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Database: PDB
Entry: 3OQ9
LinkDB: 3OQ9
Original site: 3OQ9 
HEADER    APOPTOSIS                               02-SEP-10   3OQ9              
TITLE     STRUCTURE OF THE FAS/FADD DEATH DOMAIN ASSEMBLY                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 6;       
COMPND   3 CHAIN: A, B, C, D, E;                                                
COMPND   4 FRAGMENT: UNP RESIDUES 223-308;                                      
COMPND   5 SYNONYM: FASLG RECEPTOR, APOPTOSIS-MEDIATING SURFACE ANTIGEN FAS,    
COMPND   6 APO-1 ANTIGEN;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: PROTEIN FADD;                                              
COMPND  10 CHAIN: H, I, J, K, L;                                                
COMPND  11 FRAGMENT: UNP RESIDUES 93-184;                                       
COMPND  12 SYNONYM: FAS-ASSOCIATED DEATH DOMAIN PROTEIN, FAS-ASSOCIATING DEATH  
COMPND  13 DOMAIN-CONTAINING PROTEIN, MEDIATOR OF RECEPTOR INDUCED TOXICITY,    
COMPND  14 GROWTH-INHIBITING GENE 3 PROTEIN;                                    
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: FAS, APT1, TNFRSF6;                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: FADD, MORT1, GIG3;                                             
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    APOPTOSIS, DISC, FAS, FADD                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.KABALEESWARAN,H.WU                                                  
REVDAT   3   08-NOV-17 3OQ9    1       REMARK                                   
REVDAT   2   15-DEC-10 3OQ9    1       JRNL                                     
REVDAT   1   13-OCT-10 3OQ9    0                                                
JRNL        AUTH   L.WANG,J.K.YANG,V.KABALEESWARAN,A.J.RICE,A.C.CRUZ,A.Y.PARK,  
JRNL        AUTH 2 Q.YIN,E.DAMKO,S.B.JANG,S.RAUNSER,C.V.ROBINSON,R.M.SIEGEL,    
JRNL        AUTH 3 T.WALZ,H.WU                                                  
JRNL        TITL   THE FAS-FADD DEATH DOMAIN COMPLEX STRUCTURE REVEALS THE      
JRNL        TITL 2 BASIS OF DISC ASSEMBLY AND DISEASE MUTATIONS.                
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  17  1324 2010              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   20935634                                                     
JRNL        DOI    10.1038/NSMB.1920                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    6.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 6.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 85.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 1941                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.343                           
REMARK   3   FREE R VALUE                     : 0.354                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 96                              
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7255                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 452.4                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -86.52400                                            
REMARK   3    B22 (A**2) : 102.55900                                            
REMARK   3    B33 (A**2) : -16.03600                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.014                           
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 383.7                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : CNS_TOPPAR:PROTEIN_REP.PARAM                   
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3OQ9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-SEP-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000061437.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-APR-06                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9791                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 2175                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 6.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.6                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 6.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 7.04                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 69.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.1.4                                          
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH 8.5, 100 MM MGCL2, 5 %     
