GenomeNet

Database: PDB
Entry: 6O5F
LinkDB: 6O5F
Original site: 6O5F 
HEADER    HYDROLASE/RNA                           02-MAR-19   6O5F              
TITLE     CRYSTAL STRUCTURE OF DEAD-BOX RNA HELICASE DDX3X AT PRE-UNWOUND STATE 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ATP-DEPENDENT RNA HELICASE DDX3X;                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: DEAD BOX PROTEIN 3,X-CHROMOSOMAL,DEAD BOX,X ISOFORM,        
COMPND   5 HELICASE-LIKE PROTEIN 2,HLP2;                                        
COMPND   6 EC: 3.6.4.13;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: RNA (5'-                                                   
COMPND  10 R(P*CP*AP*AP*GP*GP*UP*CP*AP*UP*UP*CP*GP*CP*AP*AP*GP*AP*GP*UP*GP*GP*CP
COMPND  11 *C)-3');                                                             
COMPND  12 CHAIN: C, D;                                                         
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: DDX3X, DBX, DDX3;                                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  11 ORGANISM_TAXID: 32630                                                
KEYWDS    DDX3X, DEAD-BOX, RNA HELICASE, HYDROLASE, HYDROLASE-RNA COMPLEX       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.SONG,X.JI                                                           
REVDAT   1   24-JUL-19 6O5F    0                                                
JRNL        AUTH   H.SONG,X.JI                                                  
JRNL        TITL   THE MECHANISM OF RNA DUPLEX RECOGNITION AND UNWINDING BY     
JRNL        TITL 2 DEAD-BOX HELICASE DDX3X.                                     
JRNL        REF    NAT COMMUN                    V.  10  3085 2019              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   31300642                                                     
JRNL        DOI    10.1038/S41467-019-11083-2                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.14_3260                                     
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.90                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.150                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 37345                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.213                           
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1010                            
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 35.9053 -  4.7861    0.93     5000   135  0.1997 0.2038        
REMARK   3     2  4.7861 -  3.8003    0.92     4924   136  0.1767 0.2166        
REMARK   3     3  3.8003 -  3.3203    0.96     5192   154  0.2044 0.2356        
REMARK   3     4  3.3203 -  3.0169    0.98     5261   143  0.2329 0.3228        
REMARK   3     5  3.0169 -  2.8007    0.99     5370   143  0.2552 0.3333        
REMARK   3     6  2.8007 -  2.6356    0.98     5274   149  0.2715 0.2931        
REMARK   3     7  2.6356 -  2.5037    0.98     5314   150  0.3008 0.3527        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.890           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
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      :  0.004           7913                                  
REMARK   3   ANGLE     :  0.700          10918                                  
REMARK   3   CHIRALITY :  0.046           1249                                  
REMARK   3   PLANARITY :  0.004           1243                                  
REMARK   3   DIHEDRAL  : 21.168           3142                                  
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 6O5F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAR-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000240016.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-FEB-18                          
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               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX300-HS                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37345                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.4                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.8000                             
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     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.900                              
