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Database: PDB
Entry: 6A2U
LinkDB: 6A2U
Original site: 6A2U 
HEADER    SIGNALING PROTEIN/OXIDOREDUCTASE        13-JUN-18   6A2U              
TITLE     CRYSTAL STRUCTURE OF GAMMA-ALPHA SUBUNIT COMPLEX FROM BURKHOLDERIA    
TITLE    2 CEPACIA FAD GLUCOSE DEHYDROGENASE                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TWIN-ARGININE TRANSLOCATION PATHWAY SIGNAL;                
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: GLUCOSE DEHYDROGENASE;                                     
COMPND   7 CHAIN: B, D;                                                         
COMPND   8 EC: 1.1.5.9;                                                         
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BURKHOLDERIA CEPACIA;                           
SOURCE   3 ORGANISM_COMMON: PSEUDOMONAS CEPACIA;                                
SOURCE   4 ORGANISM_TAXID: 292;                                                 
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PTRC99A;                                  
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: BURKHOLDERIA CEPACIA;                           
SOURCE  12 ORGANISM_COMMON: PSEUDOMONAS CEPACIA;                                
SOURCE  13 ORGANISM_TAXID: 292;                                                 
SOURCE  14 GENE: GDHALPHA;                                                      
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PTRC99A                                   
KEYWDS    GLUCOSE DEHYDROGENASE, FAD, BURKHOLDERIA CEPACIA, OXIDOREDUCTASE,     
KEYWDS   2 SIGNALING PROTEIN-OXIDOREDUCTASE COMPLEX                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.YOSHIDA,K.KOJIMA,K.YOSHIMATSU,M.SHIOTA,T.YAMAZAKI,S.FERRI,          
AUTHOR   2 W.TSUGAWA,S.KAMITORI,K.SODE                                          
REVDAT   3   18-SEP-19 6A2U    1       JRNL                                     
REVDAT   2   04-SEP-19 6A2U    1       JRNL                                     
REVDAT   1   19-JUN-19 6A2U    0                                                
JRNL        AUTH   H.YOSHIDA,K.KOJIMA,M.SHIOTA,K.YOSHIMATSU,T.YAMAZAKI,S.FERRI, 
JRNL        AUTH 2 W.TSUGAWA,S.KAMITORI,K.SODE                                  
JRNL        TITL   X-RAY STRUCTURE OF THE DIRECT ELECTRON TRANSFER-TYPE FAD     
JRNL        TITL 2 GLUCOSE DEHYDROGENASE CATALYTIC SUBUNIT COMPLEXED WITH A     
JRNL        TITL 3 HITCHHIKER PROTEIN.                                          
JRNL        REF    ACTA CRYSTALLOGR D STRUCT     V.  75   841 2019              
JRNL        REF  2 BIOL                                                         
JRNL        REFN                   ISSN 2059-7983                               
JRNL        PMID   31478907                                                     
JRNL        DOI    10.1107/S2059798319010878                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.74                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 56812                          
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) : 0.207                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.261                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3023                            
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4078                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.19                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2750                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 201                          
REMARK   3   BIN FREE R VALUE                    : 0.3760                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10020                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 120                                     
REMARK   3   SOLVENT ATOMS            : 176                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.68                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.440         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.294         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.219         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.412        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.935                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.896                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10420 ; 0.002 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  9800 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14188 ; 0.574 ; 1.981       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 22608 ; 0.463 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1284 ;11.126 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   450 ;38.290 ;23.867       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1678 ;22.308 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    68 ;20.447 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1538 ; 0.040 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11704 ; 0.001 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2298 ; 0.000 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
