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Database: PDB
Entry: 4BUR
LinkDB: 4BUR
Original site: 4BUR 
HEADER    OXIDOREDUCTASE                          23-JUN-13   4BUR              
TITLE     CRYSTAL STRUCTURE OF THE REDUCED HUMAN APOPTOSIS INDUCING             
TITLE    2 FACTOR COMPLEXED WITH NAD                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: APOPTOSIS INDUCING FACTOR 1, MITOCHONDRIAL;                
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: RESIDUES 103-613;                                          
COMPND   5 SYNONYM: PROGRAMMED CELL DEATH PROTEIN 8;                            
COMPND   6 EC: 1.-.-.-;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET28A                                     
KEYWDS    APOPTOSIS, MITOCHONDRIA, NUCLEAR CHROMATINOLYSIS, DNA-BINDING,        
KEYWDS   2 FLAVOPROTEIN, OXIDOREDUCTASE                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.MARTINEZ-JULVEZ,B.HERGUEDAS,J.A.HERMOSO,P.FERREIRA,R.VILLANUEVA,    
AUTHOR   2 M.MEDINA                                                             
REVDAT   2   16-JUL-14 4BUR    1       JRNL                                     
REVDAT   1   09-JUL-14 4BUR    0                                                
JRNL        AUTH   P.FERREIRA,R.VILLANUEVA,M.MARTINEZ-JULVEZ,B.HERGUEDAS,       
JRNL        AUTH 2 C.MARCUELLO,P.FERNANDEZ-SILVA,L.CABON,J.A.HERMOSO,A.LOSTAO,  
JRNL        AUTH 3 S.A.SUSIN,M.MEDINA                                           
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE COENZYME MEDIATED MONOMER-      
JRNL        TITL 2 DIMER TRANSITION OF THE PRO-APOPTOTIC APOPTOSIS INDUCING     
JRNL        TITL 3 FACTOR.                                                      
JRNL        REF    BIOCHEMISTRY                  V.  53  4204 2014              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   24914854                                                     
JRNL        DOI    10.1021/BI500343R                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.88 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.88                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.65                          
REMARK   3   NUMBER OF REFLECTIONS             : 61636                          
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) : 0.18014                         
REMARK   3   R VALUE            (WORKING SET) : 0.17634                         
REMARK   3   FREE R VALUE                     : 0.22973                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.2                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 4786                            
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) : 2.881                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.956                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4148                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.73                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.291                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 317                          
REMARK   3   BIN FREE R VALUE                    : 0.350                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13769                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 569                                     
REMARK   3   SOLVENT ATOMS            : 24                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.685                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.63                                                 
REMARK   3    B22 (A**2) : 1.63                                                 
REMARK   3    B33 (A**2) : -2.44                                                
REMARK   3    B12 (A**2) : 0.81                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.966         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.328         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.244         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.049        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.919                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 14668 ; 0.009 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 19933 ; 1.479 ; 2.014       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1773 ; 5.989 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   608 ;35.557 ;23.438       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2435 ;18.431 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   112 ;15.545 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2217 ; 0.100 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10906 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED 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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 6                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A   128    609       B   128    609     533  0.08  0.05     
REMARK   3    2     A   128    611       C   128    611     521  0.09  0.05     
REMARK   3    3     A   128    611       D   128    611     510  0.09  0.05     
REMARK   3    4     B   127    610       C   127    610     536  0.06  0.05     
REMARK   3    5     B   128    610       D   128    610     516  0.05  0.05     
REMARK   3    6     C   128    611       D   128    611     525  0.08  0.05     
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   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3   THE INPUT. U VALUES REFINED INDIVIDUALLY.                          
REMARK   3   RESIDUES 517-550 IN CHAIN A, 517-552 IN CHAIN B, 518-557           
REMARK   3   IN CHAIN C AND 510-558 IN CHAIN D ARE DISORDERED                   
REMARK   4                                                                      
REMARK   4 4BUR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-JUN-13.                  
REMARK 100 THE PDBE ID CODE IS EBI-57250.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-NOV-11                          
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                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97626                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AUTOPROC                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66707                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.87                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 343.36                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.6                                
REMARK 200  R MERGE                    (I) : 0.10                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.60                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.88                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.04                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7                                  
REMARK 200  R MERGE FOR SHELL          (I) : 0.47                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.40                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1M6I                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16-20% PEG 4K, 0.2 M LI2SO4 AND          
REMARK 280  0.1 M TRIS-HCL PH 8.5                                               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      228.90600            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      114.45300            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      114.45300            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      228.90600            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
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     GLY A   103                                                      
REMARK 465     LEU A   104                                                      
REMARK 465     THR A   105                                                      
REMARK 465     PRO A   106                                                      
REMARK 465     GLU A   107                                                      
REMARK 465     GLN A   108                                                      
REMARK 465     LYS A   109                                                      
REMARK 465     GLN A   110                                                      
REMARK 465     LYS A   111                                                      
REMARK 465     LYS A   112                                                      
REMARK 465     ALA A   113                                                      
REMARK 465     ALA A   114                                                      
REMARK 465     LEU A   115                                                      
REMARK 465     SER A   116                                                      
