GenomeNet

Database: PDB
Entry: 4BV6
LinkDB: 4BV6
Original site: 4BV6 
HEADER    OXIDOREDUCTASE                          25-JUN-13   4BV6              
TITLE     REFINED CRYSTAL STRUCTURE OF THE HUMAN APOPTOSIS INDUCING FACTOR      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: APOPTOSIS-INDUCING FACTOR 1, MITOCHONDRIAL;                
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 121-613;                                          
COMPND   5 SYNONYM: PROGRAMMED CELL DEATH PROTEIN 8;                            
COMPND   6 EC: 1.-.-.-;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    OXIDOREDUCTASE, APOPTOSIS, NUCLEAR CHROMATINOLYSIS, DNA BINDING       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.MARTINEZ-JULVEZ,B.HERGUEDAS,J.A.HERMOSO,P.FERREIRA,R.VILLANUEVA,    
AUTHOR   2 M.MEDINA                                                             
REVDAT   1   17-SEP-14 4BV6    0                                                
JRNL        AUTH   P.FERREIRA,R.VILLANUEVA,M.MARTINEZ-JULVEZ,B.HERGUEDAS,       
JRNL        AUTH 2 C.MARCUELLO,P.FERNANDEZ-SILVA,L.CABON,J.A.HERMOSO,A.LOSTAO,  
JRNL        AUTH 3 S.A.SUSIN,M.MEDINA                                           
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE COENZYME MEDIATED MONOMER-      
JRNL        TITL 2 DIMER TRANSITION OF THE PRO-APOPTOTIC APOPTOSIS INDUCING     
JRNL        TITL 3 FACTOR.                                                      
JRNL        REF    BIOCHEMISTRY                  V.  53  4204 2014              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   24914854                                                     
JRNL        DOI    10.1021/BI500343R                                            
REMARK   0                                                                      
REMARK   0 THIS ENTRY 4BV6 REFLECTS AN ALTERNATIVE MODELING OF THE              
REMARK   0 ORIGINAL STRUCTURAL DATA (R1M6ISF) DETERMINED BY                     
REMARK   0 AUTHORS OF THE PDB ENTRY 1M6I:                                       
REMARK   0                                                                      
REMARK   0 ORIGINAL DATA REFERENCE 1                                            
REMARK   0  PDB ID: 1M6I                                                        
REMARK   0  AUTH   H.YE,C.CANDE,N.C.STEPHANOU,S.JIANG,S.GURBUXANI,N.LAROCHETTE, 
REMARK   0  AUTH 2 E.DAUGAS,C.GARRIDO,G.KROEMER,H.WU                            
REMARK   0  TITL   DNA BINDING IS REQUIRED FOR THE APOPTOGENIC ACTION OF        
REMARK   0  TITL 2 APOPTOSIS INDUCING FACTOR.                                   
REMARK   0  REF    NAT.STRUCT.BIOL.              V.   9   680 2002              
REMARK   0  REFN                   ISSN 1072-8368                               
REMARK   0  PMID   12198487                                                     
REMARK   0  DOI    10.1038/NSB836                                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.77                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.95                          
REMARK   3   NUMBER OF REFLECTIONS             : 44509                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.19518                         
REMARK   3   R VALUE            (WORKING SET) : 0.19389                         
REMARK   3   FREE R VALUE                     : 0.21526                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2846                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.803                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.850                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2420                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 70.67                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.239                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 178                          
REMARK   3   BIN FREE R VALUE                    : 0.263                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3649                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 59                                      
REMARK   3   SOLVENT ATOMS            : 289                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.380                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.56                                                 
REMARK   3    B22 (A**2) : 0.15                                                 
REMARK   3    B33 (A**2) : -0.74                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : -0.23                                                
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.136         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.121         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.080         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.574         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.930                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3786 ; 0.009 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5128 ; 1.269 ; 1.985       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   475 ; 5.523 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   158 ;31.822 ;23.481       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   656 ;13.662 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    30 ;18.933 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   567 ; 0.081 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2826 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT      
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   3   RESIDUES 546-557 ARE DISORDERED.  AUTHOR USED THE SF DATA          
REMARK   3    FROM ENTRY 1M6I                                                   
REMARK   4                                                                      
REMARK   4 4BV6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-SEP-14.                  
