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Database: PDB
Entry: 1ML9
LinkDB: 1ML9
Original site: 1ML9 
HEADER    TRANSFERASE                             30-AUG-02   1ML9              
TITLE     STRUCTURE OF THE NEUROSPORA SET DOMAIN PROTEIN DIM-5, A               
TITLE    2 HISTONE LYSINE METHYLTRANSFERASE                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE H3 METHYLTRANSFERASE DIM-5;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 17-318;                                           
COMPND   5 EC: 2.1.1.43;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: NEUROSPORA CRASSA;                              
SOURCE   3 ORGANISM_TAXID: 5141;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PXC379                                    
KEYWDS    DIM-5, ADOMET-DEPENDENT METHYLTRANSFERASE HISTONE H3 LYSINE-          
KEYWDS   2 9 METHYLATION                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.ZHANG,H.TAMARU,S.I.KHAN,J.R.HORTON,L.J.KEEFE,E.U.SELKER,            
AUTHOR   2 X.CHENG                                                              
REVDAT   2   24-FEB-09 1ML9    1       VERSN                                    
REVDAT   1   23-OCT-02 1ML9    0                                                
JRNL        AUTH   X.ZHANG,H.TAMARU,S.I.KHAN,J.R.HORTON,L.J.KEEFE,              
JRNL        AUTH 2 E.U.SELKER,X.CHENG                                           
JRNL        TITL   STRUCTURE OF THE NEUROSPORA SET DOMAIN PROTEIN               
JRNL        TITL 2 DIM-5, A HISTONE H3 LYSINE METHYLTRANSFERASE                 
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 111   117 2002              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   12372305                                                     
JRNL        DOI    10.1016/S0092-8674(02)00999-6                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.98 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) : 1.98                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.83                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 20963                          
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) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.258                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2620                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.98                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.10                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 67.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2660                       
REMARK   3   BIN FREE R VALUE                    : 0.2810                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 342                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.015                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1923                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 3                                       
REMARK   3   SOLVENT ATOMS            : 117                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.24                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.23                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 24.83                           
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.80                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.72                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
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 : NULL                                                    
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1ML9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-SEP-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB017001.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-FEB-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0332, 1.2834, 1.2830             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20963                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.980                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.830                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 5.370                              
REMARK 200  R MERGE                    (I) : 0.05500                            
REMARK 200  R SYM                      (I) : 0.05500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.27600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.27600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.65                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, SODIUM CITRATE,        
REMARK 280  PH 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K             
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       18.36500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       50.63500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.78000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       50.63500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       18.36500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.78000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     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     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     ASP A    94                                                      
REMARK 465     PRO A    95                                                      
REMARK 465     TYR A    96                                                      
REMARK 465     THR A    97                                                      
REMARK 465     ARG A    98                                                      
REMARK 465     LYS A    99                                                      
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     GLY A   309                                                      
REMARK 465     THR A   310                                                      
REMARK 465     ALA A   311                                                      
REMARK 465     LYS A   312                                                      
REMARK 465     CYS A   313                                                      
REMARK 465     ARG A   314                                                      
REMARK 465     GLY A   315                                                      
REMARK 465     TYR A   316                                                      
REMARK 465     LEU A   317                                                      
REMARK 465     TRP A   318                                                      
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     ASP A  59    CG   OD1  OD2                                       
REMARK 470     ALA A  69    CB                                                  
REMARK 470     SER A  70    OG                                                  
REMARK 470     GLU A  72    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  73    CB   CG   CD   OE1  OE2                             
REMARK 470     ASP A  88    CG   OD1  OD2                                       
REMARK 470     LYS A 100    CG   CD   CE   NZ                                   
