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Database: PDB
Entry: 6BZH
LinkDB: 6BZH
Original site: 6BZH 
HEADER    HYDROLASE                               24-DEC-17   6BZH              
TITLE     STRUCTURE OF MOUSE RIG-I TANDEM CARDS                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROBABLE ATP-DEPENDENT RNA HELICASE DDX58;                 
COMPND   3 CHAIN: A, B, C, D, E;                                                
COMPND   4 SYNONYM: DEAD BOX PROTEIN 58,RIG-I-LIKE RECEPTOR 1,RLR-1,RETINOIC    
COMPND   5 ACID-INDUCIBLE GENE 1 PROTEIN,RIG-1,RETINOIC ACID-INDUCIBLE GENE I   
COMPND   6 PROTEIN,RIG-I;                                                       
COMPND   7 EC: 3.6.4.13;                                                        
COMPND   8 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: DDX58;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CARD RIG-I DEAD-BOX RNA HELICASES, HYDROLASE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.J.KERSHAW,A.A.D'CRUZ,J.J.BABON,S.E.NICHOLSON                        
REVDAT   2   31-JAN-18 6BZH    1       JRNL                                     
REVDAT   1   17-JAN-18 6BZH    0                                                
JRNL        AUTH   A.A.D'CRUZ,N.J.KERSHAW,T.J.HAYMAN,E.M.LINOSSI,J.J.CHIANG,    
JRNL        AUTH 2 M.K.WANG,L.F.DAGLEY,T.B.KOLESNIK,J.G.ZHANG,S.L.MASTERS,      
JRNL        AUTH 3 M.D.W.GRIFFIN,M.U.GACK,J.M.MURPHY,N.A.NICOLA,J.J.BABON,      
JRNL        AUTH 4 S.E.NICHOLSON                                                
JRNL        TITL   IDENTIFICATION OF A SECOND BINDING SITE ON THE TRIM25 B30.2  
JRNL        TITL 2 DOMAIN.                                                      
JRNL        REF    BIOCHEM. J.                   V. 475   429 2018              
JRNL        REFN                   ESSN 1470-8728                               
JRNL        PMID   29259080                                                     
JRNL        DOI    10.1042/BCJ20170427                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 73.93                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.040                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 35014                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.229                           
REMARK   3   R VALUE            (WORKING SET) : 0.226                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.630                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1970                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 73.9587 -  6.0245    0.98     2475   160  0.2017 0.2323        
REMARK   3     2  6.0245 -  4.7820    0.99     2413   146  0.1960 0.2306        
REMARK   3     3  4.7820 -  4.1776    1.00     2415   124  0.1663 0.2197        
REMARK   3     4  4.1776 -  3.7957    0.99     2358   148  0.1820 0.2092        
REMARK   3     5  3.7957 -  3.5236    1.00     2377   146  0.2068 0.2779        
REMARK   3     6  3.5236 -  3.3159    1.00     2359   140  0.2251 0.2949        
REMARK   3     7  3.3159 -  3.1498    1.00     2343   142  0.2492 0.3073        
REMARK   3     8  3.1498 -  3.0127    1.00     2357   133  0.2568 0.3181        
REMARK   3     9  3.0127 -  2.8967    1.00     2355   137  0.2574 0.3238        
REMARK   3    10  2.8967 -  2.7968    1.00     2349   149  0.2873 0.3305        
REMARK   3    11  2.7968 -  2.7093    1.00     2324   140  0.2929 0.3737        
REMARK   3    12  2.7093 -  2.6319    1.00     2353   127  0.3105 0.3846        
REMARK   3    13  2.6319 -  2.5626    1.00     2340   142  0.3260 0.3754        
REMARK   3    14  2.5626 -  2.5000    0.96     2226   136  0.3075 0.3356        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.380            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.580           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 34.06                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002           7793                                  
REMARK   3   ANGLE     :  0.501          10521                                  
REMARK   3   CHIRALITY :  0.039           1143                                  
REMARK   3   PLANARITY :  0.003           1361                                  
