GenomeNet

Database: PDB
Entry: 1OJ9
LinkDB: 1OJ9
Original site: 1OJ9 
HEADER    OXIDOREDUCTASE                          08-JUL-03   1OJ9              
TITLE     HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH                             
TITLE    2 1,4-DIPHENYL-2-BUTENE                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: AMINE OXIDASE [FLAVIN-CONTAINING] B;                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: MONOAMINE OXIDASE, MAO-B;                                   
COMPND   5 EC: 1.4.3.4;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: PICHIA PASTORIS;                                  
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 4922                                        
KEYWDS    OXIDOREDUCTASE, FAD-CONTAINING AMINE OXIDASE, MAOB                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.BINDA,D.E.EDMONDSON,A.MATTEVI                                       
REVDAT   3   24-FEB-09 1OJ9    1       VERSN                                    
REVDAT   2   21-AUG-03 1OJ9    1       JRNL                                     
REVDAT   1   15-AUG-03 1OJ9    0                                                
JRNL        AUTH   C.BINDA,M.LI,F.HUBALEK,N.RESTELLI,D.E.EDMONDSON,             
JRNL        AUTH 2 A.MATTEVI                                                    
JRNL        TITL   INSIGHTS INTO THE MODE OF INHIBITION OF HUMAN                
JRNL        TITL 2 MITOCHONDRIAL MONOAMINE OXIDASE B FROM                       
JRNL        TITL 3 HIGH-RESOLUTION CRYSTAL STRUCTURES                           
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 100  9750 2003              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   12913124                                                     
JRNL        DOI    10.1073/PNAS.1633804100                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.3  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.3                            
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.0                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 49954                          
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) : 0.212                           
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.6                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1326                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7911                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 138                                     
REMARK   3   SOLVENT ATOMS            : 230                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.632                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.44                                                 
REMARK   3    B22 (A**2) : -0.98                                                
REMARK   3    B33 (A**2) : -1.46                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.341         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.234         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.150         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.155         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1OJ9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  08-JUL-03.                 
REMARK 100 THE PDBE ID CODE IS EBI-13009.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 302811                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.6                               
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : 0.10700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 66.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.20200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 2                          
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,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z                                         
