GenomeNet

Database: PDB
Entry: 2XFO
LinkDB: 2XFO
Original site: 2XFO 
HEADER    OXIDOREDUCTASE                          26-MAY-10   2XFO              
TITLE     TRANYLCYPROMINE-INHIBITED HUMAN MONOAMINE OXIDASE B ILE199ALA MUTANT  
TITLE    2 IN COMPLEX WITH 2-(2-BENZOFURANYL)-2-IMIDAZOLINE                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: AMINE OXIDASE [FLAVIN-CONTAINING] B;                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: MONOAMINE OXIDASE TYPE B,MAO-B;                             
COMPND   5 EC: 1.4.3.4;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MAOB;                                                          
SOURCE   6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4922                                        
KEYWDS    FLAVOPROTEIN, OXIDOREDUCTASE                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.BONIVENTO,E.M.MILCZEK,G.R.MCDONALD,C.BINDA,A.HOLT,D.E.EDMONDSON,    
AUTHOR   2 A.MATTEVI                                                            
REVDAT   6   20-DEC-23 2XFO    1       REMARK LINK                              
REVDAT   5   25-JUL-18 2XFO    1       COMPND SOURCE DBREF                      
REVDAT   4   16-MAY-18 2XFO    1       REMARK                                   
REVDAT   3   20-DEC-17 2XFO    1       JRNL                                     
REVDAT   2   24-NOV-10 2XFO    1       JRNL                                     
REVDAT   1   06-OCT-10 2XFO    0                                                
JRNL        AUTH   D.BONIVENTO,E.M.MILCZEK,G.R.MCDONALD,C.BINDA,A.HOLT,         
JRNL        AUTH 2 D.E.EDMONDSON,A.MATTEVI                                      
JRNL        TITL   POTENTIATION OF LIGAND BINDING THROUGH COOPERATIVE EFFECTS   
JRNL        TITL 2 IN MONOAMINE OXIDASE B.                                      
JRNL        REF    J. BIOL. CHEM.                V. 285 36849 2010              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   20855894                                                     
JRNL        DOI    10.1074/JBC.M110.169482                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 65.27                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 67613                          
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) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 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   REFLECTION IN BIN     (WORKING SET) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE SET COUNT          : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7908                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 154                                     
REMARK   3   SOLVENT ATOMS            : 303                                     
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : NULL                          
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL                          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : NULL                                          
REMARK   3   ION PROBE RADIUS   : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 2XFO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-MAY-10.                  
REMARK 100 THE DEPOSITION ID IS D_1290043796.                                   
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                                
REMARK 200  PH                             : 6.5                                
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) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 69410                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.5                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : 0.02000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1OJB                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.78                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.5                                   
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       65.27300            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      110.93150            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       65.27300            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      110.93150            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       65.27300            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      110.93150            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       65.27300            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      110.93150            
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 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: 6380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 35940 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ILE 199 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, ILE 199 TO ALA                        
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 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   O    HOH B  2006     O    HOH B  2009              1.36            
REMARK 500   O    HOH B  2094     O    HOH B  2095              1.43            
REMARK 500   NH2  ARG B   220     O    HOH B  2093              1.81            
