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Database: PDB
Entry: 2I4I
LinkDB: 2I4I
Original site: 2I4I 
HEADER    HYDROLASE                               22-AUG-06   2I4I              
TITLE     CRYSTAL STRUCTURE OF HUMAN DEAD-BOX RNA HELICASE DDX3X                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ATP-DEPENDENT RNA HELICASE DDX3X;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: DEAD BOX PROTEIN 3, X- CHROMOSOMAL, HELICASE-LIKE PROTEIN 2,
COMPND   5 HLP2, DEAD BOX, X ISOFORM;                                           
COMPND   6 EC: 3.6.1.-;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: DDX3X;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC-BSA4                                 
KEYWDS    RNA, HELICASE, DEAD, STRUCTURAL GENOMICS, SGC, STRUCTURAL GENOMICS    
KEYWDS   2 CONSORTIUM, HYDROLASE                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.HOGBOM,T.KARLBERG,C.ARROWSMITH,H.BERGLUND,R.D.BUSAM,R.COLLINS,      
AUTHOR   2 A.EDWARDS,M.EHN,S.FLODIN,A.FLORES,S.GRASLUND,B.M.HALLBERG,           
AUTHOR   3 M.HAMMARSTROM,I.JOHANSSON,T.KOTENYOVA,A.MAGNUSDOTTIR,P.NILSSON-EHLE, 
AUTHOR   4 P.NORDLUND,T.NYMAN,D.OGG,C.PERSSON,J.SAGEMARK,P.STENMARK,            
AUTHOR   5 M.SUNDSTROM,A.G.THORSELL,J.UPPENBERG,S.VAN DEN BERG,K.WALLDEN,       
AUTHOR   6 J.WEIGELT,M.WELIN,L.HOLMBERG-SCHIAVONE,STRUCTURAL GENOMICS           
AUTHOR   7 CONSORTIUM (SGC)                                                     
REVDAT   4   13-JUL-11 2I4I    1       VERSN                                    
REVDAT   3   24-FEB-09 2I4I    1       VERSN                                    
REVDAT   2   28-AUG-07 2I4I    1       JRNL                                     
REVDAT   1   05-SEP-06 2I4I    0                                                
JRNL        AUTH   M.HOGBOM,R.COLLINS,S.VAN DEN BERG,R.-M.JENVERT,T.KARLBERG,   
JRNL        AUTH 2 T.KOTENYOVA,A.FLORES,G.B.KARLSSON HEDESTAM,                  
JRNL        AUTH 3 L.H.HOLMBERG SCHIAVONE                                       
JRNL        TITL   CRYSTAL STRUCTURE OF CONSERVED DOMAINS 1 AND 2 OF THE HUMAN  
JRNL        TITL 2 DEAD-BOX HELICASE DDX3X IN COMPLEX WITH THE MONONUCLEOTIDE   
JRNL        TITL 3 AMP                                                          
JRNL        REF    J.MOL.BIOL.                   V. 372   150 2007              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   17631897                                                     
JRNL        DOI    10.1016/J.JMB.2007.06.050                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 14.91                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 32841                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1751                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2321                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.68                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2060                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 145                          
REMARK   3   BIN FREE R VALUE                    : 0.2670                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3243                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 23                                      
REMARK   3   SOLVENT ATOMS            : 199                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.85                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.91000                                              
REMARK   3    B22 (A**2) : 1.91000                                              
REMARK   3    B33 (A**2) : -2.87000                                             
REMARK   3    B12 (A**2) : 0.96000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.180         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.159         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.119         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.982         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.948                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3328 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4493 ; 1.584 ; 1.978       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   405 ; 6.456 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   159 ;36.451 ;23.396       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   596 ;15.979 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    31 ;18.485 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   496 ; 0.113 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2508 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1446 ; 0.214 