REMARK 290       7555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       8555   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        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
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        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       66.05200            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      112.01100            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       66.05200            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      112.01100            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       66.05200            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      112.01100            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       66.05200            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      112.01100            
REMARK 290   SMTRY3   8  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 GENERATING THE BIOMOLECULE                                           
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: PQS                                                   
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     PHE A   502                                                      
REMARK 465     SER A   503                                                      
REMARK 465     ALA A   504                                                      
REMARK 465     THR A   505                                                      
REMARK 465     ALA A   506                                                      
REMARK 465     LEU A   507                                                      
REMARK 465     GLY A   508                                                      
REMARK 465     PHE A   509                                                      
REMARK 465     LEU A   510                                                      
REMARK 465     ALA A   511                                                      
REMARK 465     HIS A   512                                                      
REMARK 465     LYS A   513                                                      
REMARK 465     ARG A   514                                                      
REMARK 465     GLY A   515                                                      
REMARK 465     LEU A   516                                                      
REMARK 465     LEU A   517                                                      
REMARK 465     VAL A   518                                                      
REMARK 465     ARG A   519                                                      
REMARK 465     VAL A   520                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     GLY B   497                                                      
REMARK 465     LEU B   498                                                      
REMARK 465     THR B   499                                                      
REMARK 465     THR B   500                                                      
REMARK 465     ILE B   501                                                      
REMARK 465     PHE B   502                                                      
REMARK 465     SER B   503                                                      
REMARK 465     ALA B   504                                                      
REMARK 465     THR B   505                                                      
REMARK 465     ALA B   506                                                      
REMARK 465     LEU B   507                                                      
REMARK 465     GLY B   508                                                      
REMARK 465     PHE B   509                                                      
REMARK 465     LEU B   510                                                      
REMARK 465     ALA B   511                                                      
REMARK 465     HIS B   512                                                      