REMARK 280  GLYCEROL AND 6-10 % PEG4000, HANGING DROP, TEMPERATURE 298K         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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       65.78700            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       65.78700            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       67.60200            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       72.22350            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       67.60200            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       72.22350            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       65.78700            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       67.60200            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       72.22350            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       65.78700            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       67.60200            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       72.22350            
REMARK 290   SMTRY3   8  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: DECAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, H, I, J, K, L          
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     LEU H   185                                                      
REMARK 465     GLU H   186                                                      
REMARK 465     HIS H   187                                                      
REMARK 465     HIS H   188                                                      
REMARK 465     HIS H   189                                                      
REMARK 465     HIS H   190                                                      
REMARK 465     HIS H   191                                                      
REMARK 465     HIS H   192                                                      
REMARK 465     LEU I   185                                                      
REMARK 465     GLU I   186                                                      
REMARK 465     HIS I   187                                                      
REMARK 465     HIS I   188                                                      
REMARK 465     HIS I   189                                                      
REMARK 465     HIS I   190                                                      
REMARK 465     HIS I   191                                                      
REMARK 465     HIS I   192                                                      
REMARK 465     LEU J   185                                                      
REMARK 465     GLU J   186                                                      
REMARK 465     HIS J   187                                                      
REMARK 465     HIS J   188                                                      
REMARK 465     HIS J   189                                                      
REMARK 465     HIS J   190                                                      
REMARK 465     HIS J   191                                                      
REMARK 465     HIS J   192                                                      
REMARK 465     LEU K   185                                                      
REMARK 465     GLU K   186                                                      
REMARK 465     HIS K   187                                                      
REMARK 465     HIS K   188                                                      
REMARK 465     HIS K   189                                                      
REMARK 465     HIS K   190                                                      
REMARK 465     HIS K   191                                                      
REMARK 465     HIS K   192                                                      
REMARK 465     LEU L   185                                                      
REMARK 465     GLU L   186                                                      
REMARK 465     HIS L   187                                                      
REMARK 465     HIS L   188                                                      
REMARK 465     HIS L   189                                                      
REMARK 465     HIS L   190                                                      
REMARK 465     HIS L   191                                                      
REMARK 465     HIS L   192                                                      
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 238      -70.28    -46.94                                   
REMARK 500    PHE A 240      -87.49    -52.15                                   
REMARK 500    GLU A 243       39.50    -93.60                                   
