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Database: PDB
Entry: 5E7I
LinkDB: 5E7I
Original site: 5E7I 
HEADER    HYDROLASE                               12-OCT-15   5E7I              
TITLE     CRYSTAL STRUCTURE OF THE ACTIVE CATALYTIC CORE OF THE HUMAN DEAD-BOX  
TITLE    2 PROTEIN DDX3                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ATP-DEPENDENT RNA HELICASE DDX3X;                          
COMPND   3 CHAIN: B, A, C;                                                      
COMPND   4 FRAGMENT: DEAD-BOX DOMAINS;                                          
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: DDX3X, DBX, DDX3;                                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 STAR (DE3);                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PHMGWA                                    
KEYWDS    DEAD-BOX PROTEIN, RNA HELICASE, RECA FOLD, HYDROLASE                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.N.FLOOR,K.J.CONDON,J.A.DOUDNA                                       
REVDAT   3   10-FEB-16 5E7I    1       JRNL                                     
REVDAT   2   09-DEC-15 5E7I    1       JRNL                                     
REVDAT   1   02-DEC-15 5E7I    0                                                
JRNL        AUTH   S.N.FLOOR,K.J.CONDON,D.SHARMA,E.JANKOWSKY,J.A.DOUDNA         
JRNL        TITL   AUTOINHIBITORY INTERDOMAIN INTERACTIONS AND                  
JRNL        TITL 2 SUBFAMILY-SPECIFIC EXTENSIONS REDEFINE THE CATALYTIC CORE OF 
JRNL        TITL 3 THE HUMAN DEAD-BOX PROTEIN DDX3.                             
JRNL        REF    J.BIOL.CHEM.                  V. 291  2412 2016              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   26598523                                                     
JRNL        DOI    10.1074/JBC.M115.700625                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.22 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.22                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 86.06                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 79683                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.227                           
REMARK   3   R VALUE            (WORKING SET) : 0.226                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3985                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 86.1258 -  6.7504    1.00     2824   147  0.1593 0.1985        
REMARK   3     2  6.7504 -  5.3582    1.00     2807   148  0.1974 0.2258        
REMARK   3     3  5.3582 -  4.6809    1.00     2784   146  0.1615 0.2063        
REMARK   3     4  4.6809 -  4.2530    1.00     2754   145  0.1528 0.1758        
REMARK   3     5  4.2530 -  3.9481    1.00     2772   146  0.1823 0.2044        
REMARK   3     6  3.9481 -  3.7154    1.00     2769   146  0.1885 0.2136        
REMARK   3     7  3.7154 -  3.5293    1.00     2785   147  0.2031 0.2644        
REMARK   3     8  3.5293 -  3.3756    1.00     2715   142  0.2209 0.2627        
REMARK   3     9  3.3756 -  3.2457    1.00     2787   147  0.2331 0.2627        
REMARK   3    10  3.2457 -  3.1337    1.00     2778   146  0.2435 0.2778        
REMARK   3    11  3.1337 -  3.0357    1.00     2737   144  0.2530 0.2725        
REMARK   3    12  3.0357 -  2.9489    1.00     2773   146  0.2584 0.3370        
REMARK   3    13  2.9489 -  2.8713    1.00     2743   145  0.2560 0.2663        
REMARK   3    14  2.8713 -  2.8012    1.00     2742   144  0.2638 0.3293        
REMARK   3    15  2.8012 -  2.7375    1.00     2757   145  0.2689 0.2938        
REMARK   3    16  2.7375 -  2.6793    1.00     2757   145  0.2699 0.2778        
REMARK   3    17  2.6793 -  2.6257    1.00     2740   144  0.2772 0.3003        
REMARK   3    18  2.6257 -  2.5761    1.00     2736   145  0.2777 0.3304        
REMARK   3    19  2.5761 -  2.5301    1.00     2774   146  0.2850 0.3009        