REMARK 465     ALA A   117                                                      
REMARK 465     SER A   118                                                      
REMARK 465     GLU A   119                                                      
REMARK 465     GLY A   120                                                      
REMARK 465     GLU A   121                                                      
REMARK 465     GLU A   122                                                      
REMARK 465     VAL A   123                                                      
REMARK 465     PRO A   124                                                      
REMARK 465     GLN A   125                                                      
REMARK 465     ASP A   126                                                      
REMARK 465     LYS A   127                                                      
REMARK 465     PRO A   517                                                      
REMARK 465     LYS A   518                                                      
REMARK 465     SER A   519                                                      
REMARK 465     ALA A   520                                                      
REMARK 465     THR A   521                                                      
REMARK 465     GLU A   522                                                      
REMARK 465     GLN A   523                                                      
REMARK 465     SER A   524                                                      
REMARK 465     GLY A   525                                                      
REMARK 465     THR A   526                                                      
REMARK 465     GLY A   527                                                      
REMARK 465     ILE A   528                                                      
REMARK 465     ARG A   529                                                      
REMARK 465     SER A   530                                                      
REMARK 465     GLU A   531                                                      
REMARK 465     SER A   532                                                      
REMARK 465     GLU A   533                                                      
REMARK 465     THR A   534                                                      
REMARK 465     GLU A   535                                                      
REMARK 465     SER A   536                                                      
REMARK 465     GLU A   537                                                      
REMARK 465     ALA A   538                                                      
REMARK 465     SER A   539                                                      
REMARK 465     GLU A   540                                                      
REMARK 465     ILE A   541                                                      
REMARK 465     THR A   542                                                      
REMARK 465     ILE A   543                                                      
REMARK 465     PRO A   544                                                      
REMARK 465     PRO A   545                                                      
REMARK 465     SER A   546                                                      
REMARK 465     THR A   547                                                      
REMARK 465     PRO A   548                                                      
REMARK 465     ALA A   549                                                      
REMARK 465     VAL A   550                                                      
REMARK 465     GLU A   612                                                      
REMARK 465     ASP A   613                                                      
REMARK 465     GLY B   103                                                      
REMARK 465     LEU B   104                                                      
REMARK 465     THR B   105                                                      
REMARK 465     PRO B   106                                                      
REMARK 465     GLU B   107                                                      
REMARK 465     GLN B   108                                                      
REMARK 465     LYS B   109                                                      
REMARK 465     GLN B   110                                                      
REMARK 465     LYS B   111                                                      
REMARK 465     LYS B   112                                                      
REMARK 465     ALA B   113                                                      
REMARK 465     ALA B   114                                                      
REMARK 465     LEU B   115                                                      
REMARK 465     SER B   116                                                      
REMARK 465     ALA B   117                                                      
REMARK 465     SER B   118                                                      
REMARK 465     GLU B   119                                                      
REMARK 465     GLY B   120                                                      
REMARK 465     GLU B   121                                                      
REMARK 465     GLU B   122                                                      
REMARK 465     VAL B   123                                                      
REMARK 465     PRO B   124                                                      
REMARK 465     PRO B   517                                                      
REMARK 465     LYS B   518                                                      
REMARK 465     SER B   519                                                      
REMARK 465     ALA B   520                                                      
REMARK 465     THR B   521                                                      
REMARK 465     GLU B   522                                                      
REMARK 465     GLN B   523                                                      
REMARK 465     SER B   524                                                      
REMARK 465     GLY B   525                                                      
REMARK 465     THR B   526                                                      
REMARK 465     GLY B   527                                                      
REMARK 465     ILE B   528                                                      
REMARK 465     ARG B   529                                                      
REMARK 465     SER B   530                                                      
REMARK 465     GLU B   531                                                      
REMARK 465     SER B   532                                                      
REMARK 465     GLU B   533                                                      
REMARK 465     THR B   534                                                      
REMARK 465     GLU B   535                                                      
REMARK 465     SER B   536                                                      
REMARK 465     GLU B   537                                                      
REMARK 465     ALA B   538                                                      
REMARK 465     SER B   539                                                      
REMARK 465     GLU B   540                                                      
REMARK 465     ILE B   541                                                      
REMARK 465     THR B   542                                                      
REMARK 465     ILE B   543                                                      
REMARK 465     PRO B   544                                                      
REMARK 465     PRO B   545                                                      
REMARK 465     SER B   546                                                      
REMARK 465     THR B   547                                                      
REMARK 465     PRO B   548                                                      
REMARK 465     ALA B   549                                                      
REMARK 465     VAL B   550                                                      
REMARK 465     PRO B   551                                                      
REMARK 465     GLN B   552                                                      
REMARK 465     HIS B   611                                                      
REMARK 465     GLU B   612                                                      
REMARK 465     ASP B   613                                                      
REMARK 465     GLY C   103                                                      
REMARK 465     LEU C   104                                                      
