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Database: PDB
Entry: 1F5V
LinkDB: 1F5V
Original site: 1F5V 
HEADER    OXIDOREDUCTASE                          17-JUN-00   1F5V              
TITLE     STRUCTURE AND SITE-DIRECTED MUTAGENESIS OF A FLAVOPROTEIN             
TITLE    2 FROM ESCHERICHIA COLI THAT REDUCES NITROCOMPOUNDS.                   
TITLE    3 ALTERATION OF PYRIDINE NUCLEOTIDE BINDING BY A SINGLE                
TITLE    4 AMINO ACID SUBSTITUTION                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: OXYGEN-INSENSITIVE NADPH NITROREDUCTASE;                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.6.99.6;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PAJ102                                    
KEYWDS    NITROREDUCTASE, FLAVOPROTEIN, ESCHERICHIA COLI,                       
KEYWDS   2 OXIDOREDUCTION, NITROCOMPOUND, OXIDOREDUCTASE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.KOBORI,H.SASAKI,W.C.LEE,S.ZENNO,K.SAIGO,M.E.P.MURPHY,               
AUTHOR   2 M.TANOKURA                                                           
REVDAT   3   24-FEB-09 1F5V    1       VERSN                                    
REVDAT   2   01-APR-03 1F5V    1       JRNL                                     
REVDAT   1   14-FEB-01 1F5V    0                                                
JRNL        AUTH   T.KOBORI,H.SASAKI,W.C.LEE,S.ZENNO,K.SAIGO,                   
JRNL        AUTH 2 M.E.MURPHY,M.TANOKURA                                        
JRNL        TITL   STRUCTURE AND SITE-DIRECTED MUTAGENESIS OF A                 
JRNL        TITL 2 FLAVOPROTEIN FROM ESCHERICHIA COLI THAT REDUCES              
JRNL        TITL 3 NITROCOMPOUNDS: ALTERATION OF PYRIDINE NUCLEOTIDE            
JRNL        TITL 4 BINDING BY A SINGLE AMINO ACID SUBSTITUTION.                 
JRNL        REF    J.BIOL.CHEM.                  V. 276  2816 2001              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   11034992                                                     
JRNL        DOI    10.1074/JBC.M002617200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1, CNS                                      
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 7.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 42534                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.206                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3774                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 62                                      
REMARK   3   SOLVENT ATOMS            : 349                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.69                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1F5V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUN-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB011280.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL; 20-NOV-98                    
REMARK 200  TEMPERATURE           (KELVIN) : 100.0; 100.0                       
REMARK 200  PH                             : 6.5; 6.5                           
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N; Y                               
REMARK 200  RADIATION SOURCE               : ROTATING ANODE; PHOTON FACTORY     
REMARK 200  BEAMLINE                       : NULL; BL-6A                        
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200; NULL                 
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; NULL                            
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418; 1.00                       
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE; IMAGE PLATE           
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC; FUJI             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL                        
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.97                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, MES, SODIUM HYDROXIDE,         
REMARK 280  PEG 400, DIOXANE, PH 6.5, VAPOR DIFFUSION, SITTING DROP,            
REMARK 280  TEMPERATURE 281.0K. PEG 6000, MES, SODIUM HYDROXIDE, PEG 400,       
REMARK 280  DIOXANE, PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE         
REMARK 280  281.0K                                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER CONSTRUCTED FROM          
REMARK 300 CHAIN A A SYMMETRY PARTNER GENERATED BY THE TWO-FOLD.                
