GenomeNet

Database: PDB
Entry: 4PX9
LinkDB: 4PX9
Original site: 4PX9 
HEADER    TRANSLATION, RNA BINDING PROTEIN        22-MAR-14   4PX9              
TITLE     DEAD-BOX RNA HELICASE DDX3X DOMAIN 1 WITH N-TERMINAL ATP-BINDING LOOP 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ATP-DEPENDENT RNA HELICASE DDX3X;                          
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: UNP RESIDUES 135-407;                                      
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                                                      
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: PLE231                                    
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   3   22-NOV-17 4PX9    1       REMARK                                   
REVDAT   2   29-APR-15 4PX9    1       JRNL                                     
REVDAT   1   11-MAR-15 4PX9    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.    2.31 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) : 2.31                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.11                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1794086.670                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 34116                          
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) : 0.255                           
REMARK   3   FREE R VALUE                     : 0.285                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1755                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
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) : 2.31                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.38                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.20                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3061                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3860                       
REMARK   3   BIN FREE R VALUE                    : 0.4260                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 160                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.034                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6265                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 81                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 38.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 71.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 12.76000                                             
REMARK   3    B22 (A**2) : 12.76000                                             
REMARK   3    B33 (A**2) : -25.51000                                            
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) : 0.37                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.46                            
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) : 0.41                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.51                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.820                           
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        : 49.16                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : CONSTR                                                  
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 4PX9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-APR-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000085333.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-FEB-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.6                                
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   : 34163                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
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     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.9500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.57700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.280                              
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 ENTRY 2I4I                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.22                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM HEPES 7.6; 7% PEG 3350, VAPOR      
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291K, PH 7.6                   
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       40.46267            
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       80.92533            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: C                                     
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     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   162                                                      
REMARK 465     MET B   116                                                      
REMARK 465     GLY B   117                                                      
REMARK 465     SER B   118                                                      
REMARK 465     SER B   119                                                      
REMARK 465     HIS B   120                                                      
REMARK 465     HIS B   121                                                      
REMARK 465     HIS B   122                                                      
REMARK 465     HIS B   123                                                      
REMARK 465     HIS B   124                                                      
REMARK 465     HIS B   125                                                      
REMARK 465     SER B   126                                                      
