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Database: PDB
Entry: 5KVH
LinkDB: 5KVH
Original site: 5KVH 
HEADER    OXIDOREDUCTASE                          14-JUL-16   5KVH              
TITLE     CRYSTAL STRUCTURE OF HUMAN APOPTOSIS-INDUCING FACTOR WITH W196A       
TITLE    2 MUTATION                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: APOPTOSIS-INDUCING FACTOR 1, MITOCHONDRIAL;                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PROGRAMMED CELL DEATH PROTEIN 8;                            
COMPND   5 EC: 1.1.1.-;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 OTHER_DETAILS: EXPRESSED AS AIF(78-613). RESIDUES L614-Q619 REMAIN   
COMPND   9 FROM PRESCISSION PROTEASE CLEAVAGE.                                  
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: AIFM1, AIF, PDCD8;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA2 (DE3);                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET24B                                    
KEYWDS    OXIDOREDUCTASE, FLAVOPROTEIN, MITOCHONDRIA, CELL DEATH                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.A.BROSEY,J.NIX,T.ELLENBERGER,J.A.TAINER                             
REVDAT   4   04-DEC-19 5KVH    1       REMARK                                   
REVDAT   3   06-SEP-17 5KVH    1       REMARK                                   
REVDAT   2   14-DEC-16 5KVH    1       JRNL                                     
REVDAT   1   16-NOV-16 5KVH    0                                                
JRNL        AUTH   C.A.BROSEY,C.HO,W.Z.LONG,S.SINGH,K.BURNETT,G.L.HURA,J.C.NIX, 
JRNL        AUTH 2 G.R.BOWMAN,T.ELLENBERGER,J.A.TAINER                          
JRNL        TITL   DEFINING NADH-DRIVEN ALLOSTERY REGULATING APOPTOSIS-INDUCING 
JRNL        TITL 2 FACTOR.                                                      
JRNL        REF    STRUCTURE                     V.  24  2067 2016              
JRNL        REFN                   ISSN 1878-4186                               
JRNL        PMID   27818101                                                     
JRNL        DOI    10.1016/J.STR.2016.09.012                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.27 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10_2155: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.27                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 60.82                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 57018                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.950                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2824                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 60.8437 -  6.1683    1.00     2932   162  0.2128 0.2532        
REMARK   3     2  6.1683 -  4.8966    1.00     2818   123  0.1792 0.2264        
REMARK   3     3  4.8966 -  4.2778    1.00     2758   159  0.1302 0.1760        
REMARK   3     4  4.2778 -  3.8868    0.99     2709   162  0.1507 0.1784        
REMARK   3     5  3.8868 -  3.6082    0.98     2676   155  0.1710 0.1922        
REMARK   3     6  3.6082 -  3.3955    1.00     2752   124  0.1847 0.2145        
REMARK   3     7  3.3955 -  3.2255    1.00     2721   150  0.1830 0.2378        
REMARK   3     8  3.2255 -  3.0851    1.00     2728   146  0.1965 0.2364        
REMARK   3     9  3.0851 -  2.9663    1.00     2701   155  0.2119 0.2536        
REMARK   3    10  2.9663 -  2.8640    1.00     2695   137  0.2163 0.2886        
REMARK   3    11  2.8640 -  2.7744    1.00     2710   157  0.2356 0.2998        
REMARK   3    12  2.7744 -  2.6951    1.00     2715   149  0.2493 0.2704        
REMARK   3    13  2.6951 -  2.6241    0.99     2678   149  0.2928 0.2955        
REMARK   3    14  2.6241 -  2.5601    1.00     2693   131  0.2580 0.3106        
REMARK   3    15  2.5601 -  2.5019    1.00     2739   131  0.2654 0.3045        
REMARK   3    16  2.5019 -  2.4487    1.00     2692   115  0.2876 0.3543        
REMARK   3    17  2.4487 -  2.3997    1.00     2699   141  0.2901 0.3166        
REMARK   3    18  2.3997 -  2.3544    1.00     2688   130  0.3000 0.3654        
REMARK   3    19  2.3544 -  2.3124    1.00     2690   139  0.3095 0.3345        
REMARK   3    20  2.3124 -  2.2732    0.88     2400   109  0.3286 0.3307        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.350            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.420           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002           7033                                  
REMARK   3   ANGLE     :  0.437           9515                                  
REMARK   3   CHIRALITY :  0.045           1048                                  
REMARK   3   PLANARITY :  0.002           1212                                  
REMARK   3   DIHEDRAL  :  8.117           4170                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 129 THROUGH 245 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.6990  22.1746 -36.0383              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3128 T22:   0.2863                                     