REMARK 100 THE PDBE ID CODE IS EBI-57401.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: THIS ENTRY REFLECTS AN ALTERNATIVE MODELING OF THE           
REMARK 200  ORIGINAL STRUCTURAL DATA 1M6I.MTZ DETERMINED BY AUTHORS OF          
REMARK 200  THE PDB ENTRY 1M6I. H.YE,C.CANDE,N.C. STEPHANOU, S.JIANG,           
REMARK 200  S.GURBUXANI,N.LAROCHETTE,E.  DAUGAS, C.GARRIDO, G.KROEMER,          
REMARK 200  H.WU                                                                
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       45.25000            
REMARK 290   SMTRY3   2  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 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     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     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     HIS A   611                                                      
REMARK 465     GLU A   612                                                      
REMARK 465     ASP A   613                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A 215    CG   CD   OE1  NE2                                  
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     -107.05   -131.66                                   
REMARK 500    ALA A 259       56.82   -143.77                                   
REMARK 500    ARG A 285      -35.66   -149.81                                   
REMARK 500    SER A 376       59.90     34.50                                   
REMARK 500    LYS A 408      -70.33    -60.58                                   
REMARK 500    ASN A 424     -167.78    -79.09                                   
REMARK 500    GLU A 453       69.24   -119.08                                   
REMARK 500    ALA A 473       62.08     39.91                                   
REMARK 500    THR A 534      156.27     77.07                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A1449                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1611                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1M6I   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF APOPTOSIS INDUCING FACTOR (AIF)                
REMARK 900 RELATED ID: 4BUR   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE REDUCED HUMAN APOPTOSIS                    
REMARK 900  INDUCING FACTOR COMPLEXED WITH NAD                                  
DBREF  4BV6 A  121   613  UNP    O95831   AIFM1_HUMAN    121    613             
SEQRES   1 A  493  GLU GLU VAL PRO GLN ASP LYS ALA PRO SER HIS VAL PRO          
SEQRES   2 A  493  PHE LEU LEU ILE GLY GLY GLY THR ALA ALA PHE ALA ALA          
SEQRES   3 A  493  ALA ARG SER ILE ARG ALA ARG ASP PRO GLY ALA ARG VAL          
SEQRES   4 A  493  LEU ILE VAL SER GLU ASP PRO GLU LEU PRO TYR MET ARG          
SEQRES   5 A  493  PRO PRO LEU SER LYS GLU LEU TRP PHE SER ASP ASP PRO          
SEQRES   6 A  493  ASN VAL THR LYS THR LEU ARG PHE LYS GLN TRP ASN GLY          
SEQRES   7 A  493  LYS GLU ARG SER ILE TYR PHE GLN PRO PRO SER PHE TYR          
SEQRES   8 A  493  VAL SER ALA GLN ASP LEU PRO HIS ILE GLU ASN GLY GLY          
SEQRES   9 A  493  VAL ALA VAL LEU THR GLY LYS LYS VAL VAL GLN LEU ASP          
SEQRES  10 A  493  VAL ARG ASP ASN MET VAL LYS LEU ASN ASP GLY SER GLN          
SEQRES  11 A  493  ILE THR TYR GLU LYS CYS LEU ILE ALA THR GLY GLY THR          
SEQRES  12 A  493  PRO ARG SER LEU SER ALA ILE ASP ARG ALA GLY ALA GLU          
SEQRES  13 A  493  VAL LYS SER ARG THR THR LEU PHE ARG LYS ILE GLY ASP          
SEQRES  14 A  493  PHE ARG SER LEU GLU LYS ILE SER ARG GLU VAL LYS SER          
SEQRES  15 A  493  ILE THR ILE ILE GLY GLY GLY PHE LEU GLY SER GLU LEU          
SEQRES  16 A  493  ALA CYS ALA LEU GLY ARG LYS ALA ARG ALA LEU GLY THR          