REMARK   3    20  2.5301 -  2.4872    1.00     2748   144  0.2841 0.3465        
REMARK   3    21  2.4872 -  2.4471    1.00     2753   145  0.2854 0.3061        
REMARK   3    22  2.4471 -  2.4095    1.00     2723   143  0.2892 0.3093        
REMARK   3    23  2.4095 -  2.3740    1.00     2752   145  0.3079 0.3573        
REMARK   3    24  2.3740 -  2.3406    1.00     2759   145  0.3031 0.3457        
REMARK   3    25  2.3406 -  2.3089    0.97     2642   140  0.3094 0.3633        
REMARK   3    26  2.3089 -  2.2790    0.93     2607   137  0.3218 0.3486        
REMARK   3    27  2.2790 -  2.2505    0.88     2337   124  0.4353 0.4433        
REMARK   3    28  2.2505 -  2.2233    0.66     1843    98  0.4275 0.4370        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.340            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.080           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.82                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.72                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004          10247                                  
REMARK   3   ANGLE     :  0.816          13838                                  
REMARK   3   CHIRALITY :  0.031           1542                                  
REMARK   3   PLANARITY :  0.004           1809                                  
REMARK   3   DIHEDRAL  : 14.507           3911                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5E7I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-OCT-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000214491.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-FEB-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.3.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.115869                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 79724                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.220                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 86.060                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.16100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.1400                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.22                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 77.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.36100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.920                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.97                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, SODIUM CITRATE, PH 5.0,        
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       52.69000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
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: 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: 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: 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: 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     GLU B   133                                                      
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     TYR B   163                                                      
REMARK 465     ASP B   164                                                      
REMARK 465     ASP B   165                                                      
REMARK 465     ASN B   257                                                      
REMARK 465     GLY B   258                                                      
REMARK 465     ARG B   259                                                      
REMARK 465     TYR B   260                                                      
REMARK 465     GLY B   261                                                      
REMARK 465     ARG B   262                                                      
REMARK 465     GLY B   473                                                      
REMARK 465     ASP B   474                                                      
REMARK 465     ARG B   475                                                      
