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Database: PDB
Entry: 5FMH
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HEADER    APOPTOSIS                               04-NOV-15   5FMH              
TITLE     CRYSTAL STRUCTURE OF THE E405K MUTANT OF HUMAN APOPTOSIS              
TITLE    2 INDUCING FACTOR                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: APOPTOSIS-INDUCING FACTOR 1, MITOCHONDRIAL;                
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 104-613;                        
COMPND   5 SYNONYM: PROGRAMMED CELL DEATH PROTEIN 8, APOPTOSIS INDUCING FACTOR; 
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 OTHER_DETAILS: RESIDUES 546-559 DISORDERED                           
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PKK223-3                                  
KEYWDS    APOPTOSIS, APOPTOSIS INDUCING FACTOR, FLAVOPROTEIN, OXIDOREDUCTASE,   
KEYWDS   2 MITOCHIONDRIA                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.SEVRIOUKOVA                                                         
REVDAT   1   23-NOV-16 5FMH    0                                                
JRNL        AUTH   I.SEVRIOUKOVA                                                
JRNL        TITL   NOVEL MUTATION IN AIFM1                                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 81.48                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.19                          
REMARK   3   NUMBER OF REFLECTIONS             : 35862                          
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) : 0.19321                         
REMARK   3   R VALUE            (WORKING SET) : 0.19058                         
REMARK   3   FREE R VALUE                     : 0.24254                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1902                            
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) : 1.799                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.846                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2490                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.82                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.329                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 128                          
REMARK   3   BIN FREE R VALUE                    : 0.354                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3703                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 53                                      
REMARK   3   SOLVENT ATOMS            : 334                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.551                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.10                                                 
REMARK   3    B22 (A**2) : -0.11                                                
REMARK   3    B33 (A**2) : 0.01                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : -0.02                                                
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.164         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.153         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.116         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.607         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.928                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3844 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3739 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5221 ; 1.485 ; 1.982       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8619 ; 0.774 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   492 ; 6.336 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   162 ;31.651 ;23.333       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   671 ;15.096 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    32 ;20.182 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   578 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4328 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   863 ; 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):  1914 ; 1.510 ; 2.230       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1913 ; 1.505 ; 2.228       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2397 ; 2.398 ; 3.328       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1930 ; 1.949 ; 2.514       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2816 ; 3.192 ; 3.664       
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  : 1                                          
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   128        A  1000                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.1899  -5.7175  20.9569              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0130 T22:   0.0266                                     
REMARK   3      T33:   0.0071 T12:   0.0184                                     
REMARK   3      T13:  -0.0028 T23:  -0.0026                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6452 L22:   0.2942                                     
REMARK   3      L33:   0.1774 L12:  -0.0549                                     
REMARK   3      L13:   0.1400 L23:   0.1175                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0033 S12:   0.0044 S13:   0.0037                       
REMARK   3      S21:  -0.0057 S22:  -0.0116 S23:  -0.0276                       
REMARK   3      S31:  -0.0250 S32:  -0.0334 S33:   0.0084                       
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. U VALUES WITH TLS ADDED                          
REMARK   4                                                                      
REMARK   4 5FMH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-NOV-15.                  
REMARK 100 THE PDBE ID CODE IS EBI-65445.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-MAY-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 103                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.127                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
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   : 37766                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.80                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.39                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.7                               
REMARK 200  DATA REDUNDANCY                : 5.4                                
REMARK 200  R MERGE                    (I) : 0.13                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.20                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.84                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.1                                
REMARK 200  R MERGE FOR SHELL          (I) : 1.02                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.10                               
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 4BV6                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.2                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350; 0.2M AMMONIUM              
REMARK 280  ACETATE                                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       54.65000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.61500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       54.65000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       24.61500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A2291   LIES ON A SPECIAL POSITION.                         