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: 5E7I                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.93                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% (V/V) PEG 3350, 0.2 M MAGNESIUM      
REMARK 280  CHLORIDE, 0.1 M TRIS PH 8.5, VAPOR DIFFUSION, SITTING DROP,         
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       76.82100            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      153.64200            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7190 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 44720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -91.0 KCAL/MOL                        
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 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     ASP A   132                                                      
REMARK 465     GLU A   133                                                      
REMARK 465     SER A   152                                                      
REMARK 465     GLY A   153                                                      
REMARK 465     GLY A   154                                                      
REMARK 465     ASN A   155                                                      
REMARK 465     THR A   156                                                      
REMARK 465     GLY A   157                                                      
REMARK 465     ILE A   158                                                      
REMARK 465     ASN A   159                                                      
REMARK 465     PHE A   160                                                      
REMARK 465     GLU A   161                                                      
REMARK 465     LYS A   255                                                      
REMARK 465     GLU A   256                                                      
REMARK 465     ASN A   257                                                      
REMARK 465     GLY A   258                                                      
REMARK 465     ARG A   259                                                      
REMARK 465     TYR A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     ARG A   262                                                      
REMARK 465     ARG A   263                                                      
REMARK 465     GLY A   406                                                      
REMARK 465     ARG A   407                                                      
REMARK 465     VAL A   408                                                      
REMARK 465     GLY A   409                                                      
REMARK 465     SER A   410                                                      
REMARK 465     THR A   411                                                      
REMARK 465     SER A   412                                                      
REMARK 465     GLY A   504                                                      
REMARK 465     LEU A   505                                                      
REMARK 465     ASP A   506                                                      
REMARK 465     ILE A   507                                                      
REMARK 465     LYS A   581                                                      
REMARK 465     GLY A   582                                                      
REMARK 465     SER A   583                                                      
REMARK 465     SER A   584                                                      
REMARK 465     ARG A   585                                                      
REMARK 465     GLY A   586                                                      
REMARK 465     ARG A   587                                                      
REMARK 465     SER A   588                                                      
REMARK 465     LYS A   589                                                      
REMARK 465     SER A   590                                                      
REMARK 465     SER A   591                                                      
REMARK 465     ARG A   592                                                      
REMARK 465     PHE A   593                                                      
REMARK 465     SER A   594                                                      
REMARK 465     GLY A   595                                                      