REMARK 465     THR C   105                                                      
REMARK 465     PRO C   106                                                      
REMARK 465     GLU C   107                                                      
REMARK 465     GLN C   108                                                      
REMARK 465     LYS C   109                                                      
REMARK 465     GLN C   110                                                      
REMARK 465     LYS C   111                                                      
REMARK 465     LYS C   112                                                      
REMARK 465     ALA C   113                                                      
REMARK 465     ALA C   114                                                      
REMARK 465     LEU C   115                                                      
REMARK 465     SER C   116                                                      
REMARK 465     ALA C   117                                                      
REMARK 465     SER C   118                                                      
REMARK 465     GLU C   119                                                      
REMARK 465     GLY C   120                                                      
REMARK 465     GLU C   121                                                      
REMARK 465     GLU C   122                                                      
REMARK 465     VAL C   123                                                      
REMARK 465     PRO C   124                                                      
REMARK 465     GLN C   125                                                      
REMARK 465     ASP C   126                                                      
REMARK 465     LYS C   518                                                      
REMARK 465     SER C   519                                                      
REMARK 465     ALA C   520                                                      
REMARK 465     THR C   521                                                      
REMARK 465     GLU C   522                                                      
REMARK 465     GLN C   523                                                      
REMARK 465     SER C   524                                                      
REMARK 465     GLY C   525                                                      
REMARK 465     THR C   526                                                      
REMARK 465     GLY C   527                                                      
REMARK 465     ILE C   528                                                      
REMARK 465     ARG C   529                                                      
REMARK 465     SER C   530                                                      
REMARK 465     GLU C   531                                                      
REMARK 465     SER C   532                                                      
REMARK 465     GLU C   533                                                      
REMARK 465     THR C   534                                                      
REMARK 465     GLU C   535                                                      
REMARK 465     SER C   536                                                      
REMARK 465     GLU C   537                                                      
REMARK 465     ALA C   538                                                      
REMARK 465     SER C   539                                                      
REMARK 465     GLU C   540                                                      
REMARK 465     ILE C   541                                                      
REMARK 465     THR C   542                                                      
REMARK 465     ILE C   543                                                      
REMARK 465     PRO C   544                                                      
REMARK 465     PRO C   545                                                      
REMARK 465     SER C   546                                                      
REMARK 465     THR C   547                                                      
REMARK 465     PRO C   548                                                      
REMARK 465     ALA C   549                                                      
REMARK 465     VAL C   550                                                      
REMARK 465     PRO C   551                                                      
REMARK 465     GLN C   552                                                      
REMARK 465     ALA C   553                                                      
REMARK 465     PRO C   554                                                      
REMARK 465     VAL C   555                                                      
REMARK 465     GLN C   556                                                      
REMARK 465     GLY C   557                                                      
REMARK 465     ASP C   613                                                      
REMARK 465     GLY D   103                                                      
REMARK 465     LEU D   104                                                      
REMARK 465     THR D   105                                                      
REMARK 465     PRO D   106                                                      
REMARK 465     GLU D   107                                                      
REMARK 465     GLN D   108                                                      
REMARK 465     LYS D   109                                                      
REMARK 465     GLN D   110                                                      
REMARK 465     LYS D   111                                                      
REMARK 465     LYS D   112                                                      
REMARK 465     ALA D   113                                                      
REMARK 465     ALA D   114                                                      
REMARK 465     LEU D   115                                                      
REMARK 465     SER D   116                                                      
REMARK 465     ALA D   117                                                      
REMARK 465     SER D   118                                                      
REMARK 465     GLU D   119                                                      
REMARK 465     GLY D   120                                                      
REMARK 465     GLU D   121                                                      
REMARK 465     GLU D   122                                                      
REMARK 465     VAL D   123                                                      
REMARK 465     PRO D   124                                                      
REMARK 465     GLN D   125                                                      
REMARK 465     ASP D   126                                                      
REMARK 465     LYS D   127                                                      
REMARK 465     LYS D   510                                                      
REMARK 465     ALA D   511                                                      
REMARK 465     THR D   512                                                      
REMARK 465     ALA D   513                                                      
REMARK 465     GLN D   514                                                      
REMARK 465     ASP D   515                                                      
REMARK 465     ASN D   516                                                      
REMARK 465     PRO D   517                                                      
REMARK 465     LYS D   518                                                      
REMARK 465     SER D   519                                                      
REMARK 465     ALA D   520                                                      
REMARK 465     THR D   521                                                      
REMARK 465     GLU D   522                                                      
REMARK 465     GLN D   523                                                      
REMARK 465     SER D   524                                                      
REMARK 465     GLY D   525                                                      
REMARK 465     THR D   526                                                      
REMARK 465     GLY D   527                                                      
REMARK 465     ILE D   528                                                      
REMARK 465     ARG D   529                                                      
REMARK 465     SER D   530                                                      
REMARK 465     GLU D   531                                                      