REMARK   3      T33:   0.4545 T12:  -0.0366                                     
REMARK   3      T13:  -0.0177 T23:  -0.0583                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3860 L22:   2.4852                                     
REMARK   3      L33:   1.5304 L12:  -0.5943                                     
REMARK   3      L13:  -0.4138 L23:   0.5250                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1438 S12:  -0.0212 S13:   0.7266                       
REMARK   3      S21:  -0.0075 S22:  -0.0124 S23:  -0.1012                       
REMARK   3      S31:  -0.2540 S32:   0.0312 S33:  -0.1462                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 246 THROUGH 402 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  11.1914   1.7672 -37.9751              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3241 T22:   0.3317                                     
REMARK   3      T33:   0.3926 T12:  -0.0390                                     
REMARK   3      T13:  -0.0209 T23:  -0.0059                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8692 L22:   2.1736                                     
REMARK   3      L33:   0.4947 L12:  -1.7580                                     
REMARK   3      L13:  -0.4017 L23:   0.3370                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0510 S12:  -0.2219 S13:   0.0203                       
REMARK   3      S21:   0.1357 S22:   0.0334 S23:  -0.3128                       
REMARK   3      S31:   0.0699 S32:   0.0864 S33:   0.0149                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 403 THROUGH 611 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.9306   3.5548 -51.7212              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2978 T22:   0.3175                                     
REMARK   3      T33:   0.3046 T12:  -0.0497                                     
REMARK   3      T13:  -0.0349 T23:  -0.0178                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5530 L22:   1.9554                                     
REMARK   3      L33:   4.1831 L12:  -0.6135                                     
REMARK   3      L13:  -1.7444 L23:   0.4893                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0025 S12:   0.1711 S13:  -0.0498                       
REMARK   3      S21:  -0.1907 S22:   0.0041 S23:   0.0209                       
REMARK   3      S31:   0.1077 S32:  -0.0469 S33:   0.0191                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS WERE INCLUDED IN RIDING         
REMARK   3  POSITIONS DURING REFINEMENT. FAD COFACTOR AND GLYCEROL GEOMETRY     
REMARK   3  RESTRAINTS WERE PREPARED IN ELBOW USING MOGUL OR SIMPLE             
REMARK   3  OPTIMIZATION, RESPECTIVELY, AND INCLUDED EXPLICITLY WITH THE        
REMARK   3  REFINEMENT. RESIDUES 78-125, 511-559, AND 613-619 ARE DISORDERED    
REMARK   3  IN CHAINS A AND B.                                                  
REMARK   4                                                                      
REMARK   4 5KVH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUL-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000222634.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-JAN-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 4.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9762                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CMOS                               
REMARK 200  DETECTOR MANUFACTURER          : RDI CMOS_8M                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.5.17                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 57812                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.272                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.822                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.18400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.27                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.33                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.6.0                                          
REMARK 200 STARTING MODEL: 4BUR                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 300 MM NA2SO4, 16% PEG3350, PH 7.5,      
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       44.92250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       61.10550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.08300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       61.10550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       44.92250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.08300            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    77                                                      
REMARK 465     VAL A    78                                                      
REMARK 465     GLY A    79                                                      
REMARK 465     ALA A    80                                                      
REMARK 465     GLY A    81                                                      