REMARK 465     LYS B   513                                                      
REMARK 465     ARG B   514                                                      
REMARK 465     GLY B   515                                                      
REMARK 465     LEU B   516                                                      
REMARK 465     LEU B   517                                                      
REMARK 465     VAL B   518                                                      
REMARK 465     ARG B   519                                                      
REMARK 465     VAL B   520                                                      
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     ILE A 501    CG1  CG2  CD1                                       
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 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A1502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PB A1503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B1497                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PB B1498                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1GOS   RELATED DB: PDB                                   
REMARK 900  HUMAN MONOAMINE OXIDASE B                                           
REMARK 900 RELATED ID: 1H8R   RELATED DB: PDB                                   
REMARK 900  HUMAN MONOAMINE OXIDASE TYPE B (TRUNCATED)                          
REMARK 900 RELATED ID: 1OJB   RELATED DB: PDB                                   
REMARK 900  HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH TRANYLCYPROMINE           
REMARK 900 RELATED ID: 1OJA   RELATED DB: PDB                                   
REMARK 900  HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH ISATIN                    
REMARK 900 RELATED ID: 1OJC   RELATED DB: PDB                                   
REMARK 900  HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH                           
REMARK 900  2 N-(2-AMINOETHYL)-P-CHLOROBENZAMIDE                                
REMARK 900 RELATED ID: 1OJD   RELATED DB: PDB                                   
REMARK 900  HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH                           
REMARK 900  LAURYLDIMETHYLAMINE-N-OXIDE (LDAO)                                  
DBREF  1OJ9 A    1     1  PDB    1OJ9     1OJ9             1      1             
DBREF  1OJ9 A    2   520  UNP    P27338   AOFB_HUMAN       1    519             
DBREF  1OJ9 B    1     1  PDB    1OJ9     1OJ9             1      1             
DBREF  1OJ9 B    2   520  UNP    P27338   AOFB_HUMAN       1    519             
SEQRES   1 A  520  MET SER ASN LYS CYS ASP VAL VAL VAL VAL GLY GLY GLY          
SEQRES   2 A  520  ILE SER GLY MET ALA ALA ALA LYS LEU LEU HIS ASP SER          
SEQRES   3 A  520  GLY LEU ASN VAL VAL VAL LEU GLU ALA ARG ASP ARG VAL          
SEQRES   4 A  520  GLY GLY ARG THR TYR THR LEU ARG ASN GLN LYS VAL LYS          
SEQRES   5 A  520  TYR VAL ASP LEU GLY GLY SER TYR VAL GLY PRO THR GLN          
SEQRES   6 A  520  ASN ARG ILE LEU ARG LEU ALA LYS GLU LEU GLY LEU GLU          
SEQRES   7 A  520  THR TYR LYS VAL ASN GLU VAL GLU ARG LEU ILE HIS HIS          
SEQRES   8 A  520  VAL LYS GLY LYS SER TYR PRO PHE ARG GLY PRO PHE PRO          
SEQRES   9 A  520  PRO VAL TRP ASN PRO ILE THR TYR LEU ASP HIS ASN ASN          
SEQRES  10 A  520  PHE TRP ARG THR MET ASP ASP MET GLY ARG GLU ILE PRO          
SEQRES  11 A  520  SER ASP ALA PRO TRP LYS ALA PRO LEU ALA GLU GLU TRP          
SEQRES  12 A  520  ASP ASN MET THR MET LYS GLU LEU LEU ASP LYS LEU CYS          
SEQRES  13 A  520  TRP THR GLU SER ALA LYS GLN LEU ALA THR LEU PHE VAL          
SEQRES  14 A  520  ASN LEU CYS VAL THR ALA GLU THR HIS GLU VAL SER ALA          
SEQRES  15 A  520  LEU TRP PHE LEU TRP TYR VAL LYS GLN CYS GLY GLY THR          
SEQRES  16 A  520  THR ARG ILE ILE SER THR THR ASN GLY GLY GLN GLU ARG          
SEQRES  17 A  520  LYS PHE VAL GLY GLY SER GLY GLN VAL SER GLU ARG ILE          