REMARK 465     SER D   532                                                      
REMARK 465     GLU D   533                                                      
REMARK 465     THR D   534                                                      
REMARK 465     GLU D   535                                                      
REMARK 465     SER D   536                                                      
REMARK 465     GLU D   537                                                      
REMARK 465     ALA D   538                                                      
REMARK 465     SER D   539                                                      
REMARK 465     GLU D   540                                                      
REMARK 465     ILE D   541                                                      
REMARK 465     THR D   542                                                      
REMARK 465     ILE D   543                                                      
REMARK 465     PRO D   544                                                      
REMARK 465     PRO D   545                                                      
REMARK 465     SER D   546                                                      
REMARK 465     THR D   547                                                      
REMARK 465     PRO D   548                                                      
REMARK 465     ALA D   549                                                      
REMARK 465     VAL D   550                                                      
REMARK 465     PRO D   551                                                      
REMARK 465     GLN D   552                                                      
REMARK 465     ALA D   553                                                      
REMARK 465     PRO D   554                                                      
REMARK 465     VAL D   555                                                      
REMARK 465     GLN D   556                                                      
REMARK 465     GLY D   557                                                      
REMARK 465     GLU D   558                                                      
REMARK 465     GLU D   612                                                      
REMARK 465     ASP D   613                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 199    CG   CD   CE   NZ                                   
REMARK 470     GLN B 125    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 199    CG   CD   CE   NZ                                   
REMARK 470     LYS C 199    CG   CD   CE   NZ                                   
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    LEU C 400   CA  -  CB  -  CG  ANGL. DEV. =  16.0 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    PRO A 169      126.95    -39.03                                   
REMARK 500    LYS A 177     -101.78   -124.92                                   
REMARK 500    ASN A 197       63.83   -111.12                                   
REMARK 500    SER A 209       12.06    -65.22                                   
REMARK 500    ILE A 220      123.48    -39.04                                   
REMARK 500    ASN A 222       -9.27     86.20                                   
REMARK 500    ASN A 241       54.59     32.04                                   
REMARK 500    ALA A 259       56.64   -142.29                                   
REMARK 500    ARG A 285      -32.74   -149.29                                   
REMARK 500    SER A 376       64.77     28.27                                   
REMARK 500    ASN A 424     -167.19    -77.59                                   
REMARK 500    ALA A 429      -62.00    -98.22                                   
REMARK 500    GLU A 453       61.12   -115.90                                   
REMARK 500    TRP A 477      -55.69   -144.76                                   
REMARK 500    LYS A 510      -77.26   -110.34                                   
REMARK 500    ASP A 570     -130.11     59.84                                   
REMARK 500    ASN A 609       53.16     70.44                                   
REMARK 500    ASP B 154       90.47   -177.74                                   
REMARK 500    LYS B 177      -98.95   -130.51                                   
REMARK 500    ASN B 197     -145.88    -63.18                                   
REMARK 500    PHE B 210      -25.89   -150.67                                   
REMARK 500    ASN B 222       -4.11     88.75                                   
REMARK 500    ASN B 241       55.40     39.18                                   
REMARK 500    ALA B 275      -70.83    -13.12                                   
REMARK 500    ARG B 285      -34.88   -162.94                                   
REMARK 500    SER B 376       63.75     27.84                                   
REMARK 500    GLU B 453       55.79   -113.23                                   
REMARK 500    TRP B 477      -54.89   -135.75                                   
REMARK 500    THR B 512       57.97   -143.72                                   
REMARK 500    ASP B 570     -146.53     71.12                                   
REMARK 500    ASN B 609       61.52     69.38                                   
REMARK 500    LYS C 177     -104.79   -140.02                                   
REMARK 500    ARG C 285      -38.74   -157.49                                   
REMARK 500    SER C 376       60.31     31.42                                   
REMARK 500    ASN C 424     -168.38    -77.75                                   
REMARK 500    ASN C 432       -2.20     69.20                                   
REMARK 500    GLU C 453       67.87   -105.31                                   
REMARK 500    TRP C 477      -56.06   -151.05                                   
REMARK 500    ALA C 513       95.70    -48.98                                   
REMARK 500    TYR C 560       48.89    -96.25                                   
REMARK 500    ASP C 570     -129.56     59.13                                   
REMARK 500    PRO D 129     -172.49    -67.24                                   
REMARK 500    LYS D 177     -105.23   -131.19                                   
REMARK 500    ALA D 273     -148.44    -70.39                                   
REMARK 500    ALA D 275     -121.79     61.63                                   
REMARK 500    LEU D 283       70.96   -104.12                                   
REMARK 500    ARG D 285      -39.26   -150.40                                   
REMARK 500    LEU D 326       36.15    -97.03                                   
REMARK 500    THR D 328     -157.71    -88.13                                   
REMARK 500    ALA D 397       79.58   -103.06                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      54 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    GLU A 299        23.8      L          L   OUTSIDE RANGE           
REMARK 500    LEU A 400        23.9      L          L   OUTSIDE RANGE           
REMARK 500    LEU C 400        23.8      L          L   OUTSIDE RANGE           
REMARK 500    ILE C 433        22.7      L          L   OUTSIDE RANGE           
REMARK 500    ILE D 433        25.0      L          L   OUTSIDE RANGE           
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 NAD A 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD C 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD C 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD D 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD D 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A1612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B1612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD D1612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD C1612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D1613                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4BV6   RELATED DB: PDB                                   
REMARK 900  REFINED CRYSTAL STRUCTURE OF THE HUMAN APOPTOSIS                    
REMARK 900  INDUCING FACTOR                                                     
DBREF  4BUR A  103   613  UNP    O95831   AIFM1_HUMAN    103    613             
DBREF  4BUR B  103   613  UNP    O95831   AIFM1_HUMAN    103    613             
DBREF  4BUR C  103   613  UNP    O95831   AIFM1_HUMAN    103    613             
DBREF  4BUR D  103   613  UNP    O95831   AIFM1_HUMAN    103    613             
SEQRES   1 A  511  GLY LEU THR PRO GLU GLN LYS GLN LYS LYS ALA ALA LEU          
SEQRES   2 A  511  SER ALA SER GLU GLY GLU GLU VAL PRO GLN ASP LYS ALA          
SEQRES   3 A  511  PRO SER HIS VAL PRO PHE LEU LEU ILE GLY GLY GLY THR          
SEQRES   4 A  511  ALA ALA PHE ALA ALA ALA ARG SER ILE ARG ALA ARG ASP          
