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Database: PDB
Entry: 2V5Z
LinkDB: 2V5Z
Original site: 2V5Z 
HEADER    OXIDOREDUCTASE                          12-JUL-07   2V5Z              
TITLE     STRUCTURE OF HUMAN MAO B IN COMPLEX WITH THE SELECTIVE INHIBITOR      
TITLE    2 SAFINAMIDE                                                           
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                                                      
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: PICHIA PASTORIS;                                  
SOURCE   7 EXPRESSION_SYSTEM_COMMON: YEAST;                                     
SOURCE   8 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   6   07-FEB-24 2V5Z    1       REMARK                                   
REVDAT   5   18-JAN-23 2V5Z    1       COMPND SOURCE JRNL   REMARK              
REVDAT   5 2                   1       DBREF  HELIX  SHEET  SITE                
REVDAT   5 3                   1       ATOM                                     
REVDAT   4   24-FEB-09 2V5Z    1       VERSN                                    
REVDAT   3   20-NOV-07 2V5Z    1       JRNL                                     
REVDAT   2   30-OCT-07 2V5Z    1       REMARK                                   
REVDAT   1   16-OCT-07 2V5Z    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.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 160119                         
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) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.227                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4192                            
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) : 1.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 11773                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.52                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2900                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 314                          
REMARK   3   BIN FREE R VALUE                    : 0.2820                       
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            : 717                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.77                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.53000                                              
REMARK   3    B22 (A**2) : -0.24000                                             
REMARK   3    B33 (A**2) : -0.29000                                             
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): 0.090         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.087         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.057         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.598         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.931                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8265 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11231 ; 1.059 ; 1.987       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   991 ; 5.202 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   358 ;33.253 ;23.520       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1408 ;12.963 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    58 ;15.588 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1221 ; 0.073 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6218 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3812 ; 0.193 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5625 ; 0.301 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   583 ; 0.096 ; 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):    54 ; 0.295 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    20 ; 0.165 ; 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):  5123 ; 0.536 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8008 ; 0.804 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3682 ; 1.366 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3223 ; 2.167 ; 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 : 3                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      3       A      99      1                      
REMARK   3           1     B      3       B      99      1                      
REMARK   3           2     A    110       A     496      1                      
REMARK   3           2     B    110       B     496      1                      
REMARK   3           3     A    600       A     600      1                      
REMARK   3           3     B    600       B     600      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   3910 ;  0.04 ;  0.05           
REMARK   3   TIGHT THERMAL      1    A (A**2):   3910 ;  0.08 ;  0.50           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2V5Z 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_1290033167.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-JUL-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 164454                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
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     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.08000                            
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) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.46600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
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: 1OJ9                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z                                         