SEQRES  18 A  520  MET ASP LEU LEU GLY ASP ARG VAL LYS LEU GLU ARG PRO          
SEQRES  19 A  520  VAL ILE TYR ILE ASP GLN THR ARG GLU ASN VAL LEU VAL          
SEQRES  20 A  520  GLU THR LEU ASN HIS GLU MET TYR GLU ALA LYS TYR VAL          
SEQRES  21 A  520  ILE SER ALA ILE PRO PRO THR LEU GLY MET LYS ILE HIS          
SEQRES  22 A  520  PHE ASN PRO PRO LEU PRO MET MET ARG ASN GLN MET ILE          
SEQRES  23 A  520  THR ARG VAL PRO LEU GLY SER VAL ILE LYS CYS ILE VAL          
SEQRES  24 A  520  TYR TYR LYS GLU PRO PHE TRP ARG LYS LYS ASP TYR CYS          
SEQRES  25 A  520  GLY THR MET ILE ILE ASP GLY GLU GLU ALA PRO VAL ALA          
SEQRES  26 A  520  TYR THR LEU ASP ASP THR LYS PRO GLU GLY ASN TYR ALA          
SEQRES  27 A  520  ALA ILE MET GLY PHE ILE LEU ALA HIS LYS ALA ARG LYS          
SEQRES  28 A  520  LEU ALA ARG LEU THR LYS GLU GLU ARG LEU LYS LYS LEU          
SEQRES  29 A  520  CYS GLU LEU TYR ALA LYS VAL LEU GLY SER LEU GLU ALA          
SEQRES  30 A  520  LEU GLU PRO VAL HIS TYR GLU GLU LYS ASN TRP CYS GLU          
SEQRES  31 A  520  GLU GLN TYR SER GLY GLY CYS TYR THR THR TYR PHE PRO          
SEQRES  32 A  520  PRO GLY ILE LEU THR GLN TYR GLY ARG VAL LEU ARG GLN          
SEQRES  33 A  520  PRO VAL ASP ARG ILE TYR PHE ALA GLY THR GLU THR ALA          
SEQRES  34 A  520  THR HIS TRP SER GLY TYR MET GLU GLY ALA VAL GLU ALA          
SEQRES  35 A  520  GLY GLU ARG ALA ALA ARG GLU ILE LEU HIS ALA MET GLY          
SEQRES  36 A  520  LYS ILE PRO GLU ASP GLU ILE TRP GLN SER GLU PRO GLU          
SEQRES  37 A  520  SER VAL ASP VAL PRO ALA GLN PRO ILE THR THR THR PHE          
SEQRES  38 A  520  LEU GLU ARG HIS LEU PRO SER VAL PRO GLY LEU LEU ARG          
SEQRES  39 A  520  LEU ILE GLY LEU THR THR ILE PHE SER ALA THR ALA LEU          
SEQRES  40 A  520  GLY PHE LEU ALA HIS LYS ARG GLY LEU LEU VAL ARG VAL          
SEQRES   1 B  520  MET SER ASN LYS CYS ASP VAL VAL VAL VAL GLY GLY GLY          
SEQRES   2 B  520  ILE SER GLY MET ALA ALA ALA LYS LEU LEU HIS ASP SER          
SEQRES   3 B  520  GLY LEU ASN VAL VAL VAL LEU GLU ALA ARG ASP ARG VAL          
SEQRES   4 B  520  GLY GLY ARG THR TYR THR LEU ARG ASN GLN LYS VAL LYS          
SEQRES   5 B  520  TYR VAL ASP LEU GLY GLY SER TYR VAL GLY PRO THR GLN          
SEQRES   6 B  520  ASN ARG ILE LEU ARG LEU ALA LYS GLU LEU GLY LEU GLU          
SEQRES   7 B  520  THR TYR LYS VAL ASN GLU VAL GLU ARG LEU ILE HIS HIS          
SEQRES   8 B  520  VAL LYS GLY LYS SER TYR PRO PHE ARG GLY PRO PHE PRO          
SEQRES   9 B  520  PRO VAL TRP ASN PRO ILE THR TYR LEU ASP HIS ASN ASN          
SEQRES  10 B  520  PHE TRP ARG THR MET ASP ASP MET GLY ARG GLU ILE PRO          
SEQRES  11 B  520  SER ASP ALA PRO TRP LYS ALA PRO LEU ALA GLU GLU TRP          
SEQRES  12 B  520  ASP ASN MET THR MET LYS GLU LEU LEU ASP LYS LEU CYS          
SEQRES  13 B  520  TRP THR GLU SER ALA LYS GLN LEU ALA THR LEU PHE VAL          
SEQRES  14 B  520  ASN LEU CYS VAL THR ALA GLU THR HIS GLU VAL SER ALA          
SEQRES  15 B  520  LEU TRP PHE LEU TRP TYR VAL LYS GLN CYS GLY GLY THR          
SEQRES  16 B  520  THR ARG ILE ILE SER THR THR ASN GLY GLY GLN GLU ARG          
SEQRES  17 B  520  LYS PHE VAL GLY GLY SER GLY GLN VAL SER GLU ARG ILE          
SEQRES  18 B  520  MET ASP LEU LEU GLY ASP ARG VAL LYS LEU GLU ARG PRO          
SEQRES  19 B  520  VAL ILE TYR ILE ASP GLN THR ARG GLU ASN VAL LEU VAL          
SEQRES  20 B  520  GLU THR LEU ASN HIS GLU MET TYR GLU ALA LYS TYR VAL          
SEQRES  21 B  520  ILE SER ALA ILE PRO PRO THR LEU GLY MET LYS ILE HIS          
SEQRES  22 B  520  PHE ASN PRO PRO LEU PRO MET MET ARG ASN GLN MET ILE          
SEQRES  23 B  520  THR ARG VAL PRO LEU GLY SER VAL ILE LYS CYS ILE VAL          
SEQRES  24 B  520  TYR TYR LYS GLU PRO PHE TRP ARG LYS LYS ASP TYR CYS          
SEQRES  25 B  520  GLY THR MET ILE ILE ASP GLY GLU GLU ALA PRO VAL ALA          
SEQRES  26 B  520  TYR THR LEU ASP ASP THR LYS PRO GLU GLY ASN TYR ALA          
