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Database: PDB
Entry: 2V60
LinkDB: 2V60
Original site: 2V60 
HEADER    OXIDOREDUCTASE                          12-JUL-07   2V60              
TITLE     STRUCTURE OF HUMAN MAO B IN COMPLEX WITH THE SELECTIVE INHIBITOR 7-(3-
TITLE    2 CHLOROBENZYLOXY)-4-CARBOXALDEHYDE-COUMARIN                           
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, MONOAMINE OXIDASE;         
COMPND   5 EC: 1.4.3.4;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_TAXID: 9606;                                                
SOURCE   4 EXPRESSION_SYSTEM: PICHIA PASTORIS;                                  
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 4922                                        
KEYWDS    FAD, MEMBRANE, SAFINAMIDE, FLAVOPROTEIN, HUMAN MAO B STRUCTURE,       
KEYWDS   2 REVERSIBLE INHIBITOR BINDING, MITOCHONDRION, TRANSMEMBRANE,          
KEYWDS   3 OXIDOREDUCTASE, NEUROPROTECTION, PARKINSON'S DISEASE                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.BINDA,J.WANG,L.PISANI,C.CACCIA,A.CAROTTI,P.SALVATI,D.E.EDMONDSON,   
AUTHOR   2 A.MATTEVI                                                            
REVDAT   5   13-DEC-23 2V60    1       LINK                                     
REVDAT   4   24-FEB-09 2V60    1       VERSN                                    
REVDAT   3   20-NOV-07 2V60    1       JRNL                                     
REVDAT   2   23-OCT-07 2V60    1       FORMUL LINK   HETATM CONECT              
REVDAT   1   16-OCT-07 2V60    0                                                
JRNL        AUTH   C.BINDA,J.WANG,L.PISANI,C.CACCIA,A.CAROTTI,P.SALVATI,        
JRNL        AUTH 2 D.E.EDMONDSON,A.MATTEVI                                      
JRNL        TITL   STRUCTURES OF HUMAN MONOAMINE OXIDASE B COMPLEXES WITH       
JRNL        TITL 2 SELECTIVE NONCOVALENT INHIBITORS: SAFINAMIDE AND COUMARIN    
JRNL        TITL 3 ANALOGS.                                                     
JRNL        REF    J.MED.CHEM.                   V.  50  5848 2007              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   17915852                                                     
JRNL        DOI    10.1021/JM070677Y                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 113.23                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 83205                          
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) : 0.174                           
REMARK   3   R VALUE            (WORKING SET) : 0.172                           
REMARK   3   FREE R VALUE                     : 0.221                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2206                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6056                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2350                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 158                          
REMARK   3   BIN FREE R VALUE                    : 0.3050                       
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          : 150                                     
REMARK   3   SOLVENT ATOMS            : 756                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.57                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.25000                                             
REMARK   3    B22 (A**2) : 0.57000                                              
REMARK   3    B33 (A**2) : -0.32000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.150         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.146         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.096         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.339         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.925                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8271 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11245 ; 1.554 ; 1.989       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   991 ; 6.154 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   358 ;33.078 ;23.520       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1408 ;14.295 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    58 ;16.302 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1219 ; 0.104 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6222 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3908 ; 0.199 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5546 ; 0.301 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   648 ; 0.146 ; 0.200       
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):    30 ; 0.213 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    12 ; 0.402 ; 0.200       
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):  5144 ; 1.007 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8008 ; 1.494 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3776 ; 2.577 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3237 ; 3.877 ; 4.500       
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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 4                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      3       A      99      4                      
REMARK   3           1     B      3       B      99      4                      
REMARK   3           2     A    110       A     496      4                      
REMARK   3           2     B    110       B     496      4                      
REMARK   3           3     A    600       A     600      4                      
REMARK   3           3     B    600       B     600      4                      
REMARK   3           4     A    601       A     601      4                      
REMARK   3           4     B    601       B     601      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   3932 ;  0.20 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   3932 ;  0.97 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 2V60 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JUL-07.                  
REMARK 100 THE DEPOSITION ID IS D_1290033178.                                   