SEQRES   5 A  511  PRO GLY ALA ARG VAL LEU ILE VAL SER GLU ASP PRO GLU          
SEQRES   6 A  511  LEU PRO TYR MET ARG PRO PRO LEU SER LYS GLU LEU TRP          
SEQRES   7 A  511  PHE SER ASP ASP PRO ASN VAL THR LYS THR LEU ARG PHE          
SEQRES   8 A  511  LYS GLN TRP ASN GLY LYS GLU ARG SER ILE TYR PHE GLN          
SEQRES   9 A  511  PRO PRO SER PHE TYR VAL SER ALA GLN ASP LEU PRO HIS          
SEQRES  10 A  511  ILE GLU ASN GLY GLY VAL ALA VAL LEU THR GLY LYS LYS          
SEQRES  11 A  511  VAL VAL GLN LEU ASP VAL ARG ASP ASN MET VAL LYS LEU          
SEQRES  12 A  511  ASN ASP GLY SER GLN ILE THR TYR GLU LYS CYS LEU ILE          
SEQRES  13 A  511  ALA THR GLY GLY THR PRO ARG SER LEU SER ALA ILE ASP          
SEQRES  14 A  511  ARG ALA GLY ALA GLU VAL LYS SER ARG THR THR LEU PHE          
SEQRES  15 A  511  ARG LYS ILE GLY ASP PHE ARG SER LEU GLU LYS ILE SER          
SEQRES  16 A  511  ARG GLU VAL LYS SER ILE THR ILE ILE GLY GLY GLY PHE          
SEQRES  17 A  511  LEU GLY SER GLU LEU ALA CYS ALA LEU GLY ARG LYS ALA          
SEQRES  18 A  511  ARG ALA LEU GLY THR GLU VAL ILE GLN LEU PHE PRO GLU          
SEQRES  19 A  511  LYS GLY ASN MET GLY LYS ILE LEU PRO GLU TYR LEU SER          
SEQRES  20 A  511  ASN TRP THR MET GLU LYS VAL ARG ARG GLU GLY VAL LYS          
SEQRES  21 A  511  VAL MET PRO ASN ALA ILE VAL GLN SER VAL GLY VAL SER          
SEQRES  22 A  511  SER GLY LYS LEU LEU ILE LYS LEU LYS ASP GLY ARG LYS          
SEQRES  23 A  511  VAL GLU THR ASP HIS ILE VAL ALA ALA VAL GLY LEU GLU          
SEQRES  24 A  511  PRO ASN VAL GLU LEU ALA LYS THR GLY GLY LEU GLU ILE          
SEQRES  25 A  511  ASP SER ASP PHE GLY GLY PHE ARG VAL ASN ALA GLU LEU          
SEQRES  26 A  511  GLN ALA ARG SER ASN ILE TRP VAL ALA GLY ASP ALA ALA          
SEQRES  27 A  511  CYS PHE TYR ASP ILE LYS LEU GLY ARG ARG ARG VAL GLU          
SEQRES  28 A  511  HIS HIS ASP HIS ALA VAL VAL SER GLY ARG LEU ALA GLY          
SEQRES  29 A  511  GLU ASN MET THR GLY ALA ALA LYS PRO TYR TRP HIS GLN          
SEQRES  30 A  511  SER MET PHE TRP SER ASP LEU GLY PRO ASP VAL GLY TYR          
SEQRES  31 A  511  GLU ALA ILE GLY LEU VAL ASP SER SER LEU PRO THR VAL          
SEQRES  32 A  511  GLY VAL PHE ALA LYS ALA THR ALA GLN ASP ASN PRO LYS          
SEQRES  33 A  511  SER ALA THR GLU GLN SER GLY THR GLY ILE ARG SER GLU          
SEQRES  34 A  511  SER GLU THR GLU SER GLU ALA SER GLU ILE THR ILE PRO          
SEQRES  35 A  511  PRO SER THR PRO ALA VAL PRO GLN ALA PRO VAL GLN GLY          
SEQRES  36 A  511  GLU ASP TYR GLY LYS GLY VAL ILE PHE TYR LEU ARG ASP          
SEQRES  37 A  511  LYS VAL VAL VAL GLY ILE VAL LEU TRP ASN ILE PHE ASN          
SEQRES  38 A  511  ARG MET PRO ILE ALA ARG LYS ILE ILE LYS ASP GLY GLU          
SEQRES  39 A  511  GLN HIS GLU ASP LEU ASN GLU VAL ALA LYS LEU PHE ASN          
SEQRES  40 A  511  ILE HIS GLU ASP                                              
SEQRES   1 B  511  GLY LEU THR PRO GLU GLN LYS GLN LYS LYS ALA ALA LEU          
SEQRES   2 B  511  SER ALA SER GLU GLY GLU GLU VAL PRO GLN ASP LYS ALA          
SEQRES   3 B  511  PRO SER HIS VAL PRO PHE LEU LEU ILE GLY GLY GLY THR          
SEQRES   4 B  511  ALA ALA PHE ALA ALA ALA ARG SER ILE ARG ALA ARG ASP          
SEQRES   5 B  511  PRO GLY ALA ARG VAL LEU ILE VAL SER GLU ASP PRO GLU          
SEQRES   6 B  511  LEU PRO TYR MET ARG PRO PRO LEU SER LYS GLU LEU TRP          
SEQRES   7 B  511  PHE SER ASP ASP PRO ASN VAL THR LYS THR LEU ARG PHE          
SEQRES   8 B  511  LYS GLN TRP ASN GLY LYS GLU ARG SER ILE TYR PHE GLN          
SEQRES   9 B  511  PRO PRO SER PHE TYR VAL SER ALA GLN ASP LEU PRO HIS          
SEQRES  10 B  511  ILE GLU ASN GLY GLY VAL ALA VAL LEU THR GLY LYS LYS          
SEQRES  11 B  511  VAL VAL GLN LEU ASP VAL ARG ASP ASN MET VAL LYS LEU          
SEQRES  12 B  511  ASN ASP GLY SER GLN ILE THR TYR GLU LYS CYS LEU ILE          
SEQRES  13 B  511  ALA THR GLY GLY THR PRO ARG SER LEU SER ALA ILE ASP          
SEQRES  14 B  511  ARG ALA GLY ALA GLU VAL LYS SER ARG THR THR LEU PHE          
SEQRES  15 B  511  ARG LYS ILE GLY ASP PHE ARG SER LEU GLU LYS ILE SER          
SEQRES  16 B  511  ARG GLU VAL LYS SER ILE THR ILE ILE GLY GLY GLY PHE          
SEQRES  17 B  511  LEU GLY SER GLU LEU ALA CYS ALA LEU GLY ARG LYS ALA          
SEQRES  18 B  511  ARG ALA LEU GLY THR GLU VAL ILE GLN LEU PHE PRO GLU          
SEQRES  19 B  511  LYS GLY ASN MET GLY LYS ILE LEU PRO GLU TYR LEU SER          
SEQRES  20 B  511  ASN TRP THR MET GLU LYS VAL ARG ARG GLU GLY VAL LYS          
SEQRES  21 B  511  VAL MET PRO ASN ALA ILE VAL GLN SER VAL GLY VAL SER          
SEQRES  22 B  511  SER GLY LYS LEU LEU ILE LYS LEU LYS ASP GLY ARG LYS          
SEQRES  23 B  511  VAL GLU THR ASP HIS ILE VAL ALA ALA VAL GLY LEU GLU          
SEQRES  24 B  511  PRO ASN VAL GLU LEU ALA LYS THR GLY GLY LEU GLU ILE          
SEQRES  25 B  511  ASP SER ASP PHE GLY GLY PHE ARG VAL ASN ALA GLU LEU          
SEQRES  26 B  511  GLN ALA ARG SER ASN ILE TRP VAL ALA GLY ASP ALA ALA          
SEQRES  27 B  511  CYS PHE TYR ASP ILE LYS LEU GLY ARG ARG ARG VAL GLU          
SEQRES  28 B  511  HIS HIS ASP HIS ALA VAL VAL SER GLY ARG LEU ALA GLY          
SEQRES  29 B  511  GLU ASN MET THR GLY ALA ALA LYS PRO TYR TRP HIS GLN          
SEQRES  30 B  511  SER MET PHE TRP SER ASP LEU GLY PRO ASP VAL GLY TYR          
SEQRES  31 B  511  GLU ALA ILE GLY LEU VAL ASP SER SER LEU PRO THR VAL          
SEQRES  32 B  511  GLY VAL PHE ALA LYS ALA THR ALA GLN ASP ASN PRO LYS          
SEQRES  33 B  511  SER ALA THR GLU GLN SER GLY THR GLY ILE ARG SER GLU          
SEQRES  34 B  511  SER GLU THR GLU SER GLU ALA SER GLU ILE THR ILE PRO          
SEQRES  35 B  511  PRO SER THR PRO ALA VAL PRO GLN ALA PRO VAL GLN GLY          
SEQRES  36 B  511  GLU ASP TYR GLY LYS GLY VAL ILE PHE TYR LEU ARG ASP          
SEQRES  37 B  511  LYS VAL VAL VAL GLY ILE VAL LEU TRP ASN ILE PHE ASN          
SEQRES  38 B  511  ARG MET PRO ILE ALA ARG LYS ILE ILE LYS ASP GLY GLU          
SEQRES  39 B  511  GLN HIS GLU ASP LEU ASN GLU VAL ALA LYS LEU PHE ASN          
SEQRES  40 B  511  ILE HIS GLU ASP                                              
SEQRES   1 C  511  GLY LEU THR PRO GLU GLN LYS GLN LYS LYS ALA ALA LEU          
SEQRES   2 C  511  SER ALA SER GLU GLY GLU GLU VAL PRO GLN ASP LYS ALA          
SEQRES   3 C  511  PRO SER HIS VAL PRO PHE LEU LEU ILE GLY GLY GLY THR          
SEQRES   4 C  511  ALA ALA PHE ALA ALA ALA ARG SER ILE ARG ALA ARG ASP          
SEQRES   5 C  511  PRO GLY ALA ARG VAL LEU ILE VAL SER GLU ASP PRO GLU          
SEQRES   6 C  511  LEU PRO TYR MET ARG PRO PRO LEU SER LYS GLU LEU TRP          
SEQRES   7 C  511  PHE SER ASP ASP PRO ASN VAL THR LYS THR LEU ARG PHE          
SEQRES   8 C  511  LYS GLN TRP ASN GLY LYS GLU ARG SER ILE TYR PHE GLN          
SEQRES   9 C  511  PRO PRO SER PHE TYR VAL SER ALA GLN ASP LEU PRO HIS          
SEQRES  10 C  511  ILE GLU ASN GLY GLY VAL ALA VAL LEU THR GLY LYS LYS          
SEQRES  11 C  511  VAL VAL GLN LEU ASP VAL ARG ASP ASN MET VAL LYS LEU          
SEQRES  12 C  511  ASN ASP GLY SER GLN ILE THR TYR GLU LYS CYS LEU ILE          
SEQRES  13 C  511  ALA THR GLY GLY THR PRO ARG SER LEU SER ALA ILE ASP          
SEQRES  14 C  511  ARG ALA GLY ALA GLU VAL LYS SER ARG THR THR LEU PHE          
SEQRES  15 C  511  ARG LYS ILE GLY ASP PHE ARG SER LEU GLU LYS ILE SER          
SEQRES  16 C  511  ARG GLU VAL LYS SER ILE THR ILE ILE GLY GLY GLY PHE          
SEQRES  17 C  511  LEU GLY SER GLU LEU ALA CYS ALA LEU GLY ARG LYS ALA          
SEQRES  18 C  511  ARG ALA LEU GLY THR GLU VAL ILE GLN LEU PHE PRO GLU          
SEQRES  19 C  511  LYS GLY ASN MET GLY LYS ILE LEU PRO GLU TYR LEU SER          
SEQRES  20 C  511  ASN TRP THR MET GLU LYS VAL ARG ARG GLU GLY VAL LYS          
SEQRES  21 C  511  VAL MET PRO ASN ALA ILE VAL GLN SER VAL GLY VAL SER          
SEQRES  22 C  511  SER GLY LYS LEU LEU ILE LYS LEU LYS ASP GLY ARG LYS          
SEQRES  23 C  511  VAL GLU THR ASP HIS ILE VAL ALA ALA VAL GLY LEU GLU          
SEQRES  24 C  511  PRO ASN VAL GLU LEU ALA LYS THR GLY GLY LEU GLU ILE          
SEQRES  25 C  511  ASP SER ASP PHE GLY GLY PHE ARG VAL ASN ALA GLU LEU          
SEQRES  26 C  511  GLN ALA ARG SER ASN ILE TRP VAL ALA GLY ASP ALA ALA          
SEQRES  27 C  511  CYS PHE TYR ASP ILE LYS LEU GLY ARG ARG ARG VAL GLU          
SEQRES  28 C  511  HIS HIS ASP HIS ALA VAL VAL SER GLY ARG LEU ALA GLY          
SEQRES  29 C  511  GLU ASN MET THR GLY ALA ALA LYS PRO TYR TRP HIS GLN          
SEQRES  30 C  511  SER MET PHE TRP SER ASP LEU GLY PRO ASP VAL GLY TYR          
SEQRES  31 C  511  GLU ALA ILE GLY LEU VAL ASP SER SER LEU PRO THR VAL          
SEQRES  32 C  511  GLY VAL PHE ALA LYS ALA THR ALA GLN ASP ASN PRO LYS          
SEQRES  33 C  511  SER ALA THR GLU GLN SER GLY THR GLY ILE ARG SER GLU          
SEQRES  34 C  511  SER GLU THR GLU SER GLU ALA SER GLU ILE THR ILE PRO          
