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Database: PDB
Entry: 2E6L
LinkDB: 2E6L
Original site: 2E6L 
HEADER    HYDROLASE                               27-DEC-06   2E6L              
TITLE     STRUCTURE OF MOUSE WRN EXONUCLEASE DOMAIN                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: WERNER SYNDROME ATP-DEPENDENT HELICASE HOMOLOG;            
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: WRN EXONUCLEASE DOMAIN, RESIDUES 31-238;                   
COMPND   5 EC: 3.6.1.-;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: WRN;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-28A                                   
KEYWDS    ZN-PROTEIN COMPLEX, HYDROLASE                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.CHO,J.M.CHOI                                                        
REVDAT   2   24-FEB-09 2E6L    1       VERSN                                    
REVDAT   1   16-JAN-07 2E6L    0                                                
JRNL        AUTH   Y.CHO,J.M.CHOI                                               
JRNL        TITL   PROBING THE ROLES OF ACTIVE SITE RESIDUES IN 3'-5'           
JRNL        TITL 2 EXONUCLEASE OF WERNER SYNDROME PROTEIN                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.57                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 67763.480                      
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 10377                          
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) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 531                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.011                           
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.34                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1592                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1840                       
REMARK   3   BIN FREE R VALUE                    : 0.2250                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 83                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.025                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1465                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 7                                       
REMARK   3   SOLVENT ATOMS            : 150                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 9.40                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.65000                                             
REMARK   3    B22 (A**2) : -3.43000                                             
REMARK   3    B33 (A**2) : 5.08000                                              
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) : 0.22                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.05                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.29                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.10                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.69                            
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) : 1.390 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.190 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.370 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.340 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.40                                                 
REMARK   3   BSOL        : 46.04                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2E6L COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-JAN-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB026289.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-FEB-05; 14-FEB-05               
REMARK 200  TEMPERATURE           (KELVIN) : 93.15; NULL                        
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : PAL/PLS; PAL/PLS                   
REMARK 200  BEAMLINE                       : 4A; 4A                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.2835; 1.2831, 1.2825, 1.2699     
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : NULL; NULL                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11712                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 4.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 40.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.80                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.07600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 40.000                             
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD                         
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.28                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.5, VAPOR DIFFUSION, HANGING         
REMARK 280  DROP, TEMPERATURE 291.15K                                           
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       27.52350            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       30.12250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       29.57350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       30.12250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.52350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       29.57350            
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     LYS A    31                                                      
REMARK 465     SER A    32                                                      
REMARK 465     VAL A    33                                                      
REMARK 465     LEU A    34                                                      
REMARK 465     GLU A    35                                                      
REMARK 465     ASP A    36                                                      
REMARK 465     ILE A    82                                                      
REMARK 465     TYR A    83                                                      
REMARK 465     LYS A    84                                                      
REMARK 465     ASP A   226                                                      
REMARK 465     THR A   227                                                      
REMARK 465     VAL A   228                                                      
REMARK 465     GLN A   229                                                      
REMARK 465     VAL A   230                                                      
REMARK 465     PHE A   231                                                      
REMARK 465     ALA A   232                                                      