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     LEU A   104                                                      
REMARK 465     THR A   105                                                      
REMARK 465     PRO A   106                                                      
REMARK 465     GLU A   107                                                      
REMARK 465     GLN A   108                                                      
REMARK 465     LYS A   109                                                      
REMARK 465     GLN A   110                                                      
REMARK 465     LYS A   111                                                      
REMARK 465     LYS A   112                                                      
REMARK 465     ALA A   113                                                      
REMARK 465     ALA A   114                                                      
REMARK 465     LEU A   115                                                      
REMARK 465     SER A   116                                                      
REMARK 465     ALA A   117                                                      
REMARK 465     SER A   118                                                      
REMARK 465     GLU A   119                                                      
REMARK 465     GLY A   120                                                      
REMARK 465     GLU A   121                                                      
REMARK 465     GLU A   122                                                      
REMARK 465     VAL A   123                                                      
REMARK 465     PRO A   124                                                      
REMARK 465     GLN A   125                                                      
REMARK 465     ASP A   126                                                      
REMARK 465     LYS A   127                                                      
REMARK 465     SER A   546                                                      
REMARK 465     THR A   547                                                      
REMARK 465     PRO A   548                                                      
REMARK 465     ALA A   549                                                      
REMARK 465     VAL A   550                                                      
REMARK 465     PRO A   551                                                      
REMARK 465     GLN A   552                                                      
REMARK 465     ALA A   553                                                      
REMARK 465     PRO A   554                                                      
REMARK 465     VAL A   555                                                      
REMARK 465     GLN A   556                                                      
REMARK 465     GLY A   557                                                      
REMARK 465     GLU A   558                                                      
REMARK 465     ASP A   559                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  2031     O    HOH A  2140              2.04            
REMARK 500   O    HOH A  2107     O    HOH A  2202              2.06            
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   C    ASP A   613     O    HOH A  2226     1565     2.01            
REMARK 500   O    HOH A  2124     O    HOH A  2244     2556     1.37            
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     -101.61   -133.13                                   
REMARK 500    ASN A 186       -4.70     75.81                                   
REMARK 500    ARG A 285      -27.64   -153.86                                   
REMARK 500    SER A 376     -145.43     62.71                                   
REMARK 500    GLU A 453       64.00   -117.80                                   
REMARK 500    LEU A 486       78.00   -111.30                                   
REMARK 500    THR A 534      163.28     78.56                                   
REMARK 500    ASP A 570     -124.42     52.44                                   
REMARK 500    HIS A 611      150.70    -40.56                                   
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 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 RESIDUES 1-103 DELETED                                               
DBREF  5FMH A  104   613  UNP    O95831   AIFM1_HUMAN    104    613             
SEQADV 5FMH LYS A  405  UNP  O95831    GLU   405 ENGINEERED MUTATION            
SEQRES   1 A  510  LEU THR PRO GLU GLN LYS GLN LYS LYS ALA ALA LEU SER          
SEQRES   2 A  510  ALA SER GLU GLY GLU GLU VAL PRO GLN ASP LYS ALA PRO          
SEQRES   3 A  510  SER HIS VAL PRO PHE LEU LEU ILE GLY GLY GLY THR ALA          
SEQRES   4 A  510  ALA PHE ALA ALA ALA ARG SER ILE ARG ALA ARG ASP PRO          
SEQRES   5 A  510  GLY ALA ARG VAL LEU ILE VAL SER GLU ASP PRO GLU LEU          
SEQRES   6 A  510  PRO TYR MET ARG PRO PRO LEU SER LYS GLU LEU TRP PHE          
SEQRES   7 A  510  SER ASP ASP PRO ASN VAL THR LYS THR LEU ARG PHE LYS          