SEQRES  35 C  511  PRO SER THR PRO ALA VAL PRO GLN ALA PRO VAL GLN GLY          
SEQRES  36 C  511  GLU ASP TYR GLY LYS GLY VAL ILE PHE TYR LEU ARG ASP          
SEQRES  37 C  511  LYS VAL VAL VAL GLY ILE VAL LEU TRP ASN ILE PHE ASN          
SEQRES  38 C  511  ARG MET PRO ILE ALA ARG LYS ILE ILE LYS ASP GLY GLU          
SEQRES  39 C  511  GLN HIS GLU ASP LEU ASN GLU VAL ALA LYS LEU PHE ASN          
SEQRES  40 C  511  ILE HIS GLU ASP                                              
SEQRES   1 D  511  GLY LEU THR PRO GLU GLN LYS GLN LYS LYS ALA ALA LEU          
SEQRES   2 D  511  SER ALA SER GLU GLY GLU GLU VAL PRO GLN ASP LYS ALA          
SEQRES   3 D  511  PRO SER HIS VAL PRO PHE LEU LEU ILE GLY GLY GLY THR          
SEQRES   4 D  511  ALA ALA PHE ALA ALA ALA ARG SER ILE ARG ALA ARG ASP          
SEQRES   5 D  511  PRO GLY ALA ARG VAL LEU ILE VAL SER GLU ASP PRO GLU          
SEQRES   6 D  511  LEU PRO TYR MET ARG PRO PRO LEU SER LYS GLU LEU TRP          
SEQRES   7 D  511  PHE SER ASP ASP PRO ASN VAL THR LYS THR LEU ARG PHE          
SEQRES   8 D  511  LYS GLN TRP ASN GLY LYS GLU ARG SER ILE TYR PHE GLN          
SEQRES   9 D  511  PRO PRO SER PHE TYR VAL SER ALA GLN ASP LEU PRO HIS          
SEQRES  10 D  511  ILE GLU ASN GLY GLY VAL ALA VAL LEU THR GLY LYS LYS          
SEQRES  11 D  511  VAL VAL GLN LEU ASP VAL ARG ASP ASN MET VAL LYS LEU          
SEQRES  12 D  511  ASN ASP GLY SER GLN ILE THR TYR GLU LYS CYS LEU ILE          
SEQRES  13 D  511  ALA THR GLY GLY THR PRO ARG SER LEU SER ALA ILE ASP          
SEQRES  14 D  511  ARG ALA GLY ALA GLU VAL LYS SER ARG THR THR LEU PHE          
SEQRES  15 D  511  ARG LYS ILE GLY ASP PHE ARG SER LEU GLU LYS ILE SER          
SEQRES  16 D  511  ARG GLU VAL LYS SER ILE THR ILE ILE GLY GLY GLY PHE          
SEQRES  17 D  511  LEU GLY SER GLU LEU ALA CYS ALA LEU GLY ARG LYS ALA          
SEQRES  18 D  511  ARG ALA LEU GLY THR GLU VAL ILE GLN LEU PHE PRO GLU          
SEQRES  19 D  511  LYS GLY ASN MET GLY LYS ILE LEU PRO GLU TYR LEU SER          
SEQRES  20 D  511  ASN TRP THR MET GLU LYS VAL ARG ARG GLU GLY VAL LYS          
SEQRES  21 D  511  VAL MET PRO ASN ALA ILE VAL GLN SER VAL GLY VAL SER          
SEQRES  22 D  511  SER GLY LYS LEU LEU ILE LYS LEU LYS ASP GLY ARG LYS          
SEQRES  23 D  511  VAL GLU THR ASP HIS ILE VAL ALA ALA VAL GLY LEU GLU          
SEQRES  24 D  511  PRO ASN VAL GLU LEU ALA LYS THR GLY GLY LEU GLU ILE          
SEQRES  25 D  511  ASP SER ASP PHE GLY GLY PHE ARG VAL ASN ALA GLU LEU          
SEQRES  26 D  511  GLN ALA ARG SER ASN ILE TRP VAL ALA GLY ASP ALA ALA          
SEQRES  27 D  511  CYS PHE TYR ASP ILE LYS LEU GLY ARG ARG ARG VAL GLU          
SEQRES  28 D  511  HIS HIS ASP HIS ALA VAL VAL SER GLY ARG LEU ALA GLY          
SEQRES  29 D  511  GLU ASN MET THR GLY ALA ALA LYS PRO TYR TRP HIS GLN          
SEQRES  30 D  511  SER MET PHE TRP SER ASP LEU GLY PRO ASP VAL GLY TYR          
SEQRES  31 D  511  GLU ALA ILE GLY LEU VAL ASP SER SER LEU PRO THR VAL          
SEQRES  32 D  511  GLY VAL PHE ALA LYS ALA THR ALA GLN ASP ASN PRO LYS          
SEQRES  33 D  511  SER ALA THR GLU GLN SER GLY THR GLY ILE ARG SER GLU          
SEQRES  34 D  511  SER GLU THR GLU SER GLU ALA SER GLU ILE THR ILE PRO          
SEQRES  35 D  511  PRO SER THR PRO ALA VAL PRO GLN ALA PRO VAL GLN GLY          
SEQRES  36 D  511  GLU ASP TYR GLY LYS GLY VAL ILE PHE TYR LEU ARG ASP          
SEQRES  37 D  511  LYS VAL VAL VAL GLY ILE VAL LEU TRP ASN ILE PHE ASN          
SEQRES  38 D  511  ARG MET PRO ILE ALA ARG LYS ILE ILE LYS ASP GLY GLU          
SEQRES  39 D  511  GLN HIS GLU ASP LEU ASN GLU VAL ALA LYS LEU PHE ASN          
SEQRES  40 D  511  ILE HIS GLU ASP                                              
HET    NAD  A 700      44                                                       
HET    NAD  A 701      44                                                       
HET    NAD  B 700      44                                                       
HET    NAD  B 701      44                                                       
HET    NAD  C 700      44                                                       
HET    NAD  C 701      44                                                       
HET    NAD  D 700      44                                                       
HET    NAD  D 701      44                                                       
HET    FAD  A1612      53                                                       
HET    FAD  B1612      53                                                       
HET    FAD  D1612      53                                                       
HET    FAD  C1612      53                                                       
HET    SO4  D1613       5                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2  FAD    4(C27 H33 N9 O15 P2)                                         
FORMUL   3  NAD    8(C21 H27 N7 O14 P2)                                         
FORMUL   4  SO4    O4 S 2-                                                      
FORMUL   5  HOH   *24(H2 O)                                                     
HELIX    1   1 GLY A  140  ASP A  154  1                                  15    
HELIX    2   2 ARG A  172  SER A  176  5                                   5    
HELIX    3   3 LYS A  177  PHE A  181  5                                   5    
HELIX    4   4 ASN A  186  LEU A  191  1                                   6    
HELIX    5   5 PRO A  207  TYR A  211  5                                   5    
HELIX    6   6 LEU A  267  ARG A  272  1                                   6    
HELIX    7   7 GLY A  274  SER A  279  1                                   6    
HELIX    8   8 LYS A  286  VAL A  300  1                                  15    
HELIX    9   9 GLY A  309  GLY A  327  1                                  19    
HELIX   10  10 PRO A  345  ARG A  358  1                                  14    
HELIX   11  11 LEU A  406  GLY A  411  1                                   6    
HELIX   12  12 HIS A  454  THR A  470  1                                  17    
HELIX   13  13 ARG A  584  GLY A  595  1                                  12    
HELIX   14  14 ASP A  600  LEU A  607  1                                   8    
HELIX   15  15 GLY B  140  ARG B  153  1                                  14    
HELIX   16  16 ARG B  172  SER B  176  5                                   5    
HELIX   17  17 ASN B  186  LEU B  191  1                                   6    
HELIX   18  18 LEU B  267  ARG B  272  1                                   6    
HELIX   19  19 GLY B  274  SER B  279  1                                   6    
HELIX   20  20 LYS B  286  VAL B  300  1                                  15    
HELIX   21  21 GLY B  309  GLY B  327  1                                  19    
HELIX   22  22 PRO B  345  GLU B  359  1                                  15    
HELIX   23  23 GLU B  405  GLY B  411  1                                   7    
HELIX   24  24 HIS B  454  THR B  470  1                                  17    
HELIX   25  25 ARG B  584  GLY B  595  1                                  12    
HELIX   26  26 ASP B  600  LEU B  607  1                                   8    
HELIX   27  27 GLY C  140  ASP C  154  1                                  15    
HELIX   28  28 ARG C  172  LYS C  177  5                                   6    
HELIX   29  29 ASN C  186  LEU C  191  1                                   6    
HELIX   30  30 PRO C  207  TYR C  211  5                                   5    
HELIX   31  31 VAL C  238  ASP C  240  5                                   3    
HELIX   32  32 LEU C  267  ARG C  272  1                                   6    
HELIX   33  33 GLY C  274  SER C  279  1                                   6    
HELIX   34  34 LYS C  286  VAL C  300  1                                  15    
HELIX   35  35 GLY C  309  LEU C  326  1                                  18    
HELIX   36  36 PRO C  345  ARG C  358  1                                  14    
HELIX   37  37 LEU C  406  GLY C  411  1                                   6    
HELIX   38  38 HIS C  454  THR C  470  1                                  17    
HELIX   39  39 ARG C  584  GLY C  595  1                                  12    
HELIX   40  40 ASP C  600  ALA C  605  1                                   6    
HELIX   41  41 LYS C  606  ASN C  609  5                                   4    
HELIX   42  42 GLY D  140  ASP D  154  1                                  15    
HELIX   43  43 ARG D  172  LYS D  177  5                                   6    
HELIX   44  44 ASN D  186  LEU D  191  1                                   6    
HELIX   45  45 PRO D  207  TYR D  211  5                                   5    
HELIX   46  46 LEU D  267  ALA D  273  1                                   7    
HELIX   47  47 VAL D  277  SER D  279  5                                   3    
