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Database: PDB
Entry: 5FS9
LinkDB: 5FS9
Original site: 5FS9 
HEADER    OXIDOREDUCTASE                          31-DEC-15   5FS9              
TITLE     CRYSTAL STRUCTURE OF THE G338E 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 104-613;                        
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 104-125,531-558 AND 613-617 IN CHAIN A AND   
COMPND  10  104-125 AND 531-557 IN CHAIN B ARE DISORDERED. EACH CHAIN HAS 4     
COMPND  11  ADDITIONAL C-TERMINAL RESIDUES L614-V615- P616-R617, PART OF THE    
COMPND  12  THROMBIN CLEAVAGE SITE                                              
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    MITOCHONDRIA, FLAVOPROTEIN, OXIDOREDUCTASE                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.SEVRIOUKOVA                                                         
REVDAT   4   28-SEP-16 5FS9    1       JRNL                                     
REVDAT   3   25-MAY-16 5FS9    1       JRNL                                     
REVDAT   2   18-MAY-16 5FS9    1       REMARK SITE                              
REVDAT   1   11-MAY-16 5FS9    0                                                
JRNL        AUTH   I.F.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.    1.75 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) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 114.93                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.66                          
REMARK   3   NUMBER OF REFLECTIONS             : 121533                         
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) : 0.17588                         
REMARK   3   R VALUE            (WORKING SET) : 0.17462                         
REMARK   3   FREE R VALUE                     : 0.19995                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 6431                            
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) : 1.750                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.795                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8875                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.34                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.377                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 461                          
REMARK   3   BIN FREE R VALUE                    : 0.369                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7237                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 118                                     
REMARK   3   SOLVENT ATOMS            : 541                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.851                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.07                                                 
REMARK   3    B22 (A**2) : -0.05                                                
REMARK   3    B33 (A**2) : -0.02                                                
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): 0.092         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.091         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.073         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.867         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.972                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.964                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7523 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  7296 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10210 ; 1.440 ; 1.982       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 16811 ; 0.769 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   955 ; 5.871 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   320 ;29.775 ;23.562       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1306 ;14.238 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    59 ;16.259 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1130 ; 0.095 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8460 ; 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):  3739 ; 1.964 ; 2.694       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3738 ; 1.964 ; 2.692       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4678 ; 3.022 ; 4.023       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3784 ; 2.718 ; 3.105       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  7717 ; 4.400 ; 4.489       
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   126        A  1002                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.5554 -14.7582  32.4351              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0415 T22:   0.0144                                     
REMARK   3      T33:   0.0308 T12:   0.0176                                     
REMARK   3      T13:  -0.0106 T23:  -0.0019                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9402 L22:   1.3504                                     
REMARK   3      L33:   1.2815 L12:  -0.2028                                     
REMARK   3      L13:   0.0945 L23:   0.2592                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0226 S12:   0.0226 S13:  -0.1187                       
REMARK   3      S21:   0.0620 S22:   0.0427 S23:  -0.0909                       
REMARK   3      S31:   0.2239 S32:   0.0724 S33:  -0.0652                       
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  1000                          
REMARK   3    ORIGIN FOR THE GROUP (A): -44.6268   8.0221  42.9523              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0196 T22:   0.0213                                     
REMARK   3      T33:   0.0127 T12:   0.0082                                     
REMARK   3      T13:  -0.0005 T23:   0.0065                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6989 L22:   0.8057                                     
REMARK   3      L33:   0.6614 L12:  -0.1028                                     
REMARK   3      L13:  -0.2337 L23:   0.2013                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0435 S12:   0.1045 S13:   0.0842                       
REMARK   3      S21:   0.0343 S22:  -0.0209 S23:   0.0518                       
REMARK   3      S31:   0.0196 S32:  -0.0904 S33:  -0.0225                       
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 5FS9 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-65918.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-OCT-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.1                              