REMARK   3   DIHEDRAL  : 12.107           4747                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6BZH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JAN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000231103.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-OCT-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95371                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35016                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 73.926                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.18240                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.7300                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.840                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4A2Q                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.93                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULPHATE 26% W/V          
REMARK 280  POLYETHYLENE GLYCOL 3350 0.1 M BIS-TRIS, PH 6.5., VAPOR             
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 281K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       45.09500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       56.64500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       48.78000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       56.64500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       45.09500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       48.78000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
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    -4                                                      
REMARK 465     SER A    -3                                                      
REMARK 465     ASP A   189                                                      
REMARK 465     GLY B    -4                                                      
REMARK 465     ASP B   189                                                      
REMARK 465     GLY C    -4                                                      
REMARK 465     SER C    -3                                                      
REMARK 465     SER C    -2                                                      
REMARK 465     GLY D    -4                                                      
REMARK 465     SER D    -3                                                      
REMARK 465     SER D    -2                                                      
REMARK 465     ALA D    -1                                                      
REMARK 465     ASP D   189                                                      
REMARK 465     GLY E    -4                                                      
REMARK 465     SER E    -3                                                      
REMARK 465     ASP E   189                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A   7    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  63    NZ                                                  
REMARK 470     LYS A  96    NZ                                                  
REMARK 470     LYS A  99    CE   NZ                                             
REMARK 470     GLU A 165    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 177    CG   CD   CE   NZ                                   
REMARK 470     LYS A 181    CE   NZ                                             
REMARK 470     ARG B   0    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B   4    CG   CD   OE1  OE2                                  
REMARK 470     GLN B   7    CG   CD   OE1  NE2                                  
REMARK 470     PHE B  12    CD1  CD2  CE1  CE2  CZ                              
REMARK 470     ARG B  13    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR B  15    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS B  17    CE   NZ                                             
REMARK 470     LYS B  18    CG   CD   CE   NZ                                   
REMARK 470     TYR B  40    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN B  95    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 140    CZ   NH1  NH2                                       
REMARK 470     GLU B 176    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 177    CE   NZ                                             
