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Database: PDB
Entry: 5KVI
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Original site: 5KVI 
HEADER    OXIDOREDUCTASE                          14-JUL-16   5KVI              
TITLE     CRYSTAL STRUCTURE OF MONOMERIC HUMAN APOPTOSIS-INDUCING FACTOR WITH   
TITLE    2 E413A/R422A/R430A MUTATIONS                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: APOPTOSIS-INDUCING FACTOR 1, MITOCHONDRIAL;                
COMPND   3 CHAIN: A;                                                            
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: 469008;                                     
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 5KVI    1       REMARK                                   
REVDAT   3   06-SEP-17 5KVI    1       REMARK                                   
REVDAT   2   14-DEC-16 5KVI    1       JRNL                                     
REVDAT   1   16-NOV-16 5KVI    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.    2.00 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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.16                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 80.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 31943                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.159                           
REMARK   3   R VALUE            (WORKING SET) : 0.157                           
REMARK   3   FREE R VALUE                     : 0.194                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.980                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1590                            
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 45.1715 -  4.4352    0.99     3621   211  0.1510 0.1716        
REMARK   3     2  4.4352 -  3.5208    1.00     3459   195  0.1323 0.1711        
REMARK   3     3  3.5208 -  3.0758    1.00     3460   162  0.1513 0.1950        
REMARK   3     4  3.0758 -  2.7947    1.00     3435   194  0.1733 0.2553        
REMARK   3     5  2.7947 -  2.5944    1.00     3418   175  0.1836 0.2243        
REMARK   3     6  2.5944 -  2.4414    0.94     3238   150  0.1836 0.2080        
REMARK   3     7  2.4414 -  2.3192    0.83     2806   150  0.1656 0.2191        
REMARK   3     8  2.3192 -  2.2182    0.70     2357   129  0.1577 0.2063        
REMARK   3     9  2.2182 -  2.1328    0.56     1909    97  0.1628 0.1723        
REMARK   3    10  2.1328 -  2.0592    0.45     1513    80  0.1746 0.2233        
REMARK   3    11  2.0592 -  1.9948    0.33     1137    47  0.2106 0.2193        
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)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.880           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.37                          
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      :  0.008           3815                                  
REMARK   3   ANGLE     :  0.876           5169                                  
REMARK   3   CHIRALITY :  0.053            571                                  
REMARK   3   PLANARITY :  0.005            660                                  
REMARK   3   DIHEDRAL  : 11.514           2257                                  
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): -40.0107  87.4884  -0.5301              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3808 T22:   0.2271                                     
REMARK   3      T33:   0.1612 T12:  -0.0654                                     
REMARK   3      T13:  -0.0500 T23:  -0.0130                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4649 L22:   1.2434                                     
REMARK   3      L33:   1.9843 L12:   0.1459                                     
REMARK   3      L13:   0.4191 L23:   0.1819                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0472 S12:   0.2788 S13:  -0.1128                       
REMARK   3      S21:  -0.5348 S22:   0.0682 S23:   0.0993                       
REMARK   3      S31:  -0.0072 S32:   0.0449 S33:  -0.0241                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 246 THROUGH 402 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -53.9155  97.0826  19.7668              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2095 T22:   0.2514                                     
REMARK   3      T33:   0.2810 T12:  -0.0195                                     
REMARK   3      T13:  -0.0170 T23:   0.0171                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5079 L22:   1.5063                                     
REMARK   3      L33:   1.7953 L12:  -0.3019                                     
REMARK   3      L13:  -0.0729 L23:   0.7069                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0320 S12:  -0.0893 S13:   0.0149                       
REMARK   3      S21:  -0.0205 S22:  -0.0836 S23:   0.5254                       
REMARK   3      S31:  -0.0419 S32:  -0.4438 S33:   0.1253                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 403 THROUGH 611 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -29.6907  99.8851  17.9235              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1679 T22:   0.1732                                     
REMARK   3      T33:   0.1315 T12:  -0.0552                                     
REMARK   3      T13:   0.0117 T23:  -0.0085                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8102 L22:   2.3252                                     
REMARK   3      L33:   1.2939 L12:   0.1922                                     
REMARK   3      L13:   0.2500 L23:   0.3606                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0955 S12:   0.0016 S13:   0.0624                       
REMARK   3      S21:  -0.2430 S22:   0.1981 S23:  -0.2468                       
REMARK   3      S31:  -0.2150 S32:   0.2327 S33:  -0.0534                       
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, HEPES, AND GLYCEROL      
REMARK   3  GEOMETRY RESTRAINTS WERE PREPARED IN ELBOW USING MOGUL (FAD) OR     
REMARK   3  SIMPLE OPTIMIZATION (HEPES, GLYCEROL) AND INCLUDED EXPLICITLY       
REMARK   3  WITH THE REFINEMENT. RESIDUES 78-125, 511-559, AND 613-619 ARE      
REMARK   3  DISORDERED IN CHAINS A AND B.                                       
REMARK   4                                                                      
REMARK   4 5KVI 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_1000222632.                                   