REMARK 465     SER B   127                                                      
REMARK 465     GLY B   128                                                      
REMARK 465     LEU B   129                                                      
REMARK 465     VAL B   130                                                      
REMARK 465     PRO B   131                                                      
REMARK 465     ARG B   132                                                      
REMARK 465     GLY B   133                                                      
REMARK 465     SER B   134                                                      
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   162                                                      
REMARK 465     MET C   116                                                      
REMARK 465     GLY C   117                                                      
REMARK 465     SER C   118                                                      
REMARK 465     SER C   119                                                      
REMARK 465     HIS C   120                                                      
REMARK 465     HIS C   121                                                      
REMARK 465     HIS C   122                                                      
REMARK 465     HIS C   123                                                      
REMARK 465     HIS C   124                                                      
REMARK 465     HIS C   125                                                      
REMARK 465     SER C   126                                                      
REMARK 465     SER C   127                                                      
REMARK 465     GLY C   128                                                      
REMARK 465     LEU C   129                                                      
REMARK 465     VAL C   130                                                      
REMARK 465     PRO C   131                                                      
REMARK 465     ARG C   132                                                      
REMARK 465     GLY C   133                                                      
REMARK 465     SER C   134                                                      
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     TYR A 163    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP A 164    CG   OD1  OD2                                       
REMARK 470     GLU A 249    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 251    CG   CD1  CD2                                       
REMARK 470     ARG A 252    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR B 163    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP B 164    CG   OD1  OD2                                       
REMARK 470     GLU B 249    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 251    CG   CD1  CD2                                       
REMARK 470     ARG B 252    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE C 160    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU C 161    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 162    CG   CD   CE   NZ                                   
REMARK 470     TYR C 163    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP C 164    CG   OD1  OD2                                       
REMARK 470     ASP C 165    CG   OD1  OD2                                       
REMARK 470     GLU C 249    CG   CD   OE1  OE2                                  
REMARK 470     LEU C 251    CG   CD1  CD2                                       
REMARK 470     ARG C 252    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      170.19    -56.90                                   
REMARK 500    ASP A 164     -150.76   -118.46                                   
REMARK 500    ASP A 165       47.97     27.44                                   
REMARK 500    ASN A 174       49.49     36.18                                   
REMARK 500    ARG A 199       45.17     71.31                                   
REMARK 500    ALA A 250      -71.83    -69.40                                   
REMARK 500    MET A 254       -6.88   -177.40                                   
REMARK 500    ASP A 368     -145.16   -140.62                                   
REMARK 500    PHE A 385       51.46   -142.93                                   
REMARK 500    GLU A 399       54.15     36.63                                   
REMARK 500    LEU B 150      -74.10    -74.19                                   
REMARK 500    ASP B 164     -137.93    -87.46                                   
REMARK 500    ASP B 165       48.51     32.63                                   
REMARK 500    ASN B 174       49.44     36.65                                   
REMARK 500    ARG B 199       44.87     71.64                                   
REMARK 500    ALA B 250      -72.00    -69.02                                   
REMARK 500    MET B 254       -6.54   -177.47                                   
REMARK 500    ASP B 368     -145.57   -140.18                                   
REMARK 500    PHE B 385       51.98   -142.96                                   
REMARK 500    GLU B 399       54.32     36.67                                   
REMARK 500    PHE C 151       58.59   -109.89                                   
REMARK 500    SER C 152       50.62    -66.45                                   
REMARK 500    ASN C 155       -2.55     76.56                                   
REMARK 500    ASN C 159       65.72    -69.52                                   
