GenomeNet

Database: PDB
Entry: 4PXA
LinkDB: 4PXA
Original site: 4PXA 
HEADER    TRANSLATION, RNA BINDING PROTEIN        22-MAR-14   4PXA              
TITLE     DEAD-BOX RNA HELICASE DDX3X CANCER-ASSOCIATED MUTANT D354V            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ATP-DEPENDENT RNA HELICASE DDX3X;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: D1-D2, UNP RESIDUES 135-582;                               
COMPND   5 SYNONYM: DEAD BOX PROTEIN 3, X-CHROMOSOMAL, DEAD BOX, X ISOFORM,     
COMPND   6 HELICASE-LIKE PROTEIN 2, HLP2;                                       
COMPND   7 EC: 3.6.4.13;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: DBX, DDX3, DDX3X;                                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-RIPL;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PLE230                                    
KEYWDS    DEAD-BOX HELICASE, HYDROLASE, TRANSLATION, RNA BINDING PROTEIN        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.B.EPLING,C.R.GRACE,B.R.LOWE,J.F.PARTRIDGE,E.J.ENEMARK               
REVDAT   2   29-APR-15 4PXA    1       JRNL                                     
REVDAT   1   11-MAR-15 4PXA    0                                                
JRNL        AUTH   L.B.EPLING,C.R.GRACE,B.R.LOWE,J.F.PARTRIDGE,E.J.ENEMARK      
JRNL        TITL   CANCER-ASSOCIATED MUTANTS OF RNA HELICASE DDX3X ARE          
JRNL        TITL 2 DEFECTIVE IN RNA-STIMULATED ATP HYDROLYSIS.                  
JRNL        REF    J.MOL.BIOL.                   V. 427  1779 2015              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   25724843                                                     
JRNL        DOI    10.1016/J.JMB.2015.02.015                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.3                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.85                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1825880.700                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 14843                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 718                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.010                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.31                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1338                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2820                       
REMARK   3   BIN FREE R VALUE                    : 0.3770                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 83                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.041                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3495                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 52                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 97.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.96000                                             
REMARK   3    B22 (A**2) : -0.96000                                             
REMARK   3    B33 (A**2) : 1.92000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.34                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.47                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.48                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.63                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.500                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.400                          
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.860                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : GROUP                                     
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.33                                                 
REMARK   3   BSOL        : 73.12                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NONE                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : DNA-RNA_REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  6  : ADP.PARAM                                      
REMARK   3  PARAMETER FILE  7  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : CARBOHYDRATE.TOP                               
REMARK   3  TOPOLOGY FILE  6   : ADP.TOP                                        
REMARK   3  TOPOLOGY FILE  7   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 4PXA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-APR-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB085334.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-MAR-13                          
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) : 1.0                                
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14993                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 14.000                             
REMARK 200  R MERGE                    (I) : 0.12800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 37.1900                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 14.60                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.64100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.710                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 4PX9 AND 2JGN                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.68                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.06                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.66 M NAH2PO4   0.24 M K2HPO4, VAPOR    