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 RIDING   
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 6A2U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-JUN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1300008053.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-OCT-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : AR-NE3A                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 60005                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 21.20                              
REMARK 200  R MERGE                    (I) : 0.15000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 21.40                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.42800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: THE STRUCTURE OF SELENOMETHIONINE VARIANT            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.15                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: TACSIMATE, PH 7.0, VAPOR DIFFUSION,      
REMARK 280  SITTING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      349.91800            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      174.95900            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      262.43850            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       87.47950            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      437.39750            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      349.91800            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      174.95900            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       87.47950            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      262.43850            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      437.39750            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5500 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23860 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5480 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23750 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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     ASP A    48                                                      
REMARK 465     ASN A    49                                                      
REMARK 465     PRO A    50                                                      
REMARK 465     GLY A    51                                                      
REMARK 465     ARG A   166                                                      
REMARK 465     GLN A   167                                                      
REMARK 465     ALA A   168                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     THR B     4                                                      
REMARK 465     ASP B     5                                                      
REMARK 465     THR B     6                                                      
REMARK 465     GLN B     7                                                      
REMARK 465     LYS B     8                                                      
REMARK 465     ALA B     9                                                      
REMARK 465     HIS B   540                                                      
REMARK 465     HIS B   541                                                      
REMARK 465     HIS B   542                                                      
REMARK 465     HIS B   543                                                      
REMARK 465     HIS B   544                                                      
REMARK 465     HIS B   545                                                      
REMARK 465     ASP C    48                                                      
REMARK 465     ASN C    49                                                      
REMARK 465     PRO C    50                                                      
REMARK 465     GLY C    51                                                      
REMARK 465     ARG C   166                                                      
REMARK 465     GLN C   167                                                      
REMARK 465     ALA C   168                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     ASP D     3                                                      
REMARK 465     THR D     4                                                      
REMARK 465     ASP D     5                                                      
REMARK 465     THR D     6                                                      
REMARK 465     GLN D     7                                                      
REMARK 465     LYS D     8                                                      
