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Database: PDB
Entry: 5CFE
LinkDB: 5CFE
Original site: 5CFE 
HEADER    HYDROLASE                               08-JUL-15   5CFE              
TITLE     BACILLUS SUBTILIS AP ENDONUCLEASE EXOA                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EXODEOXYRIBONUCLEASE;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.1.11.2;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS (STRAIN 168);                 
SOURCE   3 ORGANISM_TAXID: 224308;                                              
SOURCE   4 STRAIN: 168;                                                         
SOURCE   5 GENE: EXOA, BSU40880;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HYDROLASE, AP ENDONUCLEASE                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.MORERA,A.VIGOUROUX                                                  
REVDAT   2   05-OCT-16 5CFE    1       JRNL                                     
REVDAT   1   06-JUL-16 5CFE    0                                                
JRNL        AUTH   M.REDREJO-RODRIGUEZ,A.VIGOUROUX,A.MURSALIMOV,I.GRIN,D.ALILI, 
JRNL        AUTH 2 Z.KOSHENOV,Z.AKISHEV,A.MAKSIMENKO,A.K.BISSENBAEV,            
JRNL        AUTH 3 B.T.MATKARIMOV,M.SAPARBAEV,A.A.ISHCHENKO,S.MORERA            
JRNL        TITL   STRUCTURAL COMPARISON OF AP ENDONUCLEASES FROM THE           
JRNL        TITL 2 EXONUCLEASE III FAMILY REVEALS NEW AMINO ACID RESIDUES IN    
JRNL        TITL 3 HUMAN AP ENDONUCLEASE 1 THAT ARE INVOLVED IN INCISION OF     
JRNL        TITL 4 DAMAGED DNA.                                                 
JRNL        REF    BIOCHIMIE                     V.-129    20 2016              
JRNL        REFN                   ISSN 0300-9084                               
JRNL        PMID   27343627                                                     
JRNL        DOI    10.1016/J.BIOCHI.2016.06.011                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.84 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.0                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.84                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.57                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 21096                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.169                          
REMARK   3   R VALUE            (WORKING SET)  : 0.167                          
REMARK   3   FREE R VALUE                      : 0.208                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.000                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1055                           
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               : 11                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.84                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.93                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.14                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2662                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.1985                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2529                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.1969                   
REMARK   3   BIN FREE R VALUE                        : 0.2278                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.00                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 133                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2062                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 24                                      
REMARK   3   SOLVENT ATOMS            : 189                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.09                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.78                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.46940                                              
REMARK   3    B22 (A**2) : -0.56910                                             
REMARK   3    B33 (A**2) : 0.09970                                              
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) : 0.189               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.143               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.129               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.134               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.125               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.925                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 2126   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 2868   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 759    ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 66     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 300    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 2126   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 261    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 2654   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.009                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.07                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.90                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 19.17                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -24.1666    1.7243   -1.1375           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0307 T22:   -0.0662                                    
REMARK   3     T33:   -0.0325 T12:    0.0117                                    
REMARK   3     T13:    0.0029 T23:   -0.0046                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.0230 L22:    0.7542                                    
REMARK   3     L33:    1.0622 L12:    0.0242                                    
