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Database: PDB
Entry: 4LII
LinkDB: 4LII
Original site: 4LII 
HEADER    OXIDOREDUCTASE, APOPTOSIS               02-JUL-13   4LII              
TITLE     CRYSTAL STRUCTURE OF AN APOPTOSIS-INDUCING FACTOR, MITOCHONDRION-     
TITLE    2 ASSOCIATED, 1 (AIFM1) FROM HOMO SAPIENS AT 1.88 A RESOLUTION         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: APOPTOSIS-INDUCING FACTOR 1, MITOCHONDRIAL;                
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 100-611;                                      
COMPND   5 SYNONYM: PROGRAMMED CELL DEATH PROTEIN 8;                            
COMPND   6 EC: 1.-.-.-;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: AIF, AIFM1, BC111065, PDCD8;                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: PB1;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: SPEEDET                                   
KEYWDS    FLAVOPROTEIN, FAD/NAD-LINKED REDUCTASES, STRUCTURAL GENOMICS, JOINT   
KEYWDS   2 CENTER FOR STRUCTURAL GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE,  
KEYWDS   3 PSI-BIOLOGY, OXIDOREDUCTASE, APOPTOSIS, PARTNERSHIP FOR T-CELL       
KEYWDS   4 BIOLOGY, TCELL                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG),PARTNERSHIP FOR T-CELL    
AUTHOR   2 BIOLOGY (TCELL)                                                      
REVDAT   2   15-NOV-17 4LII    1       REMARK                                   
REVDAT   1   04-SEP-13 4LII    0                                                
JRNL        AUTH   JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG),                 
JRNL        AUTH 2 PARTNERSHIP FOR T-CELL BIOLOGY (TCELL)                       
JRNL        TITL   CRYSTAL STRUCTURE OF AN APOPTOSIS-INDUCING FACTOR,           
JRNL        TITL 2 MITOCHONDRION-ASSOCIATED, 1 (AIFM1) FROM HOMO SAPIENS AT     
JRNL        TITL 3 1.88 A RESOLUTION                                            
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.88 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.88                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.90                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 42729                          
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) : 0.169                           
REMARK   3   R VALUE            (WORKING SET) : 0.167                           
REMARK   3   FREE R VALUE                     : 0.211                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2150                            
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) : 1.88                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.93                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2948                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.29                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2910                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 170                          
REMARK   3   BIN FREE R VALUE                    : 0.3140                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3659                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 61                                      
REMARK   3   SOLVENT ATOMS            : 307                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 23.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.01                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.78000                                              
REMARK   3    B22 (A**2) : -0.95000                                             
REMARK   3    B33 (A**2) : -1.77000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.43000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.132         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.129         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.090         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.887         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.946                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3855 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3748 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5228 ; 1.489 ; 1.991       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8639 ; 0.764 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   490 ; 5.783 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   165 ;31.884 ;23.576       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   647 ;14.094 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    31 ;21.098 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   576 ; 0.082 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4333 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   861 ; 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):  1912 ; 2.452 ; 3.069       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1911 ; 2.446 ; 3.065       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2391 ; 3.480 ; 5.720       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   125        A   545                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.4590  36.4170   1.9330              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0080 T22:   0.0917                                     
REMARK   3      T33:   0.1199 T12:   0.0053                                     
REMARK   3      T13:  -0.0007 T23:  -0.0034                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2165 L22:   0.2930                                     
REMARK   3      L33:   0.7048 L12:   0.0870                                     
REMARK   3      L13:  -0.0937 L23:  -0.0093                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0153 S12:   0.0034 S13:   0.0144                       
REMARK   3      S21:   0.0205 S22:   0.0187 S23:   0.0025                       
REMARK   3      S31:   0.0315 S32:  -0.0280 S33:  -0.0034                       
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 :   A   559        A   611                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.4480  16.9400 -11.1880              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1068 T22:   0.0763                                     
REMARK   3      T33:   0.1180 T12:  -0.0613                                     
REMARK   3      T13:  -0.0068 T23:  -0.0042                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3725 L22:   2.3055                                     
REMARK   3      L33:   2.2935 L12:   0.5611                                     
REMARK   3      L13:   0.3764 L23:  -0.9266                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0939 S12:   0.1215 S13:  -0.0412                       
REMARK   3      S21:  -0.1906 S22:   0.0801 S23:   0.0891                       
REMARK   3      S31:   0.3098 S32:  -0.1054 S33:   0.0138                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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: 1. HYDROGENS HAVE BEEN ADDED IN THE       
REMARK   3  RIDING POSITIONS. 2. ATOM RECORDS CONTAIN RESIDUAL B FACTORS        
REMARK   3  ONLY. 3. WATERS WERE EXCLUDED FROM AUTOMATIC TLS ASSIGNMENT. 4.     
