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Database: PDB
Entry: 2XV1
LinkDB: 2XV1
Original site: 2XV1 
HEADER    TRANSPORT PROTEIN                       22-OCT-10   2XV1              
TITLE     CRYSTAL STRUCTURE OF THE TRISCATECHOLATE SIDEROPHORE                  
TITLE    2 BINDING PROTEIN FEUA FROM BACILLUS SUBTILIS COMPLEXED WITH           
TITLE    3 FERRIC MECAM                                                         
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 2XV1    1       JRNL                                     
REVDAT   1   10-AUG-11 2XV1    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.    2.15 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) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.49                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.53                          
REMARK   3   NUMBER OF REFLECTIONS             : 12740                          
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) : 0.18312                         
REMARK   3   R VALUE            (WORKING SET) : 0.17812                         
REMARK   3   FREE R VALUE                     : 0.23659                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.6                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1206                            
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) : 2.150                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.206                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 972                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.95                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.305                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 80                           
REMARK   3   BIN FREE R VALUE                    : 0.319                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2157                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 67                                      
REMARK   3   SOLVENT ATOMS            : 90                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 39.067                         
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.326                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.11                                                 
REMARK   3    B22 (A**2) : -3.12                                                
REMARK   3    B33 (A**2) : 1.47                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 2.11                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.325         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.226         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.178         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.875        
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.967                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.941                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2262 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1494 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3067 ; 1.142 ; 2.004       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3683 ; 0.830 ; 3.003       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   284 ; 5.161 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    84 ;37.676 ;26.548       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   393 ;14.172 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     3 ;11.167 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   350 ; 0.059 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2467 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   379 ; 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):  1420 ; 0.356 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   563 ; 0.068 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2290 ; 0.641 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   842 ; 1.030 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   776 ; 1.603 ; 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):  10.4398   5.9688   1.6163              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3455 T22:   0.2411                                     
REMARK   3      T33:   0.1012 T12:  -0.0567                                     
REMARK   3      T13:   0.0096 T23:  -0.0178                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0299 L22:   4.3149                                     
REMARK   3      L33:   3.1563 L12:  -0.1578                                     
REMARK   3      L13:  -0.2967 L23:  -0.2701                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1013 S12:   0.4343 S13:  -0.0949                       
REMARK   3      S21:  -0.8414 S22:   0.0915 S23:   0.0312                       
REMARK   3      S31:   0.1736 S32:  -0.0856 S33:   0.0098                       
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):  -6.0360   1.4371  16.6236              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0982 T22:   0.4076                                     
REMARK   3      T33:   0.5455 T12:  -0.0660                                     
REMARK   3      T13:  -0.1164 T23:   0.0490                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4085 L22:   5.7043                                     
REMARK   3      L33:  15.7953 L12:  -0.2862                                     
REMARK   3      L13:  -4.3815 L23:   3.3690                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0197 S12:   0.0701 S13:  -0.4236                       
REMARK   3      S21:  -0.1860 S22:   0.0143 S23:   0.5636                       
REMARK   3      S31:   0.1077 S32:  -0.9667 S33:   0.0054                       
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   300                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.2370  16.3583  26.0033              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0855 T22:   0.1523                                     
REMARK   3      T33:   0.1546 T12:   0.0301                                     
REMARK   3      T13:  -0.0044 T23:   0.0386                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9619 L22:   4.0408                                     
REMARK   3      L33:   2.3359 L12:   0.1252                                     
REMARK   3      L13:  -0.1455 L23:   1.1724                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0177 S12:  -0.0008 S13:   0.0348                       
REMARK   3      S21:   0.2770 S22:   0.0409 S23:   0.0700                       
REMARK   3      S31:   0.0707 S32:  -0.0796 S33:  -0.0233                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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 2XV1 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-45781.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-MAR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.00                               
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   : 13962                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.15                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.55                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : 3.0                                
REMARK 200  R MERGE                    (I) : 0.05                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.40                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.27                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.9                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.60                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.20                               
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   (%): 36.23                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM            
REMARK 280  45% (V/V) PEG 300, 100 MM PHOSPHATE-CITRATE PH 5.00                 
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       31.72000            
