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Database: PDB
Entry: 4DUM
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Original site: 4DUM 
HEADER    TRANSLATION                             22-FEB-12   4DUM              
TITLE     CO-CRYSTAL STRUCTURE OF EIF4E WITH INHIBITOR                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 4E;               
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: EIF-4E, EIF4E, EIF-4F 25 KDA SUBUNIT, MRNA CAP-BINDING      
COMPND   5 PROTEIN;                                                             
COMPND   6 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: EIF4E, EIF4EL1, EIF4F;                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET101                                    
KEYWDS    CAP-BINDING PROTEIN, TRANSLATION INITIATION FACTOR, M7GTP,            
KEYWDS   2 TRANSLATION                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.MIN,S.JOHNSTONE,N.WALKER,Z.WANG                                     
REVDAT   3   27-JUN-12 4DUM    1       JRNL                                     
REVDAT   2   02-MAY-12 4DUM    1       JRNL                                     
REVDAT   1   11-APR-12 4DUM    0                                                
JRNL        AUTH   X.CHEN,D.J.KOPECKY,J.MIHALIC,S.JEFFRIES,X.MIN,J.HEATH,       
JRNL        AUTH 2 J.DEIGNAN,S.LAI,Z.FU,C.GUIMARAES,S.SHEN,S.LI,S.JOHNSTONE,    
JRNL        AUTH 3 S.THIBAULT,H.XU,M.CARDOZO,W.SHEN,N.WALKER,F.KAYSER,Z.WANG    
JRNL        TITL   STRUCTURE-GUIDED DESIGN, SYNTHESIS, AND EVALUATION OF        
JRNL        TITL 2 GUANINE-DERIVED INHIBITORS OF THE EIF4E MRNA-CAP             
JRNL        TITL 3 INTERACTION.                                                 
JRNL        REF    J.MED.CHEM.                   V.  