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2246 ; 0.306 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   199 ; 0.183 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    63 ; 0.154 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    23 ; 0.202 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2099 ; 1.027 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3269 ; 1.650 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1388 ; 2.656 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1224 ; 4.166 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   167        A   249                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.0000 -11.7850  20.3820              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1278 T22:  -0.0505                                     
REMARK   3      T33:  -0.2512 T12:  -0.1190                                     
REMARK   3      T13:  -0.0205 T23:  -0.0079                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5592 L22:   1.3003                                     
REMARK   3      L33:   7.3301 L12:   0.8584                                     
REMARK   3      L13:   1.0927 L23:   0.9687                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0909 S12:  -0.0125 S13:   0.0531                       
REMARK   3      S21:  -0.1211 S22:  -0.0857 S23:   0.1991                       
REMARK   3      S31:  -0.0871 S32:  -0.8485 S33:   0.1766                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   250        A   404                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.8590  -9.0030  15.0270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0836 T22:  -0.1568                                     
REMARK   3      T33:  -0.3230 T12:  -0.1516                                     
REMARK   3      T13:  -0.0038 T23:  -0.0074                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4818 L22:   1.6048                                     
REMARK   3      L33:   3.0366 L12:   0.3191                                     
REMARK   3      L13:  -1.1849 L23:  -0.3347                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0654 S12:  -0.0306 S13:  -0.0548                       
REMARK   3      S21:  -0.2703 S22:   0.0404 S23:  -0.1348                       
REMARK   3      S31:  -0.0213 S32:   0.2446 S33:   0.0249                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   405        A   496                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.8790 -39.1410  33.0520              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0325 T22:  -0.0406                                     
REMARK   3      T33:  -0.2790 T12:  -0.1178                                     
REMARK   3      T13:   0.0757 T23:  -0.0085                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4768 L22:   4.1568                                     
REMARK   3      L33:   5.6572 L12:  -0.0136                                     
REMARK   3      L13:   0.1620 L23:   3.9907                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0154 S12:  -0.1590 S13:  -0.0144                       
REMARK   3      S21:  -0.2341 S22:   0.2068 S23:  -0.1118                       
REMARK   3      S31:  -0.1695 S32:   0.2167 S33:  -0.1914                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   497        A   580                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.0670 -39.1790  18.4090              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2280 T22:  -0.1081                                     
REMARK   3      T33:  -0.2283 T12:  -0.2727                                     
REMARK   3      T13:   0.1325 T23:  -0.0507                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1515 L22:   2.9310                                     
REMARK   3      L33:   9.8694 L12:  -0.3504                                     
REMARK   3      L13:  -1.9278 L23:   1.2944                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1346 S12:  -0.1469 S13:   0.1399                       
REMARK   3      S21:  -0.4976 S22:   0.2931 S23:  -0.4313                       
REMARK   3      S31:  -1.1652 S32:   0.6649 S33:  -0.4277                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2I4I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-AUG-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB039126.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-MAY-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.072                              
REMARK 200  MONOCHROMATOR                  : THREE SETS OF FOUR DIFFERENT       