REMARK 465     ALA A    82                                                      
REMARK 465     TYR A    83                                                      
REMARK 465     ALA A    84                                                      
REMARK 465     TYR A    85                                                      
REMARK 465     LYS A    86                                                      
REMARK 465     THR A    87                                                      
REMARK 465     MET A    88                                                      
REMARK 465     LYS A    89                                                      
REMARK 465     GLU A    90                                                      
REMARK 465     ASP A    91                                                      
REMARK 465     GLU A    92                                                      
REMARK 465     LYS A    93                                                      
REMARK 465     ARG A    94                                                      
REMARK 465     TYR A    95                                                      
REMARK 465     ASN A    96                                                      
REMARK 465     GLU A    97                                                      
REMARK 465     ARG A    98                                                      
REMARK 465     ILE A    99                                                      
REMARK 465     SER A   100                                                      
REMARK 465     GLY A   101                                                      
REMARK 465     LEU A   102                                                      
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     ALA A   511                                                      
REMARK 465     THR A   512                                                      
REMARK 465     ALA A   513                                                      
REMARK 465     GLN A   514                                                      
REMARK 465     ASP A   515                                                      
REMARK 465     ASN A   516                                                      
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     PRO A   551                                                      
REMARK 465     GLN A   552                                                      
REMARK 465     ALA A   553                                                      
REMARK 465     PRO A   554                                                      
REMARK 465     VAL A   555                                                      
REMARK 465     GLN A   556                                                      
REMARK 465     GLY A   557                                                      
REMARK 465     GLU A   558                                                      
REMARK 465     ASP A   559                                                      
REMARK 465     ASP A   613                                                      
REMARK 465     LEU A   614                                                      
REMARK 465     GLU A   615                                                      
REMARK 465     VAL A   616                                                      
REMARK 465     LEU A   617                                                      
REMARK 465     PHE A   618                                                      
REMARK 465     GLN A   619                                                      
REMARK 465     MET B    77                                                      
REMARK 465     VAL B    78                                                      
REMARK 465     GLY B    79                                                      
REMARK 465     ALA B    80                                                      
REMARK 465     GLY B    81                                                      
REMARK 465     ALA B    82                                                      
REMARK 465     TYR B    83                                                      
REMARK 465     ALA B    84                                                      
REMARK 465     TYR B    85                                                      
REMARK 465     LYS B    86                                                      
REMARK 465     THR B    87                                                      
REMARK 465     MET B    88                                                      
REMARK 465     LYS B    89                                                      
REMARK 465     GLU B    90                                                      
REMARK 465     ASP B    91                                                      
REMARK 465     GLU B    92                                                      
REMARK 465     LYS B    93                                                      
REMARK 465     ARG B    94                                                      
REMARK 465     TYR B    95                                                      