REMARK 465     SER B   476                                                      
REMARK 465     GLN B   477                                                      
REMARK 465     ARG B   478                                                      
REMARK 465     ASP B   479                                                      
REMARK 465     ARG B   480                                                      
REMARK 465     HIS B   578                                                      
REMARK 465     HIS B   579                                                      
REMARK 465     TYR B   580                                                      
REMARK 465     LYS B   581                                                      
REMARK 465     GLY B   582                                                      
REMARK 465     SER B   583                                                      
REMARK 465     SER B   584                                                      
REMARK 465     GLU A   133                                                      
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     TYR A   163                                                      
REMARK 465     ASN A   257                                                      
REMARK 465     GLY A   258                                                      
REMARK 465     ARG A   259                                                      
REMARK 465     TYR A   260                                                      
REMARK 465     HIS A   578                                                      
REMARK 465     HIS A   579                                                      
REMARK 465     TYR A   580                                                      
REMARK 465     LYS A   581                                                      
REMARK 465     GLY A   582                                                      
REMARK 465     SER A   583                                                      
REMARK 465     SER A   584                                                      
REMARK 465     GLU C   133                                                      
REMARK 465     GLY C   154                                                      
REMARK 465     ASN C   155                                                      
REMARK 465     THR C   156                                                      
REMARK 465     GLY C   157                                                      
REMARK 465     ILE C   158                                                      
REMARK 465     ASN C   159                                                      
REMARK 465     PHE C   160                                                      
REMARK 465     GLU C   161                                                      
REMARK 465     LYS C   162                                                      
REMARK 465     TYR C   163                                                      
REMARK 465     ASP C   164                                                      
REMARK 465     GLU C   256                                                      
REMARK 465     ASN C   257                                                      
REMARK 465     GLY C   258                                                      
REMARK 465     ARG C   259                                                      
REMARK 465     TYR C   260                                                      
REMARK 465     GLY C   261                                                      
REMARK 465     ARG C   262                                                      
REMARK 465     TYR C   576                                                      
REMARK 465     GLU C   577                                                      
REMARK 465     HIS C   578                                                      
REMARK 465     HIS C   579                                                      