REMARK   3  A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE             
REMARK   3  INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE    
REMARK   3  ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75 FOR THE REDUCED       
REMARK   3  SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 5. 1,2-        
REMARK   3  ETHANEDIOL (EDO) FROM THE CRYOPROTECTION SOLUTION ARE MODELED.      
REMARK   3  6. FLAVIN-ADENINE DINUCLEOTIDE (FAD) IS MODELED BASED ON            
REMARK   3  ELECTRON DENSITY.                                                   
REMARK   4                                                                      
REMARK   4 4LII COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUL-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000080672.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-FEB-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL12-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9794                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : RHODIUM-COATED VERTICAL AND        
REMARK 200                                   HORIZONTAL FOCUSING MIRRORS;       
REMARK 200                                   LIQUID-NITROGEN COOLED DOUBLE      
REMARK 200                                   CRYSTAL SI(111) MONOCHROMATOR      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE DECEMBER 29, 2011           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42757                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.880                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.903                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.11200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.7300                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.88                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.87200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELX, SHARP, SHELXD                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20.00% POLYETHYLENE GLYCOL 6000, 0.1M    
REMARK 280  MES PH 6.0, NANODROP, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE    
REMARK 280  277K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       44.90350            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: CRYSTAL PACKING ANALYSIS SUGGESTS THE ASSIGNMENT OF A        
REMARK 300 MONOMER AS THE SIGNIFICANT OLIGOMERIZATION STATE.                    
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     0                                                      
REMARK 465     SER A   100                                                      
REMARK 465     GLY A   101                                                      
REMARK 465     LEU A   102                                                      
REMARK 465     GLY A   103                                                      
REMARK 465     LEU A   104                                                      
REMARK 465     THR A   105                                                      
REMARK 465     PRO A   106                                                      
REMARK 465     GLU A   107                                                      
REMARK 465     GLN A   108                                                      
REMARK 465     LYS A   109                                                      
REMARK 465     GLN A   110                                                      
REMARK 465     LYS A   111                                                      
REMARK 465     LYS A   112                                                      
REMARK 465     ALA A   113                                                      
REMARK 465     ALA A   114                                                      
REMARK 465     LEU A   115                                                      
REMARK 465     SER A   116                                                      
REMARK 465     ALA A   117                                                      
REMARK 465     SER A   118                                                      
REMARK 465     GLU A   119                                                      
REMARK 465     GLY A   120                                                      
REMARK 465     GLU A   121                                                      
REMARK 465     GLU A   122                                                      
REMARK 465     VAL A   123                                                      
REMARK 465     PRO A   124                                                      
REMARK 465     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 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    ASP A 126      107.88    -58.29                                   
REMARK 500    LYS A 177     -104.05   -133.88                                   
REMARK 500    ARG A 285      -33.26   -146.17                                   
REMARK 500    GLU A 453       68.82   -119.49                                   
REMARK 500    ALA A 473       66.35     38.04                                   
REMARK 500    THR A 534      171.49     64.03                                   
REMARK 500    LYS A 571       -4.98     68.38                                   
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 A 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 702                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: JCSG-422903   RELATED DB: TARGETTRACK                    
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THIS CONSTRUCT WAS EXPRESSED WITH AN N-TERMINAL PURIFICATION TAG     
REMARK 999 MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING   
REMARK 999 ONLY A GLYCINE (0) FOLLOWED BY RESIDUES 100-611 OF THE TARGET        
REMARK 999 SEQUENCE. NUMBERING IS BASED ON ISOFORM 1 OF UNIPROTKB ID O95831.    