REMARK 465     ASN B    96                                                      
REMARK 465     GLU B    97                                                      
REMARK 465     ARG B    98                                                      
REMARK 465     ILE B    99                                                      
REMARK 465     SER B   100                                                      
REMARK 465     GLY B   101                                                      
REMARK 465     LEU B   102                                                      
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     GLN B   125                                                      
REMARK 465     ALA B   511                                                      
REMARK 465     THR B   512                                                      
REMARK 465     ALA B   513                                                      
REMARK 465     GLN B   514                                                      
REMARK 465     ASP B   515                                                      
REMARK 465     ASN B   516                                                      
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     ALA B   553                                                      
REMARK 465     PRO B   554                                                      
REMARK 465     VAL B   555                                                      
REMARK 465     GLN B   556                                                      
REMARK 465     GLY B   557                                                      
REMARK 465     GLU B   558                                                      
REMARK 465     ASP B   559                                                      
REMARK 465     ASP B   613                                                      
REMARK 465     LEU B   614                                                      
REMARK 465     GLU B   615                                                      
REMARK 465     VAL B   616                                                      
REMARK 465     LEU B   617                                                      
REMARK 465     PHE B   618                                                      
REMARK 465     GLN B   619                                                      
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 189    CG   CD   CE   NZ                                   
REMARK 470     LYS A 199    CD   CE   NZ                                        
REMARK 470     GLU A 346    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 510    CD   CE   NZ                                        
REMARK 470     LYS A 571    CD   CE   NZ                                        
REMARK 470     GLU A 599    CB   CG   CD   OE1  OE2                             
REMARK 470     LYS B 127    CD   CE   NZ                                        
REMARK 470     LYS B 194    CD   CE   NZ                                        
REMARK 470     LYS B 199    CD   CE   NZ                                        
REMARK 470     LYS B 301    CD   CE   NZ                                        
REMARK 470     ARG B 324    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 337    CE   NZ                                             
REMARK 470     ARG B 358    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLN B 370    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 382    CD   CE   NZ                                        
REMARK 470     LYS B 384    CD   CE   NZ                                        
REMARK 470     LYS B 388    CD   CE   NZ                                        
REMARK 470     GLU B 405    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 408    CD   CE   NZ                                        
REMARK 470     LYS B 510    CG   CD   CE   NZ                                   
REMARK 470     LYS B 571    CG   CD   CE   NZ                                   
REMARK 470     GLU B 599    CB   CG   CD   OE1  OE2                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  1090     O    HOH A  1107              2.00            
REMARK 500   O    HOH B   881     O    HOH B   987              2.04            
REMARK 500   O    HOH B  1022     O    HOH B  1040              2.04            
REMARK 500   O    HOH B   864     O    HOH B  1052              2.04            
REMARK 500   OD2  ASP B   165     O    HOH B   801              2.05            
REMARK 500   O    HOH A   915     O    HOH A  1092              2.07            
REMARK 500   O    HOH A   871     O    HOH A  1113              2.07            
REMARK 500   O    HOH A   970     O    HOH A  1020              2.07            
REMARK 500   O    HOH B   920     O    HOH B  1070              2.08            
REMARK 500   O    HOH B   808     O    HOH B   987              2.08            
REMARK 500   O    HOH A   965     O    HOH A  1032              2.09            
REMARK 500   O    HOH A  1046     O    HOH A  1156              2.10            