SEQRES  27 B  520  ALA ILE MET GLY PHE ILE LEU ALA HIS LYS ALA ARG LYS          
SEQRES  28 B  520  LEU ALA ARG LEU THR LYS GLU GLU ARG LEU LYS LYS LEU          
SEQRES  29 B  520  CYS GLU LEU TYR ALA LYS VAL LEU GLY SER LEU GLU ALA          
SEQRES  30 B  520  LEU GLU PRO VAL HIS TYR GLU GLU LYS ASN TRP CYS GLU          
SEQRES  31 B  520  GLU GLN TYR SER GLY GLY CYS TYR THR THR TYR PHE PRO          
SEQRES  32 B  520  PRO GLY ILE LEU THR GLN TYR GLY ARG VAL LEU ARG GLN          
SEQRES  33 B  520  PRO VAL ASP ARG ILE TYR PHE ALA GLY THR GLU THR ALA          
SEQRES  34 B  520  THR HIS TRP SER GLY TYR MET GLU GLY ALA VAL GLU ALA          
SEQRES  35 B  520  GLY GLU ARG ALA ALA ARG GLU ILE LEU HIS ALA MET GLY          
SEQRES  36 B  520  LYS ILE PRO GLU ASP GLU ILE TRP GLN SER GLU PRO GLU          
SEQRES  37 B  520  SER VAL ASP VAL PRO ALA GLN PRO ILE THR THR THR PHE          
SEQRES  38 B  520  LEU GLU ARG HIS LEU PRO SER VAL PRO GLY LEU LEU ARG          
SEQRES  39 B  520  LEU ILE GLY LEU THR THR ILE PHE SER ALA THR ALA LEU          
SEQRES  40 B  520  GLY PHE LEU ALA HIS LYS ARG GLY LEU LEU VAL ARG VAL          
HET    FAD  A1502      53                                                       
HET    1PB  A1503      16                                                       
HET    FAD  B1497      53                                                       
HET    1PB  B1498      16                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     1PB 1,4-DIPHENYL-2-BUTENE                                            
HETSYN     1PB [(1E)-4-PHENYLBUT-1-ENYL]BENZENE                                 
FORMUL   3  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL   4  1PB    2(C16 H16)                                                   
FORMUL   7  HOH   *230(H2 O1)                                                   
HELIX    1   1 GLY A   13  SER A   26  1                                  14    
HELIX    2   2 GLN A   65  LEU A   75  1                                  11    
HELIX    3   3 ASN A  108  ARG A  127  1                                  20    
HELIX    4   4 ALA A  133  ALA A  137  5                                   5    
HELIX    5   5 LEU A  139  ASN A  145  1                                   7    
HELIX    6   6 THR A  147  CYS A  156  1                                  10    
HELIX    7   7 THR A  158  THR A  174  1                                  17    
HELIX    8   8 SER A  181  GLN A  191  1                                  11    
HELIX    9   9 GLY A  194  SER A  200  1                                   7    
HELIX   10  10 GLY A  215  GLY A  226  1                                  12    
HELIX   11  11 PRO A  265  ILE A  272  5                                   8    
HELIX   12  12 PRO A  279  ILE A  286  1                                   8    
HELIX   13  13 PRO A  304  LYS A  309  5                                   6    
HELIX   14  14 ALA A  346  ALA A  353  1                                   8    
HELIX   15  15 THR A  356  GLY A  373  1                                  18    
HELIX   16  16 SER A  374  GLU A  379  5                                   6    
HELIX   17  17 CYS A  389  GLU A  391  5                                   3    
HELIX   18  18 GLY A  405  GLY A  411  1                                   7    
HELIX   19  19 ARG A  412  LEU A  414  5                                   3    
HELIX   20  20 GLY A  425  ALA A  429  5                                   5    
HELIX   21  21 TYR A  435  MET A  454  1                                  20    
HELIX   22  22 PRO A  458  ILE A  462  5                                   5    
HELIX   23  23 THR A  480  LEU A  486  1                                   7    
HELIX   24  24 SER A  488  THR A  500  1                                  13    
HELIX   25  25 GLY B   13  SER B   26  1                                  14    
HELIX   26  26 GLN B   65  LEU B   75  1                                  11    
HELIX   27  27 ASN B  108  ARG B  127  1                                  20    