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 (Q315R)                        
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 128212                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.75                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 61.44                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 5.3                                
REMARK 200  R MERGE                    (I) : 0.10                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.30                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.84                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.2                                
REMARK 200  R MERGE FOR SHELL          (I) : 1.50                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.90                               
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   (%): 56.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M LITHIUM SULFATE, 0.1M              
REMARK 280  TRIS, PH 8.5, AND 25% 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       45.30950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       60.88500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.46500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       60.88500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       45.30950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       57.46500            
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     GLU A   531                                                      
REMARK 465     SER A   532                                                      
REMARK 465     GLU A   533                                                      
REMARK 465     THR A   534                                                      
REMARK 465     GLU A   535                                                      
REMARK 465     SER A   536                                                      
REMARK 465     GLU A   537                                                      
REMARK 465     ALA A   538                                                      
REMARK 465     SER A   539                                                      
REMARK 465     GLU A   540                                                      
REMARK 465     ILE A   541                                                      
REMARK 465     THR A   542                                                      
REMARK 465     ILE A   543                                                      
REMARK 465     PRO A   544                                                      
REMARK 465     PRO A   545                                                      
REMARK 465     SER A   546                                                      
REMARK 465     THR A   547                                                      
REMARK 465     PRO A   548                                                      
REMARK 465     ALA A   549                                                      
REMARK 465     VAL A   550                                                      
REMARK 465     PRO A   551                                                      
REMARK 465     GLN A   552                                                      
REMARK 465     ALA A   553                                                      
REMARK 465     PRO A   554                                                      
REMARK 465     VAL A   555                                                      
REMARK 465     GLN A   556                                                      
REMARK 465     GLY A   557                                                      
REMARK 465     GLU A   558                                                      
REMARK 465     ASP A   613                                                      
REMARK 465     LEU A   614                                                      
REMARK 465     VAL A   615                                                      
REMARK 465     PRO A   616                                                      
REMARK 465     ARG A   617                                                      
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     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 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   ND1  HIS A   454     O    HOH A  2211              2.10            
REMARK 500   O    HOH A  2007     O    HOH A  2036              2.19            
REMARK 500   O    HOH A  2258     O    HOH A  2259              2.12            
REMARK 500   O    HOH B  2012     O    HOH B  2048              2.17            
REMARK 500   O    HOH B  2057     O    HOH B  2156              2.19            
REMARK 500   O    HOH B  2249     O    HOH B  2250              1.91            
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  2246     O    HOH A  2258     2455     1.55            
REMARK 500   O    HOH B  2250     O    HOH A  2255     2455     2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP B 489   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A 177     -102.72   -132.26                                   
REMARK 500    ALA A 259       58.35   -140.41                                   
REMARK 500    SER A 266     -162.44   -106.64                                   
REMARK 500    ARG A 285      -31.65   -151.03                                   
REMARK 500    TRP A 477      -47.54   -138.50                                   
REMARK 500    LEU A 486       79.62   -105.73                                   
REMARK 500    LYS A 571       28.91     46.64                                   
REMARK 500    LYS B 177     -103.33   -136.19                                   
REMARK 500    SER B 266     -165.51   -115.29                                   
REMARK 500    ARG B 285      -29.03   -151.55                                   
REMARK 500    TRP B 477      -44.85   -135.72                                   
REMARK 500    LEU B 486       78.74   -104.90                                   
REMARK 500    ASP B 499      124.64   -177.32                                   
REMARK 500    LYS B 571       12.89     59.94                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ARG B  529     SER B  530                  149.20                    
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 GOL A1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B1000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1001                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5FS6   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE V243L MUTANT OF HUMAN                      
REMARK 900  APOPTOSIS INDUCING FACTOR                                           
