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Database: PDB
Entry: 2XUZ
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Original site: 2XUZ 
HEADER    TRANSPORT PROTEIN                       22-OCT-10   2XUZ              
TITLE     CRYSTAL STRUCTURE OF THE TRISCATECHOLATE SIDEROPHORE                  
TITLE    2 BINDING PROTEIN FEUA FROM BACILLUS SUBTILIS COMPLEXED WITH           
TITLE    3 FERRI-ENTEROBACTIN                                                   
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: SIDEROPHORE BINDING PROTEIN, TRISCATECHOLATE BINDING        
COMPND   6  PROTEIN;                                                            
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 STRAIN: 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_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PCB-28A;                                   
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: POK01                                     
KEYWDS    TRANSPORT PROTEIN, HIGH AFFINITY IRON IMPORT, BACILLIBACTIN AND       
KEYWDS   2 ENTEROBACTIN BINDING, IRON TRANSPORT                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.PEUCKERT,M.MIETHKE,C.J.SCHWOERER,A.G.ALBRECHT,M.OBERTHUER,          
AUTHOR   2 M.A.MARAHIEL                                                         
REVDAT   2   28-MAR-12 2XUZ    1       JRNL                                     
REVDAT   1   10-AUG-11 2XUZ    0                                                
JRNL        AUTH   F.PEUCKERT,A.L.RAMOS-VEGA,M.MIETHKE,C.J.SCHWOERER,           
JRNL        AUTH 2 A.G.ALBRECHT,M.OBERTHUER,M.A.MARAHIEL                        
JRNL        TITL   THE SIDEROPHORE BINDING PROTEIN FEUA SHOWS LIMITED           
JRNL        TITL 2 PROMISCUITY TOWARD EXOGENOUS TRISCATECHOLATES                
JRNL        REF    CHEM.BIOL.                    V.  18   907 2011              
JRNL        REFN                   ISSN 1074-5521                               
JRNL        PMID   21802011                                                     
JRNL        DOI    10.1016/J.CHEMBIOL.2011.05.006                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.83                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.04                          
REMARK   3   NUMBER OF REFLECTIONS             : 18136                          
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) : 0.18974                         
REMARK   3   R VALUE            (WORKING SET) : 0.18466                         
REMARK   3   FREE R VALUE                     : 0.24320                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.8                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1754                            
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) : 1.900                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.949                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1298                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.70                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.273                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 144                          
REMARK   3   BIN FREE R VALUE                    : 0.324                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2201                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 81                                      
REMARK   3   SOLVENT ATOMS            : 148                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 21.445                         
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.421                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.19                                                 
REMARK   3    B22 (A**2) : -2.46                                                
REMARK   3    B33 (A**2) : 0.79                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 1.40                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.195         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.175         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.124         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.139         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.924                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2324 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1561 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3144 ; 1.213 ; 2.008       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3876 ; 0.814 ; 3.006       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   291 ; 5.007 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    85 ;39.378 ;26.588       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   418 ;13.293 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     3 ;10.050 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   355 ; 0.063 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2530 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   396 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  1442 ; 0.448 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   570 ; 0.098 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2336 ; 0.806 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   882 ; 1.307 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   808 ; 2.122 ; 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    18        A   142                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.4012  -6.4102   3.1366              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0368 T22:   0.0281                                     
REMARK   3      T33:   0.0213 T12:   0.0120                                     
REMARK   3      T13:  -0.0109 T23:  -0.0058                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2880 L22:   2.1288                                     
REMARK   3      L33:   1.9238 L12:   0.0994                                     
REMARK   3      L13:  -0.2406 L23:   0.1347                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0126 S12:   0.1088 S13:  -0.0103                       
REMARK   3      S21:  -0.2513 S22:  -0.0888 S23:   0.0617                       
REMARK   3      S31:   0.0646 S32:  -0.0760 S33:   0.0762                       
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):  12.5885  -0.0721  19.6827              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0388 T22:   0.1320                                     
REMARK   3      T33:   0.2041 T12:  -0.0177                                     
REMARK   3      T13:  -0.0502 T23:   0.0071                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4400 L22:   3.5697                                     
REMARK   3      L33:  16.9004 L12:   0.0037                                     
REMARK   3      L13:   2.3285 L23:  -4.6886                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0416 S12:  -0.3768 S13:   0.1345                       
REMARK   3      S21:   0.1720 S22:  -0.3472 S23:  -0.4257                       
REMARK   3      S31:   0.0714 S32:   0.4154 S33:   0.3888                       
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):  -4.0799 -16.8783  27.4250              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0255 T22:   0.0408                                     
REMARK   3      T33:   0.0557 T12:   0.0075                                     
REMARK   3      T13:  -0.0138 T23:   0.0084                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7756 L22:   2.4837                                     
REMARK   3      L33:   1.7337 L12:   0.3857                                     
REMARK   3      L13:  -0.6290 L23:  -1.2568                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0669 S12:  -0.0699 S13:  -0.0749                       
REMARK   3      S21:   0.0314 S22:  -0.0099 S23:  -0.0586                       
REMARK   3      S31:   0.1127 S32:   0.0162 S33:   0.0768                       
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 2XUZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-OCT-10.                  