REMARK 500    ASN A 244       30.79   -154.01                                   
REMARK 500    LYS A 247      129.48     61.67                                   
REMARK 500    SER A 258       64.85    177.42                                   
REMARK 500    ALA A 263      -99.12    -46.71                                   
REMARK 500    GLN A 265      -34.78    -34.42                                   
REMARK 500    HIS A 277      -86.43    -90.19                                   
REMARK 500    LYS A 279      -81.73   -161.47                                   
REMARK 500    ALA A 293       31.28    -97.03                                   
REMARK 500    CYS A 295      -80.10   -104.29                                   
REMARK 500    ARG A 297      -33.83   -156.01                                   
REMARK 500    LYS B 238      -70.34    -46.89                                   
REMARK 500    PHE B 240      -88.71    -51.71                                   
REMARK 500    GLU B 243       39.47    -93.80                                   
REMARK 500    ASN B 244       31.21   -153.83                                   
REMARK 500    LYS B 247      129.19     62.58                                   
REMARK 500    SER B 258       64.66    177.51                                   
REMARK 500    ALA B 263      -98.99    -47.33                                   
REMARK 500    GLN B 265      -34.97    -34.85                                   
REMARK 500    HIS B 277      -86.36    -90.42                                   
REMARK 500    LYS B 279      -81.61   -161.47                                   
REMARK 500    ALA B 293       31.39    -96.98                                   
REMARK 500    CYS B 295      -80.17   -104.31                                   
REMARK 500    ARG B 297      -33.37   -156.10                                   
REMARK 500    LYS C 238      -70.05    -47.21                                   
REMARK 500    PHE C 240      -88.21    -51.50                                   
REMARK 500    GLU C 243       39.31    -93.40                                   
REMARK 500    ASN C 244       30.70   -154.03                                   
REMARK 500    LYS C 247      129.62     61.95                                   
REMARK 500    SER C 258       64.83    177.22                                   
REMARK 500    ALA C 263      -98.77    -47.08                                   
REMARK 500    GLN C 265      -34.76    -34.74                                   
REMARK 500    HIS C 277      -87.01    -89.96                                   
REMARK 500    LYS C 279      -82.05   -161.95                                   
REMARK 500    ALA C 293       31.08    -97.16                                   
REMARK 500    CYS C 295      -80.05   -104.75                                   
REMARK 500    ARG C 297      -33.26   -155.99                                   
REMARK 500    LYS D 238      -70.10    -46.90                                   
REMARK 500    PHE D 240      -87.94    -52.08                                   
REMARK 500    GLU D 243       39.41    -93.70                                   
REMARK 500    ASN D 244       31.17   -154.15                                   
REMARK 500    LYS D 247      128.95     62.69                                   
REMARK 500    SER D 258       64.47    176.72                                   
REMARK 500    ALA D 263      -98.80    -47.25                                   
REMARK 500    GLN D 265      -34.61    -34.77                                   
REMARK 500    HIS D 277      -86.89    -90.77                                   
REMARK 500    LYS D 279      -81.98   -161.39                                   
REMARK 500    ALA D 293       31.08    -97.00                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      95 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3OQ9 A  223   308  UNP    P25446   TNR6_MOUSE     223    308             
DBREF  3OQ9 B  223   308  UNP    P25446   TNR6_MOUSE     223    308             
DBREF  3OQ9 C  223   308  UNP    P25446   TNR6_MOUSE     223    308             
DBREF  3OQ9 D  223   308  UNP    P25446   TNR6_MOUSE     223    308             
DBREF  3OQ9 E  223   308  UNP    P25446   TNR6_MOUSE     223    308             
DBREF  3OQ9 H   93   184  UNP    Q13158   FADD_HUMAN      93    184             
DBREF  3OQ9 I   93   184  UNP    Q13158   FADD_HUMAN      93    184             
DBREF  3OQ9 J   93   184  UNP    Q13158   FADD_HUMAN      93    184             
DBREF  3OQ9 K   93   184  UNP    Q13158   FADD_HUMAN      93    184             
DBREF  3OQ9 L   93   184  UNP    Q13158   FADD_HUMAN      93    184             
