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Database: PDB
Entry: 2FC0
LinkDB: 2FC0
Original site: 2FC0 
HEADER    TRANSFERASE                             10-DEC-05   2FC0              
TITLE     WRN EXONUCLEASE, MN DGMP COMPLEX                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: WERNER SYNDROME HELICASE;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: EXONUCLEASE DOMAIN;                                        
COMPND   5 EC: 2.7.7.-;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: WRN, RECQ3, RECQL2;                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYSS;                          
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28B                                    
KEYWDS    RECQ, WRN, WERNER SYNDROME, 3'-5' EXONUCLEASE, DNAQ FAMILY,           
KEYWDS   2 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.J.PERRY,J.A.TAINER                                                  
REVDAT   5   30-AUG-23 2FC0    1       REMARK SEQADV LINK                       
REVDAT   4   13-JUL-11 2FC0    1       VERSN                                    
REVDAT   3   24-FEB-09 2FC0    1       VERSN                                    
REVDAT   2   13-JUN-06 2FC0    1       JRNL                                     
REVDAT   1   25-APR-06 2FC0    0                                                
JRNL        AUTH   J.J.PERRY,S.M.YANNONE,L.G.HOLDEN,C.HITOMI,A.ASAITHAMBY,      
JRNL        AUTH 2 S.HAN,P.K.COOPER,D.J.CHEN,J.A.TAINER                         
JRNL        TITL   WRN EXONUCLEASE STRUCTURE AND MOLECULAR MECHANISM IMPLY AN   
JRNL        TITL 2 EDITING ROLE IN DNA END PROCESSING.                          
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  13   414 2006              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   16622405                                                     
JRNL        DOI    10.1038/NSMB1088                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.90                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 397871.520                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 24008                          
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) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.238                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1148                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.13                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3601                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2630                       
REMARK   3   BIN FREE R VALUE                    : 0.2660                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.70                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 184                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.020                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1565                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 25                                      
REMARK   3   SOLVENT ATOMS            : 205                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.80000                                              
REMARK   3    B22 (A**2) : 1.80000                                              
REMARK   3    B33 (A**2) : -3.60000                                             
REMARK   3    B12 (A**2) : 0.55000                                              
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) : 0.25                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.19                            
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) : 0.26                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.19                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.200                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.790                           
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) : 1.470 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.300 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.320 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.560 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.33                                                 
REMARK   3   BSOL        : 61.14                                                
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.PARAM                                    
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : DGP.PARAM                                      
REMARK   3  PARAMETER FILE  5  : 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   : DGP.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2FC0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000035698.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 4.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95                               
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI (111)            
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   : 24008                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 6.750                              
REMARK 200  R MERGE                    (I) : 0.07500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 54.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.13                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.26                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.08500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.32100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 8.500                              
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 2FBT                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.55                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.79                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 5UL OF 4.5MG/ML WRN EXONUCLEASE          
REMARK 280  BUFFERED IN 25MM TRIS HCL, 100MM NACL, PH 7.5, MIXED WITH 5UL 1%    
REMARK 280  MPEG 2K, 200MM NA ACETATE, PH 4.5 FROM THE RESERVIOR SOLUTION       
REMARK 280  AND 1UL EDTA ADDITIVE, VAPOR DIFFUSION, SITTING DROP,               
REMARK 280  TEMPERATURE 277K, PH 4.50                                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       62.37333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       31.18667            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       31.18667            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       62.37333            
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     HIS A    32                                                      
REMARK 465     HIS A    33                                                      
REMARK 465     HIS A    34                                                      
REMARK 465     HIS A    35                                                      
REMARK 465     ASP A   232                                                      
REMARK 465     THR A   233                                                      
REMARK 465     VAL A   234                                                      
REMARK 465     GLN A   235                                                      
REMARK 465     ARG A   236                                                      
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    PRO A  87       20.14    -75.91                                   
