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Database: PDB
Entry: 5XLN
LinkDB: 5XLN
Original site: 5XLN 
HEADER    RNA BINDING PROTEIN/LIGASE              11-MAY-17   5XLN              
TITLE     CRYSTAL STRUCTURE OF THE TRS_UNE-T AND 4EHP COMPLEX                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 4E TYPE 2;        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 45-234;                                       
COMPND   5 SYNONYM: EIF4E TYPE 2,EUKARYOTIC TRANSLATION INITIATION FACTOR 4E    
COMPND   6 HOMOLOGOUS PROTEIN,EUKARYOTIC TRANSLATION INITIATION FACTOR 4E-LIKE  
COMPND   7 3,EIF4E-LIKE PROTEIN 4E-LP,MRNA CAP-BINDING PROTEIN 4EHP,H4EHP,MRNA  
COMPND   8 CAP-BINDING PROTEIN TYPE 3;                                          
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: THREONINE--TRNA LIGASE, CYTOPLASMIC;                       
COMPND  12 CHAIN: B;                                                            
COMPND  13 FRAGMENT: UNP RESIDUES 30-74;                                        
COMPND  14 SYNONYM: THREONYL-TRNA SYNTHETASE,THRRS;                             
COMPND  15 EC: 6.1.1.3;                                                         
COMPND  16 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: EIF4E2, EIF4EL3;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: TARS;                                                          
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TRS, 4EHP, COMPLEX, RNA BINDING PROTEIN-LIGASE COMPLEX                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.HWANG,L.T.NGUYEN,M.H.KIM                                            
REVDAT   3   05-JUN-19 5XLN    1       JRNL                                     
REVDAT   2   20-FEB-19 5XLN    1       SOURCE                                   
REVDAT   1   21-NOV-18 5XLN    0                                                
JRNL        AUTH   S.J.JEONG,S.PARK,L.T.NGUYEN,J.HWANG,E.Y.LEE,H.K.GIONG,       
JRNL        AUTH 2 J.S.LEE,I.YOON,J.H.LEE,J.H.KIM,H.K.KIM,D.KIM,W.S.YANG,       
JRNL        AUTH 3 S.Y.KIM,C.Y.LEE,K.YU,N.SONENBERG,M.H.KIM,S.KIM               
JRNL        TITL   A THREONYL-TRNA SYNTHETASE-MEDIATED TRANSLATION INITIATION   
JRNL        TITL 2 MACHINERY.                                                   
JRNL        REF    NAT COMMUN                    V.  10  1357 2019              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   30902983                                                     
JRNL        DOI    10.1038/S41467-019-09086-0                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.82                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 20715                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.163                           
REMARK   3   R VALUE            (WORKING SET) : 0.161                           
REMARK   3   FREE R VALUE                     : 0.196                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.140                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1064                            
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 25.8169 -  3.7900    0.99     2584   144  0.1631 0.1883        
REMARK   3     2  3.7900 -  3.0097    1.00     2537   118  0.1507 0.1895        
REMARK   3     3  3.0097 -  2.6297    1.00     2467   127  0.1653 0.2134        
REMARK   3     4  2.6297 -  2.3894    1.00     2430   166  0.1653 0.2008        
REMARK   3     5  2.3894 -  2.2183    1.00     2446   125  0.1653 0.1962        
REMARK   3     6  2.2183 -  2.0875    1.00     2431   127  0.1560 0.1774        
REMARK   3     7  2.0875 -  1.9830    1.00     2435   131  0.1559 0.2319        
REMARK   3     8  1.9830 -  1.8967    0.97     2321   126  0.1828 0.2187        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.170            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.440           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           1619                                  
REMARK   3   ANGLE     :  0.992           2191                                  
REMARK   3   CHIRALITY :  0.045            230                                  
REMARK   3   PLANARITY :  0.004            278                                  
REMARK   3   DIHEDRAL  : 13.951            596                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):   2.0946 -18.8482 -14.7696              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1465 T22:   0.1432                                     
REMARK   3      T33:   0.1214 T12:   0.0078                                     
REMARK   3      T13:  -0.0023 T23:  -0.0129                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2716 L22:   1.3353                                     
REMARK   3      L33:   0.5538 L12:   0.1117                                     
REMARK   3      L13:   0.0550 L23:  -0.0308                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0262 S12:   0.0406 S13:  -0.0116                       
REMARK   3      S21:  -0.0164 S22:   0.0103 S23:  -0.0285                       
REMARK   3      S31:   0.0066 S32:  -0.0013 S33:  -0.0001                       
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 5XLN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-MAY-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300003749.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-DEC-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 5C (4A)                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97934                            
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 : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20718                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.78                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 8000, 0.1 M CHES (PH 9.5),       
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       24.68450            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       42.61850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       30.28450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       42.61850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.68450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       30.28450            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1540 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10950 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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     PRO A    69                                                      
REMARK 465     GLY A    70                                                      
REMARK 465     ARG A    71                                                      
REMARK 465     PRO A    72                                                      
REMARK 465     THR A    73                                                      