REMARK 500   O    HOH A  1037     O    HOH A  1087              2.10            
REMARK 500   O    HOH A  1076     O    HOH A  1172              2.11            
REMARK 500   O    HOH B  1086     O    HOH B  1098              2.11            
REMARK 500   O    HOH A   965     O    HOH A  1158              2.13            
REMARK 500   O    HOH B   833     O    HOH B  1046              2.13            
REMARK 500   O    HOH A   895     O    HOH A  1012              2.14            
REMARK 500   O    HOH A  1155     O    HOH A  1175              2.15            
REMARK 500   O    HOH A   845     O    HOH A   980              2.17            
REMARK 500   O    HOH A   941     O    HOH A  1160              2.17            
REMARK 500   O    HOH B  1079     O    HOH B  1094              2.18            
REMARK 500   O    HOH B   809     O    HOH B  1051              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500  HH22  ARG A   584     O    ASN B   583     2454     1.59            
REMARK 500   O    HOH A  1058     O    HOH B   961     2454     2.00            
REMARK 500   O    HOH A  1035     O    HOH B   975     1655     2.08            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A 177      -95.42   -139.80                                   
REMARK 500    ARG A 285      -35.12   -162.96                                   
REMARK 500    ILE A 343      -60.98   -107.54                                   
REMARK 500    TRP A 477      -51.36   -132.28                                   
REMARK 500    HIS A 611     -167.10   -128.19                                   
REMARK 500    LYS B 177      -96.74   -139.79                                   
REMARK 500    ARG B 285      -34.20   -161.41                                   
REMARK 500    ARG B 324      -70.27    -53.66                                   
REMARK 500    ALA B 325       36.63    -85.73                                   
REMARK 500    LEU B 326      -23.35   -146.75                                   
REMARK 500    LEU B 486       77.98   -111.82                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B1101        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH B1102        DISTANCE =  5.92 ANGSTROMS                       
REMARK 525    HOH B1103        DISTANCE =  6.70 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD B 701                 
DBREF  5KVH A   78   613  UNP    O95831   AIFM1_HUMAN     78    613             
DBREF  5KVH B   78   613  UNP    O95831   AIFM1_HUMAN     78    613             
SEQADV 5KVH MET A   77  UNP  O95831              INITIATING METHIONINE          
SEQADV 5KVH ALA A  196  UNP  O95831    TRP   196 ENGINEERED MUTATION            
SEQADV 5KVH LEU A  614  UNP  O95831              EXPRESSION TAG                 
SEQADV 5KVH GLU A  615  UNP  O95831              EXPRESSION TAG                 
SEQADV 5KVH VAL A  616  UNP  O95831              EXPRESSION TAG                 
SEQADV 5KVH LEU A  617  UNP  O95831              EXPRESSION TAG                 
SEQADV 5KVH PHE A  618  UNP  O95831              EXPRESSION TAG                 
SEQADV 5KVH GLN A  619  UNP  O95831              EXPRESSION TAG                 
SEQADV 5KVH MET B   77  UNP  O95831              INITIATING METHIONINE          
SEQADV 5KVH ALA B  196  UNP  O95831    TRP   196 ENGINEERED MUTATION            
SEQADV 5KVH LEU B  614  UNP  O95831              EXPRESSION TAG                 
SEQADV 5KVH GLU B  615  UNP  O95831              EXPRESSION TAG                 
SEQADV 5KVH VAL B  616  UNP  O95831              EXPRESSION TAG                 
SEQADV 5KVH LEU B  617  UNP  O95831              EXPRESSION TAG                 
SEQADV 5KVH PHE B  618  UNP  O95831              EXPRESSION TAG                 
SEQADV 5KVH GLN B  619  UNP  O95831              EXPRESSION TAG                 
SEQRES   1 A  543  MET VAL GLY ALA GLY ALA TYR ALA TYR LYS THR MET LYS          
SEQRES   2 A  543  GLU ASP GLU LYS ARG TYR ASN GLU ARG ILE SER GLY LEU          
SEQRES   3 A  543  GLY LEU THR PRO GLU GLN LYS GLN LYS LYS ALA ALA LEU          
SEQRES   4 A  543  SER ALA SER GLU GLY GLU GLU VAL PRO GLN ASP LYS ALA          
SEQRES   5 A  543  PRO SER HIS VAL PRO PHE LEU LEU ILE GLY GLY GLY THR          
SEQRES   6 A  543  ALA ALA PHE ALA ALA ALA ARG SER ILE ARG ALA ARG ASP          
SEQRES   7 A  543  PRO GLY ALA ARG VAL LEU ILE VAL SER GLU ASP PRO GLU          
SEQRES   8 A  543  LEU PRO TYR MET ARG PRO PRO LEU SER LYS GLU LEU TRP          
SEQRES   9 A  543  PHE SER ASP ASP PRO ASN VAL THR LYS THR LEU ARG PHE          
SEQRES  10 A  543  LYS GLN ALA ASN GLY LYS GLU ARG SER ILE TYR PHE GLN          
SEQRES  11 A  543  PRO PRO SER PHE TYR VAL SER ALA GLN ASP LEU PRO HIS          
SEQRES  12 A  543  ILE GLU ASN GLY GLY VAL ALA VAL LEU THR GLY LYS LYS          
SEQRES  13 A  543  VAL VAL GLN LEU ASP VAL ARG ASP ASN MET VAL LYS LEU          
SEQRES  14 A  543  ASN ASP GLY SER GLN ILE THR TYR GLU LYS CYS LEU ILE          
SEQRES  15 A  543  ALA THR GLY GLY THR PRO ARG SER LEU SER ALA ILE ASP          
SEQRES  16 A  543  ARG ALA GLY ALA GLU VAL LYS SER ARG THR THR LEU PHE          
