GenomeNet

Database: PDB
Entry: 4XVG
LinkDB: 4XVG
Original site: 4XVG 
HEADER    OXIDOREDUCTASE                          27-JAN-15   4XVG              
TITLE     CRYSTAL STRUCTURE OF ALKYLHYDROPEROXIDE REDUCTASE SUBUNIT AHPF FROM   
TITLE    2 ESCHERICHIA COLI                                                     
CAVEAT     4XVG    FAD A 700 HAS PLANAR CONFIGURATION AT C2'                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALKYL HYDROPEROXIDE REDUCTASE SUBUNIT F;                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ALKYL HYDROPEROXIDE REDUCTASE F52A PROTEIN;                 
COMPND   5 EC: 1.8.1.-;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);                  
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12;                                                         
SOURCE   5 GENE: AHPF, B0606, JW0599;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    ALKYLHYDROPEROXIDE REDUCTASE, OXIDOREDUCTASE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.F.CHEN,Z.Q.GAO,Y.H.DONG,Q.S.LIU                                     
REVDAT   1   24-FEB-16 4XVG    0                                                
JRNL        AUTH   C.F.CHEN,Z.Q.GAO,Y.H.DONG,Q.S.LIU                            
JRNL        TITL   CRYSTAL STRUCTURE OF ALKYLHYDROPEROXIDE REDUCTASE SUBUNIT    
JRNL        TITL 2 AHPF FROM ESCHERICHIA COLI                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.3_928)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.16                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 28657                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.180                           
REMARK   3   R VALUE            (WORKING SET) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.120                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1467                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 46.1654 -  4.7290    0.99     2860   150  0.1744 0.2017        
REMARK   3     2  4.7290 -  3.7541    0.99     2787   154  0.1438 0.1746        
REMARK   3     3  3.7541 -  3.2797    0.99     2762   163  0.1694 0.2137        
REMARK   3     4  3.2797 -  2.9799    0.98     2750   148  0.1895 0.2204        
REMARK   3     5  2.9799 -  2.7663    0.96     2675   137  0.1952 0.2723        
REMARK   3     6  2.7663 -  2.6032    0.96     2655   159  0.1957 0.2579        
REMARK   3     7  2.6032 -  2.4729    0.97     2678   147  0.1891 0.2802        
REMARK   3     8  2.4729 -  2.3652    0.97     2686   134  0.1951 0.2526        
REMARK   3     9  2.3652 -  2.2742    0.97     2698   145  0.1955 0.2645        
REMARK   3    10  2.2742 -  2.2000    0.95     2639   130  0.2158 0.3135        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.98                                          
REMARK   3   K_SOL              : 0.33                                          
REMARK   3   B_SOL              : 18.64                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.230            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.700           
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) : -5.08130                                             
REMARK   3    B22 (A**2) : -5.55980                                             
REMARK   3    B33 (A**2) : 10.64100                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -2.51150                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           4049                                  
REMARK   3   ANGLE     :  1.035           5494                                  
REMARK   3   CHIRALITY :  0.069            634                                  
REMARK   3   PLANARITY :  0.005            710                                  