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     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  21    CG   CD   CE   NZ                                   
REMARK 470     GLU A  23    CG   CD   OE1  OE2                                  
REMARK 470     ASP A  26    CG   OD1  OD2                                       
REMARK 470     LYS A  27    CE   NZ                                             
REMARK 470     GLU A  30    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  37    CD   CE   NZ                                        
REMARK 470     GLU A  86    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  90    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  91    CG   CD   CE   NZ                                   
REMARK 470     GLU A  94    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  96    CG   CD   CE   NZ                                   
REMARK 470     LYS A 109    CE   NZ                                             
REMARK 470     GLN A 112    OE1  NE2                                            
REMARK 470     LYS A 113    CD   CE   NZ                                        
REMARK 470     LYS A 145    CG   CD   CE   NZ                                   
REMARK 470     LYS A 148    CD   CE   NZ                                        
REMARK 470     LYS A 149    CG   CD   CE   NZ                                   
REMARK 470     LYS A 164    CG   CD   CE   NZ                                   
REMARK 470     LYS A 168    CG   CD   CE   NZ                                   
REMARK 470     GLN A 181    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 190    CD   OE1  NE2                                       
REMARK 470     LYS A 204    CD   CE   NZ                                        
REMARK 470     LYS A 243    CE   NZ                                             
REMARK 470     LYS A 252    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    LEU A  25       73.15     50.23                                   
REMARK 500    ASP A  26      -18.40     71.76                                   
REMARK 500    TYR A 192     -143.21     61.31                                   
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 A1302  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ECA A1301   O31                                                    
REMARK 620 2 ECA A1301   O30  76.0                                              
REMARK 620 3 ECA A1301   O19 152.5  89.6                                        
REMARK 620 4 ECA A1301   O20  88.3 122.0  79.6                                  
REMARK 620 5 ECA A1301   O42  86.5 144.9 117.1  87.0                            
REMARK 620 6 ECA A1301   O41 119.7  86.9  81.9 145.2  75.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 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 ECA A1301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  FE A1302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A1303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A1304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1306                 
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: 2XUZ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE TRISCATECHOLATE SIDEROPHORE                
REMARK 900  BINDING PROTEIN FEUA FROM BACILLUS SUBTILIS COMPLEXED               
REMARK 900  WITH FERRI-ENTEROBACTIN                                             
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  2XV1 A    2   298  UNP    P40409   FEUA_BACSU      21    317             
SEQADV 2XV1 MET A    1  UNP  P40409              EXPRESSION TAG                 
SEQADV 2XV1 LYS A  299  UNP  P40409              EXPRESSION TAG                 
SEQADV 2XV1 LEU A  300  UNP  P40409              EXPRESSION TAG                 
SEQADV 2XV1 ALA A  301  UNP  P40409              EXPRESSION TAG                 
SEQADV 2XV1 ALA A  302  UNP  P40409              EXPRESSION TAG                 
SEQADV 2XV1 ALA A  303  UNP  P40409              EXPRESSION TAG                 
SEQADV 2XV1 LEU A  304  UNP  P40409              EXPRESSION TAG                 
SEQADV 2XV1 GLU A  305  UNP  P40409              EXPRESSION TAG                 
SEQADV 2XV1 HIS A  306  UNP  P40409              EXPRESSION TAG                 
SEQADV 2XV1 HIS A  307  UNP  P40409              EXPRESSION TAG                 
SEQADV 2XV1 HIS A  308  UNP  P40409              EXPRESSION TAG                 
SEQADV 2XV1 HIS A  309  UNP  P40409              EXPRESSION TAG                 
SEQADV 2XV1 HIS A  310  UNP  P40409              EXPRESSION TAG                 
SEQADV 2XV1 HIS A  311  UNP  P40409              EXPRESSION TAG                 
SEQADV 2XV1 THR A  161  UNP  P40409    ILE   180 SEE REMARK 999                 
SEQADV 2XV1 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    ECA  A1301      42                                                       
HET     FE  A1302       1                                                       
HET    PO4  A1303       5                                                       
HET    PO4  A1304       5                                                       
HET    PEG  A1305       7                                                       
HET    PEG  A1306       7                                                       
HETNAM     ECA N,N',N''-[BENZENE-1,3,5-TRIYLTRIS(METHYLENE)]TRIS(2,3-           
HETNAM   2 ECA  DIHYDROXYBENZAMIDE)                                             
HETNAM      FE FE (III) ION                                                     
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
FORMUL   2  ECA    C30 H27 N3 O9                                                
FORMUL   3   FE    FE 3+                                                        
FORMUL   4  PO4    2(O4 P 3-)                                                   
FORMUL   5  PEG    2(C4 H10 O3)                                                 
FORMUL   6  HOH   *90(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  1                                   5    
HELIX   12  12 ASP A  245  ASN A  253  1                                   9    
HELIX   13  13 PRO A  254  SER A  258  1                                   5    
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         O19 ECA A1301                FE    FE A1302     1555   1555  2.09  
LINK         O20 ECA A1301                FE    FE A1302     1555   1555  2.04  
LINK         O31 ECA A1301                FE    FE A1302     1555   1555  2.14  
LINK         O30 ECA A1301                FE    FE A1302     1555   1555  2.23  
LINK         O42 ECA A1301                FE    FE A1302     1555   1555  2.23  
LINK         O41 ECA A1301                FE    FE A1302     1555   1555  2.06  
CISPEP   1 VAL A   33    PRO A   34          0         2.02                     
SITE     1 AC1 15 GLY A  42  LYS A  84  MET A  85  LYS A 105                    
SITE     2 AC1 15 PHE A 106  PRO A 107  ARG A 178  ARG A 180                    
SITE     3 AC1 15 TYR A 187  VAL A 191  ALA A 214  GLN A 215                    
SITE     4 AC1 15  FE A1302  HOH A2087  HOH A2088                               
SITE     1 AC2  1 ECA A1301                                                     
SITE     1 AC3  2 LYS A 146  HOH A2090                                          
SITE     1 AC4  3 LYS A  66  LYS A 159  ASP A 238                               
SITE     1 AC5  6 PHE A 235  SER A 236  ASP A 237  ASP A 238                    
SITE     2 AC5  6 ASP A 273  LEU A 275                                          
SITE     1 AC6  6 SER A 128  TRP A 130  LYS A 131  GLU A 155                    
SITE     2 AC6  6 ASP A 200  LYS A 284                                          
SITE     1 KKR  3 LYS A  84  LYS A 105  ARG A 180                               
CRYST1   39.960   63.440   56.210  90.00 110.27  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      0.025025  0.000000  0.009242        0.00000                         
SCALE2      0.000000  0.015763  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018965        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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