REMARK 465     TYR C   580                                                      
REMARK 465     LYS C   581                                                      
REMARK 465     GLY C   582                                                      
REMARK 465     SER C   583                                                      
REMARK 465     SER C   584                                                      
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   ND2  ASN A   436     OH   TYR A   466              1.99            
REMARK 500   O    LEU B   484     N    ARG B   488              2.01            
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    GLU B 482   CB    GLU B 482   CG     -0.125                       
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    THR B 201      -68.60   -102.04                                   
REMARK 500    ASP B 368     -140.84   -125.36                                   
REMARK 500    VAL B 375      -61.22   -102.10                                   
REMARK 500    GLU B 399       58.15     39.72                                   
REMARK 500    VAL B 405       47.66    -96.72                                   
REMARK 500    GLU B 413      -26.62     75.82                                   
REMARK 500    ASP B 441      -26.20     71.23                                   
REMARK 500    GLU B 482       60.31    140.22                                   
REMARK 500    ARG A 199       26.80     41.02                                   
REMARK 500    THR A 201      -88.06   -120.00                                   
REMARK 500    MET A 254       31.60   -155.23                                   
REMARK 500    ARG A 262       74.90   -115.36                                   
REMARK 500    ASP A 368     -139.64   -119.40                                   
REMARK 500    PRO C 167      128.60    -38.48                                   
REMARK 500    ASP C 368     -133.89   -114.17                                   
REMARK 500    VAL C 375      -61.75   -102.84                                   
REMARK 500    GLU C 413      -24.12     70.53                                   
REMARK 500    LYS C 440      -11.34     72.69                                   
REMARK 500    ASN C 509       87.08    -36.66                                   
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 GLU B  481     GLU B  482                 -131.71                    
REMARK 500 SER C  508     ASN C  509                 -127.42                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5E7M   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5E7J   RELATED DB: PDB                                   
DBREF  5E7I B  133   584  UNP    O00571   DDX3X_HUMAN    133    584             
DBREF  5E7I A  133   584  UNP    O00571   DDX3X_HUMAN    133    584             
DBREF  5E7I C  133   584  UNP    O00571   DDX3X_HUMAN    133    584             
SEQRES   1 B  452  GLU ASP ASP TRP SER LYS PRO LEU PRO PRO SER GLU ARG          
SEQRES   2 B  452  LEU GLU GLN GLU LEU PHE SER GLY GLY ASN THR GLY ILE          
SEQRES   3 B  452  ASN PHE GLU LYS TYR ASP ASP ILE PRO VAL GLU ALA THR          
SEQRES   4 B  452  GLY ASN ASN CYS PRO PRO HIS ILE GLU SER PHE SER ASP          
SEQRES   5 B  452  VAL GLU MET GLY GLU ILE ILE MET GLY ASN ILE GLU LEU          
SEQRES   6 B  452  THR ARG TYR THR ARG PRO THR PRO VAL GLN LYS HIS ALA          
SEQRES   7 B  452  ILE PRO ILE ILE LYS GLU LYS ARG ASP LEU MET ALA CYS          
SEQRES   8 B  452  ALA GLN THR GLY SER GLY LYS THR ALA ALA PHE LEU LEU          
SEQRES   9 B  452  PRO ILE LEU SER GLN ILE TYR SER ASP GLY PRO GLY GLU          
SEQRES  10 B  452  ALA LEU ARG ALA MET LYS GLU ASN GLY ARG TYR GLY ARG          
SEQRES  11 B  452  ARG LYS GLN TYR PRO ILE SER LEU VAL LEU ALA PRO THR          
SEQRES  12 B  452  ARG GLU LEU ALA VAL GLN ILE TYR GLU GLU ALA ARG LYS          
SEQRES  13 B  452  PHE SER TYR ARG SER ARG VAL ARG PRO CYS VAL VAL TYR          
SEQRES  14 B  452  GLY GLY ALA ASP ILE GLY GLN GLN ILE ARG ASP LEU GLU          