HELIX   48  48 LYS D  286  ARG D  298  1                                  13    
HELIX   49  49 GLY D  309  LEU D  326  1                                  18    
HELIX   50  50 PRO D  345  ARG D  358  1                                  14    
HELIX   51  51 LEU D  406  GLY D  411  1                                   6    
HELIX   52  52 HIS D  454  THR D  470  1                                  17    
HELIX   53  53 ARG D  584  GLY D  595  1                                  12    
HELIX   54  54 ASP D  600  ALA D  605  1                                   6    
SHEET    1  AA 6 GLY A 224  THR A 229  0                                        
SHEET    2  AA 6 ARG A 158  SER A 163  1  O  VAL A 159   N  ALA A 226           
SHEET    3  AA 6 HIS A 131  ILE A 137  1  O  PHE A 134   N  LEU A 160           
SHEET    4  AA 6 GLN A 250  ILE A 258  1  O  THR A 252   N  VAL A 132           
SHEET    5  AA 6 ILE A 433  VAL A 435  1  O  TRP A 434   N  ILE A 258           
SHEET    6  AA 6 GLN A 428  ARG A 430 -1  N  ALA A 429   O  ILE A 433           
SHEET    1  AB 6 GLY A 224  THR A 229  0                                        
SHEET    2  AB 6 ARG A 158  SER A 163  1  O  VAL A 159   N  ALA A 226           
SHEET    3  AB 6 HIS A 131  ILE A 137  1  O  PHE A 134   N  LEU A 160           
SHEET    4  AB 6 GLN A 250  ILE A 258  1  O  THR A 252   N  VAL A 132           
SHEET    5  AB 6 MET A 242  LEU A 245 -1  O  VAL A 243   N  ILE A 251           
SHEET    6  AB 6 VAL A 233  ASP A 237  1  N  VAL A 234   O  LYS A 244           
SHEET    1  AC 2 ARG A 192  LYS A 194  0                                        
SHEET    2  AC 2 GLU A 200  SER A 202 -1  O  ARG A 201   N  PHE A 193           
SHEET    1  AD 2 GLY A 262  PRO A 264  0                                        
SHEET    2  AD 2 LEU A 400  PRO A 402 -1  O  GLU A 401   N  THR A 263           
SHEET    1  AE 5 THR A 281  THR A 282  0                                        
SHEET    2  AE 5 HIS A 393  ALA A 396  1  O  ILE A 394   N  THR A 282           
SHEET    3  AE 5 SER A 302  ILE A 306  1  O  THR A 304   N  VAL A 395           
SHEET    4  AE 5 GLU A 329  LEU A 333  1  O  GLU A 329   N  ILE A 303           
SHEET    5  AE 5 LYS A 362  MET A 364  1  O  LYS A 362   N  GLN A 332           
SHEET    1  AF 3 VAL A 369  SER A 375  0                                        
SHEET    2  AF 3 LYS A 378  LEU A 383 -1  O  LYS A 378   N  SER A 375           
SHEET    3  AF 3 LYS A 388  THR A 391 -1  O  VAL A 389   N  ILE A 381           
SHEET    1  AG 3 PHE A 421  ARG A 422  0                                        
SHEET    2  AG 3 ALA A 440  ASP A 444  1  N  CYS A 441   O  PHE A 421           
SHEET    3  AG 3 GLY A 448  ARG A 451 -1  O  GLY A 448   N  ASP A 444           
SHEET    1  AH 6 MET A 481  LEU A 486  0                                        
SHEET    2  AH 6 VAL A 490  GLY A 496 -1  O  VAL A 490   N  LEU A 486           
SHEET    3  AH 6 VAL A 572  TRP A 579 -1  O  ILE A 576   N  ILE A 495           
SHEET    4  AH 6 GLY A 563  ARG A 569 -1  O  GLY A 563   N  TRP A 579           
SHEET    5  AH 6 THR A 504  PHE A 508 -1  O  VAL A 505   N  PHE A 566           
SHEET    6  AH 6 GLN A 514  ASP A 515 -1  O  ASP A 515   N  THR A 504           
SHEET    1  BA 6 GLY B 224  THR B 229  0                                        
SHEET    2  BA 6 ARG B 158  SER B 163  1  O  VAL B 159   N  ALA B 226           
SHEET    3  BA 6 HIS B 131  ILE B 137  1  O  PHE B 134   N  LEU B 160           
SHEET    4  BA 6 GLN B 250  ILE B 258  1  O  THR B 252   N  VAL B 132           
SHEET    5  BA 6 ILE B 433  VAL B 435  1  O  TRP B 434   N  ILE B 258           
SHEET    6  BA 6 GLN B 428  ARG B 430 -1  N  ALA B 429   O  ILE B 433           
SHEET    1  BB 6 GLY B 224  THR B 229  0                                        
SHEET    2  BB 6 ARG B 158  SER B 163  1  O  VAL B 159   N  ALA B 226           
SHEET    3  BB 6 HIS B 131  ILE B 137  1  O  PHE B 134   N  LEU B 160           
SHEET    4  BB 6 GLN B 250  ILE B 258  1  O  THR B 252   N  VAL B 132           
SHEET    5  BB 6 MET B 242  LEU B 245 -1  O  VAL B 243   N  ILE B 251           
SHEET    6  BB 6 VAL B 233  ASP B 237  1  N  VAL B 234   O  LYS B 244           
SHEET    1  BC 2 ARG B 192  LYS B 194  0                                        
SHEET    2  BC 2 GLU B 200  SER B 202 -1  O  ARG B 201   N  PHE B 193           
SHEET    1  BD 2 GLY B 262  PRO B 264  0                                        
SHEET    2  BD 2 LEU B 400  PRO B 402 -1  O  GLU B 401   N  THR B 263           
SHEET    1  BE 5 THR B 281  THR B 282  0                                        
SHEET    2  BE 5 HIS B 393  ALA B 396  1  O  ILE B 394   N  THR B 282           
SHEET    3  BE 5 SER B 302  ILE B 306  1  O  SER B 302   N  HIS B 393           
SHEET    4  BE 5 GLU B 329  LEU B 333  1  O  GLU B 329   N  ILE B 303           
SHEET    5  BE 5 LYS B 362  MET B 364  1  O  LYS B 362   N  GLN B 332           
SHEET    1  BF 3 VAL B 369  SER B 375  0                                        
SHEET    2  BF 3 LYS B 378  LEU B 383 -1  O  LYS B 378   N  SER B 375           
SHEET    3  BF 3 LYS B 388  THR B 391 -1  O  VAL B 389   N  ILE B 381           
SHEET    1  BG 3 PHE B 421  ARG B 422  0                                        
SHEET    2  BG 3 ALA B 440  ASP B 444  1  N  CYS B 441   O  PHE B 421           
SHEET    3  BG 3 GLY B 448  ARG B 451 -1  O  GLY B 448   N  ASP B 444           
SHEET    1  BH 6 MET B 481  ASP B 485  0                                        
SHEET    2  BH 6 GLY B 491  GLY B 496 -1  O  TYR B 492   N  SER B 484           
SHEET    3  BH 6 VAL B 572  TRP B 579 -1  O  ILE B 576   N  ILE B 495           
SHEET    4  BH 6 GLY B 563  ARG B 569 -1  O  GLY B 563   N  TRP B 579           
SHEET    5  BH 6 THR B 504  PHE B 508 -1  O  VAL B 505   N  PHE B 566           
SHEET    6  BH 6 GLN B 514  ASP B 515 -1  O  ASP B 515   N  THR B 504           
SHEET    1  CA 6 GLY C 224  THR C 229  0                                        
SHEET    2  CA 6 ARG C 158  SER C 163  1  O  VAL C 159   N  ALA C 226           
SHEET    3  CA 6 HIS C 131  ILE C 137  1  O  PHE C 134   N  LEU C 160           
SHEET    4  CA 6 GLN C 250  ILE C 258  1  O  THR C 252   N  VAL C 132           
SHEET    5  CA 6 ILE C 433  VAL C 435  1  O  TRP C 434   N  ILE C 258           
SHEET    6  CA 6 GLN C 428  ARG C 430 -1  N  ALA C 429   O  ILE C 433           
SHEET    1  CB 6 GLY C 224  THR C 229  0                                        
SHEET    2  CB 6 ARG C 158  SER C 163  1  O  VAL C 159   N  ALA C 226           
SHEET    3  CB 6 HIS C 131  ILE C 137  1  O  PHE C 134   N  LEU C 160           
SHEET    4  CB 6 GLN C 250  ILE C 258  1  O  THR C 252   N  VAL C 132           
SHEET    5  CB 6 MET C 242  LEU C 245 -1  O  VAL C 243   N  ILE C 251           
SHEET    6  CB 6 VAL C 233  ASP C 237  1  N  VAL C 234   O  LYS C 244           
SHEET    1  CC 2 ARG C 192  LYS C 194  0                                        
SHEET    2  CC 2 GLU C 200  SER C 202 -1  O  ARG C 201   N  PHE C 193           
SHEET    1  CD 2 GLY C 262  PRO C 264  0                                        
SHEET    2  CD 2 LEU C 400  PRO C 402 -1  O  GLU C 401   N  THR C 263           
SHEET    1  CE 5 THR C 281  LEU C 283  0                                        
SHEET    2  CE 5 HIS C 393  ALA C 396  1  O  ILE C 394   N  THR C 282           
SHEET    3  CE 5 SER C 302  ILE C 306  1  O  THR C 304   N  VAL C 395           
SHEET    4  CE 5 GLU C 329  LEU C 333  1  O  GLU C 329   N  ILE C 303           
SHEET    5  CE 5 LYS C 362  MET C 364  1  O  LYS C 362   N  GLN C 332           
SHEET    1  CF 3 VAL C 369  SER C 375  0                                        
SHEET    2  CF 3 LYS C 378  LEU C 383 -1  O  LYS C 378   N  SER C 375           
SHEET    3  CF 3 LYS C 388  THR C 391 -1  O  VAL C 389   N  ILE C 381           
SHEET    1  CG 3 PHE C 421  VAL C 423  0                                        
SHEET    2  CG 3 ALA C 440  ASP C 444  1  O  CYS C 441   N  VAL C 423           
SHEET    3  CG 3 GLY C 448  ARG C 451 -1  O  GLY C 448   N  ASP C 444           
SHEET    1  CH 6 MET C 481  ASP C 485  0                                        
SHEET    2  CH 6 GLY C 491  GLY C 496 -1  O  TYR C 492   N  SER C 484           
SHEET    3  CH 6 VAL C 572  TRP C 579 -1  O  ILE C 576   N  ILE C 495           
SHEET    4  CH 6 GLY C 563  ARG C 569 -1  O  GLY C 563   N  TRP C 579           
SHEET    5  CH 6 THR C 504  PHE C 508 -1  O  VAL C 505   N  PHE C 566           
SHEET    6  CH 6 GLN C 514  ASN C 516 -1  O  GLN C 514   N  GLY C 506           
SHEET    1  DA 6 GLY D 224  THR D 229  0                                        
SHEET    2  DA 6 ARG D 158  SER D 163  1  O  VAL D 159   N  ALA D 226           
SHEET    3  DA 6 HIS D 131  ILE D 137  1  O  PHE D 134   N  LEU D 160           
SHEET    4  DA 6 GLN D 250  ILE D 258  1  O  THR D 252   N  VAL D 132           