REMARK 500    THR A 174       74.68   -102.41                                   
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                              MN A 237  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  82   OD1                                                    
REMARK 620 2 GLU A  84   OE2  94.8                                              
REMARK 620 3 ASP A 216   OD2  95.2  98.5                                        
REMARK 620 4 HOH A 257   O    84.1 178.5  82.7                                  
REMARK 620 5 HOH A 369   O   173.7  89.4  88.8  91.6                            
REMARK 620 6 HOH A 425   O    88.3  83.1 176.0  95.7  87.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 238  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  82   OD2                                                    
REMARK 620 2 HOH A 374   O    91.1                                              
REMARK 620 3 HOH A 424   O    94.0  82.9                                        
REMARK 620 4 HOH A 425   O    82.3  79.3 161.7                                  
REMARK 620 5 HOH A 427   O    90.0 163.7  80.8 116.9                            
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 MN A 237                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 238                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGP A 239                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2FBT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2FBV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2FBX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2FC0   RELATED DB: PDB                                   
DBREF  2FC0 A   38   236  UNP    Q14191   WRN_HUMAN       38    236             
SEQADV 2FC0 HIS A   32  UNP  Q14191              EXPRESSION TAG                 
SEQADV 2FC0 HIS A   33  UNP  Q14191              EXPRESSION TAG                 
SEQADV 2FC0 HIS A   34  UNP  Q14191              EXPRESSION TAG                 
SEQADV 2FC0 HIS A   35  UNP  Q14191              EXPRESSION TAG                 
SEQADV 2FC0 HIS A   36  UNP  Q14191              EXPRESSION TAG                 
SEQADV 2FC0 HIS A   37  UNP  Q14191              EXPRESSION TAG                 
SEQRES   1 A  205  HIS HIS HIS HIS HIS HIS SER VAL PHE GLU ASP ASP LEU          
SEQRES   2 A  205  PRO PHE LEU GLU PHE THR GLY SER ILE VAL TYR SER TYR          
SEQRES   3 A  205  ASP ALA SER ASP CYS SER PHE LEU SER GLU ASP ILE SER          
SEQRES   4 A  205  MET SER LEU SER ASP GLY ASP VAL VAL GLY PHE ASP MET          
SEQRES   5 A  205  GLU TRP PRO PRO LEU TYR ASN ARG GLY LYS LEU GLY LYS          
SEQRES   6 A  205  VAL ALA LEU ILE GLN LEU CYS VAL SER GLU SER LYS CYS          
SEQRES   7 A  205  TYR LEU PHE HIS VAL SER SER MET SER VAL PHE PRO GLN          
SEQRES   8 A  205  GLY LEU LYS MET LEU LEU GLU ASN LYS ALA VAL LYS LYS          
SEQRES   9 A  205  ALA GLY VAL GLY ILE GLU GLY ASP GLN TRP LYS LEU LEU          
SEQRES  10 A  205  ARG ASP PHE ASP ILE LYS LEU LYS ASN PHE VAL GLU LEU          
SEQRES  11 A  205  THR ASP VAL ALA ASN LYS LYS LEU LYS CYS THR GLU THR          
SEQRES  12 A  205  TRP SER LEU ASN SER LEU VAL LYS HIS LEU LEU GLY LYS          
SEQRES  13 A  205  GLN LEU LEU LYS ASP LYS SER ILE ARG CYS SER ASN TRP          
SEQRES  14 A  205  SER LYS PHE PRO LEU THR GLU ASP GLN LYS LEU TYR ALA          
SEQRES  15 A  205  ALA THR ASP ALA TYR ALA GLY PHE ILE ILE TYR ARG ASN          
SEQRES  16 A  205  LEU GLU ILE LEU ASP ASP THR VAL GLN ARG                      
HET     MN  A 237       1                                                       
HET     MN  A 238       1                                                       
HET    DGP  A 239      23                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     DGP 2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE                               
FORMUL   2   MN    2(MN 2+)                                                     
FORMUL   4  DGP    C10 H14 N5 O7 P                                              
FORMUL   5  HOH   *205(H2 O)                                                    
HELIX    1   1 SER A   38  ASP A   42  5                                   5    
HELIX    2   2 ASP A   58  LEU A   73  1                                  16    
HELIX    3   3 VAL A  114  MET A  117  5                                   4    
HELIX    4   4 PRO A  121  ASN A  130  1                                  10    
HELIX    5   5 GLY A  139  ASP A  152  1                                  14    
HELIX    6   6 LEU A  161  LEU A  169  1                                   9    
HELIX    7   7 SER A  176  GLY A  186  1                                  11    
HELIX    8   8 ASP A  192  CYS A  197  1                                   6    
HELIX    9   9 THR A  206  LEU A  230  1                                  25    
SHEET    1   A 6 SER A  52  SER A  56  0                                        
SHEET    2   A 6 LYS A 108  PHE A 112  1  O  LEU A 111   N  VAL A  54           
SHEET    3   A 6 LEU A  99  SER A 105 -1  N  ILE A 100   O  PHE A 112           
SHEET    4   A 6 VAL A  78  GLU A  84 -1  N  GLY A  80   O  CYS A 103           
SHEET    5   A 6 LYS A 134  GLY A 137  1  O  ALA A 136   N  VAL A  79           
SHEET    6   A 6 PHE A 158  GLU A 160  1  O  VAL A 159   N  LYS A 135           
SHEET    1   B 2 TYR A  89  ASN A  90  0                                        
SHEET    2   B 2 LYS A  93  LEU A  94 -1  O  LYS A  93   N  ASN A  90           
LINK         OD1 ASP A  82                MN    MN A 237     1555   1555  2.00  
LINK         OD2 ASP A  82                MN    MN A 238     1555   1555  2.19  
LINK         OE2 GLU A  84                MN    MN A 237     1555   1555  2.00  
LINK         OD2 ASP A 216                MN    MN A 237     1555   1555  2.10  
LINK        MN    MN A 237                 O   HOH A 257     1555   1555  2.22  
LINK        MN    MN A 237                 O   HOH A 369     1555   1555  2.29  
LINK        MN    MN A 237                 O   HOH A 425     1555   1555  2.24  
LINK        MN    MN A 238                 O   HOH A 374     1555   1555  2.46  
LINK        MN    MN A 238                 O   HOH A 424     1555   1555  2.32  
LINK        MN    MN A 238                 O   HOH A 425     1555   1555  2.34  
LINK        MN    MN A 238                 O   HOH A 427     1555   1555  2.27  
CISPEP   1 PHE A  203    PRO A  204          0        -1.50                     
SITE     1 AC1  6 ASP A  82  GLU A  84  ASP A 216  HOH A 257                    
SITE     2 AC1  6 HOH A 369  HOH A 425                                          
SITE     1 AC2  6 ASP A  82  HOH A 248  HOH A 374  HOH A 424                    
SITE     2 AC2  6 HOH A 425  HOH A 427                                          
SITE     1 AC3 10 TYR A  55  TYR A  57  TRP A 145  PHE A 203                    
SITE     2 AC3 10 PRO A 204  LYS A 210  HOH A 240  HOH A 331                    
SITE     3 AC3 10 HOH A 377  HOH A 407                                          
CRYST1   81.104   81.104   93.560  90.00  90.00 120.00 P 32 2 1      6          
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      0.012330  0.007119  0.000000        0.00000                         
SCALE2      0.000000  0.014237  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010688        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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