SEQRES  15 B  452  ARG GLY CYS HIS LEU LEU VAL ALA THR PRO GLY ARG LEU          
SEQRES  16 B  452  VAL ASP MET MET GLU ARG GLY LYS ILE GLY LEU ASP PHE          
SEQRES  17 B  452  CYS LYS TYR LEU VAL LEU ASP GLU ALA ASP ARG MET LEU          
SEQRES  18 B  452  ASP MET GLY PHE GLU PRO GLN ILE ARG ARG ILE VAL GLU          
SEQRES  19 B  452  GLN ASP THR MET PRO PRO LYS GLY VAL ARG HIS THR MET          
SEQRES  20 B  452  MET PHE SER ALA THR PHE PRO LYS GLU ILE GLN MET LEU          
SEQRES  21 B  452  ALA ARG ASP PHE LEU ASP GLU TYR ILE PHE LEU ALA VAL          
SEQRES  22 B  452  GLY ARG VAL GLY SER THR SER GLU ASN ILE THR GLN LYS          
SEQRES  23 B  452  VAL VAL TRP VAL GLU GLU SER ASP LYS ARG SER PHE LEU          
SEQRES  24 B  452  LEU ASP LEU LEU ASN ALA THR GLY LYS ASP SER LEU THR          
SEQRES  25 B  452  LEU VAL PHE VAL GLU THR LYS LYS GLY ALA ASP SER LEU          
SEQRES  26 B  452  GLU ASP PHE LEU TYR HIS GLU GLY TYR ALA CYS THR SER          
SEQRES  27 B  452  ILE HIS GLY ASP ARG SER GLN ARG ASP ARG GLU GLU ALA          
SEQRES  28 B  452  LEU HIS GLN PHE ARG SER GLY LYS SER PRO ILE LEU VAL          
SEQRES  29 B  452  ALA THR ALA VAL ALA ALA ARG GLY LEU ASP ILE SER ASN          
SEQRES  30 B  452  VAL LYS HIS VAL ILE ASN PHE ASP LEU PRO SER ASP ILE          
SEQRES  31 B  452  GLU GLU TYR VAL HIS ARG ILE GLY ARG THR GLY ARG VAL          
SEQRES  32 B  452  GLY ASN LEU GLY LEU ALA THR SER PHE PHE ASN GLU ARG          
SEQRES  33 B  452  ASN ILE ASN ILE THR LYS ASP LEU LEU ASP LEU LEU VAL          
SEQRES  34 B  452  GLU ALA LYS GLN GLU VAL PRO SER TRP LEU GLU ASN MET          
SEQRES  35 B  452  ALA TYR GLU HIS HIS TYR LYS GLY SER SER                      
SEQRES   1 A  452  GLU ASP ASP TRP SER LYS PRO LEU PRO PRO SER GLU ARG          
SEQRES   2 A  452  LEU GLU GLN GLU LEU PHE SER GLY GLY ASN THR GLY ILE          
SEQRES   3 A  452  ASN PHE GLU LYS TYR ASP ASP ILE PRO VAL GLU ALA THR          
SEQRES   4 A  452  GLY ASN ASN CYS PRO PRO HIS ILE GLU SER PHE SER ASP          
SEQRES   5 A  452  VAL GLU MET GLY GLU ILE ILE MET GLY ASN ILE GLU LEU          
SEQRES   6 A  452  THR ARG TYR THR ARG PRO THR PRO VAL GLN LYS HIS ALA          
SEQRES   7 A  452  ILE PRO ILE ILE LYS GLU LYS ARG ASP LEU MET ALA CYS          
SEQRES   8 A  452  ALA GLN THR GLY SER GLY LYS THR ALA ALA PHE LEU LEU          
SEQRES   9 A  452  PRO ILE LEU SER GLN ILE TYR SER ASP GLY PRO GLY GLU          
SEQRES  10 A  452  ALA LEU ARG ALA MET LYS GLU ASN GLY ARG TYR GLY ARG          
SEQRES  11 A  452  ARG LYS GLN TYR PRO ILE SER LEU VAL LEU ALA PRO THR          
SEQRES  12 A  452  ARG GLU LEU ALA VAL GLN ILE TYR GLU GLU ALA ARG LYS          
SEQRES  13 A  452  PHE SER TYR ARG SER ARG VAL ARG PRO CYS VAL VAL TYR          
SEQRES  14 A  452  GLY GLY ALA ASP ILE GLY GLN GLN ILE ARG ASP LEU GLU          
SEQRES  15 A  452  ARG GLY CYS HIS LEU LEU VAL ALA THR PRO GLY ARG LEU          
SEQRES  16 A  452  VAL ASP MET MET GLU ARG GLY LYS ILE GLY LEU ASP PHE          
SEQRES  17 A  452  CYS LYS TYR LEU VAL LEU ASP GLU ALA ASP ARG MET LEU          
SEQRES  18 A  452  ASP MET GLY PHE GLU PRO GLN ILE ARG ARG ILE VAL GLU          
SEQRES  19 A  452  GLN ASP THR MET PRO PRO LYS GLY VAL ARG HIS THR MET          
SEQRES  20 A  452  MET PHE SER ALA THR PHE PRO LYS GLU ILE GLN MET LEU          
SEQRES  21 A  452  ALA ARG ASP PHE LEU ASP GLU TYR ILE PHE LEU ALA VAL          
SEQRES  22 A  452  GLY ARG VAL GLY SER THR SER GLU ASN ILE THR GLN LYS          
SEQRES  23 A  452  VAL VAL TRP VAL GLU GLU SER ASP LYS ARG SER PHE LEU          
SEQRES  24 A  452  LEU ASP LEU LEU ASN ALA THR GLY LYS ASP SER LEU THR          
SEQRES  25 A  452  LEU VAL PHE VAL GLU THR LYS LYS GLY ALA ASP SER LEU          
SEQRES  26 A  452  GLU ASP PHE LEU TYR HIS GLU GLY TYR ALA CYS THR SER          
SEQRES  27 A  452  ILE HIS GLY ASP ARG SER GLN ARG ASP ARG GLU GLU ALA          
SEQRES  28 A  452  LEU HIS GLN PHE ARG SER GLY LYS SER PRO ILE LEU VAL          