REMARK 465     GLY A   596                                                      
REMARK 465     PHE A   597                                                      
REMARK 465     GLY A   598                                                      
REMARK 465     ALA A   599                                                      
REMARK 465     ARG A   600                                                      
REMARK 465     ASP A   601                                                      
REMARK 465     TYR A   602                                                      
REMARK 465     ARG A   603                                                      
REMARK 465     GLN A   604                                                      
REMARK 465     SER A   605                                                      
REMARK 465     SER A   606                                                      
REMARK 465     GLY A   607                                                      
REMARK 465     ASP B   132                                                      
REMARK 465     GLU B   133                                                      
REMARK 465     SER B   152                                                      
REMARK 465     GLY B   153                                                      
REMARK 465     GLY B   154                                                      
REMARK 465     ASN B   155                                                      
REMARK 465     THR B   156                                                      
REMARK 465     GLY B   157                                                      
REMARK 465     ILE B   158                                                      
REMARK 465     ASN B   159                                                      
REMARK 465     PHE B   160                                                      
REMARK 465     GLU B   161                                                      
REMARK 465     LYS B   255                                                      
REMARK 465     GLU B   256                                                      
REMARK 465     ASN B   257                                                      
REMARK 465     GLY B   258                                                      
REMARK 465     ARG B   259                                                      
REMARK 465     TYR B   260                                                      
REMARK 465     GLY B   261                                                      
REMARK 465     ARG B   262                                                      
REMARK 465     ARG B   263                                                      
REMARK 465     GLY B   406                                                      
REMARK 465     ARG B   407                                                      
REMARK 465     VAL B   408                                                      
REMARK 465     GLY B   409                                                      
REMARK 465     SER B   410                                                      
REMARK 465     THR B   411                                                      
REMARK 465     SER B   412                                                      
REMARK 465     GLY B   504                                                      
REMARK 465     LEU B   505                                                      
REMARK 465     ASP B   506                                                      
REMARK 465     ILE B   507                                                      
REMARK 465     LYS B   581                                                      
REMARK 465     GLY B   582                                                      
REMARK 465     SER B   583                                                      
REMARK 465     SER B   584                                                      
REMARK 465     ARG B   585                                                      
REMARK 465     GLY B   586                                                      
REMARK 465     ARG B   587                                                      
REMARK 465     SER B   588                                                      
REMARK 465     LYS B   589                                                      
REMARK 465     SER B   590                                                      
REMARK 465     SER B   591                                                      