REMARK 465     ALA D     9                                                      
REMARK 465     HIS D   540                                                      
REMARK 465     HIS D   541                                                      
REMARK 465     HIS D   542                                                      
REMARK 465     HIS D   543                                                      
REMARK 465     HIS D   544                                                      
REMARK 465     HIS D   545                                                      
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   OE1  GLU B    38     O2B  FAD B   701              2.09            
REMARK 500   OE2  GLU D   254     NH2  ARG D   275              2.09            
REMARK 500   CE1  HIS B   105     C8M  FAD B   701              2.11            
REMARK 500   NE2  HIS B   105     C8   FAD B   701              2.17            
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    PHE A  88       71.20     60.88                                   
REMARK 500    THR A  90     -154.84    -85.81                                   
REMARK 500    LEU A 101      -73.53    -49.26                                   
REMARK 500    SER A 103      -85.45    -96.95                                   
REMARK 500    SER A 150        1.66     90.42                                   
REMARK 500    PRO A 156      -95.00    -81.33                                   
REMARK 500    ALA B  30       21.85    -71.56                                   
REMARK 500    TYR B  76       -5.98   -144.02                                   
REMARK 500    ASN B  92       43.98    -90.43                                   
REMARK 500    LYS B 119       49.15   -140.68                                   
REMARK 500    ARG B 128      119.18    178.14                                   
REMARK 500    ASP B 135      -49.21    -27.94                                   
REMARK 500    GLU B 138      -66.57    -28.74                                   
REMARK 500    TYR B 160       -4.85     78.50                                   
REMARK 500    ASP B 207       42.88     35.81                                   
REMARK 500    ASP B 258       30.35    -86.42                                   
REMARK 500    LYS B 259       -9.75     74.87                                   
REMARK 500    ASP B 268     -169.68    -75.93                                   
REMARK 500    ALA B 285      172.76    -47.16                                   
REMARK 500    MET B 296       -8.39    -54.87                                   
REMARK 500    SER B 309      -17.30    -47.96                                   
REMARK 500    LEU B 333      -37.79   -142.77                                   
REMARK 500    TRP B 334       62.63     66.19                                   
REMARK 500    ASP B 425     -168.93   -110.82                                   
REMARK 500    PRO B 430      172.81    -46.25                                   
REMARK 500    ASN B 474       12.04   -150.60                                   
REMARK 500    ARG B 488       46.47   -147.61                                   
REMARK 500    ALA C 100      -19.28    -42.02                                   
REMARK 500    SER C 103      -27.16   -172.11                                   
REMARK 500    THR C 107      155.57    -47.09                                   
REMARK 500    ASP C 127       56.67     29.39                                   
REMARK 500    MET C 138      -58.38     -8.01                                   
REMARK 500    SER C 150       -6.54     97.61                                   
REMARK 500    PRO C 156     -115.07    -56.65                                   
REMARK 500    ILE D 221      115.39   -168.41                                   
REMARK 500    ASN D 247       50.02     29.95                                   
REMARK 500    ALA D 284       26.63   -144.41                                   
REMARK 500    ALA D 285     -177.33    -50.41                                   
REMARK 500    PHE D 327     -177.84   -178.51                                   
REMARK 500    LEU D 333      -31.43   -133.23                                   
REMARK 500    GLU D 341      119.40   -162.60                                   
REMARK 500    PRO D 386      -39.66    -36.89                                   
REMARK 500    ILE D 438       76.67   -108.23                                   
REMARK 500    ASP D 439      134.84     29.04                                   
REMARK 500    ASN D 474       21.72   -153.73                                   
REMARK 500    ASP D 493     -166.70    -75.68                                   
REMARK 500    SER D 508      157.08    179.58                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 SER A  103     GLY A  104                 -145.24                    
REMARK 500 LYS A  155     PRO A  156                 -141.04                    