REMARK 500    PHE C 160       10.72    -68.01                                   
REMARK 500    TYR C 163     -166.95   -127.92                                   
REMARK 500    ASP C 164       -7.57     89.62                                   
REMARK 500    ASP C 165       61.19   -153.32                                   
REMARK 500    ASN C 174       49.69     36.07                                   
REMARK 500    ARG C 199       45.11     71.39                                   
REMARK 500    ALA C 250      -71.52    -69.46                                   
REMARK 500    MET C 254       -6.87   -177.22                                   
REMARK 500    ASP C 368     -145.47   -140.32                                   
REMARK 500    PHE C 385       51.85   -142.42                                   
REMARK 500    GLU C 399       53.57     36.59                                   
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 ADP B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 501                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4PXA   RELATED DB: PDB                                   
REMARK 900 DDX3X D1-D2 D354V                                                    
DBREF  4PX9 A  135   407  UNP    O00571   DDX3X_HUMAN    135    407             
DBREF  4PX9 B  135   407  UNP    O00571   DDX3X_HUMAN    135    407             
DBREF  4PX9 C  135   407  UNP    O00571   DDX3X_HUMAN    135    407             
SEQADV 4PX9 MET A  116  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 GLY A  117  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 SER A  118  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 SER A  119  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 HIS A  120  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 HIS A  121  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 HIS A  122  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 HIS A  123  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 HIS A  124  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 HIS A  125  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 SER A  126  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 SER A  127  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 GLY A  128  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 LEU A  129  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 VAL A  130  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 PRO A  131  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 ARG A  132  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 GLY A  133  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 SER A  134  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 MET B  116  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 GLY B  117  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 SER B  118  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 SER B  119  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 HIS B  120  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 HIS B  121  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 HIS B  122  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 HIS B  123  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 HIS B  124  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 HIS B  125  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 SER B  126  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 SER B  127  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 GLY B  128  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 LEU B  129  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 VAL B  130  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 PRO B  131  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 ARG B  132  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 GLY B  133  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 SER B  134  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 MET C  116  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 GLY C  117  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 SER C  118  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 SER C  119  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 HIS C  120  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 HIS C  121  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 HIS C  122  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 HIS C  123  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 HIS C  124  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 HIS C  125  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 SER C  126  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 SER C  127  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 GLY C  128  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 LEU C  129  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 VAL C  130  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 PRO C  131  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 ARG C  132  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 GLY C  133  UNP  O00571              EXPRESSION TAG                 
SEQADV 4PX9 SER C  134  UNP  O00571              EXPRESSION TAG                 
SEQRES   1 A  292  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  292  LEU VAL PRO ARG GLY SER ASP TRP SER LYS PRO LEU PRO          
SEQRES   3 A  292  PRO SER GLU ARG LEU GLU GLN GLU LEU PHE SER GLY GLY          
SEQRES   4 A  292  ASN THR GLY ILE ASN PHE GLU LYS TYR ASP ASP ILE PRO          