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 : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32041                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 80.7                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.03                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 31.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38100                            
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: 4BV6                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES, PH 7.5, 50 MM NACL, 24%    
REMARK 280  PEG3350, 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       32.31150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       54.16150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.90100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       54.16150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.31150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.90100            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2230 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 KCAL/MOL                         
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 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     ASP A   126                                                      
REMARK 465     LYS A   127                                                      
REMARK 465     ALA A   128                                                      
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 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     ASP A 183    CG   OD1  OD2                                       
REMARK 470     LYS A 194    CD   CE   NZ                                        
REMARK 470     GLN A 215    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 388    CE   NZ                                             
REMARK 470     LYS A 571    CD   CE   NZ                                        
REMARK 470     LYS A 593    CE   NZ                                             
REMARK 470     LEU A 617    CB   CG   CD1  CD2                                  
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  HE21  GLN A   619     O    HOH A   805              1.58            
REMARK 500   O    HOH A   862     O    HOH A  1128              1.68            
REMARK 500   O    HOH A  1114     O    HOH A  1179              1.77            
REMARK 500   O    HOH A  1181     O    HOH A  1247              1.92            
REMARK 500   O    HOH A   855     O    HOH A  1200              1.94            
REMARK 500   O    HOH A   969     O    HOH A  1174              1.96            
REMARK 500   O    HOH A  1142     O    HOH A  1144              1.98            
REMARK 500   O    HOH A   941     O    HOH A   950              2.06            
REMARK 500   OD1  ASP A   485     NH1  ARG A   529              2.07            
REMARK 500   O    HOH A  1017     O    HOH A  1221              2.09            
REMARK 500   O    HOH A  1199     O    HOH A  1204              2.10            
REMARK 500   O    HOH A   859     O    HOH A   861              2.16            
REMARK 500   O    HOH A   966     O    HOH A  1195              2.19            
REMARK 500   O    HOH A  1150     O    HOH A  1204              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   O    HOH A   864     O    HOH A  1139     3445     2.09            
REMARK 500   O    HOH A  1135     O    HOH A  1177     4475     2.13            
REMARK 500   O    HOH A   872     O    HOH A   899     4575     2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 529   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A 177     -101.38   -133.58                                   
REMARK 500    PHE A 181       53.63    -99.64                                   
REMARK 500    ASP A 183       14.14     57.43                                   
REMARK 500    LEU A 191       29.74     49.07                                   
REMARK 500    ARG A 285      -36.36   -140.89                                   
REMARK 500    GLU A 453       68.79   -118.56                                   
REMARK 500    THR A 534      161.24     67.86                                   
REMARK 500    ASP A 559     -152.09   -152.05                                   
REMARK 500    ASP A 600       59.04     38.16                                   
REMARK 500    ILE A 610      -62.27   -120.90                                   
REMARK 500    ASP A 613       47.93    -91.53                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 HIS A  598     GLU A  599                  147.91                    
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 A1255        DISTANCE =  6.39 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 EPE A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 703                 