SEQADV 3OQ9 LEU H  185  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 GLU H  186  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 HIS H  187  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 HIS H  188  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 HIS H  189  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 HIS H  190  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 HIS H  191  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 HIS H  192  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 LEU I  185  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 GLU I  186  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 HIS I  187  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 HIS I  188  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 HIS I  189  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 HIS I  190  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 HIS I  191  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 HIS I  192  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 LEU J  185  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 GLU J  186  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 HIS J  187  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 HIS J  188  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 HIS J  189  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 HIS J  190  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 HIS J  191  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 HIS J  192  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 LEU K  185  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 GLU K  186  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 HIS K  187  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 HIS K  188  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 HIS K  189  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 HIS K  190  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 HIS K  191  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 HIS K  192  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 LEU L  185  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 GLU L  186  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 HIS L  187  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 HIS L  188  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 HIS L  189  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 HIS L  190  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 HIS L  191  UNP  Q13158              EXPRESSION TAG                 
SEQADV 3OQ9 HIS L  192  UNP  Q13158              EXPRESSION TAG                 
SEQRES   1 A   86  LYS TYR ILE PRO ARG ILE ALA GLU ASP MET THR ILE GLN          
SEQRES   2 A   86  GLU ALA LYS LYS PHE ALA ARG GLU ASN ASN ILE LYS GLU          
SEQRES   3 A   86  GLY LYS ILE ASP GLU ILE MET HIS ASP SER ILE GLN ASP          
SEQRES   4 A   86  THR ALA GLU GLN LYS VAL GLN LEU LEU LEU CYS TRP TYR          
SEQRES   5 A   86  GLN SER HIS GLY LYS SER ASP ALA TYR GLN ASP LEU ILE          
SEQRES   6 A   86  LYS GLY LEU LYS LYS ALA GLU CYS ARG ARG THR LEU ASP          
SEQRES   7 A   86  LYS PHE GLN ASP MET VAL GLN LYS                              
SEQRES   1 B   86  LYS TYR ILE PRO ARG ILE ALA GLU ASP MET THR ILE GLN          
SEQRES   2 B   86  GLU ALA LYS LYS PHE ALA ARG GLU ASN ASN ILE LYS GLU          
SEQRES   3 B   86  GLY LYS ILE ASP GLU ILE MET HIS ASP SER ILE GLN ASP          
SEQRES   4 B   86  THR ALA GLU GLN LYS VAL GLN LEU LEU LEU CYS TRP TYR          
SEQRES   5 B   86  GLN SER HIS GLY LYS SER ASP ALA TYR GLN ASP LEU ILE          
SEQRES   6 B   86  LYS GLY LEU LYS LYS ALA GLU CYS ARG ARG THR LEU ASP          
SEQRES   7 B   86  LYS PHE GLN ASP MET VAL GLN LYS                              
SEQRES   1 C   86  LYS TYR ILE PRO ARG ILE ALA GLU ASP MET THR ILE GLN          
SEQRES   2 C   86  GLU ALA LYS LYS PHE ALA ARG GLU ASN ASN ILE LYS GLU          
SEQRES   3 C   86  GLY LYS ILE ASP GLU ILE MET HIS ASP SER ILE GLN ASP          
SEQRES   4 C   86  THR ALA GLU GLN LYS VAL GLN LEU LEU LEU CYS TRP TYR          
SEQRES   5 C   86  GLN SER HIS GLY LYS SER ASP ALA TYR GLN ASP LEU ILE          
SEQRES   6 C   86  LYS GLY LEU LYS LYS ALA GLU CYS ARG ARG THR LEU ASP          
SEQRES   7 C   86  LYS PHE GLN ASP MET VAL GLN LYS                              
SEQRES   1 D   86  LYS TYR ILE PRO ARG ILE ALA GLU ASP MET THR ILE GLN          
SEQRES   2 D   86  GLU ALA LYS LYS PHE ALA ARG GLU ASN ASN ILE LYS GLU          
SEQRES   3 D   86  GLY LYS ILE ASP GLU ILE MET HIS ASP SER ILE GLN ASP          
SEQRES   4 D   86  THR ALA GLU GLN LYS VAL GLN LEU LEU LEU CYS TRP TYR          