SEQRES  17 A  493  GLU VAL ILE GLN LEU PHE PRO GLU LYS GLY ASN MET GLY          
SEQRES  18 A  493  LYS ILE LEU PRO GLU TYR LEU SER ASN TRP THR MET GLU          
SEQRES  19 A  493  LYS VAL ARG ARG GLU GLY VAL LYS VAL MET PRO ASN ALA          
SEQRES  20 A  493  ILE VAL GLN SER VAL GLY VAL SER SER GLY LYS LEU LEU          
SEQRES  21 A  493  ILE LYS LEU LYS ASP GLY ARG LYS VAL GLU THR ASP HIS          
SEQRES  22 A  493  ILE VAL ALA ALA VAL GLY LEU GLU PRO ASN VAL GLU LEU          
SEQRES  23 A  493  ALA LYS THR GLY GLY LEU GLU ILE ASP SER ASP PHE GLY          
SEQRES  24 A  493  GLY PHE ARG VAL ASN ALA GLU LEU GLN ALA ARG SER ASN          
SEQRES  25 A  493  ILE TRP VAL ALA GLY ASP ALA ALA CYS PHE TYR ASP ILE          
SEQRES  26 A  493  LYS LEU GLY ARG ARG ARG VAL GLU HIS HIS ASP HIS ALA          
SEQRES  27 A  493  VAL VAL SER GLY ARG LEU ALA GLY GLU ASN MET THR GLY          
SEQRES  28 A  493  ALA ALA LYS PRO TYR TRP HIS GLN SER MET PHE TRP SER          
SEQRES  29 A  493  ASP LEU GLY PRO ASP VAL GLY TYR GLU ALA ILE GLY LEU          
SEQRES  30 A  493  VAL ASP SER SER LEU PRO THR VAL GLY VAL PHE ALA LYS          
SEQRES  31 A  493  ALA THR ALA GLN ASP ASN PRO LYS SER ALA THR GLU GLN          
SEQRES  32 A  493  SER GLY THR GLY ILE ARG SER GLU SER GLU THR GLU SER          
SEQRES  33 A  493  GLU ALA SER GLU ILE THR ILE PRO PRO SER THR PRO ALA          
SEQRES  34 A  493  VAL PRO GLN ALA PRO VAL GLN GLY GLU ASP TYR GLY LYS          
SEQRES  35 A  493  GLY VAL ILE PHE TYR LEU ARG ASP LYS VAL VAL VAL GLY          
SEQRES  36 A  493  ILE VAL LEU TRP ASN ILE PHE ASN ARG MET PRO ILE ALA          
SEQRES  37 A  493  ARG LYS ILE ILE LYS ASP GLY GLU GLN HIS GLU ASP LEU          
SEQRES  38 A  493  ASN GLU VAL ALA LYS LEU PHE ASN ILE HIS GLU ASP              
HET    FAD  A1449      53                                                       
HET    GOL  A1611       6                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  FAD    C27 H33 N9 O15 P2                                            
FORMUL   3  GOL    C3 H8 O3                                                     
FORMUL   4  HOH   *289(H2 O)                                                    
HELIX    1   1 GLY A  140  ASP A  154  1                                  15    
HELIX    2   2 ARG A  172  LYS A  177  5                                   6    
HELIX    3   3 LYS A  177  PHE A  181  5                                   5    
HELIX    4   4 ASN A  186  LEU A  191  1                                   6    
HELIX    5   5 PRO A  207  TYR A  211  5                                   5    
HELIX    6   6 LEU A  267  ARG A  272  1                                   6    
HELIX    7   7 GLY A  274  ARG A  280  1                                   7    
HELIX    8   8 LYS A  286  VAL A  300  1                                  15    
HELIX    9   9 GLY A  309  GLY A  327  1                                  19    
HELIX   10  10 PRO A  345  GLU A  359  1                                  15    
HELIX   11  11 LEU A  406  GLY A  411  1                                   6    
HELIX   12  12 HIS A  454  THR A  470  1                                  17    
HELIX   13  13 ASN A  516  GLY A  525  1                                  10    
HELIX   14  14 ILE A  528  GLU A  533  1                                   6    
HELIX   15  15 ARG A  584  GLY A  595  1                                  12    
HELIX   16  16 ASP A  600  ALA A  605  1                                   6    
HELIX   17  17 LYS A  606  ASN A  609  5                                   4    
SHEET    1  AA 6 GLY A 224  THR A 229  0                                        
SHEET    2  AA 6 ARG A 158  SER A 163  1  O  VAL A 159   N  ALA A 226           