SEQRES  17 A  543  ARG LYS ILE GLY ASP PHE ARG SER LEU GLU LYS ILE SER          
SEQRES  18 A  543  ARG GLU VAL LYS SER ILE THR ILE ILE GLY GLY GLY PHE          
SEQRES  19 A  543  LEU GLY SER GLU LEU ALA CYS ALA LEU GLY ARG LYS ALA          
SEQRES  20 A  543  ARG ALA LEU GLY THR GLU VAL ILE GLN LEU PHE PRO GLU          
SEQRES  21 A  543  LYS GLY ASN MET GLY LYS ILE LEU PRO GLU TYR LEU SER          
SEQRES  22 A  543  ASN TRP THR MET GLU LYS VAL ARG ARG GLU GLY VAL LYS          
SEQRES  23 A  543  VAL MET PRO ASN ALA ILE VAL GLN SER VAL GLY VAL SER          
SEQRES  24 A  543  SER GLY LYS LEU LEU ILE LYS LEU LYS ASP GLY ARG LYS          
SEQRES  25 A  543  VAL GLU THR ASP HIS ILE VAL ALA ALA VAL GLY LEU GLU          
SEQRES  26 A  543  PRO ASN VAL GLU LEU ALA LYS THR GLY GLY LEU GLU ILE          
SEQRES  27 A  543  ASP SER ASP PHE GLY GLY PHE ARG VAL ASN ALA GLU LEU          
SEQRES  28 A  543  GLN ALA ARG SER ASN ILE TRP VAL ALA GLY ASP ALA ALA          
SEQRES  29 A  543  CYS PHE TYR ASP ILE LYS LEU GLY ARG ARG ARG VAL GLU          
SEQRES  30 A  543  HIS HIS ASP HIS ALA VAL VAL SER GLY ARG LEU ALA GLY          
SEQRES  31 A  543  GLU ASN MET THR GLY ALA ALA LYS PRO TYR TRP HIS GLN          
SEQRES  32 A  543  SER MET PHE TRP SER ASP LEU GLY PRO ASP VAL GLY TYR          
SEQRES  33 A  543  GLU ALA ILE GLY LEU VAL ASP SER SER LEU PRO THR VAL          
SEQRES  34 A  543  GLY VAL PHE ALA LYS ALA THR ALA GLN ASP ASN PRO LYS          
SEQRES  35 A  543  SER ALA THR GLU GLN SER GLY THR GLY ILE ARG SER GLU          
SEQRES  36 A  543  SER GLU THR GLU SER GLU ALA SER GLU ILE THR ILE PRO          
SEQRES  37 A  543  PRO SER THR PRO ALA VAL PRO GLN ALA PRO VAL GLN GLY          
SEQRES  38 A  543  GLU ASP TYR GLY LYS GLY VAL ILE PHE TYR LEU ARG ASP          
SEQRES  39 A  543  LYS VAL VAL VAL GLY ILE VAL LEU TRP ASN ILE PHE ASN          
SEQRES  40 A  543  ARG MET PRO ILE ALA ARG LYS ILE ILE LYS ASP GLY GLU          
SEQRES  41 A  543  GLN HIS GLU ASP LEU ASN GLU VAL ALA LYS LEU PHE ASN          
SEQRES  42 A  543  ILE HIS GLU ASP LEU GLU VAL LEU PHE GLN                      
SEQRES   1 B  543  MET VAL GLY ALA GLY ALA TYR ALA TYR LYS THR MET LYS          
SEQRES   2 B  543  GLU ASP GLU LYS ARG TYR ASN GLU ARG ILE SER GLY LEU          
SEQRES   3 B  543  GLY LEU THR PRO GLU GLN LYS GLN LYS LYS ALA ALA LEU          
SEQRES   4 B  543  SER ALA SER GLU GLY GLU GLU VAL PRO GLN ASP LYS ALA          
SEQRES   5 B  543  PRO SER HIS VAL PRO PHE LEU LEU ILE GLY GLY GLY THR          
SEQRES   6 B  543  ALA ALA PHE ALA ALA ALA ARG SER ILE ARG ALA ARG ASP          
SEQRES   7 B  543  PRO GLY ALA ARG VAL LEU ILE VAL SER GLU ASP PRO GLU          
SEQRES   8 B  543  LEU PRO TYR MET ARG PRO PRO LEU SER LYS GLU LEU TRP          
SEQRES   9 B  543  PHE SER ASP ASP PRO ASN VAL THR LYS THR LEU ARG PHE          
SEQRES  10 B  543  LYS GLN ALA ASN GLY LYS GLU ARG SER ILE TYR PHE GLN          
SEQRES  11 B  543  PRO PRO SER PHE TYR VAL SER ALA GLN ASP LEU PRO HIS          
SEQRES  12 B  543  ILE GLU ASN GLY GLY VAL ALA VAL LEU THR GLY LYS LYS          
SEQRES  13 B  543  VAL VAL GLN LEU ASP VAL ARG ASP ASN MET VAL LYS LEU          
SEQRES  14 B  543  ASN ASP GLY SER GLN ILE THR TYR GLU LYS CYS LEU ILE          
SEQRES  15 B  543  ALA THR GLY GLY THR PRO ARG SER LEU SER ALA ILE ASP          
SEQRES  16 B  543  ARG ALA GLY ALA GLU VAL LYS SER ARG THR THR LEU PHE          
SEQRES  17 B  543  ARG LYS ILE GLY ASP PHE ARG SER LEU GLU LYS ILE SER          
SEQRES  18 B  543  ARG GLU VAL LYS SER ILE THR ILE ILE GLY GLY GLY PHE          
SEQRES  19 B  543  LEU GLY SER GLU LEU ALA CYS ALA LEU GLY ARG LYS ALA          
SEQRES  20 B  543  ARG ALA LEU GLY THR GLU VAL ILE GLN LEU PHE PRO GLU          
SEQRES  21 B  543  LYS GLY ASN MET GLY LYS ILE LEU PRO GLU TYR LEU SER          
SEQRES  22 B  543  ASN TRP THR MET GLU LYS VAL ARG ARG GLU GLY VAL LYS          
SEQRES  23 B  543  VAL MET PRO ASN ALA ILE VAL GLN SER VAL GLY VAL SER          
SEQRES  24 B  543  SER GLY LYS LEU LEU ILE LYS LEU LYS ASP GLY ARG LYS          
SEQRES  25 B  543  VAL GLU THR ASP HIS ILE VAL ALA ALA VAL GLY LEU GLU          
SEQRES  26 B  543  PRO ASN VAL GLU LEU ALA LYS THR GLY GLY LEU GLU ILE          
SEQRES  27 B  543  ASP SER ASP PHE GLY GLY PHE ARG VAL ASN ALA GLU LEU          
SEQRES  28 B  543  GLN ALA ARG SER ASN ILE TRP VAL ALA GLY ASP ALA ALA          
SEQRES  29 B  543  CYS PHE TYR ASP ILE LYS LEU GLY ARG ARG ARG VAL GLU          
SEQRES  30 B  543  HIS HIS ASP HIS ALA VAL VAL SER GLY ARG LEU ALA GLY          
SEQRES  31 B  543  GLU ASN MET THR GLY ALA ALA LYS PRO TYR TRP HIS GLN          
SEQRES  32 B  543  SER MET PHE TRP SER ASP LEU GLY PRO ASP VAL GLY TYR          
SEQRES  33 B  543  GLU ALA ILE GLY LEU VAL ASP SER SER LEU PRO THR VAL          
SEQRES  34 B  543  GLY VAL PHE ALA LYS ALA THR ALA GLN ASP ASN PRO LYS          
SEQRES  35 B  543  SER ALA THR GLU GLN SER GLY THR GLY ILE ARG SER GLU          
SEQRES  36 B  543  SER GLU THR GLU SER GLU ALA SER GLU ILE THR ILE PRO          
SEQRES  37 B  543  PRO SER THR PRO ALA VAL PRO GLN ALA PRO VAL GLN GLY          