REMARK 465     SER A    74                                                      
REMARK 465     SER A    75                                                      
REMARK 465     GLN A    76                                                      
REMARK 465     SER A    77                                                      
REMARK 465     TYR A    78                                                      
REMARK 465     SER A   220                                                      
REMARK 465     ILE A   221                                                      
REMARK 465     LYS A   222                                                      
REMARK 465     MET A   223                                                      
REMARK 465     PRO A   224                                                      
REMARK 465     GLY A   225                                                      
REMARK 465     ARG A   226                                                      
REMARK 465     LEU A   227                                                      
REMARK 465     GLY A   228                                                      
REMARK 465     PRO A   229                                                      
REMARK 465     GLN A   230                                                      
REMARK 465     ARG A   231                                                      
REMARK 465     LEU A   232                                                      
REMARK 465     LEU A   233                                                      
REMARK 465     PHE A   234                                                      
REMARK 465     GLY B    30                                                      
REMARK 465     GLY B    31                                                      
REMARK 465     LYS B    32                                                      
REMARK 465     LYS B    33                                                      
REMARK 465     LYS B    34                                                      
REMARK 465     ASN B    35                                                      
REMARK 465     LYS B    36                                                      
REMARK 465     GLU B    37                                                      
REMARK 465     GLY B    38                                                      
REMARK 465     SER B    39                                                      
REMARK 465     GLY B    40                                                      
REMARK 465     ASP B    41                                                      
REMARK 465     GLY B    42                                                      
REMARK 465     GLY B    43                                                      
REMARK 465     ARG B    44                                                      
REMARK 465     ALA B    45                                                      
REMARK 465     GLU B    46                                                      
REMARK 465     LEU B    47                                                      
REMARK 465     ASN B    48                                                      
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   O    HOH B   120     O    HOH B   128              2.02            
REMARK 500   O    HOH A   392     O    HOH A   429              2.03            
REMARK 500   O    HOH A   425     O    HOH B   112              2.08            
REMARK 500   OD2  ASP A   106     O    HOH A   301              2.12            
REMARK 500   O    HOH A   340     O    HOH A   434              2.15            
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    GLN A  80       15.85    -61.43                                   
REMARK 500    SER B  70       27.97    -79.31                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5XLN A   45   234  UNP    O60573   IF4E2_HUMAN     45    234             
DBREF  5XLN B   30    74  UNP    P26639   SYTC_HUMAN      30     74             
SEQRES   1 A  190  LYS ALA VAL VAL PRO GLY PRO ALA GLU HIS PRO LEU GLN          
SEQRES   2 A  190  TYR ASN TYR THR PHE TRP TYR SER ARG ARG THR PRO GLY          
SEQRES   3 A  190  ARG PRO THR SER SER GLN SER TYR GLU GLN ASN ILE LYS          
SEQRES   4 A  190  GLN ILE GLY THR PHE ALA SER VAL GLU GLN PHE TRP ARG          
SEQRES   5 A  190  PHE TYR SER HIS MET VAL ARG PRO GLY ASP LEU THR GLY          
SEQRES   6 A  190  HIS SER ASP PHE HIS LEU PHE LYS GLU GLY ILE LYS PRO          
SEQRES   7 A  190  MET TRP GLU ASP ASP ALA ASN LYS ASN GLY GLY LYS TRP          
SEQRES   8 A  190  ILE ILE ARG LEU ARG LYS GLY LEU ALA SER ARG CYS TRP          
SEQRES   9 A  190  GLU ASN LEU ILE LEU ALA MET LEU GLY GLU GLN PHE MET          
SEQRES  10 A  190  VAL GLY GLU GLU ILE CYS GLY ALA VAL VAL SER VAL ARG          
SEQRES  11 A  190  PHE GLN GLU ASP ILE ILE SER ILE TRP ASN LYS THR ALA          
SEQRES  12 A  190  SER ASP GLN ALA THR THR ALA ARG ILE ARG ASP THR LEU          
SEQRES  13 A  190  ARG ARG VAL LEU ASN LEU PRO PRO ASN THR ILE MET GLU          
SEQRES  14 A  190  TYR LYS THR HIS THR ASP SER ILE LYS MET PRO GLY ARG          
SEQRES  15 A  190  LEU GLY PRO GLN ARG LEU LEU PHE                              
SEQRES   1 B   45  GLY GLY LYS LYS LYS ASN LYS GLU GLY SER GLY ASP GLY          
SEQRES   2 B   45  GLY ARG ALA GLU LEU ASN PRO TRP PRO GLU TYR ILE TYR          
SEQRES   3 B   45  THR ARG LEU GLU MET TYR ASN ILE LEU LYS ALA GLU HIS          
SEQRES   4 B   45  ASP SER ILE LEU ALA GLU                                      
FORMUL   3  HOH   *177(H2 O)                                                    
HELIX    1 AA1 VAL A   91  SER A   99  1                                   9    
HELIX    2 AA2 ARG A  103  LEU A  107  5                                   5    
HELIX    3 AA3 LEU A  143  GLY A  157  1                                  15    
HELIX    4 AA4 ASP A  189  ASN A  205  1                                  17    
HELIX    5 AA5 THR B   56  SER B   70  1                                  15    
SHEET    1 AA1 7 LYS A  83  SER A  90  0                                        
SHEET    2 AA1 7 PRO A  55  ARG A  66 -1  N  PHE A  62   O  ILE A  85           
SHEET    3 AA1 7 SER A 111  LYS A 117 -1  O  PHE A 116   N  THR A  61           
SHEET    4 AA1 7 ILE A 166  VAL A 173 -1  O  VAL A 173   N  SER A 111           
SHEET    5 AA1 7 GLU A 177  ASN A 184 -1  O  ILE A 179   N  SER A 172           
SHEET    6 AA1 7 GLY A 133  ARG A 140 -1  N  LEU A 139   O  ASP A 178           
SHEET    7 AA1 7 GLU A 213  THR A 216 -1  O  GLU A 213   N  ILE A 136           
CRYST1   49.369   60.569   85.237  90.00  90.00  90.00 P 21 21 21    4          
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      0.020256  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016510  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011732        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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