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Database: PDB
Entry: 5FS6
LinkDB: 5FS6
Original site: 5FS6 
HEADER    OXIDOREDUCTASE                          30-DEC-15   5FS6              
TITLE     CRYSTAL STRUCTURE OF THE V243L MUTANT OF HUMAN APOPTOSIS              
TITLE    2 INDUCING FACTOR                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: APOPTOSIS-INDUCING FACTOR 1, MITOCHONDRIAL;                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 103-613;                        
COMPND   5 SYNONYM: PROGRAMMED CELL DEATH PROTEIN 8, APOPTOSIS INDUCING FACTOR; 
COMPND   6 EC: 1.1.1.-;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 OTHER_DETAILS: RESIDUES 522-558 IN CHAIN A AND 523-558 IN CHAIN B    
COMPND  10  ARE DISORDERED. BOTH CHAINS HAVE ADDITIONAL C-TERMINAL RESIDUES     
COMPND  11  L614-V615-P616-R617, PART OF THE THROMBIN CLEAVAGE SITE. RESIDUES   
COMPND  12  614-617 ARE DISORDERED IN CHAIN B.                                  
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PKK233-3                                   
KEYWDS    OXIDOREDUCTASE, MITOCHONDRIA, FLAVOPROTEIN                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.SEVRIOUKOVA                                                         
REVDAT   4   28-SEP-16 5FS6    1       JRNL                                     
REVDAT   3   25-MAY-16 5FS6    1       JRNL                                     
REVDAT   2   18-MAY-16 5FS6    1       JRNL                                     
REVDAT   1   11-MAY-16 5FS6    0                                                
JRNL        AUTH   I.SEVRIOUKOVA                                                
JRNL        TITL   STRUCTURE/FUNCTION RELATIONS IN AIFM1 VARIANTS ASSOCIATED    
JRNL        TITL 2 WITH NEURODEGENERATIVE DISORDERS                             
JRNL        REF    J.MOL.BIOL.                   V. 428  3650 2016              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   27178839                                                     
JRNL        DOI    10.1016/J.JMB.2016.05.004                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,                      
REMARK   3                 STEINER,NICHOLLS,WINN,LONG,VAGIN                     
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 121.26                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.19                          
REMARK   3   NUMBER OF REFLECTIONS             : 94198                          
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) : 0.17380                         
REMARK   3   R VALUE            (WORKING SET) : 0.17206                         
REMARK   3   FREE R VALUE                     : 0.20689                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 4956                            
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) : 1.900                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.949                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6748                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.23                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.307                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 349                          
REMARK   3   BIN FREE R VALUE                    : 0.323                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7157                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 122                                     
REMARK   3   SOLVENT ATOMS            : 908                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.855                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.02                                                
REMARK   3    B22 (A**2) : -0.10                                                
REMARK   3    B33 (A**2) : 0.12                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.122         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.118         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.090         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.140         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.950                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7458 ; 0.012 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  7277 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10140 ; 1.609 ; 1.984       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 16772 ; 0.786 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   958 ; 6.017 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   317 ;31.204 ;23.375       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1305 ;14.286 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    61 ;18.816 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1120 ; 0.141 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8398 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1689 ; 0.001 ; 0.020       
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):  3687 ; 1.419 ; 2.036       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3684 ; 1.418 ; 2.034       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4617 ; 2.255 ; 3.036       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3771 ; 1.999 ; 2.324       
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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   127        A  1000                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.6547   7.8773 -42.6058              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0056 T22:   0.0075                                     
REMARK   3      T33:   0.0235 T12:  -0.0034                                     
REMARK   3      T13:   0.0024 T23:  -0.0035                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1463 L22:   0.6582                                     
REMARK   3      L33:   0.4998 L12:   0.0008                                     
REMARK   3      L13:   0.0159 L23:  -0.0438                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0122 S12:  -0.0618 S13:   0.0729                       
REMARK   3      S21:  -0.0092 S22:  -0.0145 S23:  -0.0689                       
REMARK   3      S31:   0.0060 S32:   0.0305 S33:   0.0023                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   126        B  7001                          
REMARK   3    ORIGIN FOR THE GROUP (A): -41.6558 -15.0735 -32.6738              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0189 T22:   0.0037                                     
REMARK   3      T33:   0.0176 T12:  -0.0044                                     
REMARK   3      T13:  -0.0016 T23:  -0.0017                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7534 L22:   1.0963                                     
REMARK   3      L33:   0.7904 L12:   0.0915                                     
REMARK   3      L13:   0.0707 L23:  -0.1882                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0028 S12:   0.0057 S13:  -0.0914                       
REMARK   3      S21:  -0.0422 S22:   0.0279 S23:   0.0528                       
REMARK   3      S31:   0.1191 S32:  -0.0186 S33:  -0.0251                       
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   4                                                                      
REMARK   4 5FS6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-JAN-16.                  