REMARK 500 PRO A  156     GLY A  157                 -147.30                    
REMARK 500 PHE A  158     TRP A  159                 -141.74                    
REMARK 500 LYS B   32     ALA B   33                 -146.53                    
REMARK 500 ASP B  129     TRP B  130                  148.13                    
REMARK 500 ALA B  284     ALA B  285                  139.19                    
REMARK 500 LYS B  360     LYS B  361                  145.16                    
REMARK 500 GLY B  479     SER B  480                 -145.56                    
REMARK 500 ASP B  486     ALA B  487                 -144.60                    
REMARK 500 ARG B  488     ASP B  489                  118.59                    
REMARK 500 GLY C   86     SER C   87                 -146.11                    
REMARK 500 GLY C  104     SER C  105                  137.22                    
REMARK 500 CYS C  152     PRO C  153                  140.03                    
REMARK 500 ILE C  164     GLU C  165                  -40.83                    
REMARK 500 LYS D  360     LYS D  361                  147.68                    
REMARK 500 ILE D  438     ASP D  439                  127.82                    
REMARK 500 THR D  481     ILE D  482                 -147.38                    
REMARK 500 ASN D  503     LEU D  504                 -149.59                    
REMARK 500 GLU D  538     VAL D  539                  -48.06                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B 702  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 212   SG                                                     
REMARK 620 2 F3S B 702   S1  110.2                                              
REMARK 620 3 F3S B 702   S2  103.8 142.6                                        
REMARK 620 4 F3S B 702   S3  121.9  86.7  88.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B 702  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 218   SG                                                     
REMARK 620 2 F3S B 702   S2   98.9                                              
REMARK 620 3 F3S B 702   S3  121.1  88.2                                        
REMARK 620 4 F3S B 702   S4  117.0 140.0  87.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B 702  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 222   SG                                                     
REMARK 620 2 F3S B 702   S1  107.4                                              
REMARK 620 3 F3S B 702   S3  113.5  86.7                                        
REMARK 620 4 F3S B 702   S4  108.1 143.2  87.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S D 702  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 212   SG                                                     
REMARK 620 2 F3S D 702   S1  118.6                                              
REMARK 620 3 F3S D 702   S2   97.0 139.9                                        
REMARK 620 4 F3S D 702   S3  121.8  87.0  89.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S D 702  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 218   SG                                                     
REMARK 620 2 F3S D 702   S2  103.7                                              
REMARK 620 3 F3S D 702   S3  115.8  89.1                                        
REMARK 620 4 F3S D 702   S4  115.5 137.9  87.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S D 702  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 222   SG                                                     
REMARK 620 2 F3S D 702   S1  113.4                                              
REMARK 620 3 F3S D 702   S3  115.8  86.9                                        
REMARK 620 4 F3S D 702   S4  103.8 141.0  87.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD B 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue F3S B 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue F3S D 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide FAD D 701 and HIS D    
REMARK 800  105                                                                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 SEQUENCE OF TWIN-ARGININE TRANSLOCATION PATHWAY SIGNAL WAS           
REMARK 999 DEPOSITED TO GENBANK WITH ACCESSION NUMBER CAZ78686.                 
DBREF  6A2U A   48   168  PDB    6A2U     6A2U            48    168             
DBREF  6A2U B    1   539  UNP    Q8GQE7   Q8GQE7_BURCE     1    539             
DBREF  6A2U C   48   168  PDB    6A2U     6A2U            48    168             
DBREF  6A2U D    1   539  UNP    Q8GQE7   Q8GQE7_BURCE     1    539             
SEQADV 6A2U HIS B  540  UNP  Q8GQE7              EXPRESSION TAG                 
SEQADV 6A2U HIS B  541  UNP  Q8GQE7              EXPRESSION TAG                 
SEQADV 6A2U HIS B  542  UNP  Q8GQE7              EXPRESSION TAG                 
SEQADV 6A2U HIS B  543  UNP  Q8GQE7              EXPRESSION TAG                 