REMARK 465     ARG B   592                                                      
REMARK 465     PHE B   593                                                      
REMARK 465     SER B   594                                                      
REMARK 465     GLY B   595                                                      
REMARK 465     GLY B   596                                                      
REMARK 465     PHE B   597                                                      
REMARK 465     GLY B   598                                                      
REMARK 465     ALA B   599                                                      
REMARK 465     ARG B   600                                                      
REMARK 465     ASP B   601                                                      
REMARK 465     TYR B   602                                                      
REMARK 465     ARG B   603                                                      
REMARK 465     GLN B   604                                                      
REMARK 465     SER B   605                                                      
REMARK 465     SER B   606                                                      
REMARK 465     GLY B   607                                                      
REMARK 465       U C    24                                                      
REMARK 465       U C    25                                                      
REMARK 465       G C    26                                                      
REMARK 465       C C    27                                                      
REMARK 465       G C    28                                                      
REMARK 465       C D     1                                                      
REMARK 465       A D     2                                                      
REMARK 465       A D     3                                                      
REMARK 465       G D    28                                                      
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    ALA A 253       51.95    -93.17                                   
REMARK 500    ASP A 368     -155.44   -142.13                                   
REMARK 500    VAL A 375      -62.48    -93.22                                   
REMARK 500    ALA A 499       -9.99    -57.42                                   
REMARK 500    VAL A 535       51.35     37.40                                   
REMARK 500    THR B 201      -76.10    -87.18                                   
REMARK 500    ASP B 368     -157.07   -141.14                                   
REMARK 500    VAL B 375      -61.77    -93.76                                   
REMARK 500    ASN B 414       30.50    -89.58                                   
REMARK 500    VAL B 535       69.06     20.16                                   
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 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 702                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 703                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 704                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 702                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 703                  
DBREF  6O5F A  132   607  UNP    O00571   DDX3X_HUMAN    132    607             
DBREF  6O5F B  132   607  UNP    O00571   DDX3X_HUMAN    132    607             
DBREF  6O5F C    1    28  PDB    6O5F     6O5F             1     28             
DBREF  6O5F D    1    28  PDB    6O5F     6O5F             1     28             
SEQRES   1 A  476  ASP GLU ASP ASP TRP SER LYS PRO LEU PRO PRO SER GLU          
SEQRES   2 A  476  ARG LEU GLU GLN GLU LEU PHE SER GLY GLY ASN THR GLY          
SEQRES   3 A  476  ILE ASN PHE GLU LYS TYR ASP ASP ILE PRO VAL GLU ALA          
SEQRES   4 A  476  THR GLY ASN ASN CYS PRO PRO HIS ILE GLU SER PHE SER          
SEQRES   5 A  476  ASP VAL GLU MET GLY GLU ILE ILE MET GLY ASN ILE GLU          
SEQRES   6 A  476  LEU THR ARG TYR THR ARG PRO THR PRO VAL GLN LYS HIS          
SEQRES   7 A  476  ALA ILE PRO ILE ILE LYS GLU LYS ARG ASP LEU MET ALA          
SEQRES   8 A  476  CYS ALA GLN THR GLY SER GLY LYS THR ALA ALA PHE LEU          
SEQRES   9 A  476  LEU PRO ILE LEU SER GLN ILE TYR SER ASP GLY PRO GLY          
SEQRES  10 A  476  GLU ALA LEU ARG ALA MET LYS GLU ASN GLY ARG TYR GLY          
SEQRES  11 A  476  ARG ARG LYS GLN TYR PRO ILE SER LEU VAL LEU ALA PRO          