REMARK 100 THE PDBE ID CODE IS EBI-65914.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-AUG-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (MARMOSAIC 325)                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 99250                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.90                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 83.20                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 4.2                                
REMARK 200  R MERGE                    (I) : 0.12                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.40                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.0                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.79                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.60                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 5FS8                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.3                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 0.1M             
REMARK 280  HEPES, PH 7.5, AND 20% POLY-ETHYLENE GLYCOL 3350                    
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       45.42000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       60.63000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.19000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       60.63000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       45.42000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       57.19000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   103                                                      
REMARK 465     LEU A   104                                                      
REMARK 465     THR A   105                                                      
REMARK 465     PRO A   106                                                      
REMARK 465     GLU A   107                                                      
REMARK 465     GLN A   108                                                      
REMARK 465     LYS A   109                                                      
REMARK 465     GLN A   110                                                      
REMARK 465     LYS A   111                                                      
REMARK 465     LYS A   112                                                      
REMARK 465     ALA A   113                                                      
REMARK 465     ALA A   114                                                      
REMARK 465     LEU A   115                                                      
REMARK 465     SER A   116                                                      
REMARK 465     ALA A   117                                                      
REMARK 465     SER A   118                                                      
REMARK 465     GLU A   119                                                      
REMARK 465     GLY A   120                                                      
REMARK 465     GLU A   121                                                      
REMARK 465     GLU A   122                                                      
REMARK 465     VAL A   123                                                      
REMARK 465     PRO A   124                                                      
REMARK 465     GLN A   125                                                      
REMARK 465     ASP A   126                                                      
REMARK 465     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     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     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   613                                                      
REMARK 465     LEU B   614                                                      
REMARK 465     VAL B   615                                                      
REMARK 465     PRO B   616                                                      