SEQADV 6A2U HIS B  544  UNP  Q8GQE7              EXPRESSION TAG                 
SEQADV 6A2U HIS B  545  UNP  Q8GQE7              EXPRESSION TAG                 
SEQADV 6A2U HIS D  540  UNP  Q8GQE7              EXPRESSION TAG                 
SEQADV 6A2U HIS D  541  UNP  Q8GQE7              EXPRESSION TAG                 
SEQADV 6A2U HIS D  542  UNP  Q8GQE7              EXPRESSION TAG                 
SEQADV 6A2U HIS D  543  UNP  Q8GQE7              EXPRESSION TAG                 
SEQADV 6A2U HIS D  544  UNP  Q8GQE7              EXPRESSION TAG                 
SEQADV 6A2U HIS D  545  UNP  Q8GQE7              EXPRESSION TAG                 
SEQRES   1 A  121  ASP ASN PRO GLY THR ALA PRO LEU ASP THR PHE MET THR          
SEQRES   2 A  121  LEU SER GLU SER LEU THR GLY LYS LYS GLY LEU SER ARG          
SEQRES   3 A  121  VAL ILE GLY GLU ARG LEU LEU GLN ALA LEU GLN LYS GLY          
SEQRES   4 A  121  SER PHE LYS THR ALA ASP SER LEU PRO GLN LEU ALA GLY          
SEQRES   5 A  121  ALA LEU ALA SER GLY SER LEU THR PRO GLU GLN GLU SER          
SEQRES   6 A  121  LEU ALA LEU THR ILE LEU GLU ALA TRP TYR LEU GLY ILE          
SEQRES   7 A  121  VAL ASP ASN VAL VAL ILE THR TYR GLU GLU ALA LEU MET          
SEQRES   8 A  121  PHE GLY VAL VAL SER ASP THR LEU VAL ILE ARG SER TYR          
SEQRES   9 A  121  CYS PRO ASN LYS PRO GLY PHE TRP ALA ASP LYS PRO ILE          
SEQRES  10 A  121  GLU ARG GLN ALA                                              
SEQRES   1 B  545  MET ALA ASP THR ASP THR GLN LYS ALA ASP VAL VAL VAL          
SEQRES   2 B  545  VAL GLY SER GLY VAL ALA GLY ALA ILE VAL ALA HIS GLN          
SEQRES   3 B  545  LEU ALA MET ALA GLY LYS ALA VAL ILE LEU LEU GLU ALA          
SEQRES   4 B  545  GLY PRO ARG MET PRO ARG TRP GLU ILE VAL GLU ARG PHE          
SEQRES   5 B  545  ARG ASN GLN PRO ASP LYS MET ASP PHE MET ALA PRO TYR          
SEQRES   6 B  545  PRO SER SER PRO TRP ALA PRO HIS PRO GLU TYR GLY PRO          
SEQRES   7 B  545  PRO ASN ASP TYR LEU ILE LEU LYS GLY GLU HIS LYS PHE          
SEQRES   8 B  545  ASN SER GLN TYR ILE ARG ALA VAL GLY GLY THR THR TRP          
SEQRES   9 B  545  HIS TRP ALA ALA SER ALA TRP ARG PHE ILE PRO ASN ASP          
SEQRES  10 B  545  PHE LYS MET LYS SER VAL TYR GLY VAL GLY ARG ASP TRP          
SEQRES  11 B  545  PRO ILE GLN TYR ASP ASP LEU GLU PRO TYR TYR GLN ARG          
SEQRES  12 B  545  ALA GLU GLU GLU LEU GLY VAL TRP GLY PRO GLY PRO GLU          
SEQRES  13 B  545  GLU ASP LEU TYR SER PRO ARG LYS GLN PRO TYR PRO MET          
SEQRES  14 B  545  PRO PRO LEU PRO LEU SER PHE ASN GLU GLN THR ILE LYS          
SEQRES  15 B  545  THR ALA LEU ASN ASN TYR ASP PRO LYS PHE HIS VAL VAL          
SEQRES  16 B  545  THR GLU PRO VAL ALA ARG ASN SER ARG PRO TYR ASP GLY          
SEQRES  17 B  545  ARG PRO THR CYS CYS GLY ASN ASN ASN CYS MET PRO ILE          
SEQRES  18 B  545  CYS PRO ILE GLY ALA MET TYR ASN GLY ILE VAL HIS VAL          
SEQRES  19 B  545  GLU LYS ALA GLU ARG ALA GLY ALA LYS LEU ILE GLU ASN          
SEQRES  20 B  545  ALA VAL VAL TYR LYS LEU GLU THR GLY PRO ASP LYS ARG          
SEQRES  21 B  545  ILE VAL ALA ALA LEU TYR LYS ASP LYS THR GLY ALA GLU          
SEQRES  22 B  545  HIS ARG VAL GLU GLY LYS TYR PHE VAL LEU ALA ALA ASN          
SEQRES  23 B  545  GLY ILE GLU THR PRO LYS ILE LEU LEU MET SER ALA ASN          
SEQRES  24 B  545  ARG ASP PHE PRO ASN GLY VAL ALA ASN SER SER ASP MET          
SEQRES  25 B  545  VAL GLY ARG ASN LEU MET ASP HIS PRO GLY THR GLY VAL          
SEQRES  26 B  545  SER PHE TYR ALA SER GLU LYS LEU TRP PRO GLY ARG GLY          
SEQRES  27 B  545  PRO GLN GLU MET THR SER LEU ILE GLY PHE ARG ASP GLY          
SEQRES  28 B  545  PRO PHE ARG ALA THR GLU ALA ALA LYS LYS ILE HIS LEU          
SEQRES  29 B  545  SER ASN LEU SER ARG ILE ASP GLN GLU THR GLN LYS ILE          
SEQRES  30 B  545  PHE LYS ALA GLY LYS LEU MET LYS PRO ASP GLU LEU ASP          
SEQRES  31 B  545  ALA GLN ILE ARG ASP ARG SER ALA ARG TYR VAL GLN PHE          
SEQRES  32 B  545  ASP CYS PHE HIS GLU ILE LEU PRO GLN PRO GLU ASN ARG          
SEQRES  33 B  545  ILE VAL PRO SER LYS THR ALA THR ASP ALA ILE GLY ILE          
SEQRES  34 B  545  PRO ARG PRO GLU ILE THR TYR ALA ILE ASP ASP TYR VAL          
SEQRES  35 B  545  LYS ARG GLY ALA ALA HIS THR ARG GLU VAL TYR ALA THR          
SEQRES  36 B  545  ALA ALA LYS VAL LEU GLY GLY THR ASP VAL VAL PHE ASN          
SEQRES  37 B  545  ASP GLU PHE ALA PRO ASN ASN HIS ILE THR GLY SER THR          
SEQRES  38 B  545  ILE MET GLY ALA ASP ALA ARG ASP SER VAL VAL ASP LYS          
SEQRES  39 B  545  ASP CYS ARG THR PHE ASP HIS PRO ASN LEU PHE ILE SER          
SEQRES  40 B  545  SER SER ALA THR MET PRO THR VAL GLY THR VAL ASN VAL          
SEQRES  41 B  545  THR LEU THR ILE ALA ALA LEU ALA LEU ARG MET SER ASP          
SEQRES  42 B  545  THR LEU LYS LYS GLU VAL HIS HIS HIS HIS HIS HIS              
SEQRES   1 C  121  ASP ASN PRO GLY THR ALA PRO LEU ASP THR PHE MET THR          