REMARK   3   DIHEDRAL  : 15.814           1490                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4XVG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-FEB-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000206362.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-MAY-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
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 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28666                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.12300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.24                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.690                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB CODE 1HYU                                        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM CITRATE TRIBASIC, PH      
REMARK 280  7.0 20 % W/V POLYETHYLENE GLYCOL 3350, VAPOR DIFFUSION, SITTING     
REMARK 280  DROP, TEMPERATURE 291K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       53.52000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       29.31250            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       53.52000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       29.31250            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7550 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 43330 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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     THR A   520                                                      
REMARK 465     ALA A   521                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 103    CG   CD   CE   NZ                                   
REMARK 470     ARG A 185    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 201    CD   CE   NZ                                        
REMARK 470     LYS A 325    CD   CE   NZ                                        
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   OD1  ASP A    28     OG   SER A    33              2.10            
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    ASP A  28     -142.94   -120.76                                   
REMARK 500    ASP A  55       84.79   -160.47                                   
REMARK 500    LEU A  83     -150.65   -101.32                                   
REMARK 500    ASP A 116       69.18   -112.43                                   
REMARK 500    PHE A 159       53.73   -117.52                                   
REMARK 500    VAL A 253      -99.73   -107.03                                   
REMARK 500    SER A 260       -7.06     91.24                                   
REMARK 500    SER A 422      -51.41   -129.01                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD A 700                 
DBREF  4XVG A    1   521  UNP    P35340   AHPF_ECOLI       1    521             
SEQRES   1 A  521  MET LEU ASP THR ASN MET LYS THR GLN LEU LYS ALA TYR          
SEQRES   2 A  521  LEU GLU LYS LEU THR LYS PRO VAL GLU LEU ILE ALA THR          
SEQRES   3 A  521  LEU ASP ASP SER ALA LYS SER ALA GLU ILE LYS GLU LEU          
SEQRES   4 A  521  LEU ALA GLU ILE ALA GLU LEU SER ASP LYS VAL THR PHE          
SEQRES   5 A  521  LYS GLU ASP ASN SER LEU PRO VAL ARG LYS PRO SER PHE          
SEQRES   6 A  521  LEU ILE THR ASN PRO GLY SER ASN GLN GLY PRO ARG PHE          
SEQRES   7 A  521  ALA GLY SER PRO LEU GLY HIS GLU PHE THR SER LEU VAL          
SEQRES   8 A  521  LEU ALA LEU LEU TRP THR GLY GLY HIS PRO SER LYS GLU          
SEQRES   9 A  521  ALA GLN SER LEU LEU GLU GLN ILE ARG HIS ILE ASP GLY          
SEQRES  10 A  521  ASP PHE GLU PHE GLU THR TYR TYR SER LEU SER CYS HIS          
SEQRES  11 A  521  ASN CYS PRO ASP VAL VAL GLN ALA LEU ASN LEU MET SER          
SEQRES  12 A  521  VAL LEU ASN PRO ARG ILE LYS HIS THR ALA ILE ASP GLY          
SEQRES  13 A  521  GLY THR PHE GLN ASN GLU ILE THR ASP ARG ASN VAL MET          
SEQRES  14 A  521  GLY VAL PRO ALA VAL PHE VAL ASN GLY LYS GLU PHE GLY          
SEQRES  15 A  521  GLN GLY ARG MET THR LEU THR GLU ILE VAL ALA LYS ILE          