REMARK 465     ARG B   617                                                      
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   OE2A GLU A   167     O    HOH A  2037              2.08            
REMARK 500   NH1B ARG B   321     O    HOH B  2226              2.10            
REMARK 500   O    HOH A  2066     O    HOH A  2077              2.19            
REMARK 500   O    HOH A  2121     O    HOH A  2243              2.00            
REMARK 500   O    HOH A  2434     O    HOH A  2435              2.20            
REMARK 500   O    HOH B  2148     O    HOH B  2149              2.07            
REMARK 500   O    HOH B  2172     O    HOH B  2173              2.04            
REMARK 500   O    HOH B  2195     O    HOH B  2196              2.19            
REMARK 500   O    HOH B  2226     O    HOH B  2227              2.09            
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 B  2029     O    HOH B  2273     3454     2.19            
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     -101.67   -138.25                                   
REMARK 500    ARG A 285      -29.16   -151.57                                   
REMARK 500    ALA A 397       76.62   -117.55                                   
REMARK 500    ALA A 473       58.11     37.68                                   
REMARK 500    TRP A 477      -64.28   -132.12                                   
REMARK 500    LEU A 486       72.12   -100.44                                   
REMARK 500    LYS B 177      -99.81   -135.39                                   
REMARK 500    SER B 266     -168.01   -107.06                                   
REMARK 500    ARG B 285      -28.08   -150.28                                   
REMARK 500    SER B 375      -86.95   -122.10                                   
REMARK 500    SER B 376       37.17    -88.77                                   
REMARK 500    TRP B 477      -57.82   -141.02                                   
REMARK 500    LEU B 486       66.36   -101.79                                   
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 A1000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B1000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS B7000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS B7001                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5FS7   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE G262S MUTANT OF HUMAN                      
REMARK 900  APOPTOSIS INDUCING FACTOR                                           
REMARK 900 RELATED ID: 5FS8   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE G308E MUTANT OF HUMAN                      
REMARK 900  APOPTOSIS INDUCING FACTOR                                           
REMARK 900 RELATED ID: 5FS9   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE G338E MUTANT OF HUMAN                      
REMARK 900  APOPTOSIS INDUCING FACTOR                                           
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 4 ADDITIONAL RESIDUES AT THE C-TERMINUS ARE PART OF THE              
REMARK 999 THROMBIN CLEAVAGE SITE                                               
REMARK 999 4 ADDITIONAL RESIDUES AT THE C-TERMINUS ARE PART OF THE              
REMARK 999 THROMBIN CLEAVAGE SITE                                               
DBREF  5FS6 A  103   613  UNP    O95831   AIFM1_HUMAN    103    613             
DBREF  5FS6 B  103   613  UNP    O95831   AIFM1_HUMAN    103    613             
SEQADV 5FS6 LEU A  614  UNP  O95831              EXPRESSION TAG                 
SEQADV 5FS6 VAL A  615  UNP  O95831              EXPRESSION TAG                 
SEQADV 5FS6 PRO A  616  UNP  O95831              EXPRESSION TAG                 
SEQADV 5FS6 ARG A  617  UNP  O95831              EXPRESSION TAG                 
SEQADV 5FS6 LEU A  243  UNP  O95831    VAL   243 ENGINEERED MUTATION            
SEQADV 5FS6 LEU B  614  UNP  O95831              EXPRESSION TAG                 
SEQADV 5FS6 VAL B  615  UNP  O95831              EXPRESSION TAG                 