REMARK 290       7555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       66.27550            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      111.80100            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       66.27550            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      111.80100            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       66.27550            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      111.80100            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       66.27550            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      111.80100            
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: 4770 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 44850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.4 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 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: 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      -71.37     66.90                                   
REMARK 500    SER A  59      -45.71   -142.79                                   
REMARK 500    THR A  64       -6.15     80.61                                   
REMARK 500    ALA A 133       66.77   -162.65                                   
REMARK 500    THR A 201      -80.49    -83.34                                   
REMARK 500    ALA A 346     -121.84     51.42                                   
REMARK 500    GLU A 379       62.71   -119.46                                   
REMARK 500    ASP A 419     -103.10     57.67                                   
REMARK 500    ALA A 424     -151.37   -105.53                                   
REMARK 500    LYS B  52      -72.59     65.14                                   
REMARK 500    SER B  59      -43.23   -141.84                                   
REMARK 500    THR B  64       -6.66     81.23                                   
REMARK 500    ALA B 133       67.82   -164.15                                   
REMARK 500    THR B 201      -78.09    -83.82                                   
REMARK 500    ALA B 346     -123.42     52.08                                   
REMARK 500    GLU B 379       62.70   -119.46                                   
REMARK 500    ASP B 419     -102.73     59.45                                   
REMARK 500    ALA B 424     -152.28   -105.24                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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        
DBREF  2V5Z A    1   520  UNP    P27338   AOFB_HUMAN       1    520             
DBREF  2V5Z B    1   520  UNP    P27338   AOFB_HUMAN       1    520             
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  A 600      53                                                       
HET    SAG  A 601      22                                                       
HET    FAD  B 600      53                                                       
HET    SAG  B 601      22                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     SAG (S)-(+)-2-[4-(FLUOROBENZYLOXY-BENZYLAMINO)PROPIONAMIDE]          
HETSYN     SAG SAFINAMIDE                                                       
FORMUL   3  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL   4  SAG    2(C17 H17 F N2 O2)                                           
FORMUL   7  HOH   *717(H2 O)                                                    
HELIX    1 AA1 GLY A   13  SER A   26  1                                  14    
HELIX    2 AA2 GLN A   65  LEU A   75  1                                  11    
HELIX    3 AA3 ASN A  108  ARG A  127  1                                  20    
HELIX    4 AA4 ALA A  133  ALA A  137  5                                   5    
HELIX    5 AA5 LEU A  139  ASN A  145  1                                   7    
HELIX    6 AA6 THR A  147  CYS A  156  1                                  10    
HELIX    7 AA7 THR A  158  THR A  174  1                                  17    
HELIX    8 AA8 SER A  181  GLN A  191  1                                  11    
HELIX    9 AA9 GLY A  194  SER A  200  1                                   7    
HELIX   10 AB1 SER A  214  GLY A  226  1                                  13    
HELIX   11 AB2 PRO A  265  ILE A  272  5                                   8    
HELIX   12 AB3 PRO A  279  ILE A  286  1                                   8    
HELIX   13 AB4 PRO A  304  LYS A  309  5                                   6    
HELIX   14 AB5 ALA A  346  ALA A  353  1                                   8    
HELIX   15 AB6 THR A  356  GLY A  373  1                                  18    
HELIX   16 AB7 SER A  374  GLU A  379  5                                   6    
HELIX   17 AB8 CYS A  389  GLU A  391  5                                   3    
HELIX   18 AB9 GLY A  405  GLY A  411  1                                   7    
HELIX   19 AC1 ARG A  412  LEU A  414  5                                   3    
HELIX   20 AC2 GLY A  425  ALA A  429  5                                   5    
HELIX   21 AC3 TYR A  435  MET A  454  1                                  20    
HELIX   22 AC4 PRO A  458  ILE A  462  5                                   5    
HELIX   23 AC5 THR A  480  LEU A  486  1                                   7    
HELIX   24 AC6 SER A  488  THR A  500  1                                  13    
HELIX   25 AC7 GLY B   13  SER B   26  1                                  14    
HELIX   26 AC8 GLN B   65  LEU B   75  1                                  11    
HELIX   27 AC9 ASN B  108  ARG B  127  1                                  20    
HELIX   28 AD1 ALA B  133  ALA B  137  5                                   5    
HELIX   29 AD2 LEU B  139  ASN B  145  1                                   7    
HELIX   30 AD3 THR B  147  CYS B  156  1                                  10    