REMARK 470     ASN B 179    CG   OD1  ND2                                       
REMARK 470     LYS B 181    CD   CE   NZ                                        
REMARK 470     ARG C   0    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C   4    CG   CD   OE1  OE2                                  
REMARK 470     GLN C   5    CG   CD   OE1  NE2                                  
REMARK 470     GLN C   7    CG   CD   OE1  NE2                                  
REMARK 470     GLN C  59    CG   CD   OE1  NE2                                  
REMARK 470     GLU C  67    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 129    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 177    CG   CD   CE   NZ                                   
REMARK 470     ASP C 178    CG   OD1  OD2                                       
REMARK 470     LYS C 181    CG   CD   CE   NZ                                   
REMARK 470     ASP C 189    CG   OD1  OD2                                       
REMARK 470     ARG D   0    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN D   1    CG   CD   OE1  NE2                                  
REMARK 470     GLU D   4    CG   CD   OE1  OE2                                  
REMARK 470     GLN D  10    CD   OE1  NE2                                       
REMARK 470     GLU D  67    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  99    CG   CD   CE   NZ                                   
REMARK 470     LYS D 177    CG   CD   CE   NZ                                   
REMARK 470     ASN D 179    CG   OD1  ND2                                       
REMARK 470     LYS D 181    CG   CD   CE   NZ                                   
REMARK 470     GLU D 184    CG   CD   OE1  OE2                                  
REMARK 470     LEU D 185    CG   CD1  CD2                                       
REMARK 470     ILE D 187    CG1  CG2  CD1                                       
REMARK 470     SER E  -2    OG                                                  
REMARK 470     ARG E   0    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU E   4    CG   CD   OE1  OE2                                  
REMARK 470     GLN E   7    CG   CD   OE1  NE2                                  
REMARK 470     ILE E  25    CG1  CG2  CD1                                       
REMARK 470     LEU E  26    CG   CD1  CD2                                       
REMARK 470     TYR E  28    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU E  62    CG   CD1  CD2                                       
REMARK 470     GLU E  67    CG   CD   OE1  OE2                                  
REMARK 470     GLU E  90    CG   CD   OE1  OE2                                  
REMARK 470     SER E  91    OG                                                  
REMARK 470     ARG E 109    NE   CZ   NH1  NH2                                  
REMARK 470     GLU E 111    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 169    CG   CD   CE   NZ                                   
REMARK 470     GLU E 176    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 177    CG   CD   CE   NZ                                   
REMARK 470     ASP E 178    CG   OD1  OD2                                       
REMARK 470     LYS E 181    CG   CD   CE   NZ                                   
REMARK 470     ILE E 187    CG1  CG2  CD1                                       
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    ASN A 179       76.71     53.57                                   
REMARK 500    SER B  -2     -155.56    -66.90                                   
REMARK 500    ILE B  25       50.01   -117.79                                   
REMARK 500    ASN B 179       76.24     53.92                                   
REMARK 500    ASN C 179       76.19     54.62                                   
REMARK 500    ASN D 179       77.40     55.43                                   
REMARK 500    ASN E 179       77.01     55.83                                   
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 CL A 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 201                  
DBREF  6BZH A    2   189  UNP    Q6Q899   DDX58_MOUSE      2    189             