SEQRES   5 A  292  VAL GLU ALA THR GLY ASN ASN CYS PRO PRO HIS ILE GLU          
SEQRES   6 A  292  SER PHE SER ASP VAL GLU MET GLY GLU ILE ILE MET GLY          
SEQRES   7 A  292  ASN ILE GLU LEU THR ARG TYR THR ARG PRO THR PRO VAL          
SEQRES   8 A  292  GLN LYS HIS ALA ILE PRO ILE ILE LYS GLU LYS ARG ASP          
SEQRES   9 A  292  LEU MET ALA CYS ALA GLN THR GLY SER GLY LYS THR ALA          
SEQRES  10 A  292  ALA PHE LEU LEU PRO ILE LEU SER GLN ILE TYR SER ASP          
SEQRES  11 A  292  GLY PRO GLY GLU ALA LEU ARG ALA MET LYS GLU ASN GLY          
SEQRES  12 A  292  ARG TYR GLY ARG ARG LYS GLN TYR PRO ILE SER LEU VAL          
SEQRES  13 A  292  LEU ALA PRO THR ARG GLU LEU ALA VAL GLN ILE TYR GLU          
SEQRES  14 A  292  GLU ALA ARG LYS PHE SER TYR ARG SER ARG VAL ARG PRO          
SEQRES  15 A  292  CYS VAL VAL TYR GLY GLY ALA ASP ILE GLY GLN GLN ILE          
SEQRES  16 A  292  ARG ASP LEU GLU ARG GLY CYS HIS LEU LEU VAL ALA THR          
SEQRES  17 A  292  PRO GLY ARG LEU VAL ASP MET MET GLU ARG GLY LYS ILE          
SEQRES  18 A  292  GLY LEU ASP PHE CYS LYS TYR LEU VAL LEU ASP GLU ALA          
SEQRES  19 A  292  ASP ARG MET LEU ASP MET GLY PHE GLU PRO GLN ILE ARG          
SEQRES  20 A  292  ARG ILE VAL GLU GLN ASP THR MET PRO PRO LYS GLY VAL          
SEQRES  21 A  292  ARG HIS THR MET MET PHE SER ALA THR PHE PRO LYS GLU          
SEQRES  22 A  292  ILE GLN MET LEU ALA ARG ASP PHE LEU ASP GLU TYR ILE          
SEQRES  23 A  292  PHE LEU ALA VAL GLY ARG                                      
SEQRES   1 B  292  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  292  LEU VAL PRO ARG GLY SER ASP TRP SER LYS PRO LEU PRO          
SEQRES   3 B  292  PRO SER GLU ARG LEU GLU GLN GLU LEU PHE SER GLY GLY          
SEQRES   4 B  292  ASN THR GLY ILE ASN PHE GLU LYS TYR ASP ASP ILE PRO          
SEQRES   5 B  292  VAL GLU ALA THR GLY ASN ASN CYS PRO PRO HIS ILE GLU          
SEQRES   6 B  292  SER PHE SER ASP VAL GLU MET GLY GLU ILE ILE MET GLY          
SEQRES   7 B  292  ASN ILE GLU LEU THR ARG TYR THR ARG PRO THR PRO VAL          
SEQRES   8 B  292  GLN LYS HIS ALA ILE PRO ILE ILE LYS GLU LYS ARG ASP          
SEQRES   9 B  292  LEU MET ALA CYS ALA GLN THR GLY SER GLY LYS THR ALA          
SEQRES  10 B  292  ALA PHE LEU LEU PRO ILE LEU SER GLN ILE TYR SER ASP          
SEQRES  11 B  292  GLY PRO GLY GLU ALA LEU ARG ALA MET LYS GLU ASN GLY          
SEQRES  12 B  292  ARG TYR GLY ARG ARG LYS GLN TYR PRO ILE SER LEU VAL          
SEQRES  13 B  292  LEU ALA PRO THR ARG GLU LEU ALA VAL GLN ILE TYR GLU          
SEQRES  14 B  292  GLU ALA ARG LYS PHE SER TYR ARG SER ARG VAL ARG PRO          
SEQRES  15 B  292  CYS VAL VAL TYR GLY GLY ALA ASP ILE GLY GLN GLN ILE          
SEQRES  16 B  292  ARG ASP LEU GLU ARG GLY CYS HIS LEU LEU VAL ALA THR          
SEQRES  17 B  292  PRO GLY ARG LEU VAL ASP MET MET GLU ARG GLY LYS ILE          
SEQRES  18 B  292  GLY LEU ASP PHE CYS LYS TYR LEU VAL LEU ASP GLU ALA          
SEQRES  19 B  292  ASP ARG MET LEU ASP MET GLY PHE GLU PRO GLN ILE ARG          
SEQRES  20 B  292  ARG ILE VAL GLU GLN ASP THR MET PRO PRO LYS GLY VAL          
SEQRES  21 B  292  ARG HIS THR MET MET PHE SER ALA THR PHE PRO LYS GLU          
SEQRES  22 B  292  ILE GLN MET LEU ALA ARG ASP PHE LEU ASP GLU TYR ILE          
SEQRES  23 B  292  PHE LEU ALA VAL GLY ARG                                      
SEQRES   1 C  292  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  292  LEU VAL PRO ARG GLY SER ASP TRP SER LYS PRO LEU PRO          
SEQRES   3 C  292  PRO SER GLU ARG LEU GLU GLN GLU LEU PHE SER GLY GLY          
SEQRES   4 C  292  ASN THR GLY ILE ASN PHE GLU LYS TYR ASP ASP ILE PRO          
SEQRES   5 C  292  VAL GLU ALA THR GLY ASN ASN CYS PRO PRO HIS ILE GLU          
SEQRES   6 C  292  SER PHE SER ASP VAL GLU MET GLY GLU ILE ILE MET GLY          
SEQRES   7 C  292  ASN ILE GLU LEU THR ARG TYR THR ARG PRO THR PRO VAL          
SEQRES   8 C  292  GLN LYS HIS ALA ILE PRO ILE ILE LYS GLU LYS ARG ASP          
SEQRES   9 C  292  LEU MET ALA CYS ALA GLN THR GLY SER GLY LYS THR ALA          
SEQRES  10 C  292  ALA PHE LEU LEU PRO ILE LEU SER GLN ILE TYR SER ASP          
SEQRES  11 C  292  GLY PRO GLY GLU ALA LEU ARG ALA MET LYS GLU ASN GLY          
SEQRES  12 C  292  ARG TYR GLY ARG ARG LYS GLN TYR PRO ILE SER LEU VAL          
SEQRES  13 C  292  LEU ALA PRO THR ARG GLU LEU ALA VAL GLN ILE TYR GLU          
SEQRES  14 C  292  GLU ALA ARG LYS PHE SER TYR ARG SER ARG VAL ARG PRO          
SEQRES  15 C  292  CYS VAL VAL TYR GLY GLY ALA ASP ILE GLY GLN GLN ILE          
SEQRES  16 C  292  ARG ASP LEU GLU ARG GLY CYS HIS LEU LEU VAL ALA THR          
SEQRES  17 C  292  PRO GLY ARG LEU VAL ASP MET MET GLU ARG GLY LYS ILE          
SEQRES  18 C  292  GLY LEU ASP PHE CYS LYS TYR LEU VAL LEU ASP GLU ALA          
SEQRES  19 C  292  ASP ARG MET LEU ASP MET GLY PHE GLU PRO GLN ILE ARG          
SEQRES  20 C  292  ARG ILE VAL GLU GLN ASP THR MET PRO PRO LYS GLY VAL          
SEQRES  21 C  292  ARG HIS THR MET MET PHE SER ALA THR PHE PRO LYS GLU          
SEQRES  22 C  292  ILE GLN MET LEU ALA ARG ASP PHE LEU ASP GLU TYR ILE          
SEQRES  23 C  292  PHE LEU ALA VAL GLY ARG                                      
HET    ADP  A 601      27                                                       
HET    ADP  B 501      27                                                       
HET    ADP  C 501      27                                                       
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
FORMUL   4  ADP    3(C10 H15 N5 O10 P2)                                         
HELIX    1   1 SER A  143  PHE A  151  1                                   9    