SEQRES  29 A  452  ALA THR ALA VAL ALA ALA ARG GLY LEU ASP ILE SER ASN          
SEQRES  30 A  452  VAL LYS HIS VAL ILE ASN PHE ASP LEU PRO SER ASP ILE          
SEQRES  31 A  452  GLU GLU TYR VAL HIS ARG ILE GLY ARG THR GLY ARG VAL          
SEQRES  32 A  452  GLY ASN LEU GLY LEU ALA THR SER PHE PHE ASN GLU ARG          
SEQRES  33 A  452  ASN ILE ASN ILE THR LYS ASP LEU LEU ASP LEU LEU VAL          
SEQRES  34 A  452  GLU ALA LYS GLN GLU VAL PRO SER TRP LEU GLU ASN MET          
SEQRES  35 A  452  ALA TYR GLU HIS HIS TYR LYS GLY SER SER                      
SEQRES   1 C  452  GLU ASP ASP TRP SER LYS PRO LEU PRO PRO SER GLU ARG          
SEQRES   2 C  452  LEU GLU GLN GLU LEU PHE SER GLY GLY ASN THR GLY ILE          
SEQRES   3 C  452  ASN PHE GLU LYS TYR ASP ASP ILE PRO VAL GLU ALA THR          
SEQRES   4 C  452  GLY ASN ASN CYS PRO PRO HIS ILE GLU SER PHE SER ASP          
SEQRES   5 C  452  VAL GLU MET GLY GLU ILE ILE MET GLY ASN ILE GLU LEU          
SEQRES   6 C  452  THR ARG TYR THR ARG PRO THR PRO VAL GLN LYS HIS ALA          
SEQRES   7 C  452  ILE PRO ILE ILE LYS GLU LYS ARG ASP LEU MET ALA CYS          
SEQRES   8 C  452  ALA GLN THR GLY SER GLY LYS THR ALA ALA PHE LEU LEU          
SEQRES   9 C  452  PRO ILE LEU SER GLN ILE TYR SER ASP GLY PRO GLY GLU          
SEQRES  10 C  452  ALA LEU ARG ALA MET LYS GLU ASN GLY ARG TYR GLY ARG          
SEQRES  11 C  452  ARG LYS GLN TYR PRO ILE SER LEU VAL LEU ALA PRO THR          
SEQRES  12 C  452  ARG GLU LEU ALA VAL GLN ILE TYR GLU GLU ALA ARG LYS          
SEQRES  13 C  452  PHE SER TYR ARG SER ARG VAL ARG PRO CYS VAL VAL TYR          
SEQRES  14 C  452  GLY GLY ALA ASP ILE GLY GLN GLN ILE ARG ASP LEU GLU          
SEQRES  15 C  452  ARG GLY CYS HIS LEU LEU VAL ALA THR PRO GLY ARG LEU          
SEQRES  16 C  452  VAL ASP MET MET GLU ARG GLY LYS ILE GLY LEU ASP PHE          
SEQRES  17 C  452  CYS LYS TYR LEU VAL LEU ASP GLU ALA ASP ARG MET LEU          
SEQRES  18 C  452  ASP MET GLY PHE GLU PRO GLN ILE ARG ARG ILE VAL GLU          
SEQRES  19 C  452  GLN ASP THR MET PRO PRO LYS GLY VAL ARG HIS THR MET          
SEQRES  20 C  452  MET PHE SER ALA THR PHE PRO LYS GLU ILE GLN MET LEU          
SEQRES  21 C  452  ALA ARG ASP PHE LEU ASP GLU TYR ILE PHE LEU ALA VAL          
SEQRES  22 C  452  GLY ARG VAL GLY SER THR SER GLU ASN ILE THR GLN LYS          
SEQRES  23 C  452  VAL VAL TRP VAL GLU GLU SER ASP LYS ARG SER PHE LEU          
SEQRES  24 C  452  LEU ASP LEU LEU ASN ALA THR GLY LYS ASP SER LEU THR          
SEQRES  25 C  452  LEU VAL PHE VAL GLU THR LYS LYS GLY ALA ASP SER LEU          
SEQRES  26 C  452  GLU ASP PHE LEU TYR HIS GLU GLY TYR ALA CYS THR SER          
SEQRES  27 C  452  ILE HIS GLY ASP ARG SER GLN ARG ASP ARG GLU GLU ALA          
SEQRES  28 C  452  LEU HIS GLN PHE ARG SER GLY LYS SER PRO ILE LEU VAL          
SEQRES  29 C  452  ALA THR ALA VAL ALA ALA ARG GLY LEU ASP ILE SER ASN          
SEQRES  30 C  452  VAL LYS HIS VAL ILE ASN PHE ASP LEU PRO SER ASP ILE          
SEQRES  31 C  452  GLU GLU TYR VAL HIS ARG ILE GLY ARG THR GLY ARG VAL          
SEQRES  32 C  452  GLY ASN LEU GLY LEU ALA THR SER PHE PHE ASN GLU ARG          
SEQRES  33 C  452  ASN ILE ASN ILE THR LYS ASP LEU LEU ASP LEU LEU VAL          
SEQRES  34 C  452  GLU ALA LYS GLN GLU VAL PRO SER TRP LEU GLU ASN MET          
SEQRES  35 C  452  ALA TYR GLU HIS HIS TYR LYS GLY SER SER                      
HELIX    1 AA1 SER B  143  SER B  152  1                                  10    
HELIX    2 AA2 SER B  181  VAL B  185  5                                   5    
HELIX    3 AA3 MET B  187  THR B  198  1                                  12    
HELIX    4 AA4 THR B  204  GLU B  216  1                                  13    
HELIX    5 AA5 GLY B  229  ASP B  245  1                                  17    
HELIX    6 AA6 GLY B  248  MET B  254  1                                   7    
HELIX    7 AA7 THR B  275  SER B  290  1                                  16    