DBREF  4LII A  100   611  UNP    O95831   AIFM1_HUMAN    100    611             
SEQADV 4LII GLY A    0  UNP  O95831              EXPRESSION TAG                 
SEQRES   1 A  513  GLY SER GLY LEU GLY LEU THR PRO GLU GLN LYS GLN LYS          
SEQRES   2 A  513  LYS ALA ALA LEU SER ALA SER GLU GLY GLU GLU VAL PRO          
SEQRES   3 A  513  GLN ASP LYS ALA PRO SER HIS VAL PRO PHE LEU LEU ILE          
SEQRES   4 A  513  GLY GLY GLY THR ALA ALA PHE ALA ALA ALA ARG SER ILE          
SEQRES   5 A  513  ARG ALA ARG ASP PRO GLY ALA ARG VAL LEU ILE VAL SER          
SEQRES   6 A  513  GLU ASP PRO GLU LEU PRO TYR MSE ARG PRO PRO LEU SER          
SEQRES   7 A  513  LYS GLU LEU TRP PHE SER ASP ASP PRO ASN VAL THR LYS          
SEQRES   8 A  513  THR LEU ARG PHE LYS GLN TRP ASN GLY LYS GLU ARG SER          
SEQRES   9 A  513  ILE TYR PHE GLN PRO PRO SER PHE TYR VAL SER ALA GLN          
SEQRES  10 A  513  ASP LEU PRO HIS ILE GLU ASN GLY GLY VAL ALA VAL LEU          
SEQRES  11 A  513  THR GLY LYS LYS VAL VAL GLN LEU ASP VAL ARG ASP ASN          
SEQRES  12 A  513  MSE VAL LYS LEU ASN ASP GLY SER GLN ILE THR TYR GLU          
SEQRES  13 A  513  LYS CYS LEU ILE ALA THR GLY GLY THR PRO ARG SER LEU          
SEQRES  14 A  513  SER ALA ILE ASP ARG ALA GLY ALA GLU VAL LYS SER ARG          
SEQRES  15 A  513  THR THR LEU PHE ARG LYS ILE GLY ASP PHE ARG SER LEU          
SEQRES  16 A  513  GLU LYS ILE SER ARG GLU VAL LYS SER ILE THR ILE ILE          
SEQRES  17 A  513  GLY GLY GLY PHE LEU GLY SER GLU LEU ALA CYS ALA LEU          
SEQRES  18 A  513  GLY ARG LYS ALA ARG ALA LEU GLY THR GLU VAL ILE GLN          
SEQRES  19 A  513  LEU PHE PRO GLU LYS GLY ASN MSE GLY LYS ILE LEU PRO          
SEQRES  20 A  513  GLU TYR LEU SER ASN TRP THR MSE GLU LYS VAL ARG ARG          
SEQRES  21 A  513  GLU GLY VAL LYS VAL MSE PRO ASN ALA ILE VAL GLN SER          
SEQRES  22 A  513  VAL GLY VAL SER SER GLY LYS LEU LEU ILE LYS LEU LYS          
SEQRES  23 A  513  ASP GLY ARG LYS VAL GLU THR ASP HIS ILE VAL ALA ALA          
SEQRES  24 A  513  VAL GLY LEU GLU PRO ASN VAL GLU LEU ALA LYS THR GLY          
SEQRES  25 A  513  GLY LEU GLU ILE ASP SER ASP PHE GLY GLY PHE ARG VAL          
SEQRES  26 A  513  ASN ALA GLU LEU GLN ALA ARG SER ASN ILE TRP VAL ALA          
SEQRES  27 A  513  GLY ASP ALA ALA CYS PHE TYR ASP ILE LYS LEU GLY ARG          
SEQRES  28 A  513  ARG ARG VAL GLU HIS HIS ASP HIS ALA VAL VAL SER GLY          
SEQRES  29 A  513  ARG LEU ALA GLY GLU ASN MSE THR GLY ALA ALA LYS PRO          
SEQRES  30 A  513  TYR TRP HIS GLN SER MSE PHE TRP SER ASP LEU GLY PRO          
SEQRES  31 A  513  ASP VAL GLY TYR GLU ALA ILE GLY LEU VAL ASP SER SER          
SEQRES  32 A  513  LEU PRO THR VAL GLY VAL PHE ALA LYS ALA THR ALA GLN          
SEQRES  33 A  513  ASP ASN PRO LYS SER ALA THR GLU GLN SER GLY THR GLY          
SEQRES  34 A  513  ILE ARG SER GLU SER GLU THR GLU SER GLU ALA SER GLU          
SEQRES  35 A  513  ILE THR ILE PRO PRO SER THR PRO ALA VAL PRO GLN ALA          
SEQRES  36 A  513  PRO VAL GLN GLY GLU ASP TYR GLY LYS GLY VAL ILE PHE          
SEQRES  37 A  513  TYR LEU ARG ASP LYS VAL VAL VAL GLY ILE VAL LEU TRP          
SEQRES  38 A  513  ASN ILE PHE ASN ARG MSE PRO ILE ALA ARG LYS ILE ILE          
SEQRES  39 A  513  LYS ASP GLY GLU GLN HIS GLU ASP LEU ASN GLU VAL ALA          
SEQRES  40 A  513  LYS LEU PHE ASN ILE HIS                                      
MODRES 4LII MSE A  171  MET  SELENOMETHIONINE                                   
MODRES 4LII MSE A  242  MET  SELENOMETHIONINE                                   
MODRES 4LII MSE A  340  MET  SELENOMETHIONINE                                   
MODRES 4LII MSE A  353  MET  SELENOMETHIONINE                                   
MODRES 4LII MSE A  364  MET  SELENOMETHIONINE                                   
MODRES 4LII MSE A  469  MET  SELENOMETHIONINE                                   
MODRES 4LII MSE A  481  MET  SELENOMETHIONINE                                   