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291.0K                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       76.31650            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       52.87750            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       52.87750            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      114.47475            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       52.87750            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       52.87750            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       38.15825            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       52.87750            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       52.87750            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      114.47475            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       52.87750            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       52.87750            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       38.15825            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       76.31650            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     MET A   116                                                      
REMARK 465     GLY A   117                                                      
REMARK 465     SER A   118                                                      
REMARK 465     SER A   119                                                      
REMARK 465     HIS A   120                                                      
REMARK 465     HIS A   121                                                      
REMARK 465     HIS A   122                                                      
REMARK 465     HIS A   123                                                      
REMARK 465     HIS A   124                                                      
REMARK 465     HIS A   125                                                      
REMARK 465     SER A   126                                                      
REMARK 465     SER A   127                                                      
REMARK 465     GLY A   128                                                      
REMARK 465     LEU A   129                                                      
REMARK 465     VAL A   130                                                      
REMARK 465     PRO A   131                                                      
REMARK 465     ARG A   132                                                      
REMARK 465     GLY A   133                                                      
REMARK 465     SER A   134                                                      
REMARK 465     GLU A   577                                                      
REMARK 465     HIS A   578                                                      
REMARK 465     HIS A   579                                                      
REMARK 465     TYR A   580                                                      
REMARK 465     LYS A   581                                                      
REMARK 465     GLY A   582                                                      
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     ARG A 259    CG   CD   NE   CZ   NH1  NH2                        
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    PRO A 142     -176.25    -60.62                                   
REMARK 500    ASN A 155        1.26     54.27                                   
REMARK 500    ASN A 159       84.92    -61.10                                   
REMARK 500    ASN A 174       45.83     30.56                                   
REMARK 500    HIS A 178      173.70    -48.43                                   
REMARK 500    PHE A 182       -7.93    -56.46                                   
REMARK 500    GLU A 186       99.91    -63.15                                   
REMARK 500    LEU A 197       -8.60    -48.65                                   
REMARK 500    THR A 226      155.75    -41.63                                   
REMARK 500    ALA A 253       40.05    -78.30                                   
REMARK 500    MET A 254      -18.87   -140.46                                   
REMARK 500    ARG A 259       47.62    -81.00                                   
REMARK 500    ARG A 262       59.01   -141.71                                   
REMARK 500    ARG A 263      -89.53    -73.70                                   
REMARK 500    ARG A 292       42.41     70.43                                   
REMARK 500    HIS A 318      -29.42   -148.40                                   
REMARK 500    PRO A 324      -64.72    -26.25                                   
REMARK 500    MET A 355       25.66    -68.47                                   
REMARK 500    VAL A 365      -74.35    -65.61                                   