HELIX    8 AA8 ASP B  305  GLU B  314  1                                  10    
HELIX    9 AA9 THR B  323  ARG B  333  1                                  11    
HELIX   10 AB1 GLU B  348  MET B  355  1                                   8    
HELIX   11 AB2 PHE B  357  GLU B  366  1                                  10    
HELIX   12 AB3 PRO B  386  LEU B  397  1                                  12    
HELIX   13 AB4 GLU B  423  SER B  425  5                                   3    
HELIX   14 AB5 ASP B  426  ALA B  437  1                                  12    
HELIX   15 AB6 THR B  450  GLU B  464  1                                  15    
HELIX   16 AB7 LEU B  484  GLY B  490  1                                   7    
HELIX   17 AB8 ASP B  521  GLY B  530  1                                  10    
HELIX   18 AB9 ASN B  546  ASN B  551  5                                   6    
HELIX   19 AC1 ILE B  552  ALA B  563  1                                  12    
HELIX   20 AC2 TRP B  570  TYR B  576  1                                   7    
HELIX   21 AC3 ARG A  145  SER A  152  1                                   8    
HELIX   22 AC4 MET A  187  THR A  198  1                                  12    
HELIX   23 AC5 THR A  204  GLU A  216  1                                  13    
HELIX   24 AC6 GLY A  229  GLY A  246  1                                  18    
HELIX   25 AC7 GLY A  248  ALA A  253  1                                   6    
HELIX   26 AC8 THR A  275  SER A  290  1                                  16    
HELIX   27 AC9 ASP A  305  GLU A  314  1                                  10    
HELIX   28 AD1 THR A  323  ARG A  333  1                                  11    
HELIX   29 AD2 GLU A  348  MET A  355  1                                   8    
HELIX   30 AD3 PHE A  357  GLN A  367  1                                  11    
HELIX   31 AD4 PRO A  386  LEU A  397  1                                  12    
HELIX   32 AD5 GLU A  423  SER A  425  5                                   3    
HELIX   33 AD6 ASP A  426  THR A  438  1                                  13    
HELIX   34 AD7 THR A  450  GLU A  464  1                                  15    
HELIX   35 AD8 SER A  476  SER A  489  1                                  14    
HELIX   36 AD9 THR A  498  ARG A  503  1                                   6    
HELIX   37 AE1 ASP A  521  GLY A  530  1                                  10    
HELIX   38 AE2 ASN A  546  ASN A  551  5                                   6    
HELIX   39 AE3 ILE A  552  ALA A  563  1                                  12    
HELIX   40 AE4 PRO A  568  GLU A  577  1                                  10    
HELIX   41 AE5 SER C  143  PHE C  151  1                                   9    
HELIX   42 AE6 SER C  181  VAL C  185  5                                   5    
HELIX   43 AE7 GLY C  188  THR C  198  1                                  11    
HELIX   44 AE8 THR C  204  GLU C  216  1                                  13    
HELIX   45 AE9 GLY C  229  GLY C  246  1                                  18    
HELIX   46 AF1 GLY C  248  ALA C  253  1                                   6    
HELIX   47 AF2 THR C  275  SER C  290  1                                  16    
HELIX   48 AF3 ASP C  305  ARG C  315  1                                  11    
HELIX   49 AF4 THR C  323  ARG C  333  1                                  11    
HELIX   50 AF5 GLU C  348  MET C  355  1                                   8    
HELIX   51 AF6 PHE C  357  GLN C  367  1                                  11    
HELIX   52 AF7 PRO C  386  LEU C  397  1                                  12    
HELIX   53 AF8 GLU C  423  SER C  425  5                                   3    
HELIX   54 AF9 ASP C  426  THR C  438  1                                  13    
HELIX   55 AG1 THR C  450  GLU C  464  1                                  15    
HELIX   56 AG2 SER C  476  SER C  489  1                                  14    
HELIX   57 AG3 ASP C  521  GLY C  530  1                                  10    