SEQRES   2 C  121  LEU SER GLU SER LEU THR GLY LYS LYS GLY LEU SER ARG          
SEQRES   3 C  121  VAL ILE GLY GLU ARG LEU LEU GLN ALA LEU GLN LYS GLY          
SEQRES   4 C  121  SER PHE LYS THR ALA ASP SER LEU PRO GLN LEU ALA GLY          
SEQRES   5 C  121  ALA LEU ALA SER GLY SER LEU THR PRO GLU GLN GLU SER          
SEQRES   6 C  121  LEU ALA LEU THR ILE LEU GLU ALA TRP TYR LEU GLY ILE          
SEQRES   7 C  121  VAL ASP ASN VAL VAL ILE THR TYR GLU GLU ALA LEU MET          
SEQRES   8 C  121  PHE GLY VAL VAL SER ASP THR LEU VAL ILE ARG SER TYR          
SEQRES   9 C  121  CYS PRO ASN LYS PRO GLY PHE TRP ALA ASP LYS PRO ILE          
SEQRES  10 C  121  GLU ARG GLN ALA                                              
SEQRES   1 D  545  MET ALA ASP THR ASP THR GLN LYS ALA ASP VAL VAL VAL          
SEQRES   2 D  545  VAL GLY SER GLY VAL ALA GLY ALA ILE VAL ALA HIS GLN          
SEQRES   3 D  545  LEU ALA MET ALA GLY LYS ALA VAL ILE LEU LEU GLU ALA          
SEQRES   4 D  545  GLY PRO ARG MET PRO ARG TRP GLU ILE VAL GLU ARG PHE          
SEQRES   5 D  545  ARG ASN GLN PRO ASP LYS MET ASP PHE MET ALA PRO TYR          
SEQRES   6 D  545  PRO SER SER PRO TRP ALA PRO HIS PRO GLU TYR GLY PRO          
SEQRES   7 D  545  PRO ASN ASP TYR LEU ILE LEU LYS GLY GLU HIS LYS PHE          
SEQRES   8 D  545  ASN SER GLN TYR ILE ARG ALA VAL GLY GLY THR THR TRP          
SEQRES   9 D  545  HIS TRP ALA ALA SER ALA TRP ARG PHE ILE PRO ASN ASP          
SEQRES  10 D  545  PHE LYS MET LYS SER VAL TYR GLY VAL GLY ARG ASP TRP          
SEQRES  11 D  545  PRO ILE GLN TYR ASP ASP LEU GLU PRO TYR TYR GLN ARG          
SEQRES  12 D  545  ALA GLU GLU GLU LEU GLY VAL TRP GLY PRO GLY PRO GLU          
SEQRES  13 D  545  GLU ASP LEU TYR SER PRO ARG LYS GLN PRO TYR PRO MET          
SEQRES  14 D  545  PRO PRO LEU PRO LEU SER PHE ASN GLU GLN THR ILE LYS          
SEQRES  15 D  545  THR ALA LEU ASN ASN TYR ASP PRO LYS PHE HIS VAL VAL          
SEQRES  16 D  545  THR GLU PRO VAL ALA ARG ASN SER ARG PRO TYR ASP GLY          
SEQRES  17 D  545  ARG PRO THR CYS CYS GLY ASN ASN ASN CYS MET PRO ILE          
SEQRES  18 D  545  CYS PRO ILE GLY ALA MET TYR ASN GLY ILE VAL HIS VAL          
SEQRES  19 D  545  GLU LYS ALA GLU ARG ALA GLY ALA LYS LEU ILE GLU ASN          
SEQRES  20 D  545  ALA VAL VAL TYR LYS LEU GLU THR GLY PRO ASP LYS ARG          
SEQRES  21 D  545  ILE VAL ALA ALA LEU TYR LYS ASP LYS THR GLY ALA GLU          
SEQRES  22 D  545  HIS ARG VAL GLU GLY LYS TYR PHE VAL LEU ALA ALA ASN          
SEQRES  23 D  545  GLY ILE GLU THR PRO LYS ILE LEU LEU MET SER ALA ASN          
SEQRES  24 D  545  ARG ASP PHE PRO ASN GLY VAL ALA ASN SER SER ASP MET          
SEQRES  25 D  545  VAL GLY ARG ASN LEU MET ASP HIS PRO GLY THR GLY VAL          
SEQRES  26 D  545  SER PHE TYR ALA SER GLU LYS LEU TRP PRO GLY ARG GLY          
SEQRES  27 D  545  PRO GLN GLU MET THR SER LEU ILE GLY PHE ARG ASP GLY          
SEQRES  28 D  545  PRO PHE ARG ALA THR GLU ALA ALA LYS LYS ILE HIS LEU          
SEQRES  29 D  545  SER ASN LEU SER ARG ILE ASP GLN GLU THR GLN LYS ILE          
SEQRES  30 D  545  PHE LYS ALA GLY LYS LEU MET LYS PRO ASP GLU LEU ASP          
SEQRES  31 D  545  ALA GLN ILE ARG ASP ARG SER ALA ARG TYR VAL GLN PHE          
SEQRES  32 D  545  ASP CYS PHE HIS GLU ILE LEU PRO GLN PRO GLU ASN ARG          
SEQRES  33 D  545  ILE VAL PRO SER LYS THR ALA THR ASP ALA ILE GLY ILE          
SEQRES  34 D  545  PRO ARG PRO GLU ILE THR TYR ALA ILE ASP ASP TYR VAL          
SEQRES  35 D  545  LYS ARG GLY ALA ALA HIS THR ARG GLU VAL TYR ALA THR          
SEQRES  36 D  545  ALA ALA LYS VAL LEU GLY GLY THR ASP VAL VAL PHE ASN          
SEQRES  37 D  545  ASP GLU PHE ALA PRO ASN ASN HIS ILE THR GLY SER THR          
SEQRES  38 D  545  ILE MET GLY ALA ASP ALA ARG ASP SER VAL VAL ASP LYS          
SEQRES  39 D  545  ASP CYS ARG THR PHE ASP HIS PRO ASN LEU PHE ILE SER          
SEQRES  40 D  545  SER SER ALA THR MET PRO THR VAL GLY THR VAL ASN VAL          
SEQRES  41 D  545  THR LEU THR ILE ALA ALA LEU ALA LEU ARG MET SER ASP          
SEQRES  42 D  545  THR LEU LYS LYS GLU VAL HIS HIS HIS HIS HIS HIS              
HET    FAD  B 701      53                                                       
HET    F3S  B 702       7                                                       
HET    FAD  D 701      53                                                       
HET    F3S  D 702       7                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     F3S FE3-S4 CLUSTER                                                   
FORMUL   5  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL   6  F3S    2(FE3 S4)                                                    
FORMUL   9  HOH   *176(H2 O)                                                    
HELIX    1 AA1 ALA A   53  GLY A   67  1                                  15    
HELIX    2 AA2 SER A   72  LYS A   85  1                                  14    
HELIX    3 AA3 ASP A   92  SER A  103  1                                  12    