SEQRES   5 D   86  GLN SER HIS GLY LYS SER ASP ALA TYR GLN ASP LEU ILE          
SEQRES   6 D   86  LYS GLY LEU LYS LYS ALA GLU CYS ARG ARG THR LEU ASP          
SEQRES   7 D   86  LYS PHE GLN ASP MET VAL GLN LYS                              
SEQRES   1 E   86  LYS TYR ILE PRO ARG ILE ALA GLU ASP MET THR ILE GLN          
SEQRES   2 E   86  GLU ALA LYS LYS PHE ALA ARG GLU ASN ASN ILE LYS GLU          
SEQRES   3 E   86  GLY LYS ILE ASP GLU ILE MET HIS ASP SER ILE GLN ASP          
SEQRES   4 E   86  THR ALA GLU GLN LYS VAL GLN LEU LEU LEU CYS TRP TYR          
SEQRES   5 E   86  GLN SER HIS GLY LYS SER ASP ALA TYR GLN ASP LEU ILE          
SEQRES   6 E   86  LYS GLY LEU LYS LYS ALA GLU CYS ARG ARG THR LEU ASP          
SEQRES   7 E   86  LYS PHE GLN ASP MET VAL GLN LYS                              
SEQRES   1 H  100  GLY GLU GLU ASP LEU CYS ALA ALA PHE ASN VAL ILE CYS          
SEQRES   2 H  100  ASP ASN VAL GLY LYS ASP TRP ARG ARG LEU ALA ARG GLN          
SEQRES   3 H  100  LEU LYS VAL SER ASP THR LYS ILE ASP SER ILE GLU ASP          
SEQRES   4 H  100  ARG TYR PRO ARG ASN LEU THR GLU ARG VAL ARG GLU SER          
SEQRES   5 H  100  LEU ARG ILE TRP LYS ASN THR GLU LYS GLU ASN ALA THR          
SEQRES   6 H  100  VAL ALA HIS LEU VAL GLY ALA LEU ARG SER CYS GLN MET          
SEQRES   7 H  100  ASN LEU VAL ALA ASP LEU VAL GLN GLU VAL GLN GLN ALA          
SEQRES   8 H  100  ARG LEU GLU HIS HIS HIS HIS HIS HIS                          
SEQRES   1 I  100  GLY GLU GLU ASP LEU CYS ALA ALA PHE ASN VAL ILE CYS          
SEQRES   2 I  100  ASP ASN VAL GLY LYS ASP TRP ARG ARG LEU ALA ARG GLN          
SEQRES   3 I  100  LEU LYS VAL SER ASP THR LYS ILE ASP SER ILE GLU ASP          
SEQRES   4 I  100  ARG TYR PRO ARG ASN LEU THR GLU ARG VAL ARG GLU SER          
SEQRES   5 I  100  LEU ARG ILE TRP LYS ASN THR GLU LYS GLU ASN ALA THR          
SEQRES   6 I  100  VAL ALA HIS LEU VAL GLY ALA LEU ARG SER CYS GLN MET          
SEQRES   7 I  100  ASN LEU VAL ALA ASP LEU VAL GLN GLU VAL GLN GLN ALA          
SEQRES   8 I  100  ARG LEU GLU HIS HIS HIS HIS HIS HIS                          
SEQRES   1 J  100  GLY GLU GLU ASP LEU CYS ALA ALA PHE ASN VAL ILE CYS          
SEQRES   2 J  100  ASP ASN VAL GLY LYS ASP TRP ARG ARG LEU ALA ARG GLN          
SEQRES   3 J  100  LEU LYS VAL SER ASP THR LYS ILE ASP SER ILE GLU ASP          
SEQRES   4 J  100  ARG TYR PRO ARG ASN LEU THR GLU ARG VAL ARG GLU SER          
SEQRES   5 J  100  LEU ARG ILE TRP LYS ASN THR GLU LYS GLU ASN ALA THR          
SEQRES   6 J  100  VAL ALA HIS LEU VAL GLY ALA LEU ARG SER CYS GLN MET          
SEQRES   7 J  100  ASN LEU VAL ALA ASP LEU VAL GLN GLU VAL GLN GLN ALA          
SEQRES   8 J  100  ARG LEU GLU HIS HIS HIS HIS HIS HIS                          
SEQRES   1 K  100  GLY GLU GLU ASP LEU CYS ALA ALA PHE ASN VAL ILE CYS          
SEQRES   2 K  100  ASP ASN VAL GLY LYS ASP TRP ARG ARG LEU ALA ARG GLN          
SEQRES   3 K  100  LEU LYS VAL SER ASP THR LYS ILE ASP SER ILE GLU ASP          
SEQRES   4 K  100  ARG TYR PRO ARG ASN LEU THR GLU ARG VAL ARG GLU SER          
SEQRES   5 K  100  LEU ARG ILE TRP LYS ASN THR GLU LYS GLU ASN ALA THR          
SEQRES   6 K  100  VAL ALA HIS LEU VAL GLY ALA LEU ARG SER CYS GLN MET          
SEQRES   7 K  100  ASN LEU VAL ALA ASP LEU VAL GLN GLU VAL GLN GLN ALA          
SEQRES   8 K  100  ARG LEU GLU HIS HIS HIS HIS HIS HIS                          
SEQRES   1 L  100  GLY GLU GLU ASP LEU CYS ALA ALA PHE ASN VAL ILE CYS          
SEQRES   2 L  100  ASP ASN VAL GLY LYS ASP TRP ARG ARG LEU ALA ARG GLN          
SEQRES   3 L  100  LEU LYS VAL SER ASP THR LYS ILE ASP SER ILE GLU ASP          
SEQRES   4 L  100  ARG TYR PRO ARG ASN LEU THR GLU ARG VAL ARG GLU SER          
SEQRES   5 L  100  LEU ARG ILE TRP LYS ASN THR GLU LYS GLU ASN ALA THR          
SEQRES   6 L  100  VAL ALA HIS LEU VAL GLY ALA LEU ARG SER CYS GLN MET          
SEQRES   7 L  100  ASN LEU VAL ALA ASP LEU VAL GLN GLU VAL GLN GLN ALA          
SEQRES   8 L  100  ARG LEU GLU HIS HIS HIS HIS HIS HIS                          
HELIX    1   1 LYS A  223  MET A  232  1                                  10    
HELIX    2   2 THR A  233  GLU A  243  1                                  11    
HELIX    3   3 LYS A  247  ASP A  257  1                                  11    
HELIX    4   4 GLU A  264  HIS A  277  1                                  14    
HELIX    5   5 ASP A  281  ALA A  293  1                                  13    
HELIX    6   6 ARG A  297  LYS A  308  1                                  12    
HELIX    7   7 LYS B  223  MET B  232  1                                  10    