REMARK 500   N5   FA8 A  1502     CB   3PL A  1503              2.17            
REMARK 500   CA   GLY B    27     O    HOH B  2008              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B  2111     O    HOH B  2111     2565     1.33            
REMARK 500   O    HOH A  2048     O    HOH A  2049     6565     1.95            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TRP A 184   CB    TRP A 184   CG     -0.108                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG B  87   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.8 DEGREES          
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    LYS A  52      -63.41     70.16                                   
REMARK 500    SER A  59      -54.98   -142.89                                   
REMARK 500    THR A  64      -10.36     83.41                                   
REMARK 500    ALA A 133       61.78   -159.08                                   
REMARK 500    THR A 174       46.25     33.01                                   
REMARK 500    THR A 201      -85.48    -91.73                                   
REMARK 500    ARG A 233       71.95   -116.53                                   
REMARK 500    ASN A 251       34.13    -84.27                                   
REMARK 500    HIS A 252       53.08     32.37                                   
REMARK 500    ALA A 263       43.40   -109.48                                   
REMARK 500    ALA A 346     -120.13     52.48                                   
REMARK 500    GLU A 379       60.91   -114.86                                   
REMARK 500    ASP A 419     -100.66     56.46                                   
REMARK 500    ALA A 424     -154.19   -112.47                                   
REMARK 500    LYS B  52      -70.96     63.34                                   
REMARK 500    SER B  59      -46.31   -139.63                                   
REMARK 500    THR B  64      -12.63     87.91                                   
REMARK 500    ALA B 133       68.33   -166.69                                   
REMARK 500    THR B 201      -76.08    -97.05                                   
REMARK 500    ALA B 346     -124.27     57.88                                   
REMARK 500    GLU B 379       68.74   -115.82                                   
REMARK 500    HIS B 382      163.11    176.21                                   
REMARK 500    ASP B 419      -97.59     64.41                                   
REMARK 500    ALA B 424     -153.10   -114.53                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 TRANYLCYPROMINE (TRA): CAK ATOM OF TRA IS COVALENTLY                 
REMARK 600  ATTACHED TO C4A ATOM OF FAD                                         
REMARK 600 FLAVIN-ADENINE DINUCLEOTIDE (REDUCED) (FAD): C4A ATOM OF             
REMARK 600  FAD IS COVALENTLY ATTACHED TO CAK ATOM OF TRA                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XCG A 1504                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XCG B 1499                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF RESIDUES 1502 TO       
REMARK 800  1503                                                                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF RESIDUES 1497 TO       
REMARK 800  1498                                                                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2C67   RELATED DB: PDB                                   
REMARK 900 MAO INHIBITION BY RASAGILINE ANALOGUES                               
REMARK 900 RELATED ID: 1OJA   RELATED DB: PDB                                   
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH ISATIN                     
REMARK 900 RELATED ID: 2V5Z   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN MAO B IN COMPLEX WITH THE SELECTIVE INHIBITOR     
REMARK 900 SAFINAMIDE                                                           
REMARK 900 RELATED ID: 1S3E   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MAOB IN COMPLEX WITH 6-HYDROXY-N-PROPARGYL-1(R) 
REMARK 900 -AMINOINDAN                                                          
REMARK 900 RELATED ID: 2C73   RELATED DB: PDB                                   
REMARK 900 FUNCTIONAL ROLE OF THE AROMATIC CAGE IN HUMAN MONOAMINE OXIDASE B:   
REMARK 900 STRUCTURES AND CATALYTIC PROPERTIES OF TYR435 MUTANT PROTEINS        
REMARK 900 RELATED ID: 1OJB   RELATED DB: PDB                                   
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH TRANYLCYPROMINE            
REMARK 900 RELATED ID: 2V60   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN MAO B IN COMPLEX WITH THE SELECTIVE INHIBITOR 7-  
REMARK 900 (3-CHLOROBENZYLOXY )-4-CARBOXALDEHYDE-COUMARIN                       
REMARK 900 RELATED ID: 2BYB   RELATED DB: PDB                                   
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH DEPRENYL                   
REMARK 900 RELATED ID: 2VRM   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN MAO B IN COMPLEX WITH PHENYETHYLHYDRAZINE         
REMARK 900 RELATED ID: 2C65   RELATED DB: PDB                                   
REMARK 900 MAO INHIBITION BY RASAGILINE ANALOGUES                               
REMARK 900 RELATED ID: 2C64   RELATED DB: PDB                                   
