU TRP                                                  
SEQRES   1 P   15  ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY GLY          
SEQRES   2 P   15  LYS ALA                                                      
SEQRES   1 B  302  ILE ARG SER PHE ALA THR HIS ALA GLN LEU PRO ILE SER          
SEQRES   2 B  302  ILE VAL ASN ARG GLU ASP ASP ALA PHE LEU ASN PRO ASN          
SEQRES   3 B  302  PHE ARG PHE ILE ASP HIS SER ILE ILE GLY LYS ASN VAL          
SEQRES   4 B  302  PRO VAL ALA ASP GLN SER PHE ARG VAL GLY CYS SER CYS          
SEQRES   5 B  302  ALA SER ASP GLU GLU CYS MET TYR SER THR CYS GLN CYS          
SEQRES   6 B  302  LEU ASP GLU MET ALA PRO ASP SER ASP GLU GLU ALA ASP          
SEQRES   7 B  302  PRO TYR THR ARG LYS LYS ARG PHE ALA TYR TYR SER GLN          
SEQRES   8 B  302  GLY ALA LYS LYS GLY LEU LEU ARG ASP ARG VAL LEU GLN          
SEQRES   9 B  302  SER GLN GLU PRO ILE TYR GLU CYS HIS GLN GLY CYS ALA          
SEQRES  10 B  302  CYS SER LYS ASP CYS PRO ASN ARG VAL VAL GLU ARG GLY          
SEQRES  11 B  302  ARG THR VAL PRO LEU GLN ILE PHE ARG THR LYS ASP ARG          
SEQRES  12 B  302  GLY TRP GLY VAL LYS CYS PRO VAL ASN ILE LYS ARG GLY          
SEQRES  13 B  302  GLN PHE VAL ASP ARG TYR LEU GLY GLU ILE ILE THR SER          
SEQRES  14 B  302  GLU GLU ALA ASP ARG ARG ARG ALA GLU SER THR ILE ALA          
SEQRES  15 B  302  ARG ARG LYS ASP VAL TYR LEU PHE ALA LEU ASP LYS PHE          
SEQRES  16 B  302  SER ASP PRO ASP SER LEU ASP PRO LEU LEU ALA GLY GLN          
SEQRES  17 B  302  PRO LEU GLU VAL ASP GLY GLU TYR MET SER GLY PRO THR          
SEQRES  18 B  302  ARG PHE ILE ASN HIS SER CYS ASP PRO ASN MET ALA ILE          
SEQRES  19 B  302  PHE ALA ARG VAL GLY ASP HIS ALA ASP LYS HIS ILE HIS          
SEQRES  20 B  302  ASP LEU ALA LEU PHE ALA ILE LYS ASP ILE PRO LYS GLY          
SEQRES  21 B  302  THR GLU LEU THR PHE ASP TYR VAL ASN GLY LEU THR GLY          
SEQRES  22 B  302  LEU GLU SER ASP ALA HIS ASP PRO SER LYS ILE SER GLU          
SEQRES  23 B  302  MET THR LYS CYS LEU CYS GLY THR ALA LYS CYS ARG GLY          
SEQRES  24 B  302  TYR LEU TRP                                                  
SEQRES   1 Q   15  ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY GLY          
SEQRES   2 Q   15  LYS ALA                                                      
HET     ZN  A   1       1                                                       
HET     ZN  A   2       1                                                       
HET     ZN  A   3       1                                                       
HET     ZN  A   4       1                                                       
HET     ZN  B   5       1                                                       
HET     ZN  B   6       1                                                       
HET     ZN  B   7       1                                                       
HET     ZN  B   8       1                                                       
HET    SAH  A 319      26                                                       
HET    SAH  B   2      26                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
FORMUL   5   ZN    8(ZN 2+)                                                     
FORMUL  13  SAH    2(C14 H20 N6 O5 S)                                           
HELIX    1   1 CYS A   79  ASP A   83  5                                   5    
HELIX    2   2 ARG A  115  GLN A  122  1                                   8    
HELIX    3   3 ARG A  141  GLY A  146  1                                   6    
HELIX    4   4 THR A  184  ARG A  199  1                                  16    
HELIX    5   5 GLY A  235  ILE A  240  5                                   6    
HELIX    6   6 ARG B  115  GLN B  122  1                                   8    
HELIX    7   7 ARG B  141  GLY B  146  1                                   6    
HELIX    8   8 THR B  184  ILE B  197  1                                  14    
HELIX    9   9 GLY B  235  ILE B  240  5                                   6    
SHEET    1   A 5 ILE A  28  VAL A  31  0                                        
SHEET    2   A 5 LEU A 151  ARG A 155  1  O  ILE A 153   N  SER A  29           
SHEET    3   A 5 TRP A 161  LYS A 164 -1  O  GLY A 162   N  PHE A 154           
SHEET    4   A 5 GLU A 278  PHE A 281 -1  O  LEU A 279   N  VAL A 163           
SHEET    5   A 5 ASN A 241  HIS A 242  1  N  ASN A 241   O  PHE A 281           
SHEET    1   B 2 ARG A  44  PHE A  45  0                                        
SHEET    2   B 2 MET A 233  SER A 234  1  O  SER A 234   N  ARG A  44           
SHEET    1   C 4 ILE A  50  ILE A  51  0                                        
SHEET    2   C 4 GLU A 181  ILE A 183  1  O  ILE A 182   N  ILE A  50           
SHEET    3   C 4 GLU A 227  ASP A 229 -1  O  GLU A 227   N  ILE A 183           