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                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 85456                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.13000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1OJA                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58                     
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       65.34700            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      112.20650            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       65.34700            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      112.20650            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       65.34700            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      112.20650            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       65.34700            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      112.20650            
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: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 4810 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 44460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.2 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A1038  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B1079  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B1255  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B1257  LIES ON A SPECIAL POSITION.                          
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 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  1340     O    HOH B  1343              2.14            
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 A  1037     O    HOH A  1037     3655     1.45            
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 A 448   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG B 448   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ARG B 448   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.8 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      -70.47     66.34                                   
REMARK 500    SER A  59      -49.62   -144.78                                   
REMARK 500    THR A  64       -6.93     81.62                                   
REMARK 500    ALA A 133       66.58   -156.32                                   
REMARK 500    THR A 201      -79.59    -90.06                                   
REMARK 500    ARG A 233       74.54   -118.95                                   
REMARK 500    HIS A 252        4.22     82.29                                   
REMARK 500    ALA A 346     -121.20     52.48                                   
REMARK 500    GLU A 379       61.26   -116.70                                   
REMARK 500    SER A 394      -52.19   -121.09                                   
REMARK 500    ASP A 419     -102.38     58.66                                   
REMARK 500    ALA A 424     -150.73   -110.70                                   
REMARK 500    LYS B  52      -75.66     63.10                                   
REMARK 500    SER B  59      -49.61   -138.50                                   
REMARK 500    THR B  64       -9.24     75.31                                   
REMARK 500    ALA B 133       68.56   -158.93                                   
REMARK 500    THR B 201      -75.34    -88.15                                   
REMARK 500    ALA B 346     -125.99     52.26                                   
REMARK 500    GLU B 379       67.64   -118.54                                   
REMARK 500    ASP B 419     -104.09     62.24                                   
REMARK 500    ALA B 424     -155.13   -108.75                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A1502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C17 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 C17 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: 1OJ9   RELATED DB: PDB                                   
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH 1,4-DIPHENYL-2-BUTENE      
REMARK 900 RELATED ID: 1OJA   RELATED DB: PDB                                   
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH ISATIN                     
REMARK 900 RELATED ID: 1OJB   RELATED DB: PDB                                   
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH TRANYLCYPROMINE            
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: 1OJD   RELATED DB: PDB                                   
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH LAURYLDIMETHYLAMINE-N-     
REMARK 900 OXIDE (LDAO)                                                         
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: 1S2Y   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MAOB IN COMPLEX WITH N-PROPARGYL-1(S)-          
REMARK 900 AMINOINDAN                                                           
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: 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: 2BK3   RELATED DB: PDB                                   
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH FARNESOL                   
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: 2BYB   RELATED DB: PDB                                   
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH DEPRENYL                   
REMARK 900 RELATED ID: 2C64   RELATED DB: PDB                                   
REMARK 900 MAO INHIBITION BY RASAGILINE ANALOGUES                               
REMARK 900 RELATED ID: 2C65   RELATED DB: PDB                                   