HELIX    8   8 THR B  233  GLU B  243  1                                  11    
HELIX    9   9 LYS B  247  ASP B  257  1                                  11    
HELIX   10  10 GLU B  264  HIS B  277  1                                  14    
HELIX   11  11 ASP B  281  ALA B  293  1                                  13    
HELIX   12  12 ARG B  297  LYS B  308  1                                  12    
HELIX   13  13 LYS C  223  MET C  232  1                                  10    
HELIX   14  14 THR C  233  GLU C  243  1                                  11    
HELIX   15  15 LYS C  247  ASP C  257  1                                  11    
HELIX   16  16 GLU C  264  HIS C  277  1                                  14    
HELIX   17  17 ASP C  281  ALA C  293  1                                  13    
HELIX   18  18 ARG C  297  LYS C  308  1                                  12    
HELIX   19  19 LYS D  223  MET D  232  1                                  10    
HELIX   20  20 THR D  233  GLU D  243  1                                  11    
HELIX   21  21 LYS D  247  ASP D  257  1                                  11    
HELIX   22  22 GLU D  264  HIS D  277  1                                  14    
HELIX   23  23 ASP D  281  ALA D  293  1                                  13    
HELIX   24  24 ARG D  297  LYS D  308  1                                  12    
HELIX   25  25 LYS E  223  MET E  232  1                                  10    
HELIX   26  26 THR E  233  GLU E  243  1                                  11    
HELIX   27  27 LYS E  247  ASP E  257  1                                  11    
HELIX   28  28 GLU E  264  HIS E  277  1                                  14    
HELIX   29  29 ASP E  281  ALA E  293  1                                  13    
HELIX   30  30 ARG E  297  LYS E  308  1                                  12    
HELIX   31  31 GLY H   93  ASP H  106  1                                  14    
HELIX   32  32 ASP H  111  LEU H  119  1                                   9    
HELIX   33  33 SER H  122  TYR H  133  1                                  12    
HELIX   34  34 ASN H  136  GLU H  152  1                                  17    
HELIX   35  35 THR H  157  CYS H  168  1                                  12    
HELIX   36  36 MET H  170  ARG H  184  1                                  15    
HELIX   37  37 GLY I   93  ASP I  106  1                                  14    
HELIX   38  38 ASP I  111  LEU I  119  1                                   9    
HELIX   39  39 SER I  122  TYR I  133  1                                  12    
HELIX   40  40 ASN I  136  GLU I  152  1                                  17    
HELIX   41  41 THR I  157  CYS I  168  1                                  12    
HELIX   42  42 MET I  170  ARG I  184  1                                  15    
HELIX   43  43 GLY J   93  ASP J  106  1                                  14    
HELIX   44  44 ASP J  111  LEU J  119  1                                   9    
HELIX   45  45 SER J  122  TYR J  133  1                                  12    
HELIX   46  46 ASN J  136  GLU J  152  1                                  17    
HELIX   47  47 THR J  157  CYS J  168  1                                  12    
HELIX   48  48 MET J  170  ARG J  184  1                                  15    
HELIX   49  49 GLY K   93  ASP K  106  1                                  14    
HELIX   50  50 ASP K  111  LEU K  119  1                                   9    
HELIX   51  51 SER K  122  TYR K  133  1                                  12    
HELIX   52  52 ASN K  136  GLU K  152  1                                  17    
HELIX   53  53 THR K  157  CYS K  168  1                                  12    
HELIX   54  54 MET K  170  ARG K  184  1                                  15    
HELIX   55  55 GLY L   93  ASP L  106  1                                  14    
HELIX   56  56 ASP L  111  LEU L  119  1                                   9    
HELIX   57  57 SER L  122  TYR L  133  1                                  12    
HELIX   58  58 ASN L  136  GLU L  152  1                                  17    
HELIX   59  59 THR L  157  CYS L  168  1                                  12    
HELIX   60  60 MET L  170  ARG L  184  1                                  15    
CRYST1  135.204  144.447  131.574  90.00  90.00  90.00 C 2 2 21     40          
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      0.007396  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006923  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007600        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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