SHEET    4   C 4 LEU A 205  ALA A 207 -1  N  PHE A 206   O  VAL A 228           
SHEET    1   D 4 ILE A 125  TYR A 126  0                                        
SHEET    2   D 4 MET A 248  VAL A 254  1  O  ALA A 252   N  ILE A 125           
SHEET    3   D 4 ASP A 264  ALA A 269 -1  O  PHE A 268   N  ALA A 249           
SHEET    4   D 4 PHE A 174  ARG A 177 -1  N  ASP A 176   O  LEU A 267           
SHEET    1   E 5 ILE B  28  VAL B  31  0                                        
SHEET    2   E 5 LEU B 151  ARG B 155  1  O  ILE B 153   N  SER B  29           
SHEET    3   E 5 TRP B 161  LYS B 164 -1  O  LYS B 164   N  GLN B 152           
SHEET    4   E 5 GLU B 278  PHE B 281 -1  O  LEU B 279   N  VAL B 163           
SHEET    5   E 5 ASN B 241  HIS B 242  1  N  ASN B 241   O  LEU B 279           
SHEET    1   F 2 ARG B  44  PHE B  45  0                                        
SHEET    2   F 2 MET B 233  SER B 234  1  O  SER B 234   N  ARG B  44           
SHEET    1   G 4 ILE B  50  ILE B  51  0                                        
SHEET    2   G 4 GLU B 181  ILE B 183  1  O  ILE B 182   N  ILE B  50           
SHEET    3   G 4 GLU B 227  ASP B 229 -1  O  GLU B 227   N  ILE B 183           
SHEET    4   G 4 LEU B 205  ALA B 207 -1  N  PHE B 206   O  VAL B 228           
SHEET    1   H 4 ILE B 125  TYR B 126  0                                        
SHEET    2   H 4 MET B 248  VAL B 254  1  O  ALA B 252   N  ILE B 125           
SHEET    3   H 4 ASP B 264  ALA B 269 -1  O  PHE B 268   N  ALA B 249           
SHEET    4   H 4 PHE B 174  TYR B 178 -1  N  TYR B 178   O  LEU B 265           
LINK        ZN    ZN A   1                 SG  CYS A 128     1555   1555  2.38  
LINK        ZN    ZN A   1                 SG  CYS A 132     1555   1555  2.30  
LINK        ZN    ZN A   1                 SG  CYS A  66     1555   1555  2.30  
LINK        ZN    ZN A   1                 SG  CYS A  81     1555   1555  2.28  
LINK        ZN    ZN A   2                 SG  CYS A 138     1555   1555  2.30  
LINK        ZN    ZN A   2                 SG  CYS A 128     1555   1555  2.30  
LINK        ZN    ZN A   2                 SG  CYS A 134     1555   1555  2.30  
LINK        ZN    ZN A   2                 SG  CYS A  74     1555   1555  2.24  
LINK        ZN    ZN A   3                 SG  CYS A  66     1555   1555  2.29  
LINK        ZN    ZN A   3                 SG  CYS A  68     1555   1555  2.34  
LINK        ZN    ZN A   3                 SG  CYS A  74     1555   1555  2.29  
LINK        ZN    ZN A   3                 SG  CYS A  79     1555   1555  2.30  
LINK        ZN    ZN A   4                 SG  CYS A 308     1555   1555  2.29  
LINK        ZN    ZN A   4                 SG  CYS A 313     1555   1555  2.29  
LINK        ZN    ZN A   4                 SG  CYS A 306     1555   1555  2.30  
LINK        ZN    ZN A   4                 SG  CYS A 244     1555   1555  2.33  
LINK        ZN    ZN B   8                 SG  CYS B 306     1555   1555  2.32  
LINK        ZN    ZN B   8                 SG  CYS B 244     1555   1555  2.38  
LINK        ZN    ZN B   8                 SG  CYS B 308     1555   1555  2.28  
LINK        ZN    ZN B   8                 SG  CYS B 313     1555   1555  2.38  
LINK         SG  CYS B 134                ZN    ZN B   6     1555   1555  2.82  
SITE     1 AC1  4 CYS A  66  CYS A  81  CYS A 128  CYS A 132                    
SITE     1 AC2  4 CYS A  74  CYS A 128  CYS A 134  CYS A 138                    
SITE     1 AC3  4 CYS A  66  CYS A  68  CYS A  74  CYS A  79                    
SITE     1 AC4  4 CYS A 244  CYS A 306  CYS A 308  CYS A 313                    
SITE     1 AC5  2  ZN B   6  CYS B 132                                          
SITE     1 AC6  4  ZN B   5   ZN B   7  CYS B 134  CYS B 138                    
SITE     1 AC7  1  ZN B   6                                                     
SITE     1 AC8  4 CYS B 244  CYS B 306  CYS B 308  CYS B 313                    
SITE     1 AC9 12 ARG A 159  TRP A 161  ASP A 202  VAL A 203                    
SITE     2 AC9 12 TYR A 204  ARG A 238  ASN A 241  HIS A 242                    
SITE     3 AC9 12 TYR A 283  CYS A 306  LEU A 307  LEU A 317                    
SITE     1 BC1 15 ARG B 159  TRP B 161  LYS B 201  ASP B 202                    
SITE     2 BC1 15 VAL B 203  TYR B 204  ARG B 238  ASN B 241                    
SITE     3 BC1 15 HIS B 242  TYR B 283  LYS B 305  CYS B 306                    
SITE     4 BC1 15 LEU B 307  LEU B 317  LYS Q   9                               
CRYST1   68.260   94.170  114.690  90.00  90.00  90.00 P 21 21 21    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      0.014650  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010619  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008719        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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