REMARK 100 THE PDBE ID CODE IS EBI-45778.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-MAR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.20                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933000                           
REMARK 200  MONOCHROMATOR                  : DIAMOND (111), GE(220)             
REMARK 200  OPTICS                         : TOROIDAL MIRROR                    
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   : 19907                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.90                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.83                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 3.1                                
REMARK 200  R MERGE                    (I) : 0.06                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.80                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.1                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.49                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.50                               
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 2WHY                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 33.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM            
REMARK 280  34% (V/V) PEG 600, 100 MM PHOSPHATE-CITRATE, PH 5.20                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       31.78000            
REMARK 290   SMTRY3   2  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 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     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     SER A    17                                                      
REMARK 465     GLU A    18                                                      
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     LYS A  21    CE   NZ                                             
REMARK 470     LYS A  27    CD   CE   NZ                                        
REMARK 470     GLU A  30    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  86    CD   OE1  OE2                                       
REMARK 470     GLU A  90    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  96    CD   CE   NZ                                        
REMARK 470     LYS A 113    NZ                                                  
REMARK 470     LYS A 145    CE   NZ                                             
REMARK 470     LYS A 162    CD   CE   NZ                                        
REMARK 470     LYS A 164    CG   CD   CE   NZ                                   
REMARK 470     ILE A 165    CG1  CG2  CD1                                       
REMARK 470     ASN A 166    CG   OD1  ND2                                       
REMARK 470     ASP A 167    CG   OD1  OD2                                       
REMARK 470     LYS A 168    CG   CD   CE   NZ                                   
REMARK 470     LYS A 170    CG   CD   CE   NZ                                   
REMARK 470     LYS A 213    CE   NZ                                             
REMARK 470     LYS A 222    CE   NZ                                             
REMARK 470     LYS A 252    CD   CE   NZ                                        
REMARK 470     GLN A 297    CG   CD   OE1  NE2                                  
REMARK 470     ASN A 298    CG   OD1  ND2                                       
REMARK 470     LYS A 299    CG   CD   CE   NZ                                   
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    TYR A 192     -145.37     59.54                                   
REMARK 500    ASN A 240       39.31   -142.06                                   
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                              FE A1301  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 EB4 A1300   O3                                                     
REMARK 620 2 EB4 A1300   O6   79.1                                              
REMARK 620 3 EB4 A1300   O5  118.1  84.9                                        
REMARK 620 4 EB4 A1300   O2   82.6 144.4  77.3                                  
REMARK 620 5 EB4 A1300   O4  150.5  86.4  85.5 122.0                            
REMARK 620 6 EB4 A1300   O1   87.8 127.5 143.4  81.4  81.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: PROVIDED BY DEPOSITOR                          
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: PROVIDED BY DEPOSITOR                          
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EB4 A1300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  FE A1301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A1302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A1305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KKR                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: BASIC TRIAD AS MAIN MOTIF, RESPONSIBLE             
REMARK 800 FOR BINDING OF TRISCATECHOLATES                                      
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2WHY   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE TRISCATECHOLATE SIDEROPHORE                
REMARK 900  BINDING PROTEIN FEUA FROM BACILLUS SUBTILIS COMPLEXED               
REMARK 900  WITH FERRI-BACILLIBACTIN                                            
REMARK 900 RELATED ID: 2XV1   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE TRISCATECHOLATE SIDEROPHORE                
REMARK 900  BINDING PROTEIN FEUA FROM BACILLUS SUBTILIS COMPLEXED               
REMARK 900  WITH FERRIC MECAM                                                   
REMARK 900 RELATED ID: 2WI8   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE TRISCATECHOLATE SIDEROPHORE                
REMARK 900  BINDING PROTEIN FEUA FROM BACILLUS SUBTILIS                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE TWO DIFFERRENCES BETWEEN THE COORDINATE FILE AND                 
REMARK 999 AND THE UNIPROT SEQUENCE (T161 AND I218) ARE                         
REMARK 999 MENTIONED AS VARIANTS BY THE DEPOSITORS.                             
