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Database: PDB
Entry: 2WHY
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Original site: 2WHY 
HEADER    TRANSPORT PROTEIN                       07-MAY-09   2WHY              
TITLE     CRYSTAL STRUCTURE OF THE TRISCATECHOLATE SIDEROPHORE                  
TITLE    2 BINDING PROTEIN FEUA FROM BACILLUS SUBTILIS COMPLEXED WITH           
TITLE    3 FERRI-BACILLIBACTIN                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: IRON-UPTAKE SYSTEM-BINDING PROTEIN;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 21-317;                                           
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: BACILLIBACTIN;                                             
COMPND   8 CHAIN: B;                                                            
COMPND   9 SYNONYM: CORYNEBACTIN, 9-GLN-BETA-LIPOTROPIN                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 ATCC: 21332;                                                         
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PCB-28A;                                   
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: POK01;                                    
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE  12 ORGANISM_TAXID: 1423                                                 
KEYWDS    TRANSPORT PROTEIN, BACILLIBACTIN AND ENTEROBACTIN BINDING,            
KEYWDS   2 TRISCATECHOLATE BINDING PROTEIN, IRON TRANSPORT, HIGH AFFINITY IRON  
KEYWDS   3 IMPORT, IRON, MEMBRANE, PALMITATE, TRANSPORT, ABC-TYPE TRANSPORTER   
KEYWDS   4 BINDING PROTEIN, SIDEROPHORE BINDING PROTEIN, LIPOPROTEIN, CELL      
KEYWDS   5 MEMBRANE, ION TRANSPORT                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.PEUCKERT,M.MIETHKE,A.G.ALBRECHT,L.-O.ESSEN,M.A.MARAHIEL             
REVDAT   3   28-DEC-11 2WHY    1       JRNL   DBREF                             
REVDAT   2   13-JUL-11 2WHY    1       VERSN                                    
REVDAT   1   29-SEP-09 2WHY    0                                                
JRNL        AUTH   F.PEUCKERT,M.MIETHKE,A.G.ALBRECHT,L.-O.ESSEN,M.A.MARAHIEL    
JRNL        TITL   STRUCTURAL BASIS AND STEREOCHEMISTRY OF TRISCATECHOLATE      
JRNL        TITL 2 SIDEROPHORE BINDING BY FEUA.                                 
JRNL        REF    ANGEW.CHEM.INT.ED.ENGL.       V.  48  7924 2009              
JRNL        REFN                   ISSN 1433-7851                               
JRNL        PMID   19746494                                                     
JRNL        DOI    10.1002/ANIE.200902495                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.51                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.21                          
REMARK   3   NUMBER OF REFLECTIONS             : 25537                          
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) : 0.16042                         
REMARK   3   R VALUE            (WORKING SET) : 0.15749                         
REMARK   3   FREE R VALUE                     : 0.19120                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.8                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2472                            
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) : 1.700                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.744                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1863                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.52                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.231                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 213                          
REMARK   3   BIN FREE R VALUE                    : 0.275                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2215                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 42                                      
REMARK   3   SOLVENT ATOMS            : 146                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 24.416                         
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.303                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.14                                                 
REMARK   3    B22 (A**2) : -1.08                                                
REMARK   3    B33 (A**2) : 0.54                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : -0.57                                                
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.108         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.070         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.900         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.960                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2300 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1510 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3110 ; 1.159 ; 1.993       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3745 ; 0.864 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   299 ; 5.096 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    81 ;37.670 ;26.420       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   400 ;13.482 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     3 ; 9.408 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   365 ; 0.064 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2522 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   398 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   528 ; 0.210 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1646 ; 0.186 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1168 ; 0.176 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1158 ; 0.157 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   146 ; 0.121 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):     8 ; 0.141 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    29 ; 0.228 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    11 ; 0.161 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1512 ; 0.550 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   594 ; 0.136 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2374 ; 0.850 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   888 ; 1.450 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   733 ; 2.275 ; 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    19        A   142                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.5968  -6.6227 -24.6814              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0234 T22:  -0.0494                                     
REMARK   3      T33:  -0.1273 T12:  -0.0630                                     
REMARK   3      T13:  -0.0052 T23:   0.0097                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3595 L22:   2.9162                                     
REMARK   3      L33:   2.5314 L12:   0.4453                                     
REMARK   3      L13:   0.1032 L23:  -0.1624                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1389 S12:   0.2451 S13:   0.0550                       
REMARK   3      S21:  -0.6368 S22:   0.1399 S23:  -0.0088                       
REMARK   3      S31:  -0.0778 S32:   0.0040 S33:  -0.0010                       
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):  15.8551  -2.0074  -9.6226              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1600 T22:  -0.0513                                     
REMARK   3      T33:   0.0588 T12:  -0.0865                                     
REMARK   3      T13:  -0.0177 T23:   0.0000                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2009 L22:   7.0403                                     
REMARK   3      L33:  22.2577 L12:  -1.9204                                     
REMARK   3      L13:   5.1349 L23:  -9.7798                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2657 S12:   0.1259 S13:   0.1517                       
REMARK   3      S21:   0.1789 S22:  -0.1783 S23:  -0.7507                       
REMARK   3      S31:  -0.7938 S32:   0.8595 S33:   0.4440                       
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   297                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.8233 -17.3285  -0.5295              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0880 T22:  -0.0646                                     
REMARK   3      T33:  -0.0503 T12:   0.0239                                     
REMARK   3      T13:   0.0118 T23:  -0.0108                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5601 L22:   2.4838                                     
REMARK   3      L33:   1.9445 L12:   0.2636                                     
REMARK   3      L13:   0.2229 L23:  -1.1651                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0046 S12:  -0.0328 S13:  -0.0898                       
REMARK   3      S21:   0.1670 S22:   0.0349 S23:  -0.0347                       
REMARK   3      S31:   0.0433 S32:   0.0207 S33:  -0.0302                       
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 2WHY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-MAY-09.                  