MODRES 4LII MSE A  585  MET  SELENOMETHIONINE                                   
HET    MSE  A 171       8                                                       
HET    MSE  A 242      13                                                       
HET    MSE  A 340       8                                                       
HET    MSE  A 353       8                                                       
HET    MSE  A 364       8                                                       
HET    MSE  A 469       8                                                       
HET    MSE  A 481       8                                                       
HET    MSE  A 585       8                                                       
HET    FAD  A 700      53                                                       
HET    EDO  A 701       4                                                       
HET    EDO  A 702       4                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  MSE    8(C5 H11 N O2 SE)                                            
FORMUL   2  FAD    C27 H33 N9 O15 P2                                            
FORMUL   3  EDO    2(C2 H6 O2)                                                  
FORMUL   5  HOH   *307(H2 O)                                                    
HELIX    1   1 GLY A  140  ASP A  154  1                                  15    
HELIX    2   2 ARG A  172  PHE A  181  5                                  10    
HELIX    3   3 ASN A  186  LEU A  191  1                                   6    
HELIX    4   4 PRO A  207  TYR A  211  5                                   5    
HELIX    5   5 LEU A  267  ARG A  272  1                                   6    
HELIX    6   6 GLY A  274  ARG A  280  1                                   7    
HELIX    7   7 LYS A  286  VAL A  300  1                                  15    
HELIX    8   8 GLY A  309  GLY A  327  1                                  19    
HELIX    9   9 PRO A  345  GLU A  359  1                                  15    
HELIX   10  10 LEU A  406  GLY A  411  1                                   6    
HELIX   11  11 HIS A  454  MSE A  469  1                                  16    
HELIX   12  12 ASN A  516  GLY A  525  1                                  10    
HELIX   13  13 ILE A  528  GLU A  533  1                                   6    
HELIX   14  14 ARG A  584  GLY A  595  1                                  12    
HELIX   15  15 ASP A  600  ALA A  605  1                                   6    
HELIX   16  16 LYS A  606  ASN A  609  5                                   4    
SHEET    1   A 6 GLY A 224  THR A 229  0                                        
SHEET    2   A 6 ARG A 158  SER A 163  1  N  ILE A 161   O  LEU A 228           
SHEET    3   A 6 HIS A 131  ILE A 137  1  N  LEU A 136   O  LEU A 160           
SHEET    4   A 6 GLN A 250  ILE A 258  1  O  LEU A 257   N  ILE A 137           
SHEET    5   A 6 MSE A 242  LEU A 245 -1  N  VAL A 243   O  ILE A 251           
SHEET    6   A 6 VAL A 233  ASP A 237 -1  N  ASP A 237   O  MSE A 242           
SHEET    1   B 6 GLY A 224  THR A 229  0                                        
SHEET    2   B 6 ARG A 158  SER A 163  1  N  ILE A 161   O  LEU A 228           
SHEET    3   B 6 HIS A 131  ILE A 137  1  N  LEU A 136   O  LEU A 160           
SHEET    4   B 6 GLN A 250  ILE A 258  1  O  LEU A 257   N  ILE A 137           
SHEET    5   B 6 ILE A 433  VAL A 435  1  O  TRP A 434   N  ILE A 258           
SHEET    6   B 6 GLN A 428  ARG A 430 -1  N  ALA A 429   O  ILE A 433           
SHEET    1   C 2 ARG A 192  LYS A 194  0                                        
SHEET    2   C 2 GLU A 200  SER A 202 -1  O  ARG A 201   N  PHE A 193           
SHEET    1   D 2 GLY A 262  PRO A 264  0                                        
SHEET    2   D 2 LEU A 400  PRO A 402 -1  O  GLU A 401   N  THR A 263           
SHEET    1   E 5 THR A 281  LEU A 283  0                                        