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: 11560 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 17960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -84.0 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 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    GLN A  44       67.31     38.49                                   
REMARK 500    CYS A  45       45.34   -105.11                                   
REMARK 500    ASN A 179      -41.11     65.24                                   
REMARK 500    ASN A 207       97.83    -47.98                                   
REMARK 500    GLU A 223       64.71   -114.79                                   
REMARK 500    GLN B  44       65.77     39.28                                   
REMARK 500    CYS B  45       44.71   -104.38                                   
REMARK 500    ASN B 179      -40.16     66.73                                   
REMARK 500    SER B 205      -64.63   -108.29                                   
REMARK 500    GLU B 223       68.64   -112.64                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 380        DISTANCE =  6.60 ANGSTROMS                       
REMARK 525    HOH A 393        DISTANCE =  7.97 ANGSTROMS                       
REMARK 525    HOH B 459        DISTANCE =  5.55 ANGSTROMS                       
REMARK 525    HOH A 463        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH A 464        DISTANCE =  8.85 ANGSTROMS                       
REMARK 525    HOH A 499        DISTANCE =  5.77 ANGSTROMS                       
REMARK 525    HOH B 520        DISTANCE =  5.79 ANGSTROMS                       
REMARK 525    HOH B 521        DISTANCE =  5.71 ANGSTROMS                       
REMARK 525    HOH B 527        DISTANCE =  5.32 ANGSTROMS                       
REMARK 525    HOH A 528        DISTANCE =  8.80 ANGSTROMS                       
REMARK 525    HOH A 529        DISTANCE = 10.40 ANGSTROMS                       
REMARK 525    HOH B 530        DISTANCE =  6.09 ANGSTROMS                       
REMARK 525    HOH A 530        DISTANCE = 12.16 ANGSTROMS                       
REMARK 525    HOH A 531        DISTANCE =  6.23 ANGSTROMS                       
REMARK 525    HOH B 532        DISTANCE =  8.84 ANGSTROMS                       
REMARK 525    HOH A 532        DISTANCE =  8.28 ANGSTROMS                       
REMARK 525    HOH B 533        DISTANCE = 12.02 ANGSTROMS                       
REMARK 525    HOH A 533        DISTANCE = 11.24 ANGSTROMS                       
REMARK 525    HOH B 534        DISTANCE =  9.64 ANGSTROMS                       
REMARK 525    HOH A 534        DISTANCE = 17.85 ANGSTROMS                       
REMARK 525    HOH B 535        DISTANCE =  9.78 ANGSTROMS                       
REMARK 525    HOH A 535        DISTANCE = 16.24 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN A 360                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN B 361                 
DBREF  1F5V A    1   240  UNP    P17117   NFSA_ECOLI       1    240             
DBREF  1F5V B    1   240  UNP    P17117   NFSA_ECOLI       1    240             
SEQRES   1 A  240  MET THR PRO THR ILE GLU LEU ILE CYS GLY HIS ARG SER          
SEQRES   2 A  240  ILE ARG HIS PHE THR ASP GLU PRO ILE SER GLU ALA GLN          
SEQRES   3 A  240  ARG GLU ALA ILE ILE ASN SER ALA ARG ALA THR SER SER          
SEQRES   4 A  240  SER SER PHE LEU GLN CYS SER SER ILE ILE ARG ILE THR          
SEQRES   5 A  240  ASP LYS ALA LEU ARG GLU GLU LEU VAL THR LEU THR GLY          
SEQRES   6 A  240  GLY GLN LYS HIS VAL ALA GLN ALA ALA GLU PHE TRP VAL          