SEQADV 5FS6 PRO B  616  UNP  O95831              EXPRESSION TAG                 
SEQADV 5FS6 ARG B  617  UNP  O95831              EXPRESSION TAG                 
SEQADV 5FS6 LEU B  243  UNP  O95831    VAL   243 ENGINEERED MUTATION            
SEQRES   1 A  515  GLY LEU THR PRO GLU GLN LYS GLN LYS LYS ALA ALA LEU          
SEQRES   2 A  515  SER ALA SER GLU GLY GLU GLU VAL PRO GLN ASP LYS ALA          
SEQRES   3 A  515  PRO SER HIS VAL PRO PHE LEU LEU ILE GLY GLY GLY THR          
SEQRES   4 A  515  ALA ALA PHE ALA ALA ALA ARG SER ILE ARG ALA ARG ASP          
SEQRES   5 A  515  PRO GLY ALA ARG VAL LEU ILE VAL SER GLU ASP PRO GLU          
SEQRES   6 A  515  LEU PRO TYR MET ARG PRO PRO LEU SER LYS GLU LEU TRP          
SEQRES   7 A  515  PHE SER ASP ASP PRO ASN VAL THR LYS THR LEU ARG PHE          
SEQRES   8 A  515  LYS GLN TRP ASN GLY LYS GLU ARG SER ILE TYR PHE GLN          
SEQRES   9 A  515  PRO PRO SER PHE TYR VAL SER ALA GLN ASP LEU PRO HIS          
SEQRES  10 A  515  ILE GLU ASN GLY GLY VAL ALA VAL LEU THR GLY LYS LYS          
SEQRES  11 A  515  VAL VAL GLN LEU ASP VAL ARG ASP ASN MET LEU LYS LEU          
SEQRES  12 A  515  ASN ASP GLY SER GLN ILE THR TYR GLU LYS CYS LEU ILE          
SEQRES  13 A  515  ALA THR GLY GLY THR PRO ARG SER LEU SER ALA ILE ASP          
SEQRES  14 A  515  ARG ALA GLY ALA GLU VAL LYS SER ARG THR THR LEU PHE          
SEQRES  15 A  515  ARG LYS ILE GLY ASP PHE ARG SER LEU GLU LYS ILE SER          
SEQRES  16 A  515  ARG GLU VAL LYS SER ILE THR ILE ILE GLY GLY GLY PHE          
SEQRES  17 A  515  LEU GLY SER GLU LEU ALA CYS ALA LEU GLY ARG LYS ALA          
SEQRES  18 A  515  ARG ALA LEU GLY THR GLU VAL ILE GLN LEU PHE PRO GLU          
SEQRES  19 A  515  LYS GLY ASN MET GLY LYS ILE LEU PRO GLU TYR LEU SER          
SEQRES  20 A  515  ASN TRP THR MET GLU LYS VAL ARG ARG GLU GLY VAL LYS          
SEQRES  21 A  515  VAL MET PRO ASN ALA ILE VAL GLN SER VAL GLY VAL SER          
SEQRES  22 A  515  SER GLY LYS LEU LEU ILE LYS LEU LYS ASP GLY ARG LYS          
SEQRES  23 A  515  VAL GLU THR ASP HIS ILE VAL ALA ALA VAL GLY LEU GLU          
SEQRES  24 A  515  PRO ASN VAL GLU LEU ALA LYS THR GLY GLY LEU GLU ILE          
SEQRES  25 A  515  ASP SER ASP PHE GLY GLY PHE ARG VAL ASN ALA GLU LEU          
SEQRES  26 A  515  GLN ALA ARG SER ASN ILE TRP VAL ALA GLY ASP ALA ALA          
SEQRES  27 A  515  CYS PHE TYR ASP ILE LYS LEU GLY ARG ARG ARG VAL GLU          
SEQRES  28 A  515  HIS HIS ASP HIS ALA VAL VAL SER GLY ARG LEU ALA GLY          
SEQRES  29 A  515  GLU ASN MET THR GLY ALA ALA LYS PRO TYR TRP HIS GLN          
SEQRES  30 A  515  SER MET PHE TRP SER ASP LEU GLY PRO ASP VAL GLY TYR          
SEQRES  31 A  515  GLU ALA ILE GLY LEU VAL ASP SER SER LEU PRO THR VAL          
SEQRES  32 A  515  GLY VAL PHE ALA LYS ALA THR ALA GLN ASP ASN PRO LYS          
SEQRES  33 A  515  SER ALA THR GLU GLN SER GLY THR GLY ILE ARG SER GLU          
SEQRES  34 A  515  SER GLU THR GLU SER GLU ALA SER GLU ILE THR ILE PRO          
SEQRES  35 A  515  PRO SER THR PRO ALA VAL PRO GLN ALA PRO VAL GLN GLY          
SEQRES  36 A  515  GLU ASP TYR GLY LYS GLY VAL ILE PHE TYR LEU ARG ASP          
SEQRES  37 A  515  LYS VAL VAL VAL GLY ILE VAL LEU TRP ASN ILE PHE ASN          
SEQRES  38 A  515  ARG MET PRO ILE ALA ARG LYS ILE ILE LYS ASP GLY GLU          
SEQRES  39 A  515  GLN HIS GLU ASP LEU ASN GLU VAL ALA LYS LEU PHE ASN          
SEQRES  40 A  515  ILE HIS GLU ASP LEU VAL PRO ARG                              
SEQRES   1 B  515  GLY LEU THR PRO GLU GLN LYS GLN LYS LYS ALA ALA LEU          
SEQRES   2 B  515  SER ALA SER GLU GLY GLU GLU VAL PRO GLN ASP LYS ALA          
SEQRES   3 B  515  PRO SER HIS VAL PRO PHE LEU LEU ILE GLY GLY GLY THR          
SEQRES   4 B  515  ALA ALA PHE ALA ALA ALA ARG SER ILE ARG ALA ARG ASP          
SEQRES   5 B  515  PRO GLY ALA ARG VAL LEU ILE VAL SER GLU ASP PRO GLU          
SEQRES   6 B  515  LEU PRO TYR MET ARG PRO PRO LEU SER LYS GLU LEU TRP          