HELIX    4 AA4 THR A  107  GLY A  124  1                                  18    
HELIX    5 AA5 ALA A  136  VAL A  141  1                                   6    
HELIX    6 AA6 GLY B   17  ALA B   30  1                                  14    
HELIX    7 AA7 PRO B   44  ASN B   54  1                                  11    
HELIX    8 AA8 GLY B  100  HIS B  105  5                                   6    
HELIX    9 AA9 ILE B  114  PHE B  118  5                                   5    
HELIX   10 AB1 LYS B  119  GLY B  125  1                                   7    
HELIX   11 AB2 GLN B  133  GLY B  149  1                                  17    
HELIX   12 AB3 SER B  175  ASP B  189  1                                  15    
HELIX   13 AB4 PRO B  190  PHE B  192  5                                   3    
HELIX   14 AB5 GLY B  230  ALA B  240  1                                  11    
HELIX   15 AB6 ILE B  288  MET B  296  1                                   9    
HELIX   16 AB7 GLY B  351  THR B  356  5                                   6    
HELIX   17 AB8 ARG B  369  ALA B  380  1                                  12    
HELIX   18 AB9 LYS B  385  ARG B  399  1                                  15    
HELIX   19 AC1 ASP B  439  LEU B  460  1                                  22    
HELIX   20 AC2 SER B  508  MET B  512  5                                   5    
HELIX   21 AC3 VAL B  520  LYS B  537  1                                  18    
HELIX   22 AC4 ALA C   53  GLY C   67  1                                  15    
HELIX   23 AC5 SER C   72  SER C   87  1                                  16    
HELIX   24 AC6 LEU C   94  ALA C  102  1                                   9    
HELIX   25 AC7 GLN C  110  GLY C  124  1                                  15    
HELIX   26 AC8 ALA C  136  VAL C  142  1                                   7    
HELIX   27 AC9 GLY C  157  ASP C  161  5                                   5    
HELIX   28 AD1 GLY D   17  ALA D   30  1                                  14    
HELIX   29 AD2 PRO D   44  ASN D   54  1                                  11    
HELIX   30 AD3 GLY D  100  HIS D  105  5                                   6    
HELIX   31 AD4 ILE D  114  PHE D  118  5                                   5    
HELIX   32 AD5 LYS D  119  GLY D  125  1                                   7    
HELIX   33 AD6 GLN D  133  GLY D  149  1                                  17    
HELIX   34 AD7 SER D  175  ASP D  189  1                                  15    
HELIX   35 AD8 GLY D  230  ALA D  240  1                                  11    
HELIX   36 AD9 ILE D  288  MET D  296  1                                   9    
HELIX   37 AE1 GLY D  351  THR D  356  5                                   6    
HELIX   38 AE2 ARG D  369  ALA D  380  1                                  12    
HELIX   39 AE3 LYS D  385  ARG D  399  1                                  15    
HELIX   40 AE4 ASP D  439  LEU D  460  1                                  22    
HELIX   41 AE5 SER D  508  MET D  512  5                                   5    
HELIX   42 AE6 VAL D  520  GLU D  538  1                                  19    
SHEET    1 AA1 2 ILE A 125  VAL A 126  0                                        
SHEET    2 AA1 2 VAL A 129  VAL A 130 -1  O  VAL A 129   N  VAL A 126           
SHEET    1 AA2 5 LYS B 243  ILE B 245  0                                        
SHEET    2 AA2 5 VAL B  34  LEU B  37  1  N  LEU B  36   O  LYS B 243           
SHEET    3 AA2 5 VAL B  11  VAL B  14  1  N  VAL B  13   O  ILE B  35           
SHEET    4 AA2 5 TYR B 280  LEU B 283  1  O  VAL B 282   N  VAL B  14           
SHEET    5 AA2 5 LEU B 504  ILE B 506  1  O  PHE B 505   N  PHE B 281           
SHEET    1 AA3 3 ILE B  84  GLY B  87  0                                        
SHEET    2 AA3 3 PRO B 430  TYR B 436  1  O  PRO B 432   N  ILE B  84           
SHEET    3 AA3 3 ARG B 416  THR B 424 -1  N  SER B 420   O  ARG B 431           
SHEET    1 AA4 2 VAL B 194  THR B 196  0                                        
SHEET    2 AA4 2 THR B 343  LEU B 345 -1  O  SER B 344   N  VAL B 195           
SHEET    1 AA5 3 VAL B 249  THR B 255  0                                        
SHEET    2 AA5 3 ILE B 261  LYS B 267 -1  O  LEU B 265   N  LYS B 252           
SHEET    3 AA5 3 GLU B 273  VAL B 276 -1  O  VAL B 276   N  ALA B 264           
SHEET    1 AA6 4 LYS B 360  LEU B 364  0                                        
SHEET    2 AA6 4 TYR B 400  HIS B 407 -1  O  ASP B 404   N  HIS B 363           
SHEET    3 AA6 4 GLY B 322  TYR B 328 -1  N  PHE B 327   O  VAL B 401           
SHEET    4 AA6 4 THR B 463  ALA B 472 -1  O  THR B 463   N  TYR B 328           
SHEET    1 AA7 2 ILE C 125  VAL C 126  0                                        
SHEET    2 AA7 2 VAL C 129  VAL C 130 -1  O  VAL C 129   N  VAL C 126           
SHEET    1 AA8 5 LYS D 243  ILE D 245  0                                        