SEQRES  38 B  543  GLU ASP TYR GLY LYS GLY VAL ILE PHE TYR LEU ARG ASP          
SEQRES  39 B  543  LYS VAL VAL VAL GLY ILE VAL LEU TRP ASN ILE PHE ASN          
SEQRES  40 B  543  ARG MET PRO ILE ALA ARG LYS ILE ILE LYS ASP GLY GLU          
SEQRES  41 B  543  GLN HIS GLU ASP LEU ASN GLU VAL ALA LYS LEU PHE ASN          
SEQRES  42 B  543  ILE HIS GLU ASP LEU GLU VAL LEU PHE GLN                      
HET    FAD  A 701      84                                                       
HET    GOL  A 702      14                                                       
HET    FAD  B 701      83                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL   4  GOL    C3 H8 O3                                                     
FORMUL   6  HOH   *683(H2 O)                                                    
HELIX    1 AA1 GLY A  140  ASP A  154  1                                  15    
HELIX    2 AA2 ARG A  172  LYS A  177  5                                   6    
HELIX    3 AA3 ASN A  186  LEU A  191  1                                   6    
HELIX    4 AA4 PRO A  207  TYR A  211  5                                   5    
HELIX    5 AA5 LEU A  267  ALA A  273  1                                   7    
HELIX    6 AA6 GLY A  274  ARG A  280  1                                   7    
HELIX    7 AA7 LYS A  286  ARG A  298  1                                  13    
HELIX    8 AA8 GLY A  309  GLY A  327  1                                  19    
HELIX    9 AA9 PRO A  345  GLU A  359  1                                  15    
HELIX   10 AB1 LEU A  406  GLY A  411  1                                   6    
HELIX   11 AB2 HIS A  454  MET A  469  1                                  16    
HELIX   12 AB3 ARG A  584  GLY A  595  1                                  12    
HELIX   13 AB4 ASP A  600  LYS A  606  1                                   7    
HELIX   14 AB5 LEU A  607  ASN A  609  5                                   3    
HELIX   15 AB6 GLY B  140  ASP B  154  1                                  15    
HELIX   16 AB7 ARG B  172  PHE B  181  5                                  10    
HELIX   17 AB8 ASN B  186  LEU B  191  1                                   6    
HELIX   18 AB9 PRO B  207  TYR B  211  5                                   5    
HELIX   19 AC1 LEU B  267  ALA B  273  1                                   7    
HELIX   20 AC2 GLY B  274  ARG B  280  1                                   7    
HELIX   21 AC3 LYS B  286  ARG B  298  1                                  13    
HELIX   22 AC4 GLY B  309  ALA B  325  1                                  17    
HELIX   23 AC5 PRO B  345  GLU B  359  1                                  15    
HELIX   24 AC6 LEU B  406  GLY B  411  1                                   6    
HELIX   25 AC7 HIS B  454  MET B  469  1                                  16    
HELIX   26 AC8 ARG B  584  GLY B  595  1                                  12    
HELIX   27 AC9 ASP B  600  LEU B  607  1                                   8    
SHEET    1 AA1 6 GLY A 224  THR A 229  0                                        
SHEET    2 AA1 6 ARG A 158  SER A 163  1  N  ILE A 161   O  LEU A 228           
SHEET    3 AA1 6 HIS A 131  ILE A 137  1  N  LEU A 136   O  LEU A 160           
SHEET    4 AA1 6 GLN A 250  ILE A 258  1  O  LEU A 257   N  ILE A 137           
SHEET    5 AA1 6 MET A 242  LEU A 245 -1  N  VAL A 243   O  ILE A 251           
SHEET    6 AA1 6 VAL A 233  ASP A 237 -1  N  ASP A 237   O  MET A 242           
SHEET    1 AA2 6 GLY A 224  THR A 229  0                                        
SHEET    2 AA2 6 ARG A 158  SER A 163  1  N  ILE A 161   O  LEU A 228           
SHEET    3 AA2 6 HIS A 131  ILE A 137  1  N  LEU A 136   O  LEU A 160           
SHEET    4 AA2 6 GLN A 250  ILE A 258  1  O  LEU A 257   N  ILE A 137           
SHEET    5 AA2 6 ILE A 433  VAL A 435  1  O  TRP A 434   N  ILE A 258           
SHEET    6 AA2 6 GLN A 428  ARG A 430 -1  N  ALA A 429   O  ILE A 433           
SHEET    1 AA3 2 ARG A 192  LYS A 194  0                                        
SHEET    2 AA3 2 GLU A 200  SER A 202 -1  O  ARG A 201   N  PHE A 193           
SHEET    1 AA4 2 GLY A 262  PRO A 264  0                                        
SHEET    2 AA4 2 LEU A 400  PRO A 402 -1  O  GLU A 401   N  THR A 263           
SHEET    1 AA5 5 THR A 281  LEU A 283  0                                        
SHEET    2 AA5 5 HIS A 393  ALA A 396  1  O  ILE A 394   N  THR A 282           
SHEET    3 AA5 5 SER A 302  ILE A 306  1  N  THR A 304   O  VAL A 395           
SHEET    4 AA5 5 GLU A 329  LEU A 333  1  O  ILE A 331   N  ILE A 305           
SHEET    5 AA5 5 LYS A 362  MET A 364  1  O  MET A 364   N  GLN A 332           
SHEET    1 AA6 3 VAL A 369  SER A 375  0                                        
SHEET    2 AA6 3 LYS A 378  LEU A 383 -1  O  LEU A 380   N  GLY A 373           
SHEET    3 AA6 3 LYS A 388  THR A 391 -1  O  VAL A 389   N  ILE A 381           
SHEET    1 AA7 3 PHE A 421  ARG A 422  0                                        
SHEET    2 AA7 3 ALA A 440  ASP A 444  1  O  CYS A 441   N  PHE A 421           
SHEET    3 AA7 3 GLY A 448  ARG A 451 -1  O  GLY A 448   N  ASP A 444           