REMARK 465     LEU A   233                                                      
REMARK 465     ASN A   234                                                      
REMARK 465     LYS A   235                                                      
REMARK 465     ALA A   236                                                      
REMARK 465     GLU A   237                                                      
REMARK 465     GLU A   238                                                      
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 541        DISTANCE =  6.36 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  76   OD2                                                    
REMARK 620 2 GLU A  78   OE2  82.5                                              
REMARK 620 3 ASP A 210   OD1 103.2 125.0                                        
REMARK 620 4 HOH A 544   O   104.5 117.0 114.2                                  
REMARK 620 5 HOH A 586   O   163.8  96.8  90.5  61.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 549   O                                                      
REMARK 620 2 HOH A 592   O    80.6                                              
REMARK 620 3 HOH A 544   O    80.2  65.5                                        
REMARK 620 4 HOH A 606   O   171.0 102.1  93.1                                  
REMARK 620 5 ASP A  76   OD1  83.9 155.8  93.7  90.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 503                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 501                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 502                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2E6M   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN IN APO FORM                                         
DBREF  2E6L A   31   238  UNP    O09053   WRN_MOUSE       31    238             
SEQADV 2E6L SER A  101  UNP  O09053    ASN   101 SEE REMARK 999                 
SEQRES   1 A  208  LYS SER VAL LEU GLU ASP ASN LEU PRO PHE LEU GLU PHE          
SEQRES   2 A  208  PRO GLY SER ILE VAL TYR SER TYR GLU ALA SER ASP CYS          
SEQRES   3 A  208  SER PHE LEU SER GLU ASP ILE SER MET ARG LEU SER ASP          
SEQRES   4 A  208  GLY ASP VAL VAL GLY PHE ASP MET GLU TRP PRO PRO ILE          
SEQRES   5 A  208  TYR LYS PRO GLY LYS ARG SER ARG VAL ALA VAL ILE GLN          
SEQRES   6 A  208  LEU CYS VAL SER GLU SER LYS CYS TYR LEU PHE HIS ILE          
SEQRES   7 A  208  SER SER MET SER VAL PHE PRO GLN GLY LEU LYS MET LEU          
SEQRES   8 A  208  LEU GLU ASN LYS SER ILE LYS LYS ALA GLY VAL GLY ILE          
SEQRES   9 A  208  GLU GLY ASP GLN TRP LYS LEU LEU ARG ASP PHE ASP VAL          
SEQRES  10 A  208  LYS LEU GLU SER PHE VAL GLU LEU THR ASP VAL ALA ASN          
SEQRES  11 A  208  GLU LYS LEU LYS CYS ALA GLU THR TRP SER LEU ASN GLY          
SEQRES  12 A  208  LEU VAL LYS HIS VAL LEU GLY LYS GLN LEU LEU LYS ASP          
SEQRES  13 A  208  LYS SER ILE ARG CYS SER ASN TRP SER ASN PHE PRO LEU          
SEQRES  14 A  208  THR GLU ASP GLN LYS LEU TYR ALA ALA THR ASP ALA TYR          
SEQRES  15 A  208  ALA GLY LEU ILE ILE TYR GLN LYS LEU GLY ASN LEU GLY          
SEQRES  16 A  208  ASP THR VAL GLN VAL PHE ALA LEU ASN LYS ALA GLU GLU          
HET    SO4  A 503       5                                                       
HET     ZN  A 501       1                                                       
HET     ZN  A 502       1                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM      ZN ZINC ION                                                         
FORMUL   2  SO4    O4 S 2-                                                      
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   5  HOH   *150(H2 O)                                                    
HELIX    1   1 GLU A   52  LEU A   67  1                                  16    
HELIX    2   2 ILE A  108  MET A  111  5                                   4    
HELIX    3   3 PRO A  115  ASN A  124  1                                  10    
HELIX    4   4 GLY A  133  ASP A  146  1                                  14    
HELIX    5   5 LEU A  155  LEU A  163  1                                   9    
HELIX    6   6 SER A  170  GLY A  180  1                                  11    
HELIX    7   7 ASP A  186  CYS A  191  1                                   6    
HELIX    8   8 THR A  200  ASN A  223  1                                  24    
SHEET    1   A 6 SER A  46  SER A  50  0                                        
SHEET    2   A 6 LYS A 102  PHE A 106  1  O  LEU A 105   N  VAL A  48           
SHEET    3   A 6 VAL A  93  SER A  99 -1  N  LEU A  96   O  TYR A 104           
SHEET    4   A 6 VAL A  72  GLU A  78 -1  N  ASP A  76   O  GLN A  95           
SHEET    5   A 6 LYS A 128  GLY A 131  1  O  ALA A 130   N  PHE A  75           
SHEET    6   A 6 PHE A 152  GLU A 154  1  O  VAL A 153   N  LYS A 129           
LINK        ZN    ZN A 501                 OD2 ASP A  76     1555   1555  2.14  
LINK        ZN    ZN A 501                 OE2 GLU A  78     1555   1555  2.03  
LINK        ZN    ZN A 501                 OD1 ASP A 210     1555   1555  2.08  
LINK        ZN    ZN A 501                 O   HOH A 544     1555   1555  2.35  
LINK        ZN    ZN A 501                 O   HOH A 586     1555   1555  2.66  
LINK        ZN    ZN A 502                 O   HOH A 549     1555   1555  2.18  
LINK        ZN    ZN A 502                 O   HOH A 592     1555   1555  2.39  
LINK        ZN    ZN A 502                 O   HOH A 544     1555   1555  2.33  
LINK        ZN    ZN A 502                 O   HOH A 606     1555   1555  2.32  
LINK        ZN    ZN A 502                 OD1 ASP A  76     1555   1555  2.14  
CISPEP   1 PHE A  197    PRO A  198          0         0.10                     
SITE     1 AC1  6 LYS A 119  SER A 170  LEU A 171  ASN A 172                    
SITE     2 AC1  6 LYS A 185  HOH A 607                                          
SITE     1 AC2  5 ASP A  76  GLU A  78  ASP A 210  HOH A 544                    
SITE     2 AC2  5 HOH A 586                                                     
SITE     1 AC3  5 ASP A  76  HOH A 544  HOH A 549  HOH A 592                    
SITE     2 AC3  5 HOH A 606                                                     
CRYST1   55.047   59.147   60.245  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      0.018166  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016907  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016599        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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