SEQRES   7 B  515  PHE SER ASP ASP PRO ASN VAL THR LYS THR LEU ARG PHE          
SEQRES   8 B  515  LYS GLN TRP ASN GLY LYS GLU ARG SER ILE TYR PHE GLN          
SEQRES   9 B  515  PRO PRO SER PHE TYR VAL SER ALA GLN ASP LEU PRO HIS          
SEQRES  10 B  515  ILE GLU ASN GLY GLY VAL ALA VAL LEU THR GLY LYS LYS          
SEQRES  11 B  515  VAL VAL GLN LEU ASP VAL ARG ASP ASN MET LEU LYS LEU          
SEQRES  12 B  515  ASN ASP GLY SER GLN ILE THR TYR GLU LYS CYS LEU ILE          
SEQRES  13 B  515  ALA THR GLY GLY THR PRO ARG SER LEU SER ALA ILE ASP          
SEQRES  14 B  515  ARG ALA GLY ALA GLU VAL LYS SER ARG THR THR LEU PHE          
SEQRES  15 B  515  ARG LYS ILE GLY ASP PHE ARG SER LEU GLU LYS ILE SER          
SEQRES  16 B  515  ARG GLU VAL LYS SER ILE THR ILE ILE GLY GLY GLY PHE          
SEQRES  17 B  515  LEU GLY SER GLU LEU ALA CYS ALA LEU GLY ARG LYS ALA          
SEQRES  18 B  515  ARG ALA LEU GLY THR GLU VAL ILE GLN LEU PHE PRO GLU          
SEQRES  19 B  515  LYS GLY ASN MET GLY LYS ILE LEU PRO GLU TYR LEU SER          
SEQRES  20 B  515  ASN TRP THR MET GLU LYS VAL ARG ARG GLU GLY VAL LYS          
SEQRES  21 B  515  VAL MET PRO ASN ALA ILE VAL GLN SER VAL GLY VAL SER          
SEQRES  22 B  515  SER GLY LYS LEU LEU ILE LYS LEU LYS ASP GLY ARG LYS          
SEQRES  23 B  515  VAL GLU THR ASP HIS ILE VAL ALA ALA VAL GLY LEU GLU          
SEQRES  24 B  515  PRO ASN VAL GLU LEU ALA LYS THR GLY GLY LEU GLU ILE          
SEQRES  25 B  515  ASP SER ASP PHE GLY GLY PHE ARG VAL ASN ALA GLU LEU          
SEQRES  26 B  515  GLN ALA ARG SER ASN ILE TRP VAL ALA GLY ASP ALA ALA          
SEQRES  27 B  515  CYS PHE TYR ASP ILE LYS LEU GLY ARG ARG ARG VAL GLU          
SEQRES  28 B  515  HIS HIS ASP HIS ALA VAL VAL SER GLY ARG LEU ALA GLY          
SEQRES  29 B  515  GLU ASN MET THR GLY ALA ALA LYS PRO TYR TRP HIS GLN          
SEQRES  30 B  515  SER MET PHE TRP SER ASP LEU GLY PRO ASP VAL GLY TYR          
SEQRES  31 B  515  GLU ALA ILE GLY LEU VAL ASP SER SER LEU PRO THR VAL          
SEQRES  32 B  515  GLY VAL PHE ALA LYS ALA THR ALA GLN ASP ASN PRO LYS          
SEQRES  33 B  515  SER ALA THR GLU GLN SER GLY THR GLY ILE ARG SER GLU          
SEQRES  34 B  515  SER GLU THR GLU SER GLU ALA SER GLU ILE THR ILE PRO          
SEQRES  35 B  515  PRO SER THR PRO ALA VAL PRO GLN ALA PRO VAL GLN GLY          
SEQRES  36 B  515  GLU ASP TYR GLY LYS GLY VAL ILE PHE TYR LEU ARG ASP          
SEQRES  37 B  515  LYS VAL VAL VAL GLY ILE VAL LEU TRP ASN ILE PHE ASN          
SEQRES  38 B  515  ARG MET PRO ILE ALA ARG LYS ILE ILE LYS ASP GLY GLU          
SEQRES  39 B  515  GLN HIS GLU ASP LEU ASN GLU VAL ALA LYS LEU PHE ASN          
SEQRES  40 B  515  ILE HIS GLU ASP LEU VAL PRO ARG                              
HET    FAD  A1000      53                                                       
HET    FAD  B1000      53                                                       
HET    TRS  B7000       8                                                       
HET    TRS  B7001       8                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETSYN     TRS TRIS BUFFER                                                      
FORMUL   3  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL   5  TRS    2(C4 H12 N O3 1+)                                            
FORMUL   7  HOH   *908(H2 O)                                                    
HELIX    1   1 GLY A  140  ASP A  154  1                                  15    
HELIX    2   2 ARG A  172  SER A  176  5                                   5    
HELIX    3   3 LYS A  177  SER A  182  1                                   6    
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 VAL A  238  ASP A  240  5                                   3    
HELIX    7   7 LEU A  267  ALA A  273  1                                   7    
HELIX    8   8 GLY A  274  ARG A  280  1                                   7    
HELIX    9   9 LYS A  286  VAL A  300  1                                  15    
HELIX   10  10 GLY A  309  GLY A  327  1                                  19    