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 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 G338E MUTATION AND 4 ADDITIONAL C-TERMINAL RESIDUES L614-            
REMARK 999 V615-P616-R617                                                       
REMARK 999 G338E MUTATION AND 4 ADDITIONAL C-TERMINAL RESIDUES L614-            
REMARK 999 V615-P616-R617                                                       
DBREF  5FS9 A  103   613  UNP    O95831   AIFM1_HUMAN    103    613             
DBREF  5FS9 B  103   613  UNP    O95831   AIFM1_HUMAN    103    613             
SEQADV 5FS9 LEU A  614  UNP  O95831              EXPRESSION TAG                 
SEQADV 5FS9 VAL A  615  UNP  O95831              EXPRESSION TAG                 
SEQADV 5FS9 PRO A  616  UNP  O95831              EXPRESSION TAG                 
SEQADV 5FS9 ARG A  617  UNP  O95831              EXPRESSION TAG                 
SEQADV 5FS9 GLU A  338  UNP  O95831    GLY   338 ENGINEERED MUTATION            
SEQADV 5FS9 LEU B  614  UNP  O95831              EXPRESSION TAG                 
SEQADV 5FS9 VAL B  615  UNP  O95831              EXPRESSION TAG                 
SEQADV 5FS9 PRO B  616  UNP  O95831              EXPRESSION TAG                 
SEQADV 5FS9 ARG B  617  UNP  O95831              EXPRESSION TAG                 
SEQADV 5FS9 GLU B  338  UNP  O95831    GLY   338 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 VAL 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 GLU 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 VAL 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 GLU 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    GOL  A1002       6                                                       
HET    FAD  B1000      53                                                       
HET    GOL  B1001       6                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL   4  GOL    2(C3 H8 O3)                                                  
FORMUL   7  HOH   *541(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  ALA A  273  1                                   7    
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 ARG A  584  GLY A  595  1                                  12    
HELIX   15  15 ASP A  600  LYS A  606  1                                   7    
HELIX   16  16 LEU A  607  ASN A  609  5                                   3    
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  ARG B  298  1                                  13    
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  THR B  470  1                                  17    
HELIX   29  29 ASN B  516  GLY B  525  1                                  10    
HELIX   30  30 ARG B  584  GLY B  595  1                                  12    
HELIX   31  31 ASP B  600  ALA B  605  1                                   6    
HELIX   32  32 LYS B  606  ASN B  609  5                                   4    
SHEET    1  AA 6 GLY A 224  LEU A 228  0                                        
SHEET    2  AA 6 ARG A 158  VAL A 162  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  LEU A 228  0                                        
SHEET    2  AB 6 ARG A 158  VAL A 162  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 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  VAL B 243   N  ILE B 251           
SHEET    6  BB 6 VAL B 233  ASP B 237  1  N  VAL B 234   O  LYS B 244           
SHEET    1  BC 2 ARG B 192  LYS B 194  0                                        
SHEET    2  BC 2 GLU B 200  SER B 202 -1  O  ARG B 201   N  PHE B 193           
SHEET    1  BD 2 GLY B 262  PRO B 264  0                                        
SHEET    2  BD 2 LEU B 400  PRO B 402 -1  O  GLU B 401   N  THR B 263           
SHEET    1  BE 5 THR B 281  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  SER B 375  0                                        
SHEET    2  BF 3 LYS B 378  LEU B 383 -1  O  LYS B 378   N  SER B 375           
SHEET    3  BF 3 LYS B 388  THR B 391 -1  O  VAL B 389   N  ILE B 381           
SHEET    1  BG 3 PHE B 421  ARG B 422  0                                        
SHEET    2  BG 3 ALA B 440  ASP B 444  1  N  CYS B 441   O  PHE B 421           
SHEET    3  BG 3 GLY B 448  ARG B 451 -1  O  GLY B 448   N  ASP B 444           
SHEET    1  BH 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           
CISPEP   1 SER A  524    GLY A  525          0        -5.33                     
SITE     1 AC1 36 GLY A 138  GLY A 139  GLY A 140  THR A 141                    
SITE     2 AC1 36 ALA A 142  VAL A 162  GLU A 164  ARG A 172                    
SITE     3 AC1 36 PRO A 173  SER A 176  LYS A 177  LYS A 231                    
SITE     4 AC1 36 LYS A 232  VAL A 233  ALA A 259  THR A 260                    
SITE     5 AC1 36 GLY A 261  ARG A 285  GLY A 437  ASP A 438                    
SITE     6 AC1 36 GLU A 453  HIS A 454  HIS A 455  ALA A 458                    
SITE     7 AC1 36 PHE A 482  TRP A 483  HOH A2006  HOH A2009                    
SITE     8 AC1 36 HOH A2010  HOH A2012  HOH A2029  HOH A2089                    
SITE     9 AC1 36 HOH A2090  HOH A2133  HOH A2214  HOH A2274                    
SITE     1 AC2  5 MET A 481  SER A 530  MET A 585  ARG A 589                    
SITE     2 AC2  5 HIS B 611                                                     
SITE     1 AC3 35 GLY B 138  GLY B 139  GLY B 140  THR B 141                    
SITE     2 AC3 35 ALA B 142  VAL B 162  GLU B 164  ASP B 165                    
SITE     3 AC3 35 ARG B 172  PRO B 173  SER B 176  LYS B 177                    
SITE     4 AC3 35 LYS B 231  VAL B 233  ALA B 259  THR B 260                    
SITE     5 AC3 35 GLY B 261  PHE B 284  ARG B 285  GLY B 437                    
SITE     6 AC3 35 ASP B 438  GLU B 453  HIS B 454  HIS B 455                    
SITE     7 AC3 35 ALA B 458  PHE B 482  TRP B 483  HOH B2006                    
SITE     8 AC3 35 HOH B2007  HOH B2009  HOH B2072  HOH B2073                    
SITE     9 AC3 35 HOH B2117  HOH B2167  HOH B2207                               
SITE     1 AC4  9 MET B 481  ARG B 529  SER B 530  MET B 585                    
SITE     2 AC4  9 PRO B 586  ARG B 589  HOH B2275  HOH B2276                    
SITE     3 AC4  9 HOH B2277                                                     
CRYST1   90.619  114.930  121.770  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      0.011035  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008701  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008212        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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