SEQRES  12 A  476  THR ARG GLU LEU ALA VAL GLN ILE TYR GLU GLU ALA ARG          
SEQRES  13 A  476  LYS PHE SER TYR ARG SER ARG VAL ARG PRO CYS VAL VAL          
SEQRES  14 A  476  TYR GLY GLY ALA ASP ILE GLY GLN GLN ILE ARG ASP LEU          
SEQRES  15 A  476  GLU ARG GLY CYS HIS LEU LEU VAL ALA THR PRO GLY ARG          
SEQRES  16 A  476  LEU VAL ASP MET MET GLU ARG GLY LYS ILE GLY LEU ASP          
SEQRES  17 A  476  PHE CYS LYS TYR LEU VAL LEU ASP GLU ALA ASP ARG MET          
SEQRES  18 A  476  LEU ASP MET GLY PHE GLU PRO GLN ILE ARG ARG ILE VAL          
SEQRES  19 A  476  GLU GLN ASP THR MET PRO PRO LYS GLY VAL ARG HIS THR          
SEQRES  20 A  476  MET MET PHE SER ALA THR PHE PRO LYS GLU ILE GLN MET          
SEQRES  21 A  476  LEU ALA ARG ASP PHE LEU ASP GLU TYR ILE PHE LEU ALA          
SEQRES  22 A  476  VAL GLY ARG VAL GLY SER THR SER GLU ASN ILE THR GLN          
SEQRES  23 A  476  LYS VAL VAL TRP VAL GLU GLU SER ASP LYS ARG SER PHE          
SEQRES  24 A  476  LEU LEU ASP LEU LEU ASN ALA THR GLY LYS ASP SER LEU          
SEQRES  25 A  476  THR LEU VAL PHE VAL GLU THR LYS LYS GLY ALA ASP SER          
SEQRES  26 A  476  LEU GLU ASP PHE LEU TYR HIS GLU GLY TYR ALA CYS THR          
SEQRES  27 A  476  SER ILE HIS GLY ASP ARG SER GLN ARG ASP ARG GLU GLU          
SEQRES  28 A  476  ALA LEU HIS GLN PHE ARG SER GLY LYS SER PRO ILE LEU          
SEQRES  29 A  476  VAL ALA THR ALA VAL ALA ALA ARG GLY LEU ASP ILE SER          
SEQRES  30 A  476  ASN VAL LYS HIS VAL ILE ASN PHE ASP LEU PRO SER ASP          
SEQRES  31 A  476  ILE GLU GLU TYR VAL HIS ARG ILE GLY ARG THR GLY ARG          
SEQRES  32 A  476  VAL GLY ASN LEU GLY LEU ALA THR SER PHE PHE ASN GLU          
SEQRES  33 A  476  ARG ASN ILE ASN ILE THR LYS ASP LEU LEU ASP LEU LEU          
SEQRES  34 A  476  VAL GLU ALA LYS GLN GLU VAL PRO SER TRP LEU GLU ASN          
SEQRES  35 A  476  MET ALA TYR GLU HIS HIS TYR LYS GLY SER SER ARG GLY          
SEQRES  36 A  476  ARG SER LYS SER SER ARG PHE SER GLY GLY PHE GLY ALA          
SEQRES  37 A  476  ARG ASP TYR ARG GLN SER SER GLY                              
SEQRES   1 B  476  ASP GLU ASP ASP TRP SER LYS PRO LEU PRO PRO SER GLU          
SEQRES   2 B  476  ARG LEU GLU GLN GLU LEU PHE SER GLY GLY ASN THR GLY          
SEQRES   3 B  476  ILE ASN PHE GLU LYS TYR ASP ASP ILE PRO VAL GLU ALA          
SEQRES   4 B  476  THR GLY ASN ASN CYS PRO PRO HIS ILE GLU SER PHE SER          
SEQRES   5 B  476  ASP VAL GLU MET GLY GLU ILE ILE MET GLY ASN ILE GLU          
SEQRES   6 B  476  LEU THR ARG TYR THR ARG PRO THR PRO VAL GLN LYS HIS          
SEQRES   7 B  476  ALA ILE PRO ILE ILE LYS GLU LYS ARG ASP LEU MET ALA          
SEQRES   8 B  476  CYS ALA GLN THR GLY SER GLY LYS THR ALA ALA PHE LEU          
SEQRES   9 B  476  LEU PRO ILE LEU SER GLN ILE TYR SER ASP GLY PRO GLY          
SEQRES  10 B  476  GLU ALA LEU ARG ALA MET LYS GLU ASN GLY ARG TYR GLY          
SEQRES  11 B  476  ARG ARG LYS GLN TYR PRO ILE SER LEU VAL LEU ALA PRO          
SEQRES  12 B  476  THR ARG GLU LEU ALA VAL GLN ILE TYR GLU GLU ALA ARG          
SEQRES  13 B  476  LYS PHE SER TYR ARG SER ARG VAL ARG PRO CYS VAL VAL          
SEQRES  14 B  476  TYR GLY GLY ALA ASP ILE GLY GLN GLN ILE ARG ASP LEU          
SEQRES  15 B  476  GLU ARG GLY CYS HIS LEU LEU VAL ALA THR PRO GLY ARG          
SEQRES  16 B  476  LEU VAL ASP MET MET GLU ARG GLY LYS ILE GLY LEU ASP          
SEQRES  17 B  476  PHE CYS LYS TYR LEU VAL LEU ASP GLU ALA ASP ARG MET          
SEQRES  18 B  476  LEU ASP MET GLY PHE GLU PRO GLN ILE ARG ARG ILE VAL          
SEQRES  19 B  476  GLU GLN ASP THR MET PRO PRO LYS GLY VAL ARG HIS THR          
SEQRES  20 B  476  MET MET PHE SER ALA THR PHE PRO LYS GLU ILE GLN MET          
SEQRES  21 B  476  LEU ALA ARG ASP PHE LEU ASP GLU TYR ILE PHE LEU ALA          
SEQRES  22 B  476  VAL GLY ARG VAL GLY SER THR SER GLU ASN ILE THR GLN          
SEQRES  23 B  476  LYS VAL VAL TRP VAL GLU GLU SER ASP LYS ARG SER PHE          
SEQRES  24 B  476  LEU LEU ASP LEU LEU ASN ALA THR GLY LYS ASP SER LEU          
SEQRES  25 B  476  THR LEU VAL PHE VAL GLU THR LYS LYS GLY ALA ASP SER          
SEQRES  26 B  476  LEU GLU ASP PHE LEU TYR HIS GLU GLY TYR ALA CYS THR          
SEQRES  27 B  476  SER ILE HIS GLY ASP ARG SER GLN ARG ASP ARG GLU GLU          
SEQRES  28 B  476  ALA LEU HIS GLN PHE ARG SER GLY LYS SER PRO ILE LEU          
SEQRES  29 B  476  VAL ALA THR ALA VAL ALA ALA ARG GLY LEU ASP ILE SER          