REMARK 900 MAO INHIBITION BY RASAGILINE ANALOGUES                               
REMARK 900 RELATED ID: 2C66   RELATED DB: PDB                                   
REMARK 900 MAO INHIBITION BY RASAGILINE ANALOGUES                               
REMARK 900 RELATED ID: 2C67   RELATED DB: PDB                                   
REMARK 900 MAO INHIBITION BY RASAGILINE ANALOGUES                               
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: 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: 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: 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: 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: 2V5Z   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN MAO B IN COMPLEX WITH THE SELECTIVE INHIBITOR     
REMARK 900 SAFINAMIDE                                                           
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                  
DBREF  2V60 A    1     1  PDB    2V60     2V60             1      1             
DBREF  2V60 A    2   520  UNP    P27338   AOFB_HUMAN       1    519             
DBREF  2V60 B    1     1  PDB    2V60     2V60             1      1             
DBREF  2V60 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    C17  A1503      22                                                       
HET    FAD  B1497      53                                                       
HET    C17  B1498      22                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     C17 7-[(3-CHLOROBENZYL)OXY]-2-OXO-2H-CHROMENE-4-                     
HETNAM   2 C17  CARBALDEHYDE                                                    
FORMUL   3  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL   4  C17    2(C17 H11 CL O4)                                             
FORMUL   7  HOH   *756(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 SER A  214  GLY A  226  1                                  13    
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  LEU B  495  1                                   8    
SHEET    1  AA 5 VAL A 229  LEU A 231  0                                        
SHEET    2  AA 5 VAL A  30  GLU A  34  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  LEU B 231  0                                        
SHEET    2  BA 5 VAL B  30  GLU B  34  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  ASN B  48  0                                        
SHEET    2  BB 2 LYS B  52  ASP B  55 -1  O  LYS B  52   N  ASN B  48           
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  1.67  
LINK         SG  CYS B 397                 C8M FAD B1497     1555   1555  1.68  
CISPEP   1 ASN A  275    PRO A  276          0        -4.43                     
CISPEP   2 CYS A  397    TYR A  398          0        -8.47                     
CISPEP   3 ASN B  275    PRO B  276          0        -1.12                     
CISPEP   4 CYS B  397    TYR B  398          0         2.68                     
SITE     1 AC1 39 VAL A  10  GLY A  11  GLY A  12  GLY A  13                    
SITE     2 AC1 39 ILE A  14  SER A  15  LEU A  33  GLU A  34                    
SITE     3 AC1 39 ALA A  35  ARG A  36  GLY A  40  GLY A  41                    
SITE     4 AC1 39 ARG A  42  THR A  43  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 A1027                    
SITE     9 AC1 39 HOH A1055  HOH A1206  HOH A1347  HOH A1348                    
SITE    10 AC1 39 HOH A1349  HOH A1350  HOH A1352                               
SITE     1 AC2 13 PRO A 102  LEU A 164  LEU A 171  CYS A 172                    
SITE     2 AC2 13 ILE A 198  ILE A 199  GLN A 206  ILE A 316                    
SITE     3 AC2 13 TYR A 326  PHE A 343  TYR A 435  HOH A1159                    
SITE     4 AC2 13 HOH A1351                                                     
SITE     1 AC3 41 VAL B  10  GLY B  11  GLY B  13  ILE B  14                    
SITE     2 AC3 41 SER B  15  LEU B  33  GLU B  34  ALA B  35                    
SITE     3 AC3 41 ARG B  36  GLY B  40  GLY B  41  ARG B  42                    
SITE     4 AC3 41 THR B  43  GLY B  58  SER B  59  TYR B  60                    
SITE     5 AC3 41 ARG B 233  PRO B 234  VAL B 235  ALA B 263                    
SITE     6 AC3 41 ILE B 264  TRP B 388  TYR B 393  CYS B 397                    
SITE     7 AC3 41 TYR B 398  GLY B 425  THR B 426  GLY B 434                    
SITE     8 AC3 41 TYR B 435  MET B 436  ALA B 439  HOH B1036                    
SITE     9 AC3 41 HOH B1037  HOH B1065  HOH B1207  HOH B1228                    
SITE    10 AC3 41 HOH B1249  HOH B1401  HOH B1402  HOH B1403                    
SITE    11 AC3 41 HOH B1404                                                     
SITE     1 AC4 15 TYR B  60  PRO B 102  LEU B 164  LEU B 171                    
SITE     2 AC4 15 CYS B 172  ILE B 198  ILE B 199  GLN B 206                    
SITE     3 AC4 15 ILE B 316  TYR B 326  PHE B 343  TYR B 398                    
SITE     4 AC4 15 TYR B 435  HOH B1193  HOH B1401                               
CRYST1  130.694  224.413   86.811  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      0.007651  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004456  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011519        0.00000                         
MTRIX1   1 -0.525740 -0.495390 -0.691510      140.00504    1                    
MTRIX2   1 -0.495940 -0.481970  0.722320      210.02158    1                    
MTRIX3   1 -0.691120  0.722700  0.007710      -54.68348    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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