HELIX   11  11 PRO A  345  GLU A  359  1                                  15    
HELIX   12  12 LEU A  406  GLY A  411  1                                   6    
HELIX   13  13 HIS A  454  MET A  469  1                                  16    
HELIX   14  14 ARG A  584  GLY A  595  1                                  12    
HELIX   15  15 ASP A  600  ALA A  605  1                                   6    
HELIX   16  16 LYS A  606  ASN A  609  5                                   4    
HELIX   17  17 GLY B  140  ASP B  154  1                                  15    
HELIX   18  18 ARG B  172  LYS B  177  5                                   6    
HELIX   19  19 LYS B  177  PHE B  181  5                                   5    
HELIX   20  20 ASN B  186  LEU B  191  1                                   6    
HELIX   21  21 PRO B  207  TYR B  211  5                                   5    
HELIX   22  22 LEU B  267  ALA B  273  1                                   7    
HELIX   23  23 GLY B  274  ARG B  280  1                                   7    
HELIX   24  24 LYS B  286  VAL B  300  1                                  15    
HELIX   25  25 GLY B  309  GLY B  327  1                                  19    
HELIX   26  26 PRO B  345  GLU B  359  1                                  15    
HELIX   27  27 LEU B  406  GLY B  411  1                                   6    
HELIX   28  28 HIS B  454  MET B  469  1                                  16    
HELIX   29  29 LYS B  518  GLU B  522  5                                   5    
HELIX   30  30 ARG B  584  GLY B  595  1                                  12    
HELIX   31  31 ASP B  600  LYS B  606  1                                   7    
HELIX   32  32 LEU B  607  ASN B  609  5                                   3    
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  LEU A 243   N  ILE A 251           
SHEET    6  AB 6 VAL A 233  ASP A 237  1  N  VAL A 234   O  LYS A 244           
SHEET    1  AC 2 ARG A 192  LYS A 194  0                                        
SHEET    2  AC 2 GLU A 200  SER A 202 -1  O  ARG A 201   N  PHE A 193           
SHEET    1  AD 2 GLY A 262  PRO A 264  0                                        
SHEET    2  AD 2 LEU A 400  PRO A 402 -1  O  GLU A 401   N  THR A 263           
SHEET    1  AE 5 THR A 281  THR A 282  0                                        
SHEET    2  AE 5 HIS A 393  ALA A 396  1  O  ILE A 394   N  THR A 282           
SHEET    3  AE 5 SER A 302  ILE A 306  1  O  THR A 304   N  VAL A 395           
SHEET    4  AE 5 GLU A 329  LEU A 333  1  O  GLU A 329   N  ILE A 303           
SHEET    5  AE 5 LYS A 362  MET A 364  1  O  LYS A 362   N  GLN A 332           
SHEET    1  AF 3 VAL A 369  SER A 375  0                                        
SHEET    2  AF 3 LYS A 378  LEU A 383 -1  O  LYS A 378   N  SER A 375           
SHEET    3  AF 3 LYS A 388  THR A 391 -1  O  VAL A 389   N  ILE A 381           
SHEET    1  AG 3 PHE A 421  ARG A 422  0                                        
SHEET    2  AG 3 ALA A 440  ASP A 444  1  N  CYS A 441   O  PHE A 421           
SHEET    3  AG 3 GLY A 448  ARG A 451 -1  O  GLY A 448   N  ASP A 444           
SHEET    1  AH 5 MET A 481  ASP A 485  0                                        
SHEET    2  AH 5 GLY A 491  GLY A 496 -1  O  TYR A 492   N  SER A 484           
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           
SHEET    1  BA 6 GLY B 224  THR B 229  0                                        
SHEET    2  BA 6 ARG B 158  SER B 163  1  O  VAL B 159   N  ALA B 226           
SHEET    3  BA 6 HIS B 131  ILE B 137  1  O  PHE B 134   N  LEU B 160           
SHEET    4  BA 6 GLN B 250  ILE B 258  1  O  THR B 252   N  VAL B 132           
SHEET    5  BA 6 ILE B 433  VAL B 435  1  O  TRP B 434   N  ILE B 258           
SHEET    6  BA 6 GLN B 428  ARG B 430 -1  N  ALA B 429   O  ILE B 433           
SHEET    1  BB 6 GLY B 224  THR B 229  0                                        