SEQRES  16 A  521  ASP THR GLY ALA GLU LYS ARG ALA ALA GLU GLU LEU ASN          
SEQRES  17 A  521  LYS ARG ASP ALA TYR ASP VAL LEU ILE VAL GLY SER GLY          
SEQRES  18 A  521  PRO ALA GLY ALA ALA ALA ALA ILE TYR SER ALA ARG LYS          
SEQRES  19 A  521  GLY ILE ARG THR GLY LEU MET GLY GLU ARG PHE GLY GLY          
SEQRES  20 A  521  GLN ILE LEU ASP THR VAL ASP ILE GLU ASN TYR ILE SER          
SEQRES  21 A  521  VAL PRO LYS THR GLU GLY GLN LYS LEU ALA GLY ALA LEU          
SEQRES  22 A  521  LYS VAL HIS VAL ASP GLU TYR ASP VAL ASP VAL ILE ASP          
SEQRES  23 A  521  SER GLN SER ALA SER LYS LEU ILE PRO ALA ALA VAL GLU          
SEQRES  24 A  521  GLY GLY LEU HIS GLN ILE GLU THR ALA SER GLY ALA VAL          
SEQRES  25 A  521  LEU LYS ALA ARG SER ILE ILE VAL ALA THR GLY ALA LYS          
SEQRES  26 A  521  TRP ARG ASN MET ASN VAL PRO GLY GLU ASP GLN TYR ARG          
SEQRES  27 A  521  THR LYS GLY VAL THR TYR CYS PRO HIS CYS ASP GLY PRO          
SEQRES  28 A  521  LEU PHE LYS GLY LYS ARG VAL ALA VAL ILE GLY GLY GLY          
SEQRES  29 A  521  ASN SER GLY VAL GLU ALA ALA ILE ASP LEU ALA GLY ILE          
SEQRES  30 A  521  VAL GLU HIS VAL THR LEU LEU GLU PHE ALA PRO GLU MET          
SEQRES  31 A  521  LYS ALA ASP GLN VAL LEU GLN ASP LYS LEU ARG SER LEU          
SEQRES  32 A  521  LYS ASN VAL ASP ILE ILE LEU ASN ALA GLN THR THR GLU          
SEQRES  33 A  521  VAL LYS GLY ASP GLY SER LYS VAL VAL GLY LEU GLU TYR          
SEQRES  34 A  521  ARG ASP ARG VAL SER GLY ASP ILE HIS ASN ILE GLU LEU          
SEQRES  35 A  521  ALA GLY ILE PHE VAL GLN ILE GLY LEU LEU PRO ASN THR          
SEQRES  36 A  521  ASN TRP LEU GLU GLY ALA VAL GLU ARG ASN ARG MET GLY          
SEQRES  37 A  521  GLU ILE ILE ILE ASP ALA LYS CYS GLU THR ASN VAL LYS          
SEQRES  38 A  521  GLY VAL PHE ALA ALA GLY ASP CYS THR THR VAL PRO TYR          
SEQRES  39 A  521  LYS GLN ILE ILE ILE ALA THR GLY GLU GLY ALA LYS ALA          
SEQRES  40 A  521  SER LEU SER ALA PHE ASP TYR LEU ILE ARG THR LYS THR          
SEQRES  41 A  521  ALA                                                          
HET    FAD  A 700      53                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
FORMUL   2  FAD    C27 H33 N9 O15 P2                                            
FORMUL   3  HOH   *250(H2 O)                                                    
HELIX    1 AA1 ASP A    3  GLU A   15  1                                  13    
HELIX    2 AA2 SER A   30  GLU A   45  1                                  16    
HELIX    3 AA3 LEU A   83  HIS A   85  5                                   3    
HELIX    4 AA4 GLU A   86  GLY A   98  1                                  13    
HELIX    5 AA5 ALA A  105  HIS A  114  1                                  10    
HELIX    6 AA6 ASN A  131  ASN A  146  1                                  16    
HELIX    7 AA7 PHE A  159  ARG A  166  1                                   8    
HELIX    8 AA8 THR A  187  ASP A  196  1                                  10    
HELIX    9 AA9 GLY A  198  LYS A  209  1                                  12    
HELIX   10 AB1 GLY A  221  ARG A  233  1                                  13    
HELIX   11 AB2 GLY A  246  THR A  252  5                                   7    
HELIX   12 AB3 GLY A  266  GLU A  279  1                                  14    
HELIX   13 AB4 GLU A  334  ARG A  338  5                                   5    
HELIX   14 AB5 CYS A  345  GLY A  350  1                                   6    
HELIX   15 AB6 PRO A  351  LYS A  354  5                                   4    
HELIX   16 AB7 GLY A  364  GLY A  376  1                                  13    
HELIX   17 AB8 ASP A  393  SER A  402  1                                  10    
HELIX   18 AB9 THR A  455  GLU A  459  5                                   5    
HELIX   19 AC1 GLN A  496  LYS A  519  1                                  24    