HELIX    2   2 SER A  181  VAL A  185  5                                   5    
HELIX    3   3 MET A  187  ARG A  199  1                                  13    
HELIX    4   4 THR A  204  GLU A  216  1                                  13    
HELIX    5   5 GLY A  229  GLY A  246  1                                  18    
HELIX    6   6 PRO A  247  ALA A  253  1                                   7    
HELIX    7   7 THR A  275  SER A  290  1                                  16    
HELIX    8   8 ASP A  305  ARG A  315  1                                  11    
HELIX    9   9 THR A  323  ARG A  333  1                                  11    
HELIX   10  10 GLU A  348  MET A  355  1                                   8    
HELIX   11  11 PHE A  357  GLU A  366  1                                  10    
HELIX   12  12 PRO A  386  LEU A  397  1                                  12    
HELIX   13  13 SER B  143  LEU B  150  1                                   8    
HELIX   14  14 SER B  181  VAL B  185  5                                   5    
HELIX   15  15 MET B  187  ARG B  199  1                                  13    
HELIX   16  16 THR B  204  GLU B  216  1                                  13    
HELIX   17  17 GLY B  229  GLY B  246  1                                  18    
HELIX   18  18 PRO B  247  ALA B  253  1                                   7    
HELIX   19  19 THR B  275  SER B  290  1                                  16    
HELIX   20  20 ASP B  305  ARG B  315  1                                  11    
HELIX   21  21 THR B  323  ARG B  333  1                                  11    
HELIX   22  22 GLU B  348  MET B  355  1                                   8    
HELIX   23  23 PHE B  357  GLN B  367  1                                  11    
HELIX   24  24 PRO B  386  LEU B  397  1                                  12    
HELIX   25  25 SER C  143  PHE C  151  1                                   9    
HELIX   26  26 SER C  181  VAL C  185  5                                   5    
HELIX   27  27 MET C  187  ARG C  199  1                                  13    
HELIX   28  28 THR C  204  GLU C  216  1                                  13    
HELIX   29  29 GLY C  229  GLY C  246  1                                  18    
HELIX   30  30 PRO C  247  ALA C  253  1                                   7    
HELIX   31  31 THR C  275  SER C  290  1                                  16    
HELIX   32  32 ASP C  305  ARG C  315  1                                  11    
HELIX   33  33 THR C  323  ARG C  333  1                                  11    
HELIX   34  34 GLU C  348  MET C  355  1                                   8    
HELIX   35  35 PHE C  357  GLU C  366  1                                  10    
HELIX   36  36 PRO C  386  LEU C  397  1                                  12    
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  MET A 221   O  LEU A 403           
SHEET    4   A 8 HIS A 377  PHE A 381  1  O  MET A 380   N  LEU A 220           
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 270   O  TYR A 343           
SHEET    7   A 8 LEU A 319  ALA A 322  1  O  LEU A 320   N  VAL A 271           
SHEET    8   A 8 PRO A 297  VAL A 300  1  N  VAL A 300   O  VAL A 321           
SHEET    1   B 8 VAL B 168  THR B 171  0                                        
SHEET    2   B 8 ILE B 401  VAL B 405 -1  O  PHE B 402   N  THR B 171           
SHEET    3   B 8 LEU B 220  CYS B 223  1  N  MET B 221   O  LEU B 403           
SHEET    4   B 8 HIS B 377  PHE B 381  1  O  MET B 380   N  LEU B 220           
SHEET    5   B 8 TYR B 343  ASP B 347  1  N  LEU B 344   O  HIS B 377           
SHEET    6   B 8 SER B 269  LEU B 272  1  N  LEU B 270   O  TYR B 343           
SHEET    7   B 8 LEU B 319  ALA B 322  1  O  LEU B 320   N  VAL B 271           
SHEET    8   B 8 PRO B 297  VAL B 300  1  N  VAL B 300   O  VAL B 321           
SHEET    1   C 8 VAL C 168  THR C 171  0                                        
SHEET    2   C 8 ILE C 401  VAL C 405 -1  O  PHE C 402   N  THR C 171           
SHEET    3   C 8 LEU C 220  CYS C 223  1  N  MET C 221   O  LEU C 403           
SHEET    4   C 8 HIS C 377  PHE C 381  1  O  MET C 380   N  ALA C 222           
SHEET    5   C 8 TYR C 343  ASP C 347  1  N  LEU C 346   O  PHE C 381           
SHEET    6   C 8 SER C 269  LEU C 272  1  N  LEU C 270   O  TYR C 343           
SHEET    7   C 8 LEU C 319  ALA C 322  1  O  LEU C 320   N  VAL C 271           
SHEET    8   C 8 PRO C 297  VAL C 300  1  N  VAL C 300   O  VAL C 321           
SITE     1 AC1  8 TYR A 200  ARG A 202  GLN A 207  THR A 226                    
SITE     2 AC1  8 GLY A 227  GLY A 229  LYS A 230  THR A 231                    
SITE     1 AC2  9 TYR B 200  ARG B 202  GLN B 207  THR B 226                    
SITE     2 AC2  9 GLY B 227  SER B 228  GLY B 229  LYS B 230                    
SITE     3 AC2  9 THR B 231                                                     
SITE     1 AC3 11 THR C 156  ILE C 158  PHE C 182  TYR C 200                    
SITE     2 AC3 11 ARG C 202  GLN C 207  THR C 226  GLY C 227                    
SITE     3 AC3 11 GLY C 229  LYS C 230  THR C 231                               
CRYST1   75.637   75.637  121.388  90.00  90.00 120.00 P 31          9          
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      0.013221  0.007633  0.000000        0.00000                         
SCALE2      0.000000  0.015266  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008238        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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