HELIX   58 AG4 ASN C  546  ASN C  551  5                                   6    
HELIX   59 AG5 ILE C  552  ALA C  563  1                                  12    
SHEET    1 AA1 8 GLU B 169  THR B 171  0                                        
SHEET    2 AA1 8 ILE B 401  ALA B 404 -1  O  PHE B 402   N  THR B 171           
SHEET    3 AA1 8 LEU B 220  CYS B 223  1  N  CYS B 223   O  LEU B 403           
SHEET    4 AA1 8 HIS B 377  PHE B 381  1  O  MET B 380   N  LEU B 220           
SHEET    5 AA1 8 TYR B 343  LEU B 346  1  N  LEU B 346   O  PHE B 381           
SHEET    6 AA1 8 SER B 269  LEU B 272  1  N  LEU B 270   O  TYR B 343           
SHEET    7 AA1 8 LEU B 319  ALA B 322  1  O  LEU B 320   N  VAL B 271           
SHEET    8 AA1 8 PRO B 297  VAL B 300  1  N  CYS B 298   O  VAL B 321           
SHEET    1 AA2 6 ILE B 415  TRP B 421  0                                        
SHEET    2 AA2 6 GLY B 539  PHE B 545  1  O  ALA B 541   N  LYS B 418           
SHEET    3 AA2 6 HIS B 512  ASN B 515  1  N  VAL B 513   O  LEU B 540           
SHEET    4 AA2 6 THR B 444  PHE B 447  1  N  LEU B 445   O  ILE B 514           
SHEET    5 AA2 6 ILE B 494  ALA B 497  1  O  LEU B 495   N  VAL B 446           
SHEET    6 AA2 6 CYS B 468  ILE B 471  1  N  THR B 469   O  VAL B 496           
SHEET    1 AA3 8 GLU A 169  THR A 171  0                                        
SHEET    2 AA3 8 ILE A 401  ALA A 404 -1  O  ALA A 404   N  GLU A 169           
SHEET    3 AA3 8 LEU A 220  CYS A 223  1  N  CYS A 223   O  LEU A 403           
SHEET    4 AA3 8 HIS A 377  PHE A 381  1  O  MET A 380   N  LEU A 220           
SHEET    5 AA3 8 TYR A 343  LEU A 346  1  N  LEU A 344   O  HIS A 377           
SHEET    6 AA3 8 SER A 269  LEU A 272  1  N  LEU A 272   O  VAL A 345           
SHEET    7 AA3 8 LEU A 319  ALA A 322  1  O  LEU A 320   N  VAL A 271           
SHEET    8 AA3 8 PRO A 297  VAL A 300  1  N  CYS A 298   O  VAL A 321           
SHEET    1 AA4 6 ILE A 415  TRP A 421  0                                        
SHEET    2 AA4 6 GLY A 539  PHE A 545  1  O  ALA A 541   N  THR A 416           
SHEET    3 AA4 6 HIS A 512  ASN A 515  1  N  VAL A 513   O  LEU A 540           
SHEET    4 AA4 6 THR A 444  PHE A 447  1  N  LEU A 445   O  ILE A 514           
SHEET    5 AA4 6 ILE A 494  ALA A 497  1  O  LEU A 495   N  VAL A 446           
SHEET    6 AA4 6 CYS A 468  ILE A 471  1  N  THR A 469   O  VAL A 496           
SHEET    1 AA5 8 GLU C 169  THR C 171  0                                        
SHEET    2 AA5 8 ILE C 401  ALA C 404 -1  O  PHE C 402   N  THR C 171           
SHEET    3 AA5 8 LEU C 220  CYS C 223  1  N  CYS C 223   O  LEU C 403           
SHEET    4 AA5 8 HIS C 377  SER C 382  1  O  MET C 380   N  LEU C 220           
SHEET    5 AA5 8 TYR C 343  LEU C 346  1  N  LEU C 344   O  HIS C 377           
SHEET    6 AA5 8 SER C 269  LEU C 272  1  N  LEU C 272   O  VAL C 345           
SHEET    7 AA5 8 LEU C 319  ALA C 322  1  O  LEU C 320   N  VAL C 271           
SHEET    8 AA5 8 PRO C 297  VAL C 300  1  N  CYS C 298   O  VAL C 321           
SHEET    1 AA6 6 THR C 416  TRP C 421  0                                        
SHEET    2 AA6 6 LEU C 540  PHE C 545  1  O  ALA C 541   N  LYS C 418           
SHEET    3 AA6 6 HIS C 512  ASN C 515  1  N  ASN C 515   O  THR C 542           
SHEET    4 AA6 6 THR C 444  VAL C 448  1  N  LEU C 445   O  ILE C 514           
SHEET    5 AA6 6 ILE C 494  THR C 498  1  O  LEU C 495   N  VAL C 446           
SHEET    6 AA6 6 CYS C 468  ILE C 471  1  N  THR C 469   O  VAL C 496           
CRYST1   92.710  105.380   94.610  90.00 114.54  90.00 P 1 21 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      0.010786  0.000000  0.004926        0.00000                         
SCALE2      0.000000  0.009489  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011620        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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