SEQRES  30 B  476  ASN VAL LYS HIS VAL ILE ASN PHE ASP LEU PRO SER ASP          
SEQRES  31 B  476  ILE GLU GLU TYR VAL HIS ARG ILE GLY ARG THR GLY ARG          
SEQRES  32 B  476  VAL GLY ASN LEU GLY LEU ALA THR SER PHE PHE ASN GLU          
SEQRES  33 B  476  ARG ASN ILE ASN ILE THR LYS ASP LEU LEU ASP LEU LEU          
SEQRES  34 B  476  VAL GLU ALA LYS GLN GLU VAL PRO SER TRP LEU GLU ASN          
SEQRES  35 B  476  MET ALA TYR GLU HIS HIS TYR LYS GLY SER SER ARG GLY          
SEQRES  36 B  476  ARG SER LYS SER SER ARG PHE SER GLY GLY PHE GLY ALA          
SEQRES  37 B  476  ARG ASP TYR ARG GLN SER SER GLY                              
SEQRES   1 C   28    C   A   A   G   G   U   C   A   U   U   C   G   C          
SEQRES   2 C   28    A   A   G   A   G   U   G   G   C   C   U   U   G          
SEQRES   3 C   28    C   G                                                      
SEQRES   1 D   28    C   A   A   G   G   U   C   A   U   U   C   G   C          
SEQRES   2 D   28    A   A   G   A   G   U   G   G   C   C   U   U   G          
SEQRES   3 D   28    C   G                                                      
HET     CL  A 701       1                                                       
HET     CL  A 702       1                                                       
HET     CL  A 703       1                                                       
HET     CL  A 704       1                                                       
HET     CL  B 701       1                                                       
HET     CL  B 702       1                                                       
HET     CL  B 703       1                                                       
HETNAM      CL CHLORIDE ION                                                     
FORMUL   5   CL    7(CL 1-)                                                     
FORMUL  12  HOH   *72(H2 O)                                                     
HELIX    1 AA1 SER A  143  PHE A  151  1                                   9    
HELIX    2 AA2 SER A  181  VAL A  185  5                                   5    
HELIX    3 AA3 MET A  187  ARG A  199  1                                  13    
HELIX    4 AA4 THR A  204  GLU A  216  1                                  13    
HELIX    5 AA5 GLY A  229  GLY A  246  1                                  18    
HELIX    6 AA6 PRO A  247  ALA A  253  1                                   7    
HELIX    7 AA7 THR A  275  SER A  290  1                                  16    
HELIX    8 AA8 ASP A  305  GLU A  314  1                                  10    
HELIX    9 AA9 THR A  323  ARG A  333  1                                  11    
HELIX   10 AB1 GLU A  348  MET A  355  1                                   8    
HELIX   11 AB2 PHE A  357  GLU A  366  1                                  10    
HELIX   12 AB3 PRO A  386  LEU A  397  1                                  12    
HELIX   13 AB4 GLU A  423  SER A  425  5                                   3    
HELIX   14 AB5 ASP A  426  ALA A  437  1                                  12    
HELIX   15 AB6 THR A  450  GLU A  464  1                                  15    
HELIX   16 AB7 SER A  476  SER A  489  1                                  14    
HELIX   17 AB8 ALA A  499  ALA A  502  5                                   4    
HELIX   18 AB9 ASP A  521  GLY A  530  1                                  10    
HELIX   19 AC1 ASN A  546  ASN A  551  5                                   6    
HELIX   20 AC2 ILE A  552  ALA A  563  1                                  12    
HELIX   21 AC3 PRO A  568  HIS A  579  1                                  12    
HELIX   22 AC4 SER B  143  PHE B  151  1                                   9    
HELIX   23 AC5 SER B  181  VAL B  185  5                                   5    
HELIX   24 AC6 MET B  187  ARG B  199  1                                  13    
HELIX   25 AC7 THR B  204  GLU B  216  1                                  13    
HELIX   26 AC8 GLY B  229  GLY B  246  1                                  18    
HELIX   27 AC9 PRO B  247  ALA B  253  1                                   7    
HELIX   28 AD1 THR B  275  SER B  290  1                                  16    
HELIX   29 AD2 ASP B  305  GLU B  314  1                                  10    
HELIX   30 AD3 THR B  323  ARG B  333  1                                  11    
HELIX   31 AD4 GLU B  348  MET B  355  1                                   8    