SEQRES   7 A  240  PHE CYS ALA ASP PHE ASN ARG HIS LEU GLN ILE CYS PRO          
SEQRES   8 A  240  ASP ALA GLN LEU GLY LEU ALA GLU GLN LEU LEU LEU GLY          
SEQRES   9 A  240  VAL VAL ASP THR ALA MET MET ALA GLN ASN ALA LEU ILE          
SEQRES  10 A  240  ALA ALA GLU SER LEU GLY LEU GLY GLY VAL TYR ILE GLY          
SEQRES  11 A  240  GLY LEU ARG ASN ASN ILE GLU ALA VAL THR LYS LEU LEU          
SEQRES  12 A  240  LYS LEU PRO GLN HIS VAL LEU PRO LEU PHE GLY LEU CYS          
SEQRES  13 A  240  LEU GLY TRP PRO ALA ASP ASN PRO ASP LEU LYS PRO ARG          
SEQRES  14 A  240  LEU PRO ALA SER ILE LEU VAL HIS GLU ASN SER TYR GLN          
SEQRES  15 A  240  PRO LEU ASP LYS GLY ALA LEU ALA GLN TYR ASP GLU GLN          
SEQRES  16 A  240  LEU ALA GLU TYR TYR LEU THR ARG GLY SER ASN ASN ARG          
SEQRES  17 A  240  ARG ASP THR TRP SER ASP HIS ILE ARG ARG THR ILE ILE          
SEQRES  18 A  240  LYS GLU SER ARG PRO PHE ILE LEU ASP TYR LEU HIS LYS          
SEQRES  19 A  240  GLN GLY TRP ALA THR ARG                                      
SEQRES   1 B  240  MET THR PRO THR ILE GLU LEU ILE CYS GLY HIS ARG SER          
SEQRES   2 B  240  ILE ARG HIS PHE THR ASP GLU PRO ILE SER GLU ALA GLN          
SEQRES   3 B  240  ARG GLU ALA ILE ILE ASN SER ALA ARG ALA THR SER SER          
SEQRES   4 B  240  SER SER PHE LEU GLN CYS SER SER ILE ILE ARG ILE THR          
SEQRES   5 B  240  ASP LYS ALA LEU ARG GLU GLU LEU VAL THR LEU THR GLY          
SEQRES   6 B  240  GLY GLN LYS HIS VAL ALA GLN ALA ALA GLU PHE TRP VAL          
SEQRES   7 B  240  PHE CYS ALA ASP PHE ASN ARG HIS LEU GLN ILE CYS PRO          
SEQRES   8 B  240  ASP ALA GLN LEU GLY LEU ALA GLU GLN LEU LEU LEU GLY          
SEQRES   9 B  240  VAL VAL ASP THR ALA MET MET ALA GLN ASN ALA LEU ILE          
SEQRES  10 B  240  ALA ALA GLU SER LEU GLY LEU GLY GLY VAL TYR ILE GLY          
SEQRES  11 B  240  GLY LEU ARG ASN ASN ILE GLU ALA VAL THR LYS LEU LEU          
SEQRES  12 B  240  LYS LEU PRO GLN HIS VAL LEU PRO LEU PHE GLY LEU CYS          
SEQRES  13 B  240  LEU GLY TRP PRO ALA ASP ASN PRO ASP LEU LYS PRO ARG          
SEQRES  14 B  240  LEU PRO ALA SER ILE LEU VAL HIS GLU ASN SER TYR GLN          
SEQRES  15 B  240  PRO LEU ASP LYS GLY ALA LEU ALA GLN TYR ASP GLU GLN          
SEQRES  16 B  240  LEU ALA GLU TYR TYR LEU THR ARG GLY SER ASN ASN ARG          
SEQRES  17 B  240  ARG ASP THR TRP SER ASP HIS ILE ARG ARG THR ILE ILE          
SEQRES  18 B  240  LYS GLU SER ARG PRO PHE ILE LEU ASP TYR LEU HIS LYS          
SEQRES  19 B  240  GLN GLY TRP ALA THR ARG                                      
HET    FMN  A 360      31                                                       
HET    FMN  B 361      31                                                       
HETNAM     FMN FLAVIN MONONUCLEOTIDE                                            
HETSYN     FMN RIBOFLAVIN MONOPHOSPHATE                                         
FORMUL   3  FMN    2(C17 H21 N4 O9 P)                                           
FORMUL   5  HOH   *349(H2 O)                                                    
HELIX    1   1 THR A    2  GLY A   10  1                                   9    
HELIX    2   2 SER A   23  ALA A   36  1                                  14    
HELIX    3   3 SER A   39  LEU A   43  5                                   5    
HELIX    4   4 ASP A   53  THR A   64  1                                  12    
HELIX    5   5 LYS A   68  ALA A   73  1                                   6    
HELIX    6   6 PHE A   83  CYS A   90  1                                   8    
HELIX    7   7 LEU A   97  LEU A  122  1                                  26    
HELIX    8   8 GLY A  130  ASN A  134  5                                   5    