REMARK 500    ASP A 368     -168.99   -129.72                                   
REMARK 500    THR A 369        1.66    -63.92                                   
REMARK 500    VAL A 405       62.77   -113.30                                   
REMARK 500    LYS A 440       -1.88     35.51                                   
REMARK 500    ARG A 475      153.31    -43.85                                   
REMARK 500    SER A 489       28.22    -77.06                                   
REMARK 500    LYS A 491      -47.22    -14.75                                   
REMARK 500    VAL A 500      -70.55    -48.81                                   
REMARK 500    ALA A 501      -34.72    -32.12                                   
REMARK 500    ARG A 503      103.43    -51.17                                   
REMARK 500    ASN A 509       37.86     83.65                                   
REMARK 500    ARG A 531      -10.39    -49.78                                   
REMARK 500    VAL A 535      136.00    -23.57                                   
REMARK 500    ALA A 563        1.70    -68.07                                   
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 ADP A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 606                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4PX9   RELATED DB: PDB                                   
REMARK 900 DDX3X WILD-TYPE D1                                                   
DBREF  4PXA A  135   582  UNP    O00571   DDX3X_HUMAN    135    582             
SEQADV 4PXA MET A  116  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PXA GLY A  117  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PXA SER A  118  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PXA SER A  119  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PXA HIS A  120  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PXA HIS A  121  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PXA HIS A  122  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PXA HIS A  123  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PXA HIS A  124  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PXA HIS A  125  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PXA SER A  126  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PXA SER A  127  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PXA GLY A  128  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PXA LEU A  129  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PXA VAL A  130  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PXA PRO A  131  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PXA ARG A  132  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PXA GLY A  133  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PXA SER A  134  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PXA VAL A  354  UNP  O00571    ASP   354 ENGINEERED MUTATION            
SEQRES   1 A  467  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  467  LEU VAL PRO ARG GLY SER ASP TRP SER LYS PRO LEU PRO          
SEQRES   3 A  467  PRO SER GLU ARG LEU GLU GLN GLU LEU PHE SER GLY GLY          
SEQRES   4 A  467  ASN THR GLY ILE ASN PHE GLU LYS TYR ASP ASP ILE PRO          
SEQRES   5 A  467  VAL GLU ALA THR GLY ASN ASN CYS PRO PRO HIS ILE GLU          
SEQRES   6 A  467  SER PHE SER ASP VAL GLU MET GLY GLU ILE ILE MET GLY          
SEQRES   7 A  467  ASN ILE GLU LEU THR ARG TYR THR ARG PRO THR PRO VAL          
SEQRES   8 A  467  GLN LYS HIS ALA ILE PRO ILE ILE LYS GLU LYS ARG ASP          
SEQRES   9 A  467  LEU MET ALA CYS ALA GLN THR GLY SER GLY LYS THR ALA          
SEQRES  10 A  467  ALA PHE LEU LEU PRO ILE LEU SER GLN ILE TYR SER ASP          
SEQRES  11 A  467  GLY PRO GLY GLU ALA LEU ARG ALA MET LYS GLU ASN GLY          
SEQRES  12 A  467  ARG TYR GLY ARG ARG LYS GLN TYR PRO ILE SER LEU VAL          
SEQRES  13 A  467  LEU ALA PRO THR ARG GLU LEU ALA VAL GLN ILE TYR GLU          
SEQRES  14 A  467  GLU ALA ARG LYS PHE SER TYR ARG SER ARG VAL ARG PRO          
SEQRES  15 A  467  CYS VAL VAL TYR GLY GLY ALA ASP ILE GLY GLN GLN ILE          
SEQRES  16 A  467  ARG ASP LEU GLU ARG GLY CYS HIS LEU LEU VAL ALA THR          
SEQRES  17 A  467  PRO GLY ARG LEU VAL ASP MET MET GLU ARG GLY LYS ILE          
SEQRES  18 A  467  GLY LEU ASP PHE CYS LYS TYR LEU VAL LEU ASP GLU ALA          
SEQRES  19 A  467  ASP ARG MET LEU VAL MET GLY PHE GLU PRO GLN ILE ARG          
SEQRES  20 A  467  ARG ILE VAL GLU GLN ASP THR MET PRO PRO LYS GLY VAL          
SEQRES  21 A  467  ARG HIS THR MET MET PHE SER ALA THR PHE PRO LYS GLU          
SEQRES  22 A  467  ILE GLN MET LEU ALA ARG ASP PHE LEU ASP GLU TYR ILE          
SEQRES  23 A  467  PHE LEU ALA VAL GLY ARG VAL GLY SER THR SER GLU ASN          
SEQRES  24 A  467  ILE THR GLN LYS VAL VAL TRP VAL GLU GLU SER ASP LYS          
SEQRES  25 A  467  ARG SER PHE LEU LEU ASP LEU LEU ASN ALA THR GLY LYS          
SEQRES  26 A  467  ASP SER LEU THR LEU VAL PHE VAL GLU THR LYS LYS GLY          
SEQRES  27 A  467  ALA ASP SER LEU GLU ASP PHE LEU TYR HIS GLU GLY TYR          
SEQRES  28 A  467  ALA CYS THR SER ILE HIS GLY ASP ARG SER GLN ARG ASP          
SEQRES  29 A  467  ARG GLU GLU ALA LEU HIS GLN PHE ARG SER GLY LYS SER          