DBREF  5KVI A   78   613  UNP    O95831   AIFM1_HUMAN     78    613             
SEQADV 5KVI MET A   77  UNP  O95831              INITIATING METHIONINE          
SEQADV 5KVI ALA A  413  UNP  O95831    GLU   413 ENGINEERED MUTATION            
SEQADV 5KVI ALA A  422  UNP  O95831    ARG   422 ENGINEERED MUTATION            
SEQADV 5KVI ALA A  430  UNP  O95831    ARG   430 ENGINEERED MUTATION            
SEQADV 5KVI LEU A  614  UNP  O95831              EXPRESSION TAG                 
SEQADV 5KVI GLU A  615  UNP  O95831              EXPRESSION TAG                 
SEQADV 5KVI VAL A  616  UNP  O95831              EXPRESSION TAG                 
SEQADV 5KVI LEU A  617  UNP  O95831              EXPRESSION TAG                 
SEQADV 5KVI PHE A  618  UNP  O95831              EXPRESSION TAG                 
SEQADV 5KVI GLN A  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 TRP 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 ALA ILE          
SEQRES  27 A  543  ASP SER ASP PHE GLY GLY PHE ALA VAL ASN ALA GLU LEU          
SEQRES  28 A  543  GLN ALA ALA 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                      
HET    FAD  A 701      84                                                       
HET    EPE  A 702      32                                                       
HET    GOL  A 703      14                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID              
HETNAM     GOL GLYCEROL                                                         
HETSYN     EPE HEPES                                                            
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  FAD    C27 H33 N9 O15 P2                                            
FORMUL   3  EPE    C8 H18 N2 O4 S                                               
FORMUL   4  GOL    C3 H8 O3                                                     
FORMUL   5  HOH   *455(H2 O)                                                    
HELIX    1 AA1 GLY A  140  ASP A  154  1                                  15    
HELIX    2 AA2 ARG A  172  PHE A  181  5                                  10    
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  VAL A  300  1                                  15    
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 VAL A  404  GLY A  410  5                                   7    
HELIX   11 AB2 HIS A  454  MET A  469  1                                  16    
HELIX   12 AB3 ASN A  516  GLY A  525  1                                  10    
HELIX   13 AB4 ILE A  528  THR A  534  1                                   7    
HELIX   14 AB5 ARG A  584  GLY A  595  1                                  12    
HELIX   15 AB6 ASP A  600  ALA A  605  1                                   6    
HELIX   16 AB7 ALA A  605  ILE A  610  1                                   6    
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  ALA 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  ILE A 306   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  ALA 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 450 -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 2 ALA A 538  THR A 542  0                                        
SHEET    2 AA9 2 GLU A 615  PHE A 618 -1  O  LEU A 617   N  SER A 539           
SITE     1 AC1 39 GLY A 138  GLY A 139  GLY A 140  THR A 141                    
SITE     2 AC1 39 ALA A 142  VAL A 162  GLU A 164  ASP A 165                    
SITE     3 AC1 39 ARG A 172  PRO A 173  SER A 176  LYS A 177                    
SITE     4 AC1 39 LYS A 232  VAL A 233  ALA A 259  THR A 260                    
SITE     5 AC1 39 GLY A 261  ARG A 285  LYS A 286  LEU A 311                    
SITE     6 AC1 39 GLY A 437  ASP A 438  GLU A 453  HIS A 454                    
SITE     7 AC1 39 HIS A 455  ALA A 458  PHE A 482  TRP A 483                    
SITE     8 AC1 39 HOH A 823  HOH A 830  HOH A 840  HOH A 843                    
SITE     9 AC1 39 HOH A 848  HOH A 857  HOH A 866  HOH A 883                    
SITE    10 AC1 39 HOH A 964  HOH A1007  HOH A1009                               
SITE     1 AC2 10 ARG A 265  LYS A 342  ILE A 343  VAL A 398                    
SITE     2 AC2 10 GLY A 399  HIS A 454  PHE A 482  HOH A 942                    
SITE     3 AC2 10 HOH A1050  HOH A1091                                          
SITE     1 AC3  7 VAL A 423  ASN A 424  ARG A 449  HOH A 804                    
SITE     2 AC3  7 HOH A 807  HOH A1150  HOH A1197                               
CRYST1   64.623   81.802  108.323  90.00  90.00  90.00 P 21 21 21    4          
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      0.015474  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012225  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009232        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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