SHEET    2 AA8 5 VAL D  34  LEU D  37  1  N  LEU D  36   O  LYS D 243           
SHEET    3 AA8 5 VAL D  11  VAL D  14  1  N  VAL D  13   O  ILE D  35           
SHEET    4 AA8 5 TYR D 280  LEU D 283  1  O  TYR D 280   N  VAL D  12           
SHEET    5 AA8 5 LEU D 504  ILE D 506  1  O  PHE D 505   N  LEU D 283           
SHEET    1 AA9 3 ILE D  84  LYS D  86  0                                        
SHEET    2 AA9 3 PRO D 430  THR D 435  1  O  ILE D 434   N  LYS D  86           
SHEET    3 AA9 3 ARG D 416  THR D 424 -1  N  VAL D 418   O  GLU D 433           
SHEET    1 AB1 2 VAL D 194  THR D 196  0                                        
SHEET    2 AB1 2 THR D 343  LEU D 345 -1  O  SER D 344   N  VAL D 195           
SHEET    1 AB2 3 VAL D 249  THR D 255  0                                        
SHEET    2 AB2 3 ILE D 261  LYS D 267 -1  O  LEU D 265   N  LYS D 252           
SHEET    3 AB2 3 GLU D 273  GLU D 277 -1  O  VAL D 276   N  ALA D 264           
SHEET    1 AB3 4 LYS D 360  LEU D 364  0                                        
SHEET    2 AB3 4 TYR D 400  HIS D 407 -1  O  ASP D 404   N  HIS D 363           
SHEET    3 AB3 4 GLY D 322  TYR D 328 -1  N  PHE D 327   O  VAL D 401           
SHEET    4 AB3 4 THR D 463  ALA D 472 -1  O  THR D 463   N  TYR D 328           
SSBOND   1 CYS A  152    CYS B  213                          1555   1555  2.03  
SSBOND   2 CYS C  152    CYS D  213                          1555   1555  2.03  
LINK         NE2 HIS B 105                 C8M FAD B 701     1555   1555  1.47  
LINK         SG  CYS B 212                FE1  F3S B 702     1555   1555  2.29  
LINK         SG  CYS B 218                FE4  F3S B 702     1555   1555  2.29  
LINK         SG  CYS B 222                FE3  F3S B 702     1555   1555  2.30  
LINK         NE2 HIS D 105                 C8M FAD D 701     1555   1555  1.48  
LINK         SG  CYS D 212                FE1  F3S D 702     1555   1555  2.29  
LINK         SG  CYS D 218                FE4  F3S D 702     1555   1555  2.30  
LINK         SG  CYS D 222                FE3  F3S D 702     1555   1555  2.29  
CISPEP   1 GLY B   77    PRO B   78          0       -25.65                     
CISPEP   2 MET B  219    PRO B  220          0         2.64                     
CISPEP   3 GLY D   77    PRO D   78          0         1.83                     
CISPEP   4 MET D  219    PRO D  220          0        -2.91                     
SITE     1 AC1 34 GLY B  15  GLY B  17  VAL B  18  ALA B  19                    
SITE     2 AC1 34 GLU B  38  ALA B  39  GLN B  94  ILE B  96                    
SITE     3 AC1 34 ARG B  97  ALA B  98  GLY B 101  THR B 102                    
SITE     4 AC1 34 THR B 103  HIS B 105  TRP B 106  ALA B 107                    
SITE     5 AC1 34 ALA B 108  SER B 109  ALA B 248  VAL B 249                    
SITE     6 AC1 34 VAL B 250  ALA B 284  ALA B 285  GLU B 289                    
SITE     7 AC1 34 ILE B 293  ASN B 475  ASN B 519  VAL B 520                    
SITE     8 AC1 34 THR B 521  HOH B 802  HOH B 810  HOH B 815                    
SITE     9 AC1 34 HOH B 826  HOH B 859                                          
SITE     1 AC2  9 ARG B 201  CYS B 212  CYS B 213  GLY B 214                    
SITE     2 AC2  9 ASN B 215  ASN B 217  CYS B 218  CYS B 222                    
SITE     3 AC2  9 PRO B 339                                                     
SITE     1 AC3 10 ARG D 201  CYS D 212  CYS D 213  GLY D 214                    
SITE     2 AC3 10 ASN D 215  ASN D 217  CYS D 218  CYS D 222                    
SITE     3 AC3 10 ALA D 226  PRO D 339                                          
SITE     1 AC4 42 VAL D  14  GLY D  15  GLY D  17  VAL D  18                    
SITE     2 AC4 42 ALA D  19  GLU D  38  ALA D  39  PHE D  61                    
SITE     3 AC4 42 TYR D  65  GLN D  94  ILE D  96  ARG D  97                    
SITE     4 AC4 42 ALA D  98  GLY D 101  THR D 102  THR D 103                    
SITE     5 AC4 42 TRP D 104  TRP D 106  ALA D 107  ALA D 108                    
SITE     6 AC4 42 SER D 109  MET D 219  PRO D 220  ALA D 248                    
SITE     7 AC4 42 VAL D 250  ALA D 284  ALA D 285  GLU D 289                    
SITE     8 AC4 42 ILE D 293  ASN D 475  ASN D 519  VAL D 520                    
SITE     9 AC4 42 THR D 521  HOH D 801  HOH D 810  HOH D 813                    
SITE    10 AC4 42 HOH D 816  HOH D 833  HOH D 838  HOH D 842                    
SITE    11 AC4 42 HOH D 871  HOH D 874                                          
CRYST1  110.521  110.521  524.877  90.00  90.00 120.00 P 65 2 2     24          
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      0.009048  0.005224  0.000000        0.00000                         
SCALE2      0.000000  0.010448  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.001905        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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