SEQRES  30 A  467  PRO ILE LEU VAL ALA THR ALA VAL ALA ALA ARG GLY LEU          
SEQRES  31 A  467  ASP ILE SER ASN VAL LYS HIS VAL ILE ASN PHE ASP LEU          
SEQRES  32 A  467  PRO SER ASP ILE GLU GLU TYR VAL HIS ARG ILE GLY ARG          
SEQRES  33 A  467  THR GLY ARG VAL GLY ASN LEU GLY LEU ALA THR SER PHE          
SEQRES  34 A  467  PHE ASN GLU ARG ASN ILE ASN ILE THR LYS ASP LEU LEU          
SEQRES  35 A  467  ASP LEU LEU VAL GLU ALA LYS GLN GLU VAL PRO SER TRP          
SEQRES  36 A  467  LEU GLU ASN MET ALA TYR GLU HIS HIS TYR LYS GLY              
HET    ADP  A 601      27                                                       
HET    PO4  A 602       5                                                       
HET    PO4  A 603       5                                                       
HET    PO4  A 604       5                                                       
HET    PO4  A 605       5                                                       
HET    PO4  A 606       5                                                       
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   2  ADP    C10 H15 N5 O10 P2                                            
FORMUL   3  PO4    5(O4 P 3-)                                                   
HELIX    1   1 SER A  143  PHE A  151  1                                   9    
HELIX    2   2 MET A  187  THR A  198  1                                  12    
HELIX    3   3 THR A  204  GLU A  216  1                                  13    
HELIX    4   4 GLY A  229  GLY A  246  1                                  18    
HELIX    5   5 GLY A  248  GLU A  256  1                                   9    
HELIX    6   6 THR A  275  SER A  290  1                                  16    
HELIX    7   7 ASP A  305  ARG A  315  1                                  11    
HELIX    8   8 THR A  323  ARG A  333  1                                  11    
HELIX    9   9 GLU A  348  MET A  355  1                                   8    
HELIX   10  10 PHE A  357  GLU A  366  1                                  10    
HELIX   11  11 PRO A  386  LEU A  397  1                                  12    
HELIX   12  12 ASP A  426  GLY A  439  1                                  14    
HELIX   13  13 THR A  450  GLU A  464  1                                  15    
HELIX   14  14 SER A  476  SER A  489  1                                  14    
HELIX   15  15 ALA A  499  ARG A  503  1                                   5    
HELIX   16  16 ASP A  521  GLY A  530  1                                  10    
HELIX   17  17 ASN A  546  ASN A  551  5                                   6    
HELIX   18  18 ILE A  552  ALA A  563  1                                  12    
HELIX   19  19 PRO A  568  MET A  574  1                                   7    
SHEET    1   A 8 GLU A 169  THR A 171  0                                        
SHEET    2   A 8 ILE A 401  ALA A 404 -1  O  ALA A 404   N  GLU A 169           
SHEET    3   A 8 LEU A 220  CYS A 223  1  N  CYS A 223   O  LEU A 403           
SHEET    4   A 8 HIS A 377  PHE A 381  1  O  MET A 380   N  ALA A 222           
SHEET    5   A 8 TYR A 343  ASP A 347  1  N  LEU A 344   O  HIS A 377           
SHEET    6   A 8 SER A 269  LEU A 272  1  N  LEU A 272   O  VAL A 345           
SHEET    7   A 8 LEU A 319  ALA A 322  1  O  ALA A 322   N  VAL A 271           
SHEET    8   A 8 PRO A 297  VAL A 299  1  N  CYS A 298   O  VAL A 321           
SHEET    1   B 6 ILE A 415  TRP A 421  0                                        
SHEET    2   B 6 GLY A 539  PHE A 545  1  O  ALA A 541   N  THR A 416           
SHEET    3   B 6 HIS A 512  ASN A 515  1  N  ASN A 515   O  THR A 542           
SHEET    4   B 6 THR A 444  VAL A 448  1  N  LEU A 445   O  HIS A 512           
SHEET    5   B 6 ILE A 494  THR A 498  1  O  LEU A 495   N  VAL A 446           
SHEET    6   B 6 CYS A 468  SER A 470  1  N  THR A 469   O  VAL A 496           
SITE     1 AC1 12 THR A 156  ILE A 158  TYR A 200  ARG A 202                    
SITE     2 AC1 12 PRO A 203  THR A 204  GLN A 207  THR A 226                    
SITE     3 AC1 12 GLY A 227  GLY A 229  LYS A 230  THR A 231                    
SITE     1 AC2  7 GLY A 302  THR A 323  GLY A 325  ARG A 326                    
SITE     2 AC2  7 PHE A 357  GLN A 477  PO4 A 604                               
SITE     1 AC3  5 LYS A 264  TYR A 266  ASP A 339  SER A 569                    
SITE     2 AC3  5 TRP A 570                                                     
SITE     1 AC4  4 ARG A 326  ASP A 329  PO4 A 602  PO4 A 605                    
SITE     1 AC5  7 GLY A 302  GLY A 303  ARG A 326  SER A 476                    
SITE     2 AC5  7 GLN A 477  ARG A 478  PO4 A 604                               
SITE     1 AC6  4 LYS A 217  LYS A 342  HIS A 377  ASP A 426                    
CRYST1  105.755  105.755  152.633  90.00  90.00  90.00 P 43 21 2     8          
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      0.009456  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009456  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006552        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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