DBREF  6BZH B    2   189  UNP    Q6Q899   DDX58_MOUSE      2    189             
DBREF  6BZH C    2   189  UNP    Q6Q899   DDX58_MOUSE      2    189             
DBREF  6BZH D    2   189  UNP    Q6Q899   DDX58_MOUSE      2    189             
DBREF  6BZH E    2   189  UNP    Q6Q899   DDX58_MOUSE      2    189             
SEQADV 6BZH GLY A   -4  UNP  Q6Q899              EXPRESSION TAG                 
SEQADV 6BZH SER A   -3  UNP  Q6Q899              EXPRESSION TAG                 
SEQADV 6BZH SER A   -2  UNP  Q6Q899              EXPRESSION TAG                 
SEQADV 6BZH ALA A   -1  UNP  Q6Q899              EXPRESSION TAG                 
SEQADV 6BZH ARG A    0  UNP  Q6Q899              EXPRESSION TAG                 
SEQADV 6BZH GLN A    1  UNP  Q6Q899              EXPRESSION TAG                 
SEQADV 6BZH GLY B   -4  UNP  Q6Q899              EXPRESSION TAG                 
SEQADV 6BZH SER B   -3  UNP  Q6Q899              EXPRESSION TAG                 
SEQADV 6BZH SER B   -2  UNP  Q6Q899              EXPRESSION TAG                 
SEQADV 6BZH ALA B   -1  UNP  Q6Q899              EXPRESSION TAG                 
SEQADV 6BZH ARG B    0  UNP  Q6Q899              EXPRESSION TAG                 
SEQADV 6BZH GLN B    1  UNP  Q6Q899              EXPRESSION TAG                 
SEQADV 6BZH GLY C   -4  UNP  Q6Q899              EXPRESSION TAG                 
SEQADV 6BZH SER C   -3  UNP  Q6Q899              EXPRESSION TAG                 
SEQADV 6BZH SER C   -2  UNP  Q6Q899              EXPRESSION TAG                 
SEQADV 6BZH ALA C   -1  UNP  Q6Q899              EXPRESSION TAG                 
SEQADV 6BZH ARG C    0  UNP  Q6Q899              EXPRESSION TAG                 
SEQADV 6BZH GLN C    1  UNP  Q6Q899              EXPRESSION TAG                 
SEQADV 6BZH GLY D   -4  UNP  Q6Q899              EXPRESSION TAG                 
SEQADV 6BZH SER D   -3  UNP  Q6Q899              EXPRESSION TAG                 
SEQADV 6BZH SER D   -2  UNP  Q6Q899              EXPRESSION TAG                 
SEQADV 6BZH ALA D   -1  UNP  Q6Q899              EXPRESSION TAG                 
SEQADV 6BZH ARG D    0  UNP  Q6Q899              EXPRESSION TAG                 
SEQADV 6BZH GLN D    1  UNP  Q6Q899              EXPRESSION TAG                 
SEQADV 6BZH GLY E   -4  UNP  Q6Q899              EXPRESSION TAG                 
SEQADV 6BZH SER E   -3  UNP  Q6Q899              EXPRESSION TAG                 
SEQADV 6BZH SER E   -2  UNP  Q6Q899              EXPRESSION TAG                 
SEQADV 6BZH ALA E   -1  UNP  Q6Q899              EXPRESSION TAG                 
SEQADV 6BZH ARG E    0  UNP  Q6Q899              EXPRESSION TAG                 
SEQADV 6BZH GLN E    1  UNP  Q6Q899              EXPRESSION TAG                 
SEQRES   1 A  194  GLY SER SER ALA ARG GLN THR ALA GLU GLN ARG GLN ASN          
SEQRES   2 A  194  LEU GLN ALA PHE ARG ASP TYR ILE LYS LYS ILE LEU ASP          
SEQRES   3 A  194  PRO THR TYR ILE LEU SER TYR MET SER SER TRP LEU GLU          
SEQRES   4 A  194  ASP GLU GLU VAL GLN TYR ILE GLN ALA GLU LYS ASN ASN          
SEQRES   5 A  194  LYS GLY PRO MET GLU ALA ALA SER LEU PHE LEU GLN TYR          
SEQRES   6 A  194  LEU LEU LYS LEU GLN SER GLU GLY TRP PHE GLN ALA PHE          
SEQRES   7 A  194  LEU ASP ALA LEU TYR HIS ALA GLY TYR CYS GLY LEU CYS          
SEQRES   8 A  194  GLU ALA ILE GLU SER TRP ASP PHE GLN LYS ILE GLU LYS          
SEQRES   9 A  194  LEU GLU GLU HIS ARG LEU LEU LEU ARG ARG LEU GLU PRO          
SEQRES  10 A  194  GLU PHE LYS ALA THR VAL ASP PRO ASN ASP ILE LEU SER          
SEQRES  11 A  194  GLU LEU SER GLU CYS LEU ILE ASN GLN GLU CYS GLU GLU          
SEQRES  12 A  194  ILE ARG GLN ILE ARG ASP THR LYS GLY ARG MET ALA GLY          
SEQRES  13 A  194  ALA GLU LYS MET ALA GLU CYS LEU ILE ARG SER ASP LYS          
SEQRES  14 A  194  GLU ASN TRP PRO LYS VAL LEU GLN LEU ALA LEU GLU LYS          
SEQRES  15 A  194  ASP ASN SER LYS PHE SER GLU LEU TRP ILE VAL ASP              
SEQRES   1 B  194  GLY SER SER ALA ARG GLN THR ALA GLU GLN ARG GLN ASN          
SEQRES   2 B  194  LEU GLN ALA PHE ARG ASP TYR ILE LYS LYS ILE LEU ASP          
SEQRES   3 B  194  PRO THR TYR ILE LEU SER TYR MET SER SER TRP LEU GLU          
SEQRES   4 B  194  ASP GLU GLU VAL GLN TYR ILE GLN ALA GLU LYS ASN ASN          