HELIX    9   9 ASN A  135  LEU A  143  1                                   9    
HELIX   10  10 PRO A  171  LEU A  175  1                                   5    
HELIX   11  11 ASP A  185  THR A  202  1                                  18    
HELIX   12  12 THR A  211  ILE A  221  1                                  11    
HELIX   13  13 PHE A  227  GLN A  235  1                                   9    
HELIX   14  14 THR B    2  GLY B   10  1                                   9    
HELIX   15  15 SER B   23  ALA B   36  1                                  14    
HELIX   16  16 SER B   39  LEU B   43  5                                   5    
HELIX   17  17 ASP B   53  THR B   64  1                                  12    
HELIX   18  18 LYS B   68  ALA B   73  1                                   6    
HELIX   19  19 PHE B   83  CYS B   90  1                                   8    
HELIX   20  20 LEU B   97  LEU B  122  1                                  26    
HELIX   21  21 GLY B  130  ASN B  134  5                                   5    
HELIX   22  22 ASN B  135  LEU B  143  1                                   9    
HELIX   23  23 PRO B  171  LEU B  175  1                                   5    
HELIX   24  24 ASP B  185  THR B  202  1                                  18    
HELIX   25  25 THR B  211  ILE B  221  1                                  11    
HELIX   26  26 PHE B  227  GLN B  235  1                                   9    
SHEET    1   A 5 GLY A 125  ILE A 129  0                                        
SHEET    2   A 5 VAL A 149  GLY A 158 -1  O  GLY A 154   N  ILE A 129           
SHEET    3   A 5 GLU A  75  ASP A  82 -1  N  GLU A  75   O  LEU A 157           
SHEET    4   A 5 SER A  46  ARG A  50 -1  O  SER A  47   N  CYS A  80           
SHEET    5   A 5 VAL B 176  GLU B 178  1  O  HIS B 177   N  ARG A  50           
SHEET    1   B 5 VAL A 176  GLU A 178  0                                        
SHEET    2   B 5 SER B  46  ARG B  50  1  O  ILE B  48   N  HIS A 177           
SHEET    3   B 5 GLU B  75  ASP B  82 -1  O  VAL B  78   N  ILE B  49           
SHEET    4   B 5 VAL B 149  GLY B 158 -1  N  LEU B 150   O  ALA B  81           
SHEET    5   B 5 GLY B 125  ILE B 129 -1  N  GLY B 125   O  GLY B 158           
SITE     1 AC1 22 HIS A  11  SER A  13  ARG A  15  GLN A  67                    
SITE     2 AC1 22 VAL A 127  TYR A 128  ILE A 129  GLY A 130                    
SITE     3 AC1 22 GLY A 131  LYS A 167  ARG A 169  HOH A 367                    
SITE     4 AC1 22 HOH A 380  HOH A 403  HOH A 475  SER B  38                    
SITE     5 AC1 22 SER B  39  SER B  40  PHE B  42  VAL B 106                    
SITE     6 AC1 22 ASP B 107  HOH B 504                                          
SITE     1 AC2 23 SER A  38  SER A  39  SER A  40  PHE A  42                    
SITE     2 AC2 23 VAL A 106  ASP A 107  HIS B  11  ARG B  12                    
SITE     3 AC2 23 SER B  13  ARG B  15  GLN B  67  VAL B 127                    
SITE     4 AC2 23 TYR B 128  ILE B 129  GLY B 130  GLY B 131                    
SITE     5 AC2 23 LYS B 167  ARG B 169  HOH B 381  HOH B 416                    
SITE     6 AC2 23 HOH B 425  HOH B 427  HOH B 498                               
CRYST1   51.560   52.860   52.830  75.79  60.71  61.17 P 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      0.019395 -0.010676 -0.010747        0.00000                         
SCALE2      0.000000  0.021594 -0.000270        0.00000                         
SCALE3      0.000000  0.000000  0.021705        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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