DBREF  2XUZ A    2   298  UNP    P40409   FEUA_BACSU      21    317             
SEQADV 2XUZ MET A    1  UNP  P40409              EXPRESSION TAG                 
SEQADV 2XUZ LYS A  299  UNP  P40409              EXPRESSION TAG                 
SEQADV 2XUZ LEU A  300  UNP  P40409              EXPRESSION TAG                 
SEQADV 2XUZ ALA A  301  UNP  P40409              EXPRESSION TAG                 
SEQADV 2XUZ ALA A  302  UNP  P40409              EXPRESSION TAG                 
SEQADV 2XUZ ALA A  303  UNP  P40409              EXPRESSION TAG                 
SEQADV 2XUZ LEU A  304  UNP  P40409              EXPRESSION TAG                 
SEQADV 2XUZ GLU A  305  UNP  P40409              EXPRESSION TAG                 
SEQADV 2XUZ HIS A  306  UNP  P40409              EXPRESSION TAG                 
SEQADV 2XUZ HIS A  307  UNP  P40409              EXPRESSION TAG                 
SEQADV 2XUZ HIS A  308  UNP  P40409              EXPRESSION TAG                 
SEQADV 2XUZ HIS A  309  UNP  P40409              EXPRESSION TAG                 
SEQADV 2XUZ HIS A  310  UNP  P40409              EXPRESSION TAG                 
SEQADV 2XUZ HIS A  311  UNP  P40409              EXPRESSION TAG                 
SEQADV 2XUZ THR A  161  UNP  P40409    ILE   180 SEE REMARK 999                 
SEQADV 2XUZ ILE A  218  UNP  P40409    SER   237 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    EB4  A1300      48                                                       
HET     FE  A1301       1                                                       
HET    PG4  A1302      13                                                       
HET    PEG  A1303       7                                                       
HET    PEG  A1304       7                                                       
HET    PO4  A1305       5                                                       
HETNAM     EB4 N,N',N''-[(3S,7S,11S)-2,6,10-TRIOXO-1,5,9-                       
HETNAM   2 EB4  TRIOXACYCLODODECANE-3,7,11-TRIYL]TRIS(2,3-                      
HETNAM   3 EB4  DIHYDROXYBENZAMIDE)                                             
HETNAM      FE FE (III) ION                                                     
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     PO4 PHOSPHATE ION                                                    
HETSYN     EB4 ENTEROBACTIN                                                     
FORMUL   2  EB4    C30 H27 N3 O15                                               
FORMUL   3   FE    FE 3+                                                        
FORMUL   4  PG4    C8 H18 O5                                                    
FORMUL   5  PEG    2(C4 H10 O3)                                                 
FORMUL   6  PO4    O4 P 3-                                                      
FORMUL   7  HOH   *148(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  SER A  115  1                                   9    
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  TYR A  198  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  ALA A  241  5                                   5    
HELIX   12  12 ASP A  245  LYS A  252  1                                   8    
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 LYS A  20  TYR A  24  0                                        
SHEET    2  AA 2 LYS A  27  VAL A  31 -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 5 GLU A 216  LEU A 217  0                                        
SHEET    2  AD 5 ASN A 183  ILE A 186 -1  O  ILE A 186   N  GLU A 216           
SHEET    3  AD 5 ALA A 174  ARG A 180 -1  O  ARG A 178   N  TYR A 185           
SHEET    4  AD 5 HIS A 230  PHE A 235  1  O  HIS A 230   N  LEU A 175           
SHEET    5  AD 5 VAL A 267  VAL A 269  1  O  TYR A 268   N  VAL A 233           
LINK         O3  EB4 A1300                FE    FE A1301     1555   1555  2.09  
LINK         O6  EB4 A1300                FE    FE A1301     1555   1555  2.14  
LINK         O5  EB4 A1300                FE    FE A1301     1555   1555  2.15  
LINK         O2  EB4 A1300                FE    FE A1301     1555   1555  2.08  
LINK         O4  EB4 A1300                FE    FE A1301     1555   1555  2.07  
LINK         O1  EB4 A1300                FE    FE A1301     1555   1555  2.00  
CISPEP   1 VAL A   33    PRO A   34          0        -3.44                     
SITE     1 AC1 15 LYS A  84  MET A  85  LYS A 105  PHE A 106                    
SITE     2 AC1 15 PRO A 107  ARG A 178  ARG A 180  GLN A 181                    
SITE     3 AC1 15 TYR A 187  ALA A 214  GLN A 215   FE A1301                    
SITE     4 AC1 15 HOH A2142  HOH A2143  HOH A2144                               
SITE     1 AC2  2 ARG A 180  EB4 A1300                                          
SITE     1 AC3  7 GLY A  65  LYS A  66  PHE A  67  MET A 135                    
SITE     2 AC3  7 GLN A 139  LYS A 148  HOH A2146                               
SITE     1 AC4  3 VAL A 267  VAL A 269  HOH A2147                               
SITE     1 AC5  2 GLN A 112  LYS A 263                                          
SITE     1 AC6  6 LYS A 173  PRO A 206  ASN A 207  GLU A 208                    
SITE     2 AC6  6 MET A 226  HOH A2148                                          
SITE     1 KKR  3 LYS A  84  LYS A 105  ARG A 180                               
CRYST1   36.440   63.560   56.520  90.00 100.65  90.00 P 1 21 1      2          
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      0.027442  0.000000  0.005160        0.00000                         
SCALE2      0.000000  0.015733  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018003        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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