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Database: PDB
Entry: 2WI8
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Original site: 2WI8 
HEADER    TRANSPORT PROTEIN                       08-MAY-09   2WI8              
TITLE     CRYSTAL STRUCTURE OF THE TRISCATECHOLATE SIDEROPHORE                  
TITLE    2 BINDING PROTEIN FEUA FROM BACILLUS SUBTILIS                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: IRON-UPTAKE SYSTEM-BINDING PROTEIN;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 21-317;                                           
COMPND   5 SYNONYM: SUBSTRATE BINDING PROTEIN;                                  
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 ATCC: 21332;                                                         
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PCB-28A;                                   
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: POK01                                     
KEYWDS    BACILLIBACTIN AND ENTEROBACTIN BINDING, TRISCATECHOLATE BINDING       
KEYWDS   2 PROTEIN, IRON TRANSPORT, HIGH AFFINITY IRON IMPORT, IRON, MEMBRANE,  
KEYWDS   3 PALMITATE, TRANSPORT, ABC-TYPE TRANSPORTER BINDING PROTEIN,          
KEYWDS   4 SIDEROPHORE BINDING PROTEIN, TRANSPORT PROTEIN, LIPOPROTEIN, CELL    
KEYWDS   5 MEMBRANE, ION TRANSPORT                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.PEUCKERT,M.MIETHKE,A.G.ALBRECHT,L.-O.ESSEN,M.A.MARAHIEL             
REVDAT   3   07-DEC-11 2WI8    1       JRNL                                     
REVDAT   2   13-JUL-11 2WI8    1       VERSN                                    
REVDAT   1   22-SEP-09 2WI8    0                                                
JRNL        AUTH   F.PEUCKERT,M.MIETHKE,A.G.ALBRECHT,L.-O.ESSEN,M.A.MARAHIEL    
JRNL        TITL   STRUCTURAL BASIS AND STEREOCHEMISTRY OF TRISCATECHOLATE      
JRNL        TITL 2 SIDEROPHORE BINDING BY FEUA.                                 
JRNL        REF    ANGEW.CHEM.INT.ED.ENGL.       V.  48  7924 2009              
JRNL        REFN                   ISSN 1433-7851                               
JRNL        PMID   19746494                                                     
JRNL        DOI    10.1002/ANIE.200902495                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.23                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.58                          
REMARK   3   NUMBER OF REFLECTIONS             : 38175                          
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) : 0.18267                         
REMARK   3   R VALUE            (WORKING SET) : 0.18178                         
REMARK   3   FREE R VALUE                     : 0.21544                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.6                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 999                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.551                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.592                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2591                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.65                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.263                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 69                           
REMARK   3   BIN FREE R VALUE                    : 0.257                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2247                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 3                                       
REMARK   3   SOLVENT ATOMS            : 239                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 16.698                         
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.372                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.25                                                
REMARK   3    B22 (A**2) : -0.25                                                
REMARK   3    B33 (A**2) : 0.51                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.085         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.087         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.063         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.525         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.948                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2292 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3102 ; 1.349 ; 1.983       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   294 ; 5.221 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    87 ;34.511 ;26.667       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   448 ;12.687 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     3 ;11.566 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   356 ; 0.090 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1665 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1138 ; 0.202 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1636 ; 0.312 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   218 ; 0.117 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    61 ; 0.180 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    33 ; 0.216 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1481 ; 0.855 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2359 ; 1.393 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   895 ; 2.425 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   743 ; 3.973 ; 4.500       
REMARK   3                                                                      
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT      
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP :     1                                                  
REMARK   3    NUMBER OF COMPONENTS GROUP :    1                                 
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    17        A   142                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.3081  19.1790  78.3047              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0187 T22:  -0.0049                                     
REMARK   3      T33:  -0.0179 T12:   0.0181                                     
REMARK   3      T13:   0.0049 T23:  -0.0093                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2236 L22:   0.5931                                     
REMARK   3      L33:   0.7854 L12:   0.0861                                     
REMARK   3      L13:  -0.1225 L23:   0.3556                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0072 S12:  -0.0077 S13:  -0.0290                       
REMARK   3      S21:  -0.0100 S22:  -0.0135 S23:   0.0038                       
REMARK   3      S31:  -0.0224 S32:   0.0380 S33:   0.0063                       
REMARK   3                                                                      
REMARK   3   TLS GROUP :     2                                                  
REMARK   3    NUMBER OF COMPONENTS GROUP :    1                                 
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   143        A   165                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.8590  15.5980  79.0140              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0351 T22:  -0.0244                                     
REMARK   3      T33:   0.0364 T12:  -0.0175                                     
REMARK   3      T13:   0.0161 T23:  -0.0136                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.9822 L22:   4.2943                                     
REMARK   3      L33:   1.9553 L12:  -5.6099                                     
REMARK   3      L13:   3.7707 L23:  -2.8974                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0822 S12:  -0.0965 S13:  -0.4330                       
REMARK   3      S21:  -0.0465 S22:   0.0876 S23:   0.3122                       
REMARK   3      S31:   0.0670 S32:  -0.0695 S33:  -0.1698                       
REMARK   3                                                                      
REMARK   3   TLS GROUP :     3                                                  
REMARK   3    NUMBER OF COMPONENTS GROUP :    1                                 
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   166        A   299                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.7990  38.1710  73.7592              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0220 T22:   0.0082                                     
REMARK   3      T33:  -0.0248 T12:  -0.0062                                     
REMARK   3      T13:   0.0008 T23:  -0.0141                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3277 L22:   0.6090                                     
REMARK   3      L33:   0.2556 L12:  -0.0669                                     
REMARK   3      L13:  -0.0147 L23:   0.0987                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0102 S12:   0.0343 S13:  -0.0235                       
REMARK   3      S21:  -0.0053 S22:   0.0120 S23:   0.0203                       
REMARK   3      S31:  -0.0292 S32:   0.0141 S33:  -0.0019                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   4                                                                      
REMARK   4 2WI8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-MAY-09.                  