SEQRES   5 B  194  LYS GLY PRO MET GLU ALA ALA SER LEU PHE LEU GLN TYR          
SEQRES   6 B  194  LEU LEU LYS LEU GLN SER GLU GLY TRP PHE GLN ALA PHE          
SEQRES   7 B  194  LEU ASP ALA LEU TYR HIS ALA GLY TYR CYS GLY LEU CYS          
SEQRES   8 B  194  GLU ALA ILE GLU SER TRP ASP PHE GLN LYS ILE GLU LYS          
SEQRES   9 B  194  LEU GLU GLU HIS ARG LEU LEU LEU ARG ARG LEU GLU PRO          
SEQRES  10 B  194  GLU PHE LYS ALA THR VAL ASP PRO ASN ASP ILE LEU SER          
SEQRES  11 B  194  GLU LEU SER GLU CYS LEU ILE ASN GLN GLU CYS GLU GLU          
SEQRES  12 B  194  ILE ARG GLN ILE ARG ASP THR LYS GLY ARG MET ALA GLY          
SEQRES  13 B  194  ALA GLU LYS MET ALA GLU CYS LEU ILE ARG SER ASP LYS          
SEQRES  14 B  194  GLU ASN TRP PRO LYS VAL LEU GLN LEU ALA LEU GLU LYS          
SEQRES  15 B  194  ASP ASN SER LYS PHE SER GLU LEU TRP ILE VAL ASP              
SEQRES   1 C  194  GLY SER SER ALA ARG GLN THR ALA GLU GLN ARG GLN ASN          
SEQRES   2 C  194  LEU GLN ALA PHE ARG ASP TYR ILE LYS LYS ILE LEU ASP          
SEQRES   3 C  194  PRO THR TYR ILE LEU SER TYR MET SER SER TRP LEU GLU          
SEQRES   4 C  194  ASP GLU GLU VAL GLN TYR ILE GLN ALA GLU LYS ASN ASN          
SEQRES   5 C  194  LYS GLY PRO MET GLU ALA ALA SER LEU PHE LEU GLN TYR          
SEQRES   6 C  194  LEU LEU LYS LEU GLN SER GLU GLY TRP PHE GLN ALA PHE          
SEQRES   7 C  194  LEU ASP ALA LEU TYR HIS ALA GLY TYR CYS GLY LEU CYS          
SEQRES   8 C  194  GLU ALA ILE GLU SER TRP ASP PHE GLN LYS ILE GLU LYS          
SEQRES   9 C  194  LEU GLU GLU HIS ARG LEU LEU LEU ARG ARG LEU GLU PRO          
SEQRES  10 C  194  GLU PHE LYS ALA THR VAL ASP PRO ASN ASP ILE LEU SER          
SEQRES  11 C  194  GLU LEU SER GLU CYS LEU ILE ASN GLN GLU CYS GLU GLU          
SEQRES  12 C  194  ILE ARG GLN ILE ARG ASP THR LYS GLY ARG MET ALA GLY          
SEQRES  13 C  194  ALA GLU LYS MET ALA GLU CYS LEU ILE ARG SER ASP LYS          
SEQRES  14 C  194  GLU ASN TRP PRO LYS VAL LEU GLN LEU ALA LEU GLU LYS          
SEQRES  15 C  194  ASP ASN SER LYS PHE SER GLU LEU TRP ILE VAL ASP              
SEQRES   1 D  194  GLY SER SER ALA ARG GLN THR ALA GLU GLN ARG GLN ASN          
SEQRES   2 D  194  LEU GLN ALA PHE ARG ASP TYR ILE LYS LYS ILE LEU ASP          
SEQRES   3 D  194  PRO THR TYR ILE LEU SER TYR MET SER SER TRP LEU GLU          
SEQRES   4 D  194  ASP GLU GLU VAL GLN TYR ILE GLN ALA GLU LYS ASN ASN          
SEQRES   5 D  194  LYS GLY PRO MET GLU ALA ALA SER LEU PHE LEU GLN TYR          
SEQRES   6 D  194  LEU LEU LYS LEU GLN SER GLU GLY TRP PHE GLN ALA PHE          
SEQRES   7 D  194  LEU ASP ALA LEU TYR HIS ALA GLY TYR CYS GLY LEU CYS          
SEQRES   8 D  194  GLU ALA ILE GLU SER TRP ASP PHE GLN LYS ILE GLU LYS          
SEQRES   9 D  194  LEU GLU GLU HIS ARG LEU LEU LEU ARG ARG LEU GLU PRO          
SEQRES  10 D  194  GLU PHE LYS ALA THR VAL ASP PRO ASN ASP ILE LEU SER          
SEQRES  11 D  194  GLU LEU SER GLU CYS LEU ILE ASN GLN GLU CYS GLU GLU          
SEQRES  12 D  194  ILE ARG GLN ILE ARG ASP THR LYS GLY ARG MET ALA GLY          
SEQRES  13 D  194  ALA GLU LYS MET ALA GLU CYS LEU ILE ARG SER ASP LYS          
SEQRES  14 D  194  GLU ASN TRP PRO LYS VAL LEU GLN LEU ALA LEU GLU LYS          
SEQRES  15 D  194  ASP ASN SER LYS PHE SER GLU LEU TRP ILE VAL ASP              
SEQRES   1 E  194  GLY SER SER ALA ARG GLN THR ALA GLU GLN ARG GLN ASN          
SEQRES   2 E  194  LEU GLN ALA PHE ARG ASP TYR ILE LYS LYS ILE LEU ASP          
SEQRES   3 E  194  PRO THR TYR ILE LEU SER TYR MET SER SER TRP LEU GLU          
SEQRES   4 E  194  ASP GLU GLU VAL GLN TYR ILE GLN ALA GLU LYS ASN ASN          
SEQRES   5 E  194  LYS GLY PRO MET GLU ALA ALA SER LEU PHE LEU GLN TYR          
SEQRES   6 E  194  LEU LEU LYS LEU GLN SER GLU GLY TRP PHE GLN ALA PHE          
SEQRES   7 E  194  LEU ASP ALA LEU TYR HIS ALA GLY TYR CYS GLY LEU CYS          
SEQRES   8 E  194  GLU ALA ILE GLU SER TRP ASP PHE GLN LYS ILE GLU LYS          
SEQRES   9 E  194  LEU GLU GLU HIS ARG LEU LEU LEU ARG ARG LEU GLU PRO          
SEQRES  10 E  194  GLU PHE LYS ALA THR VAL ASP PRO ASN ASP ILE LEU SER          
SEQRES  11 E  194  GLU LEU SER GLU CYS LEU ILE ASN GLN GLU CYS GLU GLU          
SEQRES  12 E  194  ILE ARG GLN ILE ARG ASP THR LYS GLY ARG MET ALA GLY          