SHEET    1 AA8 5 MET A 481  ASP A 485  0                                        
SHEET    2 AA8 5 GLY A 491  GLY A 496 -1  O  TYR A 492   N  SER A 484           
SHEET    3 AA8 5 VAL A 572  TRP A 579 -1  O  LEU A 578   N  GLU A 493           
SHEET    4 AA8 5 LYS A 562  ARG A 569 -1  N  TYR A 567   O  GLY A 575           
SHEET    5 AA8 5 THR A 504  ALA A 509 -1  N  VAL A 505   O  PHE A 566           
SHEET    1 AA9 6 GLY B 224  THR B 229  0                                        
SHEET    2 AA9 6 ARG B 158  SER B 163  1  N  ILE B 161   O  LEU B 228           
SHEET    3 AA9 6 HIS B 131  ILE B 137  1  N  LEU B 136   O  LEU B 160           
SHEET    4 AA9 6 GLN B 250  ILE B 258  1  O  LEU B 257   N  ILE B 137           
SHEET    5 AA9 6 MET B 242  LEU B 245 -1  N  VAL B 243   O  ILE B 251           
SHEET    6 AA9 6 VAL B 233  ASP B 237 -1  N  ASP B 237   O  MET B 242           
SHEET    1 AB1 6 GLY B 224  THR B 229  0                                        
SHEET    2 AB1 6 ARG B 158  SER B 163  1  N  ILE B 161   O  LEU B 228           
SHEET    3 AB1 6 HIS B 131  ILE B 137  1  N  LEU B 136   O  LEU B 160           
SHEET    4 AB1 6 GLN B 250  ILE B 258  1  O  LEU B 257   N  ILE B 137           
SHEET    5 AB1 6 ILE B 433  VAL B 435  1  O  TRP B 434   N  ILE B 258           
SHEET    6 AB1 6 GLN B 428  ARG B 430 -1  N  ALA B 429   O  ILE B 433           
SHEET    1 AB2 2 ARG B 192  LYS B 194  0                                        
SHEET    2 AB2 2 GLU B 200  SER B 202 -1  O  ARG B 201   N  PHE B 193           
SHEET    1 AB3 2 GLY B 262  PRO B 264  0                                        
SHEET    2 AB3 2 LEU B 400  PRO B 402 -1  O  GLU B 401   N  THR B 263           
SHEET    1 AB4 5 THR B 281  LEU B 283  0                                        
SHEET    2 AB4 5 HIS B 393  ALA B 396  1  O  ALA B 396   N  THR B 282           
SHEET    3 AB4 5 SER B 302  ILE B 306  1  N  THR B 304   O  VAL B 395           
SHEET    4 AB4 5 GLU B 329  LEU B 333  1  O  ILE B 331   N  ILE B 305           
SHEET    5 AB4 5 LYS B 362  MET B 364  1  O  MET B 364   N  GLN B 332           
SHEET    1 AB5 3 VAL B 369  SER B 375  0                                        
SHEET    2 AB5 3 LYS B 378  LEU B 383 -1  O  LEU B 380   N  GLY B 373           
SHEET    3 AB5 3 LYS B 388  THR B 391 -1  O  VAL B 389   N  ILE B 381           
SHEET    1 AB6 3 PHE B 421  ARG B 422  0                                        
SHEET    2 AB6 3 ALA B 440  ASP B 444  1  O  CYS B 441   N  PHE B 421           
SHEET    3 AB6 3 GLY B 448  ARG B 450 -1  O  GLY B 448   N  ASP B 444           
SHEET    1 AB7 5 MET B 481  ASP B 485  0                                        
SHEET    2 AB7 5 GLY B 491  GLY B 496 -1  O  ALA B 494   N  PHE B 482           
SHEET    3 AB7 5 VAL B 572  TRP B 579 -1  O  LEU B 578   N  GLU B 493           
SHEET    4 AB7 5 LYS B 562  ARG B 569 -1  N  TYR B 567   O  GLY B 575           
SHEET    5 AB7 5 THR B 504  ALA B 509 -1  N  VAL B 505   O  PHE B 566           
SITE     1 AC1 37 GLY A 138  GLY A 139  GLY A 140  THR A 141                    
SITE     2 AC1 37 ALA A 142  VAL A 162  GLU A 164  ARG A 172                    
SITE     3 AC1 37 PRO A 173  SER A 176  LYS A 177  LYS A 232                    
SITE     4 AC1 37 VAL A 233  ALA A 259  THR A 260  GLY A 261                    
SITE     5 AC1 37 PHE A 284  ARG A 285  LEU A 311  GLY A 437                    
SITE     6 AC1 37 ASP A 438  GLU A 453  HIS A 454  HIS A 455                    
SITE     7 AC1 37 ALA A 458  PHE A 482  TRP A 483  HOH A 818                    
SITE     8 AC1 37 HOH A 849  HOH A 852  HOH A 854  HOH A 867                    
SITE     9 AC1 37 HOH A 882  HOH A 885  HOH A 892  HOH A 904                    
SITE    10 AC1 37 HOH A 913                                                     
SITE     1 AC2  4 TYR A 347  TRP A 351  PHE A 508  TYR A 560                    
SITE     1 AC3 38 GLY B 138  GLY B 139  GLY B 140  THR B 141                    
SITE     2 AC3 38 ALA B 142  VAL B 162  GLU B 164  ARG B 172                    
SITE     3 AC3 38 PRO B 173  SER B 176  LYS B 177  LYS B 231                    
SITE     4 AC3 38 LYS B 232  VAL B 233  ALA B 259  THR B 260                    
SITE     5 AC3 38 GLY B 261  PHE B 284  ARG B 285  LEU B 311                    
SITE     6 AC3 38 GLU B 314  GLY B 437  ASP B 438  GLU B 453                    
SITE     7 AC3 38 HIS B 454  HIS B 455  ALA B 458  PHE B 482                    
SITE     8 AC3 38 TRP B 483  HOH B 805  HOH B 818  HOH B 821                    
SITE     9 AC3 38 HOH B 822  HOH B 830  HOH B 836  HOH B 841                    
SITE    10 AC3 38 HOH B 871  HOH B 957                                          
CRYST1   89.845  112.166  122.211  90.00  90.00  90.00 P 21 21 21    8          
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      0.011130  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008915  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008183        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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