SHEET    2  BB 6 ARG B 158  SER B 163  1  O  VAL B 159   N  ALA B 226           
SHEET    3  BB 6 HIS B 131  ILE B 137  1  O  PHE B 134   N  LEU B 160           
SHEET    4  BB 6 GLN B 250  ILE B 258  1  O  THR B 252   N  VAL B 132           
SHEET    5  BB 6 MET B 242  LEU B 245 -1  O  LEU B 243   N  ILE B 251           
SHEET    6  BB 6 VAL B 233  ASP B 237  1  N  VAL B 234   O  LYS B 244           
SHEET    1  BC 2 ARG B 192  LYS B 194  0                                        
SHEET    2  BC 2 GLU B 200  SER B 202 -1  O  ARG B 201   N  PHE B 193           
SHEET    1  BD 2 GLY B 262  PRO B 264  0                                        
SHEET    2  BD 2 LEU B 400  PRO B 402 -1  O  GLU B 401   N  THR B 263           
SHEET    1  BE 5 THR B 281  LEU B 283  0                                        
SHEET    2  BE 5 HIS B 393  ALA B 396  1  O  ILE B 394   N  THR B 282           
SHEET    3  BE 5 SER B 302  ILE B 306  1  O  THR B 304   N  VAL B 395           
SHEET    4  BE 5 GLU B 329  LEU B 333  1  O  GLU B 329   N  ILE B 303           
SHEET    5  BE 5 LYS B 362  MET B 364  1  O  LYS B 362   N  GLN B 332           
SHEET    1  BF 3 VAL B 369  VAL B 374  0                                        
SHEET    2  BF 3 LEU B 379  LEU B 383 -1  O  LEU B 380   N  GLY B 373           
SHEET    3  BF 3 LYS B 388  THR B 391 -1  O  VAL B 389   N  ILE B 381           
SHEET    1  BG 3 PHE B 421  ARG B 422  0                                        
SHEET    2  BG 3 ALA B 440  ASP B 444  1  N  CYS B 441   O  PHE B 421           
SHEET    3  BG 3 GLY B 448  ARG B 451 -1  O  GLY B 448   N  ASP B 444           
SHEET    1  BH 5 MET B 481  ASP B 485  0                                        
SHEET    2  BH 5 GLY B 491  GLY B 496 -1  O  TYR B 492   N  SER B 484           
SHEET    3  BH 5 VAL B 572  TRP B 579 -1  O  ILE B 576   N  ILE B 495           
SHEET    4  BH 5 LYS B 562  ARG B 569 -1  O  GLY B 563   N  TRP B 579           
SHEET    5  BH 5 THR B 504  ALA B 509 -1  O  VAL B 505   N  PHE B 566           
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  PHE A 284  ARG A 285  LYS A 286                    
SITE     6 AC1 39 LEU A 311  GLY A 437  ASP A 438  GLU A 453                    
SITE     7 AC1 39 HIS A 454  HIS A 455  ALA A 458  PHE A 482                    
SITE     8 AC1 39 TRP A 483  HOH A2008  HOH A2009  HOH A2013                    
SITE     9 AC1 39 HOH A2015  HOH A2137  HOH A2138  HOH A2214                    
SITE    10 AC1 39 HOH A2215  HOH A2299  HOH A2362                               
SITE     1 AC2 39 GLY B 138  GLY B 139  GLY B 140  THR B 141                    
SITE     2 AC2 39 ALA B 142  VAL B 162  GLU B 164  ASP B 165                    
SITE     3 AC2 39 ARG B 172  PRO B 173  SER B 176  LYS B 177                    
SITE     4 AC2 39 LYS B 231  LYS B 232  VAL B 233  ALA B 259                    
SITE     5 AC2 39 THR B 260  GLY B 261  ARG B 285  LYS B 286                    
SITE     6 AC2 39 GLY B 437  ASP B 438  GLU B 453  HIS B 454                    
SITE     7 AC2 39 HIS B 455  ALA B 458  PHE B 482  TRP B 483                    
SITE     8 AC2 39 HOH B2009  HOH B2012  HOH B2013  HOH B2014                    
SITE     9 AC2 39 HOH B2044  HOH B2145  HOH B2146  HOH B2184                    
SITE    10 AC2 39 HOH B2291  HOH B2342  TRS B7000                               
SITE     1 AC3  9 GLU B 164  LYS B 232  THR B 263  ASN B 403                    
SITE     2 AC3  9 GLU B 405  FAD B1000  HOH B2149  HOH B2286                    
SITE     3 AC3  9 HOH B2445                                                     
SITE     1 AC4  8 THR B 328  GLU B 329  VAL B 330  GLY B 360                    
SITE     2 AC4  8 THR B 470  HOH B2025  HOH B2236  HOH B2446                    
CRYST1   90.840  114.380  121.260  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      0.011008  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008743  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008247        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system