SEQRES  13 E  194  ALA GLU LYS MET ALA GLU CYS LEU ILE ARG SER ASP LYS          
SEQRES  14 E  194  GLU ASN TRP PRO LYS VAL LEU GLN LEU ALA LEU GLU LYS          
SEQRES  15 E  194  ASP ASN SER LYS PHE SER GLU LEU TRP ILE VAL ASP              
HET    EDO  A 201      10                                                       
HET     CL  A 202       1                                                       
HET     CL  A 203       1                                                       
HET    EDO  B 201      10                                                       
HET    EDO  C 201       4                                                       
HET    EDO  C 202      10                                                       
HET     CL  D 201       1                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM      CL CHLORIDE ION                                                     
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   6  EDO    4(C2 H6 O2)                                                  
FORMUL   7   CL    3(CL 1-)                                                     
FORMUL  13  HOH   *34(H2 O)                                                     
HELIX    1 AA1 SER A   -2  PHE A   12  1                                  15    
HELIX    2 AA2 PHE A   12  LEU A   20  1                                   9    
HELIX    3 AA3 ASP A   21  TYR A   24  5                                   4    
HELIX    4 AA4 ILE A   25  SER A   30  1                                   6    
HELIX    5 AA5 GLU A   34  LYS A   48  1                                  15    
HELIX    6 AA6 GLY A   49  LEU A   62  1                                  14    
HELIX    7 AA7 GLY A   68  GLY A   81  1                                  14    
HELIX    8 AA8 TYR A   82  TRP A   92  1                                  11    
HELIX    9 AA9 PHE A   94  LYS A   99  1                                   6    
HELIX   10 AB1 LEU A  100  LEU A  110  1                                  11    
HELIX   11 AB2 LEU A  110  VAL A  118  1                                   9    
HELIX   12 AB3 ASP A  119  SER A  128  1                                  10    
HELIX   13 AB4 GLU A  129  LEU A  131  5                                   3    
HELIX   14 AB5 ILE A  132  GLY A  147  1                                  16    
HELIX   15 AB6 GLY A  147  ARG A  161  1                                  15    
HELIX   16 AB7 ASN A  166  ASP A  178  1                                  13    
HELIX   17 AB8 SER A  180  TRP A  186  5                                   7    
HELIX   18 AB9 SER B   -2  PHE B   12  1                                  15    
HELIX   19 AC1 PHE B   12  LYS B   18  1                                   7    
HELIX   20 AC2 ASP B   21  TYR B   24  5                                   4    
HELIX   21 AC3 ILE B   25  LEU B   33  1                                   9    
HELIX   22 AC4 GLU B   34  GLY B   49  1                                  16    
HELIX   23 AC5 GLY B   49  LEU B   62  1                                  14    
HELIX   24 AC6 GLY B   68  GLY B   81  1                                  14    
HELIX   25 AC7 TYR B   82  TRP B   92  1                                  11    
HELIX   26 AC8 PHE B   94  LYS B   99  1                                   6    
HELIX   27 AC9 LEU B  100  LEU B  110  1                                  11    
HELIX   28 AD1 LEU B  110  VAL B  118  1                                   9    
HELIX   29 AD2 ASP B  119  LEU B  124  1                                   6    
HELIX   30 AD3 LEU B  127  LEU B  131  5                                   5    
HELIX   31 AD4 ILE B  132  LYS B  146  1                                  15    
HELIX   32 AD5 GLY B  147  ARG B  161  1                                  15    
HELIX   33 AD6 ASN B  166  ASN B  179  1                                  14    
HELIX   34 AD7 PHE B  182  TRP B  186  5                                   5    
HELIX   35 AD8 ARG C    0  PHE C   12  1                                  13    
HELIX   36 AD9 PHE C   12  LEU C   20  1                                   9    
HELIX   37 AE1 ASP C   21  ILE C   25  5                                   5    
HELIX   38 AE2 GLU C   34  GLY C   49  1                                  16    
HELIX   39 AE3 GLY C   49  LEU C   62  1                                  14    