REMARK   3     L13:    0.5352 L23:   -0.1293                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0897 S12:    0.0363 S13:   -0.0591                     
REMARK   3     S21:   -0.0179 S22:   -0.0428 S23:   -0.0048                     
REMARK   3     S31:    0.1122 S32:    0.0249 S33:   -0.0468                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5CFE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-JUL-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000211533.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-FEB-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 1                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : SI III                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21097                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.840                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.0900                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.84                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.62000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.990                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1BIX                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% (W/V) PEG 4000, 0.2 M CACL2, 0.1 M   
REMARK 280  TRIS-HCL, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K   
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       26.14000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       36.68000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       30.96000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       36.68000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.14000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       30.96000            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1050 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11610 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
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 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    GLN A  40     -168.81   -122.71                                   
REMARK 500    ASP A  41     -112.00     16.67                                   
REMARK 500    GLN A  43      -37.69   -132.08                                   
REMARK 500    ASP A  50      -12.40     90.88                                   
REMARK 500    SER A  64     -144.10     51.06                                   
REMARK 500    ARG A 111      163.21     73.28                                   
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                              CA A 301  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A   9   OD1                                                    
REMARK 620 2 GLU A  36   OE1  85.3                                              
REMARK 620 3 GLU A  36   OE2 112.9  54.7                                        
REMARK 620 4 HOH A 415   O    90.3 162.8 141.4                                  
REMARK 620 5 HOH A 462   O    81.5 112.8  71.3  82.9                            
REMARK 620 6 HOH A 557   O   167.5  96.6  77.9  84.2 108.9                      
REMARK 620 7 HOH A 529   O    79.6  80.6 130.5  82.2 155.7  88.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 305  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  98   OE1                                                    
REMARK 620 2 GLU A  98   OE2  54.1                                              
REMARK 620 3 HOH A 549   O    80.3  78.5                                        
REMARK 620 4 GLU A  27   OE1  45.3  97.9  99.7                                  
REMARK 620 5 GLU A  27   OE2  44.4  97.0  99.8   1.0                            
REMARK 620 6 GLU A 247   OE1  44.3  94.8 105.6   7.2   6.6                      
REMARK 620 7 GLU A 247   OE2  42.0  92.8 103.9   7.2   6.4   2.4                
REMARK 620 8 HOH A 514   O    87.9 138.1  78.2  53.1  54.0  59.2  60.1          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 306  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 195   OE1                                                    
REMARK 620 2 GLU A 195   OE2  52.0                                              
REMARK 620 3 HOH A 562   O    76.3 113.6                                        
REMARK 620 4 HOH A 548   O   127.5  76.8 122.3                                  
REMARK 620 5 HOH A 572   O    80.6 131.1  56.1 151.8                            
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 CA A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 305                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 306                  
DBREF  5CFE A    1   252  UNP    P37454   EXOA_BACSU       1    252             
SEQRES   1 A  252  MET LYS LEU ILE SER TRP ASN VAL ASN GLY LEU ARG ALA          
SEQRES   2 A  252  VAL MET ARG LYS MET ASP PHE LEU SER TYR LEU LYS GLU          
SEQRES   3 A  252  GLU ASP ALA ASP ILE ILE CYS LEU GLN GLU THR LYS ILE          
SEQRES   4 A  252  GLN ASP GLY GLN VAL ASP LEU GLN PRO GLU ASP TYR HIS          
SEQRES   5 A  252  VAL TYR TRP ASN TYR ALA VAL LYS LYS GLY TYR SER GLY          
SEQRES   6 A  252  THR ALA VAL PHE SER LYS GLN GLU PRO LEU GLN VAL ILE          
SEQRES   7 A  252  TYR GLY ILE GLY VAL GLU GLU HIS ASP GLN GLU GLY ARG          
SEQRES   8 A  252  VAL ILE THR LEU GLU PHE GLU ASN VAL PHE VAL MET THR          
SEQRES   9 A  252  VAL TYR THR PRO ASN SER ARG ARG GLY LEU GLU ARG ILE          
SEQRES  10 A  252  ASP TYR ARG MET GLN TRP GLU GLU ALA LEU LEU SER TYR          
SEQRES  11 A  252  ILE LEU GLU LEU ASP GLN LYS LYS PRO VAL ILE LEU CYS          
SEQRES  12 A  252  GLY ASP LEU ASN VAL ALA HIS GLN GLU ILE ASP LEU LYS          
SEQRES  13 A  252  ASN PRO LYS ALA ASN ARG ASN ASN ALA GLY PHE SER ASP          
SEQRES  14 A  252  GLN GLU ARG GLU ALA PHE THR ARG PHE LEU GLU ALA GLY          
SEQRES  15 A  252  PHE VAL ASP SER PHE ARG HIS VAL TYR PRO ASP LEU GLU          