SHEET    5  DA 6 ILE D 433  VAL D 435  1  O  TRP D 434   N  ILE D 258           
SHEET    6  DA 6 GLN D 428  ARG D 430 -1  N  ALA D 429   O  ILE D 433           
SHEET    1  DB 6 GLY D 224  THR D 229  0                                        
SHEET    2  DB 6 ARG D 158  SER D 163  1  O  VAL D 159   N  ALA D 226           
SHEET    3  DB 6 HIS D 131  ILE D 137  1  O  PHE D 134   N  LEU D 160           
SHEET    4  DB 6 GLN D 250  ILE D 258  1  O  THR D 252   N  VAL D 132           
SHEET    5  DB 6 MET D 242  LEU D 245 -1  O  VAL D 243   N  ILE D 251           
SHEET    6  DB 6 VAL D 233  ASP D 237  1  N  VAL D 234   O  LYS D 244           
SHEET    1  DC 2 ARG D 192  LYS D 194  0                                        
SHEET    2  DC 2 GLU D 200  SER D 202 -1  O  ARG D 201   N  PHE D 193           
SHEET    1  DD 2 GLY D 262  PRO D 264  0                                        
SHEET    2  DD 2 LEU D 400  PRO D 402 -1  O  GLU D 401   N  THR D 263           
SHEET    1  DE 5 THR D 281  THR D 282  0                                        
SHEET    2  DE 5 HIS D 393  ALA D 396  1  O  ILE D 394   N  THR D 282           
SHEET    3  DE 5 SER D 302  ILE D 306  1  O  SER D 302   N  HIS D 393           
SHEET    4  DE 5 GLU D 329  LEU D 333  1  O  GLU D 329   N  ILE D 303           
SHEET    5  DE 5 LYS D 362  MET D 364  1  O  LYS D 362   N  GLN D 332           
SHEET    1  DF 3 VAL D 369  SER D 375  0                                        
SHEET    2  DF 3 LYS D 378  LEU D 383 -1  O  LYS D 378   N  SER D 375           
SHEET    3  DF 3 LYS D 388  THR D 391 -1  O  VAL D 389   N  ILE D 381           
SHEET    1  DG 3 PHE D 421  ARG D 422  0                                        
SHEET    2  DG 3 ALA D 440  ASP D 444  1  N  CYS D 441   O  PHE D 421           
SHEET    3  DG 3 GLY D 448  ARG D 451 -1  O  GLY D 448   N  ASP D 444           
SHEET    1  DH 5 MET D 481  LEU D 486  0                                        
SHEET    2  DH 5 VAL D 490  GLY D 496 -1  O  VAL D 490   N  LEU D 486           
SHEET    3  DH 5 VAL D 572  TRP D 579 -1  O  ILE D 576   N  ILE D 495           
SHEET    4  DH 5 GLY D 563  ARG D 569 -1  O  GLY D 563   N  TRP D 579           
SHEET    5  DH 5 THR D 504  PHE D 508 -1  O  VAL D 505   N  PHE D 566           
CISPEP   1 ILE A  610    HIS A  611          0       -15.21                     
CISPEP   2 GLY D  274    ALA D  275          0        22.85                     
SITE     1 AC1 17 LEU A 267  GLY A 308  GLY A 309  PHE A 310                    
SITE     2 AC1 17 LEU A 311  GLU A 314  PRO A 335  GLU A 336                    
SITE     3 AC1 17 LYS A 342  ALA A 397  VAL A 398  GLY A 399                    
SITE     4 AC1 17 GLU A 453  HIS A 454  TRP A 483  FAD A1612                    
SITE     5 AC1 17 HOH A2006                                                     
SITE     1 AC2  5 TRP A 196  TRP A 483  GLU A 493  PHE A 582                    
SITE     2 AC2  5 ASN A 583                                                     
SITE     1 AC3 18 LEU B 267  GLY B 307  GLY B 308  GLY B 309                    
SITE     2 AC3 18 PHE B 310  LEU B 311  GLU B 314  PRO B 335                    
SITE     3 AC3 18 GLU B 336  LYS B 342  ALA B 397  VAL B 398                    
SITE     4 AC3 18 GLY B 399  GLU B 453  HIS B 454  TRP B 483                    
SITE     5 AC3 18 FAD B1612  HOH B2004                                          
SITE     1 AC4  5 TRP B 196  TRP B 483  GLU B 493  PHE B 582                    
SITE     2 AC4  5 ASN B 583                                                     
SITE     1 AC5 17 LEU C 267  GLY C 308  GLY C 309  PHE C 310                    
SITE     2 AC5 17 LEU C 311  GLU C 314  PRO C 335  GLU C 336                    
SITE     3 AC5 17 LYS C 342  ALA C 397  VAL C 398  GLY C 399                    
SITE     4 AC5 17 GLU C 453  HIS C 454  TRP C 483  FAD C1612                    
SITE     5 AC5 17 HOH C2003                                                     
SITE     1 AC6  7 ALA A 275  TRP C 196  TRP C 483  GLU C 493                    
SITE     2 AC6  7 PHE C 582  ASN C 583  HOH C2007                               
SITE     1 AC7 16 LEU D 267  GLY D 307  GLY D 308  GLY D 309                    
SITE     2 AC7 16 PHE D 310  LEU D 311  GLU D 314  PRO D 335                    
SITE     3 AC7 16 GLU D 336  ALA D 397  VAL D 398  GLY D 399                    
SITE     4 AC7 16 GLU D 453  HIS D 454  TRP D 483  FAD D1612                    
SITE     1 AC8  7 TRP D 196  ASP D 456  MET D 481  TRP D 483                    
SITE     2 AC8  7 GLU D 493  PHE D 582  ASN D 583                               
SITE     1 AC9 28 GLY A 138  GLY A 139  GLY A 140  THR A 141                    
SITE     2 AC9 28 ALA A 142  VAL A 162  GLU A 164  ARG A 172                    
SITE     3 AC9 28 PRO A 173  SER A 176  LYS A 177  VAL A 233                    
SITE     4 AC9 28 ALA A 259  THR A 260  GLY A 261  ARG A 285                    
SITE     5 AC9 28 GLY A 437  ASP A 438  GLU A 453  HIS A 454                    
SITE     6 AC9 28 HIS A 455  ALA A 458  PHE A 482  TRP A 483                    
SITE     7 AC9 28 NAD A 700  HOH A2001  HOH A2002  HOH A2004                    
SITE     1 BC1 26 GLY B 138  GLY B 139  GLY B 140  THR B 141                    
SITE     2 BC1 26 ALA B 142  VAL B 162  GLU B 164  ARG B 172                    
SITE     3 BC1 26 PRO B 173  SER B 176  LYS B 231  LYS B 232                    
SITE     4 BC1 26 VAL B 233  ALA B 259  THR B 260  GLY B 261                    
SITE     5 BC1 26 PHE B 284  ARG B 285  GLY B 437  ASP B 438                    
SITE     6 BC1 26 GLU B 453  HIS B 454  HIS B 455  ALA B 458                    
SITE     7 BC1 26 PHE B 482  NAD B 700                                          
SITE     1 BC2 25 GLY D 138  GLY D 139  GLY D 140  THR D 141                    
SITE     2 BC2 25 ALA D 142  VAL D 162  GLU D 164  ARG D 172                    
SITE     3 BC2 25 PRO D 173  SER D 176  LYS D 177  LYS D 232                    
SITE     4 BC2 25 VAL D 233  ALA D 259  THR D 260  GLY D 261                    
SITE     5 BC2 25 ARG D 285  GLY D 437  ASP D 438  GLU D 453                    
SITE     6 BC2 25 HIS D 454  HIS D 455  ALA D 458  PHE D 482                    
SITE     7 BC2 25 NAD D 700                                                     
SITE     1 BC3 29 GLY C 138  GLY C 139  GLY C 140  THR C 141                    
SITE     2 BC3 29 ALA C 142  VAL C 162  GLU C 164  ARG C 172                    
SITE     3 BC3 29 PRO C 173  SER C 176  LYS C 177  LYS C 231                    
SITE     4 BC3 29 LYS C 232  VAL C 233  ALA C 259  THR C 260                    
SITE     5 BC3 29 GLY C 261  ARG C 285  GLY C 437  ASP C 438                    
SITE     6 BC3 29 GLU C 453  HIS C 454  HIS C 455  ALA C 458                    
SITE     7 BC3 29 PHE C 482  TRP C 483  NAD C 700  HOH C2001                    
SITE     8 BC3 29 HOH C2002                                                     
SITE     1 BC4  3 ARG B 584  ASN D 583  ARG D 584                               
CRYST1  120.766  120.766  343.359  90.00  90.00 120.00 P 32 2 1     24          
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      0.008280  0.004781  0.000000        0.00000                         
SCALE2      0.000000  0.009561  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002912        0.00000                         
MTRIX1   1 -0.874080 -0.484150 -0.039800       66.01836    1                    
MTRIX2   1 -0.474600  0.833620  0.282540       38.94597    1                    
MTRIX3   1 -0.103620  0.265850 -0.958430     -148.03976    1                    
MTRIX1   2 -0.991750  0.034560 -0.123410      124.31247    1                    
MTRIX2   2 -0.004960 -0.972570 -0.232570     -120.62219    1                    
MTRIX3   2 -0.128070 -0.230040  0.964720       -6.16794    1                    
MTRIX1   3  0.880830  0.447530  0.154480       75.09617    1                    
MTRIX2   3  0.457230 -0.888760 -0.032340     -121.54403    1                    
MTRIX3   3  0.122830  0.099120 -0.987470     -167.84200    1                    
MTRIX1   4  0.881970  0.456450  0.117420       10.15357    1                    
MTRIX2   4  0.443340 -0.888010  0.122020     -123.59381    1                    
MTRIX3   4  0.159970 -0.055560 -0.985560     -183.31473    1                    
MTRIX1   5 -0.999640  0.020650 -0.016920       70.36703    1                    
MTRIX2   5 -0.013090 -0.931350 -0.363900     -143.39383    1                    
MTRIX3   5 -0.023270 -0.363550  0.931280      -26.69025    1                    
MTRIX1   6 -0.890300 -0.454420 -0.029540       68.92381    1                    
MTRIX2   6 -0.445420  0.855520  0.263990       36.38877    1                    
MTRIX3   6 -0.094690  0.248190 -0.964070     -149.65079    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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