HELIX   40 AE4 GLY C   68  GLY C   81  1                                  14    
HELIX   41 AE5 TYR C   82  TRP C   92  1                                  11    
HELIX   42 AE6 PHE C   94  LYS C   99  1                                   6    
HELIX   43 AE7 LEU C  100  LEU C  110  1                                  11    
HELIX   44 AE8 LEU C  110  VAL C  118  1                                   9    
HELIX   45 AE9 ASP C  119  SER C  128  1                                  10    
HELIX   46 AF1 ILE C  132  GLY C  147  1                                  16    
HELIX   47 AF2 GLY C  147  ARG C  161  1                                  15    
HELIX   48 AF3 ASN C  166  ASN C  179  1                                  14    
HELIX   49 AF4 SER C  180  TRP C  186  5                                   7    
HELIX   50 AF5 GLN D    1  LYS D   17  1                                  17    
HELIX   51 AF6 ASP D   21  TYR D   24  5                                   4    
HELIX   52 AF7 ILE D   25  SER D   30  1                                   6    
HELIX   53 AF8 GLU D   34  GLY D   49  1                                  16    
HELIX   54 AF9 GLY D   49  LEU D   62  1                                  14    
HELIX   55 AG1 GLY D   68  GLY D   81  1                                  14    
HELIX   56 AG2 TYR D   82  TRP D   92  1                                  11    
HELIX   57 AG3 PHE D   94  LYS D   99  1                                   6    
HELIX   58 AG4 LEU D  100  LEU D  110  1                                  11    
HELIX   59 AG5 LEU D  110  VAL D  118  1                                   9    
HELIX   60 AG6 ASP D  119  LEU D  124  1                                   6    
HELIX   61 AG7 LEU D  127  LEU D  131  5                                   5    
HELIX   62 AG8 ILE D  132  GLY D  147  1                                  16    
HELIX   63 AG9 GLY D  147  ARG D  161  1                                  15    
HELIX   64 AH1 ASN D  166  ASP D  178  1                                  13    
HELIX   65 AH2 PHE D  182  TRP D  186  5                                   5    
HELIX   66 AH3 ALA E   -1  PHE E   12  1                                  14    
HELIX   67 AH4 PHE E   12  LYS E   18  1                                   7    
HELIX   68 AH5 ASP E   21  TYR E   24  5                                   4    
HELIX   69 AH6 ILE E   25  SER E   30  1                                   6    
HELIX   70 AH7 GLU E   34  GLY E   49  1                                  16    
HELIX   71 AH8 GLY E   49  LEU E   62  1                                  14    
HELIX   72 AH9 GLY E   68  GLY E   81  1                                  14    
HELIX   73 AI1 TYR E   82  TRP E   92  1                                  11    
HELIX   74 AI2 PHE E   94  LYS E   99  1                                   6    
HELIX   75 AI3 LEU E  100  LEU E  110  1                                  11    
HELIX   76 AI4 LEU E  110  VAL E  118  1                                   9    
HELIX   77 AI5 ASP E  119  LEU E  124  1                                   6    
HELIX   78 AI6 ILE E  132  LYS E  146  1                                  15    
HELIX   79 AI7 GLY E  147  ARG E  161  1                                  15    
HELIX   80 AI8 ASN E  166  ASP E  178  1                                  13    
HELIX   81 AI9 SER E  180  TRP E  186  5                                   7    
SITE     1 AC1  1 ASN A 133                                                     
SITE     1 AC2  5 THR A 117  ARG A 148  SER B  -2  SER B  -3                    
SITE     2 AC2  5 GLU B  67                                                     
SITE     1 AC3  4 LYS B  48  GLU C  36  GLU C  37  TYR C  60                    
SITE     1 AC4  3 GLN C  71  ASP C  75  GLU C  90                               
SITE     1 AC5  2 ARG D  13  SER D  55                                          
CRYST1   90.190   97.560  113.290  90.00  90.00  90.00 P 21 21 21   20          
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      0.011088  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010250  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008827        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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