REMARK 100 THE PDBE ID CODE IS EBI-39729.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-NOV-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9184                             
REMARK 200  MONOCHROMATOR                  : SI (111)                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSALE                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28022                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.70                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.76                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 3.7                                
REMARK 200  R MERGE                    (I) : 0.04                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.10                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.79                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.7                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.52                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.40                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2PHZ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 33.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM            
REMARK 280  30% (V/V) PEG 600, 100 MM PHOSPHATE-CITRATE, PH 5.2; THEN           
REMARK 280  SOAKED IN MOTHER LIQUOR CONTAINING 30% (V/V) GLYCEROL FOR           
REMARK 280  CRYO PROTECTION.                                                    
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       31.57000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3260 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -89.08 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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     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  19    NZ                                                  
REMARK 470     LYS A  20    CG   CD   CE   NZ                                   
REMARK 470     LYS A  21    CG   CD   CE   NZ                                   
REMARK 470     LYS A  27    CG   CD   CE   NZ                                   
REMARK 470     GLU A  30    CG   CD   OE1  OE2                                  
REMARK 470     ASP A  36    OD1  OD2                                            
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     LYS A  96    CG   CD   CE   NZ                                   
REMARK 470     LYS A 113    CG   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    CE   NZ                                             
REMARK 470     GLN A 156    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 160    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 167    CG   OD1  OD2                                       
REMARK 470     GLN A 190    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 204    CE   NZ                                             
REMARK 470     LYS A 222    CE   NZ                                             
REMARK 470     ASP A 242    CG   OD1  OD2                                       
REMARK 470     LYS A 243    CE   NZ                                             
REMARK 470     LYS A 248    CD   CE   NZ                                        
REMARK 470     LYS A 252    CG   CD   CE   NZ                                   
REMARK 470     LYS A 289    CG   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 470     LEU A 300    CG   CD1  CD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   C    THR B    13     OG1  THR B    33              1.16            
REMARK 500   O    THR B    13     OG1  THR B    33              2.12            
REMARK 500   OG1  THR B    13     C    THR B    23              1.05            
REMARK 500   OG1  THR B    13     O    THR B    23              1.92            
REMARK 500   CB   THR B    23     C    THR B    33              2.13            
REMARK 500   OG1  THR B    23     CA   THR B    33              2.19            
REMARK 500   OG1  THR B    23     O    THR B    33              2.02            
REMARK 500   OG1  THR B    23     C    THR B    33              1.06            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A 192     -143.01     60.27                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     DBH B   31                                                       
REMARK 610     DBH B   11                                                       
REMARK 610     DBH B   21                                                       
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 B1001  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 DBH B  11   O3                                                     
REMARK 620 2 DBH B  11   O6   79.4                                              
REMARK 620 3 DBH B  21   O3   92.7 107.7                                        
REMARK 620 4 DBH B  31   O6  102.4  85.1 161.9                                  
REMARK 620 5 DBH B  21   O6  162.4  86.7  81.2  86.9                            
REMARK 620 6 DBH B  31   O3   92.2 160.8  89.8  79.8 104.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.                               