REMARK 900 MAO INHIBITION BY RASAGILINE ANALOGUES                               
REMARK 900 RELATED ID: 2XCG   RELATED DB: PDB                                   
REMARK 900 TRANYLCYPROMINE-INHIBITED HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH  
REMARK 900 2-(2- BENZOFURANYL)-2-IMIDAZOLINE                                    
REMARK 900 RELATED ID: 1OJ9   RELATED DB: PDB                                   
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH 1,4-DIPHENYL-2-BUTENE      
REMARK 900 RELATED ID: 2VZ2   RELATED DB: PDB                                   
REMARK 900 HUMAN MAO B IN COMPLEX WITH MOFEGILINE                               
REMARK 900 RELATED ID: 1OJD   RELATED DB: PDB                                   
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH LAURYLDIMETHYLAMINE-N-     
REMARK 900 OXIDE (LDAO)                                                         
REMARK 900 RELATED ID: 1S3B   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MAOB IN COMPLEX WITH N-METHYL-N-PROPARGYL-1(R)- 
REMARK 900 AMINOINDAN                                                           
REMARK 900 RELATED ID: 2C66   RELATED DB: PDB                                   
REMARK 900 MAO INHIBITION BY RASAGILINE ANALOGUES                               
REMARK 900 RELATED ID: 2BK4   RELATED DB: PDB                                   
REMARK 900 HUMAN MONOAMINE OXIDASE B: I199F MUTANT IN COMPLEX WITH RASAGILINE   
REMARK 900 RELATED ID: 2BK5   RELATED DB: PDB                                   
REMARK 900 HUMAN MONOAMINE OXIDASE B: I199F MUTANT IN COMPLEX WITH ISATIN       
REMARK 900 RELATED ID: 1H8R   RELATED DB: PDB                                   
REMARK 900 HUMAN MONOAMINE OXIDASE TYPE B (TRUNCATED)                           
REMARK 900 RELATED ID: 2C70   RELATED DB: PDB                                   
REMARK 900 FUNCTIONAL ROLE OF THE AROMATIC CAGE IN HUMAN MONOAMINE OXIDASE B:   
REMARK 900 STRUCTURES AND CATALYTIC PROPERTIES OF TYR435 MUTANT PROTEINS        
REMARK 900 RELATED ID: 2BK3   RELATED DB: PDB                                   
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH FARNESOL                   
REMARK 900 RELATED ID: 2C75   RELATED DB: PDB                                   
REMARK 900 FUNCTIONAL ROLE OF THE AROMATIC CAGE IN HUMAN MONOAMINE OXIDASE B:   
REMARK 900 STRUCTURES AND CATALYTIC PROPERTIES OF TYR435 MUTANT PROTEINS        
REMARK 900 RELATED ID: 2V61   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN MAO B IN COMPLEX WITH THE SELECTIVE INHIBITOR 7-  
REMARK 900 (3-CHLOROBENZYLOXY )-4-(METHYLAMINO)METHYL-COUMARIN                  
REMARK 900 RELATED ID: 2C72   RELATED DB: PDB                                   
REMARK 900 FUNCTIONAL ROLE OF THE AROMATIC CAGE IN HUMAN MONOAMINE OXIDASE B:   
REMARK 900 STRUCTURES AND CATALYTIC PROPERTIES OF TYR435 MUTANT PROTEINS        
REMARK 900 RELATED ID: 1S2Y   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MAOB IN COMPLEX WITH N-PROPARGYL-1(S)-          
REMARK 900 AMINOINDAN                                                           
REMARK 900 RELATED ID: 1GOS   RELATED DB: PDB                                   
REMARK 900 HUMAN MONOAMINE OXIDASE B                                            
REMARK 900 RELATED ID: 1S2Q   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MAOB IN COMPLEX WITH N-PROPARGYL-1(R)-          
REMARK 900 AMINOINDAN (RASAGILINE)                                              
REMARK 900 RELATED ID: 2C76   RELATED DB: PDB                                   
REMARK 900 FUNCTIONAL ROLE OF THE AROMATIC CAGE IN HUMAN MONOAMINE OXIDASE B:   
REMARK 900 STRUCTURES AND CATALYTIC PROPERTIES OF TYR435 MUTANT PROTEINS        
REMARK 900 RELATED ID: 2VRL   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN MAO B IN COMPLEX WITH BENZYLHYDRAZINE             
REMARK 900 RELATED ID: 1OJC   RELATED DB: PDB                                   
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH N-(2-AMINOETHYL)-P-        
REMARK 900 CHLOROBENZAMIDE                                                      
REMARK 900 RELATED ID: 2XFQ   RELATED DB: PDB                                   
REMARK 900 RASAGILINE-INHIBITED HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH 2-(2- 
REMARK 900 BENZOFURANYL)-2- IMIDAZOLINE                                         
REMARK 900 RELATED ID: 2XFN   RELATED DB: PDB                                   
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH 2-(2-BENZOFURANYL)-2-      
REMARK 900 IMIDAZOLINE                                                          
REMARK 900 RELATED ID: 2XFP   RELATED DB: PDB                                   
REMARK 900 ISATIN-INHIBITED HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH 2-(2-     
REMARK 900 BENZOFURANYL)-2- IMIDAZOLINE                                         
DBREF  2XFO A    1   520  UNP    P27338   AOFB_HUMAN       1    520             
DBREF  2XFO B    1   520  UNP    P27338   AOFB_HUMAN       1    520             
SEQADV 2XFO ALA A  199  UNP  P27338    ILE   199 ENGINEERED MUTATION            
SEQADV 2XFO ALA B  199  UNP  P27338    ILE   199 ENGINEERED MUTATION            