HELIX   28  28 ALA B  133  ALA B  137  5                                   5    
HELIX   29  29 LEU B  139  ASN B  145  1                                   7    
HELIX   30  30 THR B  147  CYS B  156  1                                  10    
HELIX   31  31 THR B  158  THR B  174  1                                  17    
HELIX   32  32 SER B  181  GLN B  191  1                                  11    
HELIX   33  33 GLY B  194  SER B  200  1                                   7    
HELIX   34  34 GLY B  215  GLY B  226  1                                  12    
HELIX   35  35 PRO B  265  ILE B  272  5                                   8    
HELIX   36  36 PRO B  279  ILE B  286  1                                   8    
HELIX   37  37 PRO B  304  LYS B  309  5                                   6    
HELIX   38  38 ALA B  346  ALA B  353  1                                   8    
HELIX   39  39 THR B  356  GLY B  373  1                                  18    
HELIX   40  40 SER B  374  GLU B  379  5                                   6    
HELIX   41  41 CYS B  389  GLU B  391  5                                   3    
HELIX   42  42 GLY B  405  GLY B  411  1                                   7    
HELIX   43  43 ARG B  412  LEU B  414  5                                   3    
HELIX   44  44 GLY B  425  ALA B  429  5                                   5    
HELIX   45  45 TYR B  435  MET B  454  1                                  20    
HELIX   46  46 PRO B  458  ILE B  462  5                                   5    
HELIX   47  47 THR B  480  LEU B  486  1                                   7    
HELIX   48  48 SER B  488  ILE B  496  1                                   9    
SHEET    1  AA 5 VAL A 229  LYS A 230  0                                        
SHEET    2  AA 5 VAL A  30  LEU A  33  1  O  VAL A  32   N  LYS A 230           
SHEET    3  AA 5 VAL A   7  VAL A  10  1  O  VAL A   7   N  VAL A  31           
SHEET    4  AA 5 TYR A 259  SER A 262  1  O  TYR A 259   N  VAL A   8           
SHEET    5  AA 5 ILE A 421  PHE A 423  1  O  TYR A 422   N  SER A 262           
SHEET    1  AB 2 THR A  45  LEU A  46  0                                        
SHEET    2  AB 2 VAL A  54  ASP A  55 -1  O  VAL A  54   N  LEU A  46           
SHEET    1  AC 3 TYR A  60  VAL A  61  0                                        
SHEET    2  AC 3 ARG A 208  PHE A 210 -1  O  ARG A 208   N  VAL A  61           
SHEET    3  AC 3 THR A  79  LYS A  81 -1  O  TYR A  80   N  LYS A 209           
SHEET    1  AD 7 LYS A  95  PHE A  99  0                                        
SHEET    2  AD 7 ARG A  87  VAL A  92 -1  O  LEU A  88   N  PHE A  99           
SHEET    3  AD 7 TYR A 311  ILE A 317  1  N  CYS A 312   O  ARG A  87           
SHEET    4  AD 7 TYR A 326  ASP A 329 -1  O  THR A 327   N  MET A 315           
SHEET    5  AD 7 ALA A 339  LEU A 345 -1  O  MET A 341   N  LEU A 328           
SHEET    6  AD 7 VAL A 294  TYR A 300 -1  O  ILE A 295   N  ILE A 344           
SHEET    7  AD 7 HIS A 382  ASN A 387 -1  O  HIS A 382   N  TYR A 300           
SHEET    1  AE 4 MET A 254  ALA A 257  0                                        
SHEET    2  AE 4 VAL A 245  THR A 249 -1  O  VAL A 245   N  ALA A 257           
SHEET    3  AE 4 VAL A 235  ASP A 239 -1  N  ILE A 236   O  GLU A 248           
SHEET    4  AE 4 HIS A 273  ASN A 275  1  O  HIS A 273   N  ILE A 238           
SHEET    1  BA 5 VAL B 229  LYS B 230  0                                        
SHEET    2  BA 5 VAL B  30  LEU B  33  1  O  VAL B  32   N  LYS B 230           
SHEET    3  BA 5 VAL B   7  VAL B  10  1  O  VAL B   7   N  VAL B  31           
SHEET    4  BA 5 TYR B 259  SER B 262  1  O  TYR B 259   N  VAL B   8           
SHEET    5  BA 5 ILE B 421  PHE B 423  1  O  TYR B 422   N  SER B 262           
SHEET    1  BB 2 THR B  45  LEU B  46  0                                        
SHEET    2  BB 2 VAL B  54  ASP B  55 -1  O  VAL B  54   N  LEU B  46           