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1310                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  FE B1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KKR                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: MAIN MOTIF RESPONSIBLE FOR BINDING OF              
REMARK 800 TRISCATECHOLATES                                                     
DBREF  2WHY A    1     1  PDB    2WHY     2WHY             1      1             
DBREF  2WHY A    2   298  UNP    P40409   FEUA_BACSU      21    317             
DBREF  2WHY A  299   311  PDB    2WHY     2WHY           299    311             
DBREF  2WHY B   11    13  NOR    NOR00330 NOR00330         1      3             
DBREF  2WHY B   21    23  NOR    NOR00330 NOR00330         6      4             
DBREF  2WHY B   31    33  NOR    NOR00330 NOR00330         9      7             
SEQADV 2WHY THR A  161  UNP  P40409    ILE   180 CONFLICT                       
SEQADV 2WHY ILE A  218  UNP  P40409    SER   237 CONFLICT                       
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              
SEQRES   1 B    9  DBH GLY THR DBH GLY THR DBH GLY THR                          
HET     CL  A1302       1                                                       
HET     CL  A1303       1                                                       
HET     CL  A1304       1                                                       
HET     CL  A1305       1                                                       
HET     CL  A1306       1                                                       
HET     CL  A1307       1                                                       
HET     CL  A1308       1                                                       
HET     CL  A1309       1                                                       
HET     CL  A1310       1                                                       
HET     CL  A1311       1                                                       
HET     CL  A1312       1                                                       
HET    DBH  B  11      10                                                       
HET    DBH  B  21      10                                                       
HET    DBH  B  31      10                                                       
HET     FE  B1001       1                                                       
HETNAM      FE FE (III) ION                                                     
HETNAM      CL CHLORIDE ION                                                     
HETNAM     DBH 2,3-DIHYDROXY-BENZOIC ACID                                       
FORMUL   3   FE    FE 3+                                                        
FORMUL   4   CL    11(CL 1-)                                                    
FORMUL   5  DBH    3(C7 H6 O4)                                                  
FORMUL   6  HOH   *146(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   6 ASN A  129  GLY A  142  1                                  14    
HELIX    6   7 LYS A  143  ILE A  165  1                                  23    
HELIX    7   8 ASN A  166  ASP A  171  1                                   6    
HELIX    8   9 PHE A  193  TYR A  198  1                                   6    
HELIX    9  10 PRO A  206  ALA A  211  1                                   6    
HELIX   10  11 SER A  219  ASN A  227  1                                   9    
HELIX   11  12 ASP A  237  ALA A  241  5                                   5    
HELIX   12  13 ASP A  245  ASN A  253  1                                   9    
HELIX   13  14 ILE A  255  SER A  258  5                                   4    
HELIX   14  15 LEU A  259  ASP A  265  1                                   7    
HELIX   15  16 THR A  280  GLN A  297  1                                  18    
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 3 GLY A  59  SER A  62  0                                        
SHEET    2  AC 3 GLU A  79  GLU A  83  1  O  GLU A  79   N  ALA A  60           
SHEET    1  AD 5 ASN A 183  ILE A 186 -1  O  ILE A 186   N  GLU A 216           
SHEET    2  AD 5 ALA A 174  ARG A 180 -1  O  ARG A 178   N  TYR A 185           
SHEET    3  AD 5 HIS A 230  PHE A 235  1  O  HIS A 230   N  LEU A 175           
SHEET    4  AD 5 VAL A 267  VAL A 269  1  O  TYR A 268   N  VAL A 233           
LINK         C21 DBH B  11                 N   GLY B  12     1555   1555  1.03  
LINK         C21 DBH B  21                 N   GLY B  22     1555   1555  0.86  
LINK         C21 DBH B  31                 N   GLY B  32     1555   1555  0.89  
LINK        FE    FE B1001                 O6  DBH B  31     1555   1555  2.04  
LINK        FE    FE B1001                 O6  DBH B  21     1555   1555  2.09  
LINK        FE    FE B1001                 O3  DBH B  31     1555   1555  2.08  
LINK        FE    FE B1001                 O3  DBH B  21     1555   1555  1.93  
LINK        FE    FE B1001                 O6  DBH B  11     1555   1555  2.07  
LINK        FE    FE B1001                 O3  DBH B  11     1555   1555  2.06  
CISPEP   1 VAL A   33    PRO A   34          0         0.79                     
SITE     1 AC1  2 LYS A 173  GLU A 208                                          
SITE     1 AC2  1 THR A 120                                                     
SITE     1 AC3  2 ASP A 237  HOH A2104                                          
SITE     1 AC4  4 TRP A 130  ASP A 200  HOH A2082  HOH A2132                    
SITE     1 AC5  3 ASP A 153  ASP A 157  HOH A2067                               
SITE     1 AC6  3 SER A 219  LEU A 220  GLU A 221                               
SITE     1 AC7  1 HOH A2124                                                     
SITE     1 AC8  3 DBH B  11  DBH B  21  DBH B  31                               
SITE     1 KKR  3 LYS A  84  LYS A 105  ARG A 180                               
CRYST1   39.530   63.140   55.530  90.00 110.44  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      0.025297  0.000000  0.009428        0.00000                         
SCALE2      0.000000  0.015838  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019218        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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