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 ALA 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 ALA 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    FA8  A1502      53                                                       
HET    3PL  A1503      10                                                       
HET    XCG  A1504      14                                                       
HET    FAD  B1497      53                                                       
HET    3PL  B1498      10                                                       
HET    XCG  B1499      14                                                       
HETNAM     FA8 [[(2R,3S,4S)-5-[(4AS)-7,8-DIMETHYL-2,4-DIOXO-4A,5-               
HETNAM   2 FA8  DIHYDROBENZO[G]PTERIDIN-10-YL]-2,3,4-TRIHYDROXY-                
HETNAM   3 FA8  PENTOXY]-HYDROXY-PHOSPHORYL] [(2R,3S,4R,5R)-5-(6-               
HETNAM   4 FA8  AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL               
HETNAM   5 FA8  HYDROGEN PHOSPHATE                                              
HETNAM     3PL 3-PHENYLPROPANAL                                                 
HETNAM     XCG 2-(2-BENZOFURANYL)-2-IMIDAZOLINE                                 
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
FORMUL   3  FA8    C27 H35 N9 O15 P2                                            
FORMUL   4  3PL    2(C9 H10 O)                                                  
FORMUL   5  XCG    2(C11 H8 N2 O)                                               
FORMUL   6  FAD    C27 H33 N9 O15 P2                                            
FORMUL   9  HOH   *303(H2 O)                                                    
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  CYS A  192  1                                  12    
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  LEU A  372  1                                  17    
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 SER B  214  GLY B  226  1                                  13    
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  ARG B  494  1                                   7    
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 2 THR A  79  LYS A  81  0                                        
SHEET    2  AC 2 ARG A 208  PHE A 210 -1  O  LYS A 209   N  TYR A  80           
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 FA8 A1502     1555   1555  1.65  
LINK         C4X FA8 A1502                 CB  3PL A1503     1555   1555  1.75  
LINK         SG  CYS B 397                 C8M FAD B1497     1555   1555  1.66  
LINK         C4X FAD B1497                 CB  3PL B1498     1555   1555  1.75  
CISPEP   1 ASN A  275    PRO A  276          0        -2.58                     
CISPEP   2 CYS A  397    TYR A  398          0        -3.52                     
CISPEP   3 ASN B  275    PRO B  276          0         2.34                     
CISPEP   4 CYS B  397    TYR B  398          0         6.46                     
SITE     1 AC1  7 PRO A 102  LEU A 164  PHE A 168  ALA A 199                    
SITE     2 AC1  7 THR A 201  ILE A 316  TYR A 326                               
SITE     1 AC2  9 PRO B 102  LEU B 164  LEU B 167  PHE B 168                    
SITE     2 AC2  9 ALA B 199  THR B 201  ILE B 316  TYR B 326                    
SITE     3 AC2  9 HOH B2039                                                     
SITE     1 AC3 40 VAL A  10  GLY A  11  GLY A  13  ILE A  14                    
SITE     2 AC3 40 SER A  15  LEU A  33  GLU A  34  ALA A  35                    
SITE     3 AC3 40 ARG A  36  GLY A  41  ARG A  42  THR A  43                    
SITE     4 AC3 40 GLY A  57  GLY A  58  SER A  59  TYR A  60                    
SITE     5 AC3 40 CYS A 172  TYR A 188  ARG A 233  PRO A 234                    
SITE     6 AC3 40 VAL A 235  ALA A 263  ILE A 264  TRP A 388                    
SITE     7 AC3 40 TYR A 393  CYS A 397  TYR A 398  GLY A 425                    
SITE     8 AC3 40 THR A 426  GLY A 434  TYR A 435  MET A 436                    
SITE     9 AC3 40 ALA A 439  HOH A2003  HOH A2004  HOH A2072                    
SITE    10 AC3 40 HOH A2105  HOH A2127  HOH A2128  HOH A2130                    
SITE     1 AC4 41 VAL B  10  GLY B  11  GLY B  13  ILE B  14                    
SITE     2 AC4 41 SER B  15  LEU B  33  GLU B  34  ALA B  35                    
SITE     3 AC4 41 ARG B  36  GLY B  40  GLY B  41  ARG B  42                    
SITE     4 AC4 41 THR B  43  GLY B  58  SER B  59  TYR B  60                    
SITE     5 AC4 41 CYS B 172  TYR B 188  GLN B 206  ARG B 233                    
SITE     6 AC4 41 PRO B 234  VAL B 235  ALA B 263  ILE B 264                    
SITE     7 AC4 41 TRP B 388  TYR B 393  CYS B 397  TYR B 398                    
SITE     8 AC4 41 GLY B 425  THR B 426  GLY B 434  TYR B 435                    
SITE     9 AC4 41 MET B 436  HOH B2003  HOH B2028  HOH B2107                    
SITE    10 AC4 41 HOH B2141  HOH B2170  HOH B2171  HOH B2172                    
SITE    11 AC4 41 HOH B2173                                                     
CRYST1  130.546  221.863   86.033  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      0.007660  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004507  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011623        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system