SHEET    3  AA 6 HIS A 131  ILE A 137  1  O  PHE A 134   N  LEU A 160           
SHEET    4  AA 6 GLN A 250  ILE A 258  1  O  THR A 252   N  VAL A 132           
SHEET    5  AA 6 ILE A 433  VAL A 435  1  O  TRP A 434   N  ILE A 258           
SHEET    6  AA 6 GLN A 428  ARG A 430 -1  N  ALA A 429   O  ILE A 433           
SHEET    1  AB 6 GLY A 224  THR A 229  0                                        
SHEET    2  AB 6 ARG A 158  SER A 163  1  O  VAL A 159   N  ALA A 226           
SHEET    3  AB 6 HIS A 131  ILE A 137  1  O  PHE A 134   N  LEU A 160           
SHEET    4  AB 6 GLN A 250  ILE A 258  1  O  THR A 252   N  VAL A 132           
SHEET    5  AB 6 MET A 242  LEU A 245 -1  O  VAL A 243   N  ILE A 251           
SHEET    6  AB 6 VAL A 233  ASP A 237  1  N  VAL A 234   O  LYS A 244           
SHEET    1  AC 2 ARG A 192  LYS A 194  0                                        
SHEET    2  AC 2 GLU A 200  SER A 202 -1  O  ARG A 201   N  PHE A 193           
SHEET    1  AD 2 GLY A 262  PRO A 264  0                                        
SHEET    2  AD 2 LEU A 400  PRO A 402 -1  O  GLU A 401   N  THR A 263           
SHEET    1  AE 5 THR A 281  LEU A 283  0                                        
SHEET    2  AE 5 HIS A 393  ALA A 396  1  O  ILE A 394   N  THR A 282           
SHEET    3  AE 5 SER A 302  ILE A 306  1  O  THR A 304   N  VAL A 395           
SHEET    4  AE 5 GLU A 329  LEU A 333  1  O  GLU A 329   N  ILE A 303           
SHEET    5  AE 5 LYS A 362  MET A 364  1  O  LYS A 362   N  GLN A 332           
SHEET    1  AF 3 VAL A 369  SER A 375  0                                        
SHEET    2  AF 3 LYS A 378  LEU A 383 -1  O  LYS A 378   N  SER A 375           
SHEET    3  AF 3 LYS A 388  THR A 391 -1  O  VAL A 389   N  ILE A 381           
SHEET    1  AG 3 PHE A 421  ARG A 422  0                                        
SHEET    2  AG 3 ALA A 440  ASP A 444  1  N  CYS A 441   O  PHE A 421           
SHEET    3  AG 3 GLY A 448  ARG A 450 -1  O  GLY A 448   N  ASP A 444           
SHEET    1  AH 5 MET A 481  GLY A 487  0                                        
SHEET    2  AH 5 VAL A 490  GLY A 496 -1  O  VAL A 490   N  LEU A 486           
SHEET    3  AH 5 VAL A 572  TRP A 579 -1  O  ILE A 576   N  ILE A 495           
SHEET    4  AH 5 LYS A 562  ARG A 569 -1  O  GLY A 563   N  TRP A 579           
SHEET    5  AH 5 THR A 504  ALA A 509 -1  O  VAL A 505   N  PHE A 566           
SITE     1 AC1 34 GLY A 138  GLY A 139  GLY A 140  THR A 141                    
SITE     2 AC1 34 ALA A 142  VAL A 162  GLU A 164  ASP A 165                    
SITE     3 AC1 34 ARG A 172  PRO A 173  SER A 176  LYS A 177                    
SITE     4 AC1 34 LYS A 231  LYS A 232  VAL A 233  ALA A 259                    
SITE     5 AC1 34 THR A 260  GLY A 261  ARG A 285  GLY A 437                    
SITE     6 AC1 34 ASP A 438  GLU A 453  HIS A 454  HIS A 455                    
SITE     7 AC1 34 ALA A 458  PHE A 482  TRP A 483  HOH A2011                    
SITE     8 AC1 34 HOH A2012  HOH A2014  HOH A2094  HOH A2095                    
SITE     9 AC1 34 HOH A2232  HOH A2287                                          
SITE     1 AC2  7 PHE A 310  ILE A 343  HIS A 454  PHE A 482                    
SITE     2 AC2  7 HOH A2227  HOH A2228  HOH A2231                               
CRYST1   50.900   90.500   60.500  90.00  94.60  90.00 P 1 21 1      2          
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      0.019646  0.000000  0.001581        0.00000                         
SCALE2      0.000000  0.011050  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016582        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system