REMARK 470     ARG A 101    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 107    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 111    CG   CD   CE   NZ                                   
REMARK 470     ARG A 117    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 120    CG   CD   OE1  NE2                                  
REMARK 470     SER A 135    CB   OG                                             
REMARK 470     LYS A 136    CG   CD   CE   NZ                                   
REMARK 470     ASP A 137    CG   OD1  OD2                                       
REMARK 470     LYS A 157    CG   CD   CE   NZ                                   
REMARK 470     SER A 216    CB   OG                                             
REMARK 470     LEU A 217    CB   CG   CD1  CD2                                  
REMARK 470     ASP A 218    CG   OD1  OD2                                       
REMARK 470     LEU A 220    CG   CD1  CD2                                       
REMARK 470     ASN A 285    CG   OD1  ND2                                       
REMARK 470     LYS A 299    N    C    O    CB   CG   CD   CE                    
REMARK 470     LYS A 299    NZ                                                  
REMARK 470     ILE A 300    N    C    O    CB   CG1  CG2  CD1                   
REMARK 470     SER A 301    N    C    O    CB   OG                              
REMARK 470     GLU A 302    N    C    O    CB   CG   CD   OE1                   
REMARK 470     GLU A 302    OE2                                                 
REMARK 470     MET A 303    N    C    O    CB   CG   SD   CE                    
REMARK 470     THR A 304    N    C    O    CB   OG1  CG2                        
REMARK 470     LYS A 305    N    C    O    CB   CG   CD   CE                    
REMARK 470     LYS A 305    NZ                                                  
REMARK 470     CYS A 306    N    C    O    CB   SG                              
REMARK 470     LEU A 307    N    C    O    CB   CG   CD1  CD2                   
REMARK 470     CYS A 308    N    C    O    CB   SG                              
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    ALA A  58      131.12    -38.99                                   
REMARK 500    ASP A  71      -17.57    -47.37                                   
REMARK 500    SER A 106      -72.18    -66.36                                   
REMARK 500    ASP A 158       23.36   -150.17                                   
REMARK 500    PRO A 214       77.53    -63.30                                   
REMARK 500    ASP A 215     -146.65   -162.82                                   
REMARK 500    LEU A 217       15.99    139.33                                   
REMARK 500    ASP A 218      156.52     72.80                                   
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  66   SG                                                     
REMARK 620 2 CYS A  81   SG  117.0                                              
REMARK 620 3 CYS A 132   SG  106.0  97.8                                        
REMARK 620 4 CYS A 128   SG  109.7 115.0 110.3                                  
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  74   SG                                                     
REMARK 620 2 CYS A 138   SG  109.7                                              
REMARK 620 3 CYS A 128   SG  107.8 108.4                                        
REMARK 620 4 CYS A 134   SG  117.3 107.6 105.7                                  
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  68   SG                                                     
REMARK 620 2 CYS A  79   SG  111.0                                              
REMARK 620 3 CYS A  74   SG  101.0 119.4                                        
REMARK 620 4 CYS A  66   SG  117.4 105.5 103.0                                  
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                    
DBREF  1ML9 A   17   318  GB     17063801 AAL35215        17    318             
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                                                  
HET     ZN  A   1       1                                                       
HET     ZN  A   2       1                                                       
HET     ZN  A   3       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   2   ZN    3(ZN 2+)                                                     
FORMUL  11  HOH   *111(H2 O)                                                    
HELIX    1   1 ASP A   59  ARG A   63  5                                   5    
HELIX    2   2 GLU A   72  TYR A   76  5                                   5    
HELIX    3   3 CYS A   79  ASP A   83  5                                   5    
HELIX    4   4 ARG A  115  GLN A  122  1                                   8    
HELIX    5   5 ARG A  141  GLY A  146  1                                   6    
HELIX    6   6 THR A  184  SER A  195  1                                  12    
HELIX    7   7 THR A  196  ARG A  199  5                                   4    
HELIX    8   8 ARG A  200  TYR A  204  1                                   5    
HELIX    9   9 ASP A  218  GLY A  223  1                                   6    
HELIX   10  10 GLY A  235  ILE A  240  5                                   6    
HELIX   11  11 ASP A  256  HIS A  263  5                                   8    
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  LYS A 164   N  GLN A 152           
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  VAL A 254   N  ILE A 125           
SHEET    3   D 4 ASP A 264  ALA A 269 -1  O  ALA A 266   N  PHE A 251           
SHEET    4   D 4 PHE A 174  ARG A 177 -1  N  ASP A 176   O  LEU A 267           
LINK        ZN    ZN A   1                 SG  CYS A  66     1555   1555  2.35  
LINK        ZN    ZN A   1                 SG  CYS A  81     1555   1555  2.29  
LINK        ZN    ZN A   1                 SG  CYS A 132     1555   1555  2.24  
LINK        ZN    ZN A   1                 SG  CYS A 128     1555   1555  2.37  
LINK        ZN    ZN A   2                 SG  CYS A  74     1555   1555  2.32  
LINK        ZN    ZN A   2                 SG  CYS A 138     1555   1555  2.35  
LINK        ZN    ZN A   2                 SG  CYS A 128     1555   1555  2.33  
LINK        ZN    ZN A   2                 SG  CYS A 134     1555   1555  2.29  
LINK        ZN    ZN A   3                 SG  CYS A  68     1555   1555  2.33  
LINK        ZN    ZN A   3                 SG  CYS A  79     1555   1555  2.32  
LINK        ZN    ZN A   3                 SG  CYS A  74     1555   1555  2.37  
LINK        ZN    ZN A   3                 SG  CYS A  66     1555   1555  2.33  
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                    
CRYST1   36.730   81.560  101.270  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.027226  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012261  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009875        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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