SEQRES  16 A  252  GLY ALA TYR SER TRP TRP SER TYR ARG ALA GLY ALA ARG          
SEQRES  17 A  252  ASP ARG ASN ILE GLY TRP ARG ILE ASP TYR PHE VAL VAL          
SEQRES  18 A  252  SER GLU SER LEU LYS GLU GLN ILE GLU ASP ALA SER ILE          
SEQRES  19 A  252  SER ALA ASP VAL MET GLY SER ASP HIS CYS PRO VAL GLU          
SEQRES  20 A  252  LEU ILE ILE ASN ILE                                          
HET     CA  A 301       1                                                       
HET    PEG  A 302       7                                                       
HET    PEG  A 303       7                                                       
HET    PEG  A 304       7                                                       
HET     CA  A 305       1                                                       
HET     CA  A 306       1                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
FORMUL   2   CA    3(CA 2+)                                                     
FORMUL   3  PEG    3(C4 H10 O3)                                                 
FORMUL   8  HOH   *189(H2 O)                                                    
HELIX    1 AA1 GLY A   10  MET A   18  1                                   9    
HELIX    2 AA2 ASP A   19  ASP A   28  1                                  10    
HELIX    3 AA3 VAL A   83  ASP A   87  5                                   5    
HELIX    4 AA4 ARG A  111  GLU A  115  5                                   5    
HELIX    5 AA5 ARG A  116  LYS A  138  1                                  23    
HELIX    6 AA6 GLN A  151  LEU A  155  5                                   5    
HELIX    7 AA7 ASN A  157  ASN A  161  5                                   5    
HELIX    8 AA8 SER A  168  ALA A  181  1                                  14    
HELIX    9 AA9 SER A  186  TYR A  191  1                                   6    
HELIX   10 AB1 SER A  224  GLU A  227  5                                   4    
SHEET    1 AA1 6 HIS A  52  ASN A  56  0                                        
SHEET    2 AA1 6 THR A  66  SER A  70 -1  O  SER A  70   N  HIS A  52           
SHEET    3 AA1 6 ILE A  31  GLN A  35 -1  N  ILE A  32   O  PHE A  69           
SHEET    4 AA1 6 LYS A   2  ASN A   7  1  N  ILE A   4   O  CYS A  33           
SHEET    5 AA1 6 VAL A 246  ILE A 250 -1  O  LEU A 248   N  LEU A   3           
SHEET    6 AA1 6 ILE A 229  ILE A 234 -1  N  ASP A 231   O  ILE A 249           
SHEET    1 AA2 6 GLN A  76  TYR A  79  0                                        
SHEET    2 AA2 6 VAL A  92  GLU A  96 -1  O  THR A  94   N  ILE A  78           
SHEET    3 AA2 6 PHE A 101  TYR A 106 -1  O  VAL A 102   N  LEU A  95           
SHEET    4 AA2 6 VAL A 140  ASP A 145  1  O  ILE A 141   N  MET A 103           
SHEET    5 AA2 6 ASP A 217  SER A 222 -1  O  VAL A 220   N  LEU A 142           
SHEET    6 AA2 6 PHE A 183  ASP A 185 -1  N  VAL A 184   O  VAL A 221           
SHEET    1 AA3 2 TRP A 200  TRP A 201  0                                        
SHEET    2 AA3 2 GLY A 213  TRP A 214 -1  O  TRP A 214   N  TRP A 200           
LINK         OD1 ASN A   9                CA    CA A 301     1555   1555  2.46  
LINK         OE1 GLU A  36                CA    CA A 301     1555   1555  2.20  
LINK         OE2 GLU A  36                CA    CA A 301     1555   1555  2.54  
LINK         OE1 GLU A  98                CA    CA A 305     1555   1555  2.41  
LINK         OE2 GLU A  98                CA    CA A 305     1555   1555  2.42  
LINK         OE1 GLU A 195                CA    CA A 306     1555   1555  2.52  
LINK         OE2 GLU A 195                CA    CA A 306     1555   1555  2.49  
LINK        CA    CA A 301                 O   HOH A 415     1555   1555  2.31  
LINK        CA    CA A 301                 O   HOH A 462     1555   1555  2.42  
LINK        CA    CA A 301                 O   HOH A 557     1555   1555  2.44  
LINK        CA    CA A 301                 O   HOH A 529     1555   1555  2.33  
LINK        CA    CA A 305                 O   HOH A 549     1555   1555  2.39  
LINK        CA    CA A 306                 O   HOH A 562     1555   1555  2.64  
LINK        CA    CA A 306                 O   HOH A 548     1555   1555  2.40  
LINK        CA    CA A 306                 O   HOH A 572     1555   1555  3.00  
LINK         OE1 GLU A  27                CA    CA A 305     1555   4445  2.55  
LINK         OE2 GLU A  27                CA    CA A 305     1555   4445  2.45  
LINK         OE1 GLU A 247                CA    CA A 305     1555   4445  2.53  
LINK         OE2 GLU A 247                CA    CA A 305     1555   4445  2.48  
LINK        CA    CA A 305                 O   HOH A 514     1555   4545  2.37  
CISPEP   1 ASP A   41    GLY A   42          0        -2.81                     
SITE     1 AC1  6 ASN A   9  GLU A  36  HOH A 415  HOH A 462                    
SITE     2 AC1  6 HOH A 529  HOH A 557                                          
SITE     1 AC2  3 GLU A 133  LEU A 134  LYS A 137                               
SITE     1 AC3  5 ILE A  78  TYR A  79  ILE A  81  GLY A  82                    
SITE     2 AC3  5 HOH A 404                                                     
SITE     1 AC4  7 ALA A 165  TRP A 200  TRP A 214  HOH A 417                    
SITE     2 AC4  7 HOH A 418  HOH A 465  HOH A 484                               
SITE     1 AC5  5 GLU A  27  GLU A  98  GLU A 247  HOH A 514                    
SITE     2 AC5  5 HOH A 549                                                     
SITE     1 AC6  4 GLU A 195  HOH A 548  HOH A 562  HOH A 572                    
CRYST1   52.280   61.920   73.360  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      0.019128  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016150  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013631        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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