REMARK 200                                   THICKNESS OF ALUMINIUM OR CARBON   
REMARK 200                                   FOILS                              
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32841                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 14.910                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 10.600                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.7                               
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         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1WRB FOR THE DEAD DOMAIN AND 2DB3 FOR      
REMARK 200  THE HELICASE DOMAIN                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.51                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.75M NA FORMATE, 0.1M TRIS PH 7.5,      
REMARK 280  20MM ATPGS AND MGCL2, VAPOR DIFFUSION, TEMPERATURE 277K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
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       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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       84.49000            
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      168.98000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      168.98000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       84.49000            
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 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     SER A   166                                                      
REMARK 465     ARG A   407                                                      
REMARK 465     VAL A   408                                                      
REMARK 465     GLY A   409                                                      
REMARK 465     SER A   410                                                      
REMARK 465     VAL A   535                                                      
REMARK 465     GLY A   536                                                      
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     THR A 411    OG1  CG2                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   CB   CYS A   223     O    HOH A   797              1.85            
REMARK 500   O    HOH A   692     O    HOH A   795              2.01            
REMARK 500   O    HOH A   664     O    HOH A   784              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS A 578   CG    HIS A 578   CD2     0.091                       
REMARK 500    HIS A 578   CE1   HIS A 578   NE2     0.146                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 252   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 245       57.65   -151.86                                   
REMARK 500    ASP A 368     -143.63   -124.71                                   
REMARK 500    SER A 412      -87.55   -100.23                                   
REMARK 500    LYS A 440     -157.12     48.33                                   
REMARK 500    ASN A 509       31.68    -69.05                                   
REMARK 500    ASN A 546     -158.92   -145.84                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LYS A  440     ASP A  441                  147.98                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    PHE A 234        24.7      L          L   OUTSIDE RANGE           
REMARK 500    LEU A 505        22.4      L          L   OUTSIDE RANGE           
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 AMP A 600                 
DBREF  2I4I A  168   582  UNP    O00571   DDX3X_HUMAN    167    581             
SEQADV 2I4I SER A  166  UNP  O00571              CLONING ARTIFACT               
SEQADV 2I4I MET A  167  UNP  O00571              CLONING ARTIFACT               
SEQRES   1 A  417  SER MET VAL GLU ALA THR GLY ASN ASN CYS PRO PRO HIS          
SEQRES   2 A  417  ILE GLU SER PHE SER ASP VAL GLU MET GLY GLU ILE ILE          
SEQRES   3 A  417  MET GLY ASN ILE GLU LEU THR ARG TYR THR ARG PRO THR          
SEQRES   4 A  417  PRO VAL GLN LYS HIS ALA ILE PRO ILE ILE LYS GLU LYS          
SEQRES   5 A  417  ARG ASP LEU MET ALA CYS ALA GLN THR GLY SER GLY LYS          
SEQRES   6 A  417  THR ALA ALA PHE LEU LEU PRO ILE LEU SER GLN ILE TYR          
SEQRES   7 A  417  SER ASP GLY PRO GLY GLU ALA LEU ARG ALA MET LYS GLU          
SEQRES   8 A  417  ASN GLY ARG TYR GLY ARG ARG LYS GLN TYR PRO ILE SER          
SEQRES   9 A  417  LEU VAL LEU ALA PRO THR ARG GLU LEU ALA VAL GLN ILE          
SEQRES  10 A  417  TYR GLU GLU ALA ARG LYS PHE SER TYR ARG SER ARG VAL          
SEQRES  11 A  417  ARG PRO CYS VAL VAL TYR GLY GLY ALA ASP ILE GLY GLN          
SEQRES  12 A  417  GLN ILE ARG ASP LEU GLU ARG GLY CYS HIS LEU LEU VAL          