REMARK 100 THE PDBE ID CODE IS EBI-39753.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-FEB-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97623                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39175                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.55                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.26                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 4.7                                
REMARK 200  R MERGE                    (I) : 0.06                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.50                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.7                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.37                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.80                               
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: PDB ENTRY 2PHZ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 35.88                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM            
REMARK 280  30% (V/V) JEFFAMINE ED-2001 PH 7.0, 100 MM HEPES, PH 8.0;           
REMARK 280  THEN SOAKED IN MOTHER LIQUOR CONTAINING 30% (V/V) GLYCEROL          
REMARK 280  FOR CRYOPROTECTION                                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       88.83000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       27.35500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       27.35500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       44.41500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       27.35500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       27.35500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      133.24500            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       27.35500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       27.35500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       44.41500            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       27.35500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       27.35500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      133.24500            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       88.83000            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3200 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -68.17 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 350   BIOMT1   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      177.66000            
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     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     ASN A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     SER A     7                                                      
REMARK 465     THR A     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     LYS A    11                                                      
REMARK 465     ALA A    12                                                      
REMARK 465     SER A    13                                                      
REMARK 465     GLY A    14                                                      
REMARK 465     THR A    15                                                      
REMARK 465     ALA A    16                                                      
REMARK 465     LEU A   300                                                      
REMARK 465     ALA A   301                                                      
REMARK 465     ALA A   302                                                      
REMARK 465     ALA A   303                                                      
REMARK 465     LEU A   304                                                      
REMARK 465     GLU A   305                                                      
REMARK 465     HIS A   306                                                      
REMARK 465     HIS A   307                                                      
REMARK 465     HIS A   308                                                      
REMARK 465     HIS A   309                                                      
REMARK 465     HIS A   310                                                      
REMARK 465     HIS A   311                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  18    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  20    CG   CD   CE   NZ                                   
REMARK 470     ASP A  36    CG   OD1  OD2                                       
REMARK 470     GLU A  94    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 109    CG   CD   CE   NZ                                   
REMARK 470     LYS A 159    CG   CD   CE   NZ                                   
REMARK 470     GLN A 190    CD   OE1  NE2                                       
REMARK 470     ASP A 242    CG   OD1  OD2                                       
REMARK 470     LYS A 289    CG   CD   CE   NZ                                   
REMARK 470     GLU A 293    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  2079     O    HOH A  2203              2.20            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    SER A 103   N   -  CA  -  CB  ANGL. DEV. =  -9.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A 102     -166.00   -102.74                                   
REMARK 500    TYR A 192     -141.33     65.07                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.                               
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1302                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2WHY   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE TRISCATECHOLATE                            
REMARK 900  SIDEROPHORE BINDING PROTEIN FEUA FROM BACILLUS                      