HELIX   31 AD4 THR B  158  THR B  174  1                                  17    
HELIX   32 AD5 SER B  181  GLN B  191  1                                  11    
HELIX   33 AD6 GLY B  194  SER B  200  1                                   7    
HELIX   34 AD7 GLY B  215  GLY B  226  1                                  12    
HELIX   35 AD8 PRO B  265  ILE B  272  5                                   8    
HELIX   36 AD9 PRO B  279  ILE B  286  1                                   8    
HELIX   37 AE1 PRO B  304  LYS B  309  5                                   6    
HELIX   38 AE2 ALA B  346  ALA B  353  1                                   8    
HELIX   39 AE3 THR B  356  GLY B  373  1                                  18    
HELIX   40 AE4 SER B  374  GLU B  379  5                                   6    
HELIX   41 AE5 CYS B  389  GLU B  391  5                                   3    
HELIX   42 AE6 GLY B  405  GLY B  411  1                                   7    
HELIX   43 AE7 ARG B  412  LEU B  414  5                                   3    
HELIX   44 AE8 GLY B  425  ALA B  429  5                                   5    
HELIX   45 AE9 TYR B  435  MET B  454  1                                  20    
HELIX   46 AF1 PRO B  458  ILE B  462  5                                   5    
HELIX   47 AF2 THR B  480  LEU B  486  1                                   7    
HELIX   48 AF3 SER B  488  ILE B  496  1                                   9    
SHEET    1 AA1 5 VAL A 229  LEU A 231  0                                        
SHEET    2 AA1 5 VAL A  30  GLU A  34  1  N  VAL A  32   O  LYS A 230           
SHEET    3 AA1 5 VAL A   7  VAL A  10  1  N  VAL A   9   O  VAL A  31           
SHEET    4 AA1 5 TYR A 259  SER A 262  1  O  ILE A 261   N  VAL A  10           
SHEET    5 AA1 5 ILE A 421  PHE A 423  1  O  TYR A 422   N  SER A 262           
SHEET    1 AA2 2 THR A  45  LEU A  46  0                                        
SHEET    2 AA2 2 VAL A  54  ASP A  55 -1  O  VAL A  54   N  LEU A  46           
SHEET    1 AA3 3 TYR A  60  VAL A  61  0                                        
SHEET    2 AA3 3 ARG A 208  PHE A 210 -1  O  ARG A 208   N  VAL A  61           
SHEET    3 AA3 3 THR A  79  LYS A  81 -1  N  TYR A  80   O  LYS A 209           
SHEET    1 AA4 7 LYS A  95  PHE A  99  0                                        
SHEET    2 AA4 7 ARG A  87  VAL A  92 -1  N  LEU A  88   O  PHE A  99           
SHEET    3 AA4 7 TYR A 311  ILE A 317  1  O  ILE A 316   N  HIS A  91           
SHEET    4 AA4 7 TYR A 326  ASP A 329 -1  O  THR A 327   N  MET A 315           
SHEET    5 AA4 7 ALA A 339  LEU A 345 -1  O  MET A 341   N  LEU A 328           
SHEET    6 AA4 7 VAL A 294  TYR A 300 -1  N  CYS A 297   O  GLY A 342           
SHEET    7 AA4 7 HIS A 382  ASN A 387 -1  O  GLU A 384   N  ILE A 298           
SHEET    1 AA5 4 MET A 254  ALA A 257  0                                        
SHEET    2 AA5 4 VAL A 245  THR A 249 -1  N  VAL A 247   O  TYR A 255           
SHEET    3 AA5 4 VAL A 235  ASP A 239 -1  N  ASP A 239   O  LEU A 246           
SHEET    4 AA5 4 HIS A 273  ASN A 275  1  O  HIS A 273   N  ILE A 236           
SHEET    1 AA6 5 VAL B 229  LYS B 230  0                                        
SHEET    2 AA6 5 VAL B  30  LEU B  33  1  N  VAL B  32   O  LYS B 230           
SHEET    3 AA6 5 VAL B   7  VAL B  10  1  N  VAL B   9   O  VAL B  31           
SHEET    4 AA6 5 TYR B 259  SER B 262  1  O  ILE B 261   N  VAL B  10           
SHEET    5 AA6 5 ILE B 421  PHE B 423  1  O  TYR B 422   N  SER B 262           
SHEET    1 AA7 2 THR B  45  ASN B  48  0                                        
SHEET    2 AA7 2 LYS B  52  ASP B  55 -1  O  VAL B  54   N  LEU B  46           
SHEET    1 AA8 3 TYR B  60  VAL B  61  0                                        
SHEET    2 AA8 3 ARG B 208  PHE B 210 -1  O  ARG B 208   N  VAL B  61           
SHEET    3 AA8 3 THR B  79  LYS B  81 -1  N  TYR B  80   O  LYS B 209           
SHEET    1 AA9 7 LYS B  95  PHE B  99  0                                        
SHEET    2 AA9 7 ARG B  87  VAL B  92 -1  N  LEU B  88   O  PHE B  99           
SHEET    3 AA9 7 TYR B 311  ILE B 317  1  O  ILE B 316   N  HIS B  91           
SHEET    4 AA9 7 TYR B 326  ASP B 329 -1  O  THR B 327   N  MET B 315           
SHEET    5 AA9 7 ALA B 339  LEU B 345 -1  O  MET B 341   N  LEU B 328           
SHEET    6 AA9 7 VAL B 294  TYR B 300 -1  N  CYS B 297   O  GLY B 342           
SHEET    7 AA9 7 HIS B 382  ASN B 387 -1  O  GLU B 384   N  ILE B 298           
SHEET    1 AB1 4 MET B 254  ALA B 257  0                                        
SHEET    2 AB1 4 VAL B 245  THR B 249 -1  N  VAL B 247   O  TYR B 255           
SHEET    3 AB1 4 VAL B 235  ASP B 239 -1  N  TYR B 237   O  GLU B 248           
SHEET    4 AB1 4 HIS B 273  ASN B 275  1  O  HIS B 273   N  ILE B 236           
CISPEP   1 ASN A  275    PRO A  276          0        -3.44                     
CISPEP   2 CYS A  397    TYR A  398          0         0.35                     
CISPEP   3 ASN B  275    PRO B  276          0        -2.53                     
CISPEP   4 CYS B  397    TYR B  398          0         1.05                     
CRYST1  132.551  223.602   86.589  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      0.007544  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004472  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011549        0.00000                         
MTRIX1   1 -0.527350 -0.495610 -0.690120      140.46417    1                    
MTRIX2   1 -0.494970 -0.480980  0.723640      209.12799    1                    
MTRIX3   1 -0.690580  0.723210  0.008340      -54.12844    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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