HELIX   32 AD5 PHE B  357  GLU B  366  1                                  10    
HELIX   33 AD6 PRO B  386  LEU B  397  1                                  12    
HELIX   34 AD7 GLU B  423  SER B  425  5                                   3    
HELIX   35 AD8 ASP B  426  ASN B  436  1                                  11    
HELIX   36 AD9 THR B  450  GLU B  464  1                                  15    
HELIX   37 AE1 SER B  476  SER B  489  1                                  14    
HELIX   38 AE2 ALA B  499  ALA B  502  5                                   4    
HELIX   39 AE3 ASP B  521  GLY B  530  1                                  10    
HELIX   40 AE4 ASN B  546  ASN B  551  5                                   6    
HELIX   41 AE5 ILE B  552  ALA B  563  1                                  12    
HELIX   42 AE6 PRO B  568  HIS B  579  1                                  12    
SHEET    1 AA1 8 GLU A 169  THR A 171  0                                        
SHEET    2 AA1 8 ILE A 401  ALA A 404 -1  O  PHE A 402   N  THR A 171           
SHEET    3 AA1 8 LEU A 220  CYS A 223  1  N  MET A 221   O  LEU A 403           
SHEET    4 AA1 8 HIS A 377  SER A 382  1  O  MET A 380   N  ALA A 222           
SHEET    5 AA1 8 TYR A 343  LEU A 346  1  N  LEU A 346   O  PHE A 381           
SHEET    6 AA1 8 SER A 269  LEU A 272  1  N  LEU A 270   O  TYR A 343           
SHEET    7 AA1 8 LEU A 319  ALA A 322  1  O  LEU A 320   N  VAL A 271           
SHEET    8 AA1 8 PRO A 297  VAL A 300  1  N  CYS A 298   O  LEU A 319           
SHEET    1 AA2 6 ILE A 415  TRP A 421  0                                        
SHEET    2 AA2 6 GLY A 539  PHE A 545  1  O  ALA A 541   N  LYS A 418           
SHEET    3 AA2 6 HIS A 512  ASN A 515  1  N  ASN A 515   O  THR A 542           
SHEET    4 AA2 6 THR A 444  PHE A 447  1  N  LEU A 445   O  ILE A 514           
SHEET    5 AA2 6 ILE A 494  ALA A 497  1  O  LEU A 495   N  VAL A 446           
SHEET    6 AA2 6 CYS A 468  ILE A 471  1  N  THR A 469   O  VAL A 496           
SHEET    1 AA3 8 GLU B 169  THR B 171  0                                        
SHEET    2 AA3 8 ILE B 401  ALA B 404 -1  O  ALA B 404   N  GLU B 169           
SHEET    3 AA3 8 LEU B 220  CYS B 223  1  N  MET B 221   O  ILE B 401           
SHEET    4 AA3 8 HIS B 377  SER B 382  1  O  MET B 380   N  ALA B 222           
SHEET    5 AA3 8 TYR B 343  LEU B 346  1  N  LEU B 346   O  PHE B 381           
SHEET    6 AA3 8 SER B 269  LEU B 272  1  N  LEU B 270   O  TYR B 343           
SHEET    7 AA3 8 LEU B 319  ALA B 322  1  O  LEU B 320   N  SER B 269           
SHEET    8 AA3 8 PRO B 297  VAL B 300  1  N  CYS B 298   O  LEU B 319           
SHEET    1 AA4 6 ILE B 415  TRP B 421  0                                        
SHEET    2 AA4 6 GLY B 539  PHE B 545  1  O  ALA B 541   N  LYS B 418           
SHEET    3 AA4 6 HIS B 512  ASN B 515  1  N  ASN B 515   O  THR B 542           
SHEET    4 AA4 6 THR B 444  PHE B 447  1  N  LEU B 445   O  ILE B 514           
SHEET    5 AA4 6 ILE B 494  ALA B 497  1  O  LEU B 495   N  VAL B 446           
SHEET    6 AA4 6 CYS B 468  ILE B 471  1  N  THR B 469   O  VAL B 496           
SITE     1 AC1  3 THR A 323  GLY A 325  ARG A 326                               
SITE     1 AC2  5 SER A 476  GLN A 477  ARG A 478  ASN B 173                    
SITE     2 AC2  5 HOH B 821                                                     
SITE     1 AC3  7 TYR A 266  PRO A 267  GLY A 337  LEU A 338                    
SITE     2 AC3  7 ASP A 339  PHE A 340  CYS A 341                               
SITE     1 AC4  4 GLY A 227  SER A 228  GLY A 229  LYS A 230                    
SITE     1 AC5  3 THR B 323  GLY B 325  ARG B 326                               
SITE     1 AC6  7 TYR B 266  PRO B 267  GLY B 337  LEU B 338                    
SITE     2 AC6  7 ASP B 339  PHE B 340  CYS B 341                               
SITE     1 AC7  5 GLY A 172  ASN A 173  SER B 476  GLN B 477                    
SITE     2 AC7  5 ARG B 478                                                     
CRYST1   66.102   66.102  230.463  90.00  90.00 120.00 P 31          6          
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      0.015128  0.008734  0.000000        0.00000                         
SCALE2      0.000000  0.017468  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004339        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system