SHEET    1 AA1 8 VAL A  50  GLU A  54  0                                        
SHEET    2 AA1 8 VAL A  21  THR A  26  1  N  ALA A  25   O  LYS A  53           
SHEET    3 AA1 8 SER A  64  THR A  68 -1  O  THR A  68   N  GLU A  22           
SHEET    4 AA1 8 ARG A  77  ALA A  79 -1  O  PHE A  78   N  PHE A  65           
SHEET    5 AA1 8 ILE A 149  ASP A 155  1  O  ALA A 153   N  ALA A  79           
SHEET    6 AA1 8 PHE A 119  TYR A 125  1  N  THR A 123   O  ILE A 154           
SHEET    7 AA1 8 ALA A 173  VAL A 176 -1  O  ALA A 173   N  TYR A 124           
SHEET    8 AA1 8 LYS A 179  GLN A 183 -1  O  PHE A 181   N  VAL A 174           
SHEET    1 AA2 6 VAL A 282  ASP A 286  0                                        
SHEET    2 AA2 6 THR A 238  GLY A 242  1  N  LEU A 240   O  ILE A 285           
SHEET    3 AA2 6 TYR A 213  VAL A 218  1  N  ILE A 217   O  GLY A 239           
SHEET    4 AA2 6 VAL A 312  VAL A 320  1  O  ILE A 319   N  VAL A 218           
SHEET    5 AA2 6 HIS A 303  THR A 307 -1  N  HIS A 303   O  ALA A 315           
SHEET    6 AA2 6 ALA A 290  ILE A 294 -1  N  SER A 291   O  GLU A 306           
SHEET    1 AA3 5 VAL A 282  ASP A 286  0                                        
SHEET    2 AA3 5 THR A 238  GLY A 242  1  N  LEU A 240   O  ILE A 285           
SHEET    3 AA3 5 TYR A 213  VAL A 218  1  N  ILE A 217   O  GLY A 239           
SHEET    4 AA3 5 VAL A 312  VAL A 320  1  O  ILE A 319   N  VAL A 218           
SHEET    5 AA3 5 VAL A 483  ALA A 485  1  O  PHE A 484   N  VAL A 320           
SHEET    1 AA4 2 ASP A 254  ILE A 255  0                                        
SHEET    2 AA4 2 THR A 264  GLU A 265 -1  O  THR A 264   N  ILE A 255           
SHEET    1 AA5 2 ALA A 324  TRP A 326  0                                        
SHEET    2 AA5 2 LEU A 451  PRO A 453 -1  O  LEU A 452   N  LYS A 325           
SHEET    1 AA6 5 VAL A 342  THR A 343  0                                        
SHEET    2 AA6 5 GLY A 444  VAL A 447  1  O  ILE A 445   N  THR A 343           
SHEET    3 AA6 5 ARG A 357  ILE A 361  1  N  ALA A 359   O  PHE A 446           
SHEET    4 AA6 5 HIS A 380  LEU A 384  1  O  THR A 382   N  VAL A 360           
SHEET    5 AA6 5 VAL A 406  ILE A 409  1  O  ILE A 409   N  LEU A 383           
SHEET    1 AA7 3 ALA A 412  GLY A 419  0                                        
SHEET    2 AA7 3 VAL A 424  ASP A 431 -1  O  ARG A 430   N  GLN A 413           
SHEET    3 AA7 3 ILE A 437  GLU A 441 -1  O  HIS A 438   N  TYR A 429           
SSBOND   1 CYS A  345    CYS A  348                          1555   1555  2.04  
CISPEP   1 LYS A   62    PRO A   63          0        -0.76                     
CISPEP   2 VAL A  171    PRO A  172          0        -1.02                     
SITE     1 AC1 38 GLY A 219  GLY A 221  PRO A 222  ALA A 223                    
SITE     2 AC1 38 TYR A 230  GLY A 242  GLU A 243  ARG A 244                    
SITE     3 AC1 38 GLY A 247  GLN A 248  ILE A 249  THR A 252                    
SITE     4 AC1 38 ILE A 255  ASN A 257  GLN A 288  SER A 289                    
SITE     5 AC1 38 ALA A 290  ALA A 321  THR A 322  GLY A 323                    
SITE     6 AC1 38 ALA A 324  CYS A 348  ASN A 454  GLY A 487                    
SITE     7 AC1 38 ASP A 488  LYS A 495  GLN A 496  ILE A 497                    
SITE     8 AC1 38 ALA A 500  HOH A 810  HOH A 834  HOH A 874                    
SITE     9 AC1 38 HOH A 875  HOH A 876  HOH A 879  HOH A 882                    
SITE    10 AC1 38 HOH A 897  HOH A 950                                          
CRYST1  107.040   58.625   94.941  90.00 103.52  90.00 C 1 2 1       4          
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      0.009342  0.000000  0.002246        0.00000                         
SCALE2      0.000000  0.017058  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010833        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system