SEQRES  13 A  417  ALA THR PRO GLY ARG LEU VAL ASP MET MET GLU ARG GLY          
SEQRES  14 A  417  LYS ILE GLY LEU ASP PHE CYS LYS TYR LEU VAL LEU ASP          
SEQRES  15 A  417  GLU ALA ASP ARG MET LEU ASP MET GLY PHE GLU PRO GLN          
SEQRES  16 A  417  ILE ARG ARG ILE VAL GLU GLN ASP THR MET PRO PRO LYS          
SEQRES  17 A  417  GLY VAL ARG HIS THR MET MET PHE SER ALA THR PHE PRO          
SEQRES  18 A  417  LYS GLU ILE GLN MET LEU ALA ARG ASP PHE LEU ASP GLU          
SEQRES  19 A  417  TYR ILE PHE LEU ALA VAL GLY ARG VAL GLY SER THR SER          
SEQRES  20 A  417  GLU ASN ILE THR GLN LYS VAL VAL TRP VAL GLU GLU SER          
SEQRES  21 A  417  ASP LYS ARG SER PHE LEU LEU ASP LEU LEU ASN ALA THR          
SEQRES  22 A  417  GLY LYS ASP SER LEU THR LEU VAL PHE VAL GLU THR LYS          
SEQRES  23 A  417  LYS GLY ALA ASP SER LEU GLU ASP PHE LEU TYR HIS GLU          
SEQRES  24 A  417  GLY TYR ALA CYS THR SER ILE HIS GLY ASP ARG SER GLN          
SEQRES  25 A  417  ARG ASP ARG GLU GLU ALA LEU HIS GLN PHE ARG SER GLY          
SEQRES  26 A  417  LYS SER PRO ILE LEU VAL ALA THR ALA VAL ALA ALA ARG          
SEQRES  27 A  417  GLY LEU ASP ILE SER ASN VAL LYS HIS VAL ILE ASN PHE          
SEQRES  28 A  417  ASP LEU PRO SER ASP ILE GLU GLU TYR VAL HIS ARG ILE          
SEQRES  29 A  417  GLY ARG THR GLY ARG VAL GLY ASN LEU GLY LEU ALA THR          
SEQRES  30 A  417  SER PHE PHE ASN GLU ARG ASN ILE ASN ILE THR LYS ASP          
SEQRES  31 A  417  LEU LEU ASP LEU LEU VAL GLU ALA LYS GLN GLU VAL PRO          
SEQRES  32 A  417  SER TRP LEU GLU ASN MET ALA TYR GLU HIS HIS TYR LYS          
SEQRES  33 A  417  GLY                                                          
HET    AMP  A 600      23                                                       
HETNAM     AMP ADENOSINE MONOPHOSPHATE                                          
FORMUL   2  AMP    C10 H14 N5 O7 P                                              
FORMUL   3  HOH   *199(H2 O)                                                    
HELIX    1   1 SER A  181  VAL A  185  5                                   5    
HELIX    2   2 GLY A  188  ARG A  199  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  ASN A  257  1                                  10    
HELIX    6   6 THR A  275  TYR A  291  1                                  17    
HELIX    7   7 ASP A  305  GLU A  314  1                                  10    
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 GLU A  423  SER A  425  5                                   3    
HELIX   13  13 ASP A  426  ALA A  437  1                                  12    
HELIX   14  14 THR A  450  GLU A  464  1                                  15    
HELIX   15  15 SER A  476  SER A  489  1                                  14    
HELIX   16  16 THR A  498  ARG A  503  1                                   6    
HELIX   17  17 ASP A  521  GLY A  530  1                                  10    
HELIX   18  18 ASN A  546  ASN A  551  5                                   6    
HELIX   19  19 ILE A  552  ALA A  563  1                                  12    
HELIX   20  20 PRO A  568  TYR A  576  1                                   9    
SHEET    1   A 8 VAL A 168  THR A 171  0                                        
SHEET    2   A 8 ILE A 401  VAL A 405 -1  O  PHE A 402   N  THR A 171           
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  SER A 382  1  O  MET A 380   N  ALA A 222           
SHEET    5   A 8 TYR A 343  LEU A 346  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 300  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  LYS A 418           
SHEET    3   B 6 VAL A 510  ASN A 515  1  N  ASN A 515   O  PHE A 544           
SHEET    4   B 6 LEU A 443  PHE A 447  1  N  LEU A 445   O  ILE A 514           
SHEET    5   B 6 ILE A 494  ALA A 497  1  O  LEU A 495   N  VAL A 446           
SHEET    6   B 6 CYS A 468  ILE A 471  1  N  THR A 469   O  VAL A 496           
SITE     1 AC1 14 TYR A 200  ARG A 202  GLN A 207  THR A 226                    
SITE     2 AC1 14 GLY A 227  SER A 228  GLY A 229  LYS A 230                    
SITE     3 AC1 14 THR A 231  HOH A 609  HOH A 670  HOH A 683                    
SITE     4 AC1 14 HOH A 687  HOH A 782                                          
CRYST1   67.288   67.288  253.470  90.00  90.00 120.00 P 31 2 1      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      0.014861  0.008580  0.000000        0.00000                         
SCALE2      0.000000  0.017161  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003945        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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