SEQRES   8 A  510  GLN TRP ASN GLY LYS GLU ARG SER ILE TYR PHE GLN PRO          
SEQRES   9 A  510  PRO SER PHE TYR VAL SER ALA GLN ASP LEU PRO HIS ILE          
SEQRES  10 A  510  GLU ASN GLY GLY VAL ALA VAL LEU THR GLY LYS LYS VAL          
SEQRES  11 A  510  VAL GLN LEU ASP VAL ARG ASP ASN MET VAL LYS LEU ASN          
SEQRES  12 A  510  ASP GLY SER GLN ILE THR TYR GLU LYS CYS LEU ILE ALA          
SEQRES  13 A  510  THR GLY GLY THR PRO ARG SER LEU SER ALA ILE ASP ARG          
SEQRES  14 A  510  ALA GLY ALA GLU VAL LYS SER ARG THR THR LEU PHE ARG          
SEQRES  15 A  510  LYS ILE GLY ASP PHE ARG SER LEU GLU LYS ILE SER ARG          
SEQRES  16 A  510  GLU VAL LYS SER ILE THR ILE ILE GLY GLY GLY PHE LEU          
SEQRES  17 A  510  GLY SER GLU LEU ALA CYS ALA LEU GLY ARG LYS ALA ARG          
SEQRES  18 A  510  ALA LEU GLY THR GLU VAL ILE GLN LEU PHE PRO GLU LYS          
SEQRES  19 A  510  GLY ASN MET GLY LYS ILE LEU PRO GLU TYR LEU SER ASN          
SEQRES  20 A  510  TRP THR MET GLU LYS VAL ARG ARG GLU GLY VAL LYS VAL          
SEQRES  21 A  510  MET PRO ASN ALA ILE VAL GLN SER VAL GLY VAL SER SER          
SEQRES  22 A  510  GLY LYS LEU LEU ILE LYS LEU LYS ASP GLY ARG LYS VAL          
SEQRES  23 A  510  GLU THR ASP HIS ILE VAL ALA ALA VAL GLY LEU GLU PRO          
SEQRES  24 A  510  ASN VAL LYS LEU ALA LYS THR GLY GLY LEU GLU ILE ASP          
SEQRES  25 A  510  SER ASP PHE GLY GLY PHE ARG VAL ASN ALA GLU LEU GLN          
SEQRES  26 A  510  ALA ARG SER ASN ILE TRP VAL ALA GLY ASP ALA ALA CYS          
SEQRES  27 A  510  PHE TYR ASP ILE LYS LEU GLY ARG ARG ARG VAL GLU HIS          
SEQRES  28 A  510  HIS ASP HIS ALA VAL VAL SER GLY ARG LEU ALA GLY GLU          
SEQRES  29 A  510  ASN MET THR GLY ALA ALA LYS PRO TYR TRP HIS GLN SER          
SEQRES  30 A  510  MET PHE TRP SER ASP LEU GLY PRO ASP VAL GLY TYR GLU          
SEQRES  31 A  510  ALA ILE GLY LEU VAL ASP SER SER LEU PRO THR VAL GLY          
SEQRES  32 A  510  VAL PHE ALA LYS ALA THR ALA GLN ASP ASN PRO LYS SER          
SEQRES  33 A  510  ALA THR GLU GLN SER GLY THR GLY ILE ARG SER GLU SER          
SEQRES  34 A  510  GLU THR GLU SER GLU ALA SER GLU ILE THR ILE PRO PRO          
SEQRES  35 A  510  SER THR PRO ALA VAL PRO GLN ALA PRO VAL GLN GLY GLU          
SEQRES  36 A  510  ASP TYR GLY LYS GLY VAL ILE PHE TYR LEU ARG ASP LYS          
SEQRES  37 A  510  VAL VAL VAL GLY ILE VAL LEU TRP ASN ILE PHE ASN ARG          
SEQRES  38 A  510  MET PRO ILE ALA ARG LYS ILE ILE LYS ASP GLY GLU GLN          
SEQRES  39 A  510  HIS GLU ASP LEU ASN GLU VAL ALA LYS LEU PHE ASN ILE          
SEQRES  40 A  510  HIS GLU ASP                                                  
HET    FAD  A1000      53                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
FORMUL   2  FAD    C27 H33 N9 O15 P2                                            
FORMUL   3  HOH   *334(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 LEU A  267  ALA A  273  1                                   7    
HELIX    7   7 GLY A  274  SER A  279  1                                   6    
HELIX    8   8 LYS A  286  VAL A  300  1                                  15    
HELIX    9   9 GLY A  309  GLY A  327  1                                  19    
HELIX   10  10 PRO A  345  GLU A  359  1                                  15    
HELIX   11  11 LEU A  406  GLY A  411  1                                   6    
HELIX   12  12 HIS A  454  THR A  470  1                                  17    
HELIX   13  13 ASN A  516  GLY A  525  1                                  10    
HELIX   14  14 ILE A  528  THR A  534  1                                   7    
HELIX   15  15 ARG A  584  GLY A  595  1                                  12    
HELIX   16  16 ASP A  600  ILE A  610  1                                  11    
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 450 -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           
CISPEP   1 GLU A  612    ASP A  613          0       -19.80                     
SITE     1 AC1 40 GLY A 138  GLY A 139  GLY A 140  THR A 141                    
SITE     2 AC1 40 ALA A 142  VAL A 162  GLU A 164  ASP A 165                    
SITE     3 AC1 40 ARG A 172  PRO A 173  SER A 176  LYS A 177                    
SITE     4 AC1 40 LYS A 231  LYS A 232  VAL A 233  ALA A 259                    
SITE     5 AC1 40 THR A 260  GLY A 261  PHE A 284  ARG A 285                    
SITE     6 AC1 40 LYS A 286  LEU A 311  GLY A 437  ASP A 438                    
SITE     7 AC1 40 GLU A 453  HIS A 454  HIS A 455  ALA A 458                    
SITE     8 AC1 40 PHE A 482  TRP A 483  HOH A2011  HOH A2014                    
SITE     9 AC1 40 HOH A2015  HOH A2017  HOH A2109  HOH A2110                    
SITE    10 AC1 40 HOH A2132  HOH A2163  HOH A2280  HOH A2334                    
CRYST1  109.300   49.230   81.480  90.00  90.00  90.00 C 1 2 1       1          
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      0.009149  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.020313  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012273        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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