REMARK 900   SUBTILIS COMPLEXED WITH FERRI-BACILLIBACTIN                        
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 I180T S237I ARE SEQUENCE VARIANTS                                    
DBREF  2WI8 A    1     1  PDB    2WI8     2WI8             1      1             
DBREF  2WI8 A    2   298  UNP    P40409   FEUA_BACSU      21    317             
DBREF  2WI8 A  299   311  PDB    2WI8     2WI8           299    311             
SEQADV 2WI8 THR A  161  UNP  P40409    ILE   180 CONFLICT SEE REMARK 999        
SEQADV 2WI8 ILE A  218  UNP  P40409    SER   237 CONFLICT SEE REMARK 999        
SEQRES   1 A  311  MET GLY SER LYS ASN GLU SER THR ALA SER LYS ALA SER          
SEQRES   2 A  311  GLY THR ALA SER GLU LYS LYS LYS ILE GLU TYR LEU ASP          
SEQRES   3 A  311  LYS THR TYR GLU VAL THR VAL PRO THR ASP LYS ILE ALA          
SEQRES   4 A  311  ILE THR GLY SER VAL GLU SER MET GLU ASP ALA LYS LEU          
SEQRES   5 A  311  LEU ASP VAL HIS PRO GLN GLY ALA ILE SER PHE SER GLY          
SEQRES   6 A  311  LYS PHE PRO ASP MET PHE LYS ASP ILE THR ASP LYS ALA          
SEQRES   7 A  311  GLU PRO THR GLY GLU LYS MET GLU PRO ASN ILE GLU LYS          
SEQRES   8 A  311  ILE LEU GLU MET LYS PRO ASP VAL ILE LEU ALA SER THR          
SEQRES   9 A  311  LYS PHE PRO GLU LYS THR LEU GLN LYS ILE SER THR ALA          
SEQRES  10 A  311  GLY THR THR ILE PRO VAL SER HIS ILE SER SER ASN TRP          
SEQRES  11 A  311  LYS GLU ASN MET MET LEU LEU ALA GLN LEU THR GLY LYS          
SEQRES  12 A  311  GLU LYS LYS ALA LYS LYS ILE ILE ALA ASP TYR GLU GLN          
SEQRES  13 A  311  ASP LEU LYS GLU THR LYS THR LYS ILE ASN ASP LYS ALA          
SEQRES  14 A  311  LYS ASP SER LYS ALA LEU VAL ILE ARG ILE ARG GLN GLY          
SEQRES  15 A  311  ASN ILE TYR ILE TYR PRO GLU GLN VAL TYR PHE ASN SER          
SEQRES  16 A  311  THR LEU TYR GLY ASP LEU GLY LEU LYS ALA PRO ASN GLU          
SEQRES  17 A  311  VAL LYS ALA ALA LYS ALA GLN GLU LEU ILE SER LEU GLU          
SEQRES  18 A  311  LYS LEU SER GLU MET ASN PRO ASP HIS ILE PHE VAL GLN          
SEQRES  19 A  311  PHE SER ASP ASP GLU ASN ALA ASP LYS PRO ASP ALA LEU          
SEQRES  20 A  311  LYS ASP LEU GLU LYS ASN PRO ILE TRP LYS SER LEU LYS          
SEQRES  21 A  311  ALA VAL LYS GLU ASP HIS VAL TYR VAL ASN SER VAL ASP          
SEQRES  22 A  311  PRO LEU ALA GLN GLY GLY THR ALA TRP SER LYS VAL ARG          
SEQRES  23 A  311  PHE LEU LYS ALA ALA ALA GLU LYS LEU THR GLN ASN LYS          
SEQRES  24 A  311  LEU ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS              
HET     CL  A1300       1                                                       
HET     CL  A1301       1                                                       
HET     CL  A1302       1                                                       
HETNAM      CL CHLORIDE ION                                                     
FORMUL   2   CL    3(CL 1-)                                                     
FORMUL   3  HOH   *239(H2 O)                                                    
HELIX    1   1 SER A   43  ASP A   54  1                                  12    
HELIX    2   2 PRO A   68  LYS A   72  5                                   5    
HELIX    3   3 ASN A   88  LYS A   96  1                                   9    
HELIX    4   4 PRO A  107  THR A  116  1                                  10    
HELIX    5   5 ASN A  129  GLY A  142  1                                  14    
HELIX    6   6 LYS A  143  ILE A  165  1                                  23    
HELIX    7   7 ASN A  166  ASP A  171  1                                   6    
HELIX    8   8 PHE A  193  GLY A  202  1                                   6    
HELIX    9   9 PRO A  206  ALA A  212  1                                   7    
HELIX   10  10 SER A  219  ASN A  227  1                                   9    
HELIX   11  11 ASP A  237  ASN A  240  5                                   4    
HELIX   12  12 ASP A  245  ASN A  253  1                                   9    
HELIX   13  13 ASN A  253  SER A  258  1                                   6    
HELIX   14  14 LEU A  259  GLU A  264  1                                   6    
HELIX   15  15 THR A  280  THR A  296  1                                  17    
SHEET    1  AA 2 GLU A  18  TYR A  24  0                                        
SHEET    2  AA 2 LYS A  27  VAL A  33 -1  O  LYS A  27   N  TYR A  24           
SHEET    1  AB 3 ILE A  38  ILE A  40  0                                        
SHEET    2  AB 3 VAL A  99  SER A 103  1  O  VAL A  99   N  ALA A  39           
SHEET    3  AB 3 THR A 120  VAL A 123  1  O  ILE A 121   N  ALA A 102           
SHEET    1  AC 2 GLY A  59  SER A  62  0                                        
SHEET    2  AC 2 GLU A  79  GLU A  83  1  O  GLU A  79   N  ALA A  60           
SHEET    1  AD 4 ASN A 183  ILE A 186 -1  O  ILE A 186   N  GLU A 216           
SHEET    2  AD 4 ALA A 174  ARG A 180 -1  O  ARG A 178   N  TYR A 185           
SHEET    3  AD 4 HIS A 230  PHE A 235  1  O  HIS A 230   N  LEU A 175           
SHEET    4  AD 4 VAL A 267  VAL A 269  1  O  TYR A 268   N  VAL A 233           
CISPEP   1 VAL A   33    PRO A   34          0        -2.41                     
SITE     1 AC1  3 LYS A  72  HOH A2041  HOH A2052                               
SITE     1 AC2  1 THR A 161                                                     
CRYST1   54.710   54.710  177.660  90.00  90.00  90.00 P 41 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018278  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018278  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005629        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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