SHEET    1  BC 3 TYR B  60  VAL B  61  0                                        
SHEET    2  BC 3 ARG B 208  PHE B 210 -1  O  ARG B 208   N  VAL B  61           
SHEET    3  BC 3 THR B  79  LYS B  81 -1  O  TYR B  80   N  LYS B 209           
SHEET    1  BD 7 LYS B  95  PHE B  99  0                                        
SHEET    2  BD 7 ARG B  87  VAL B  92 -1  O  LEU B  88   N  PHE B  99           
SHEET    3  BD 7 TYR B 311  ILE B 317  1  N  CYS B 312   O  ARG B  87           
SHEET    4  BD 7 TYR B 326  ASP B 329 -1  O  THR B 327   N  MET B 315           
SHEET    5  BD 7 ALA B 339  LEU B 345 -1  O  MET B 341   N  LEU B 328           
SHEET    6  BD 7 VAL B 294  TYR B 300 -1  O  ILE B 295   N  ILE B 344           
SHEET    7  BD 7 HIS B 382  ASN B 387 -1  O  HIS B 382   N  TYR B 300           
SHEET    1  BE 4 MET B 254  ALA B 257  0                                        
SHEET    2  BE 4 VAL B 245  THR B 249 -1  O  VAL B 245   N  ALA B 257           
SHEET    3  BE 4 VAL B 235  ASP B 239 -1  N  ILE B 236   O  GLU B 248           
SHEET    4  BE 4 HIS B 273  ASN B 275  1  O  HIS B 273   N  ILE B 238           
LINK         SG  CYS A 397                 C8M FAD A1502     1555   1555  1.64  
LINK         SG  CYS B 397                 C8M FAD B1497     1555   1555  1.62  
CISPEP   1 ASN A  275    PRO A  276          0         2.11                     
CISPEP   2 CYS A  397    TYR A  398          0        -0.75                     
CISPEP   3 ASN B  275    PRO B  276          0         2.70                     
CISPEP   4 CYS B  397    TYR B  398          0         0.55                     
SITE     1 AC1 39 VAL A  10  GLY A  11  GLY A  13  ILE A  14                    
SITE     2 AC1 39 SER A  15  LEU A  33  GLU A  34  ALA A  35                    
SITE     3 AC1 39 ARG A  36  GLY A  40  GLY A  41  ARG A  42                    
SITE     4 AC1 39 THR A  43  GLY A  57  GLY A  58  SER A  59                    
SITE     5 AC1 39 TYR A  60  PRO A 234  VAL A 235  ALA A 263                    
SITE     6 AC1 39 ILE A 264  TRP A 388  TYR A 393  CYS A 397                    
SITE     7 AC1 39 TYR A 398  GLY A 425  THR A 426  GLY A 434                    
SITE     8 AC1 39 TYR A 435  MET A 436  ALA A 439  HOH A2001                    
SITE     9 AC1 39 HOH A2009  HOH A2052  HOH A2096  HOH A2097                    
SITE    10 AC1 39 HOH A2098  HOH A2099  HOH A2100                               
SITE     1 AC2  3 LEU A 171  ILE A 199  GLN A 206                               
SITE     1 AC3 40 VAL B  10  GLY B  11  GLY B  13  ILE B  14                    
SITE     2 AC3 40 SER B  15  LEU B  33  GLU B  34  ALA B  35                    
SITE     3 AC3 40 ARG B  36  GLY B  40  GLY B  41  ARG B  42                    
SITE     4 AC3 40 THR B  43  GLY B  57  GLY B  58  SER B  59                    
SITE     5 AC3 40 TYR B  60  ARG B 233  PRO B 234  VAL B 235                    
SITE     6 AC3 40 ALA B 263  ILE B 264  TRP B 388  TYR B 393                    
SITE     7 AC3 40 CYS B 397  TYR B 398  GLY B 425  THR B 426                    
SITE     8 AC3 40 GLY B 434  TYR B 435  MET B 436  ALA B 439                    
SITE     9 AC3 40 HOH B2017  HOH B2074  HOH B2102  HOH B2126                    
SITE    10 AC3 40 HOH B2127  HOH B2128  HOH B2129  HOH B2130                    
SITE     1 AC4  3 LEU B 171  ILE B 199  GLN B 206                               
CRYST1  132.104  224.022   86.833  90.00  90.00  90.00 C 2 2 2      16          
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      0.007570  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004464  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011516        0.00000                         
MTRIX1   1 -0.530150 -0.493700 -0.689350      140.08148    1                    
MTRIX2   1 -0.495400 -0.479440  0.724370      209.34830    1                    
MTRIX3   1 -0.688120  0.725530  0.009590      -54.66193    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system