SHEET    2   E 5 HIS A 393  ALA A 396  1  O  ALA A 396   N  THR A 282           
SHEET    3   E 5 SER A 302  ILE A 306  1  N  ILE A 306   O  VAL A 395           
SHEET    4   E 5 GLU A 329  LEU A 333  1  O  ILE A 331   N  ILE A 305           
SHEET    5   E 5 LYS A 362  MSE A 364  1  O  MSE A 364   N  GLN A 332           
SHEET    1   F 3 VAL A 369  SER A 375  0                                        
SHEET    2   F 3 LYS A 378  LEU A 383 -1  O  LYS A 378   N  SER A 375           
SHEET    3   F 3 LYS A 388  THR A 391 -1  O  VAL A 389   N  ILE A 381           
SHEET    1   G 3 PHE A 421  ARG A 422  0                                        
SHEET    2   G 3 ALA A 440  ASP A 444  1  O  CYS A 441   N  PHE A 421           
SHEET    3   G 3 GLY A 448  ARG A 450 -1  O  GLY A 448   N  ASP A 444           
SHEET    1   H 5 MSE A 481  ASP A 485  0                                        
SHEET    2   H 5 GLY A 491  GLY A 496 -1  O  TYR A 492   N  SER A 484           
SHEET    3   H 5 VAL A 572  TRP A 579 -1  O  LEU A 578   N  GLU A 493           
SHEET    4   H 5 LYS A 562  ARG A 569 -1  N  GLY A 563   O  TRP A 579           
SHEET    5   H 5 THR A 504  ALA A 509 -1  N  VAL A 505   O  PHE A 566           
LINK         C   TYR A 170                 N   MSE A 171     1555   1555  1.33  
LINK         C   MSE A 171                 N   ARG A 172     1555   1555  1.34  
LINK         C   ASN A 241                 N   MSE A 242     1555   1555  1.33  
LINK         C   MSE A 242                 N   VAL A 243     1555   1555  1.33  
LINK         C   ASN A 339                 N   MSE A 340     1555   1555  1.33  
LINK         C   MSE A 340                 N   GLY A 341     1555   1555  1.34  
LINK         C   THR A 352                 N   MSE A 353     1555   1555  1.33  
LINK         C   MSE A 353                 N   GLU A 354     1555   1555  1.33  
LINK         C   VAL A 363                 N   MSE A 364     1555   1555  1.33  
LINK         C   MSE A 364                 N   PRO A 365     1555   1555  1.35  
LINK         C   ASN A 468                 N   MSE A 469     1555   1555  1.33  
LINK         C   MSE A 469                 N   THR A 470     1555   1555  1.33  
LINK         C   SER A 480                 N   MSE A 481     1555   1555  1.33  
LINK         C   MSE A 481                 N   PHE A 482     1555   1555  1.33  
LINK         C   ARG A 584                 N   MSE A 585     1555   1555  1.33  
LINK         C   MSE A 585                 N   PRO A 586     1555   1555  1.35  
SITE     1 AC1 35 GLY A 138  GLY A 139  GLY A 140  THR A 141                    
SITE     2 AC1 35 ALA A 142  VAL A 162  GLU A 164  ASP A 165                    
SITE     3 AC1 35 ARG A 172  PRO A 173  SER A 176  LYS A 177                    
SITE     4 AC1 35 LYS A 232  VAL A 233  ALA A 259  THR A 260                    
SITE     5 AC1 35 GLY A 261  ARG A 285  LYS A 286  GLY A 437                    
SITE     6 AC1 35 ASP A 438  GLU A 453  HIS A 454  HIS A 455                    
SITE     7 AC1 35 ALA A 458  PHE A 482  TRP A 483  HOH A 803                    
SITE     8 AC1 35 HOH A 804  HOH A 805  HOH A 818  HOH A 837                    
SITE     9 AC1 35 HOH A 840  HOH A1002  HOH A1065                               
SITE     1 AC2  5 LEU A 168  TYR A 211  VAL A 212  ALA A 226                    
SITE     2 AC2  5 VAL A 227                                                     
SITE     1 AC3  6 GLY A 309  MSE A 340  GLY A 341  LYS A 342                    
SITE     2 AC3  6 HOH A 807  HOH A 867                                          
CRYST1   50.680   89.807   60.471  90.00  94.78  90.00 P 1 21 1      2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.019732  0.000000  0.001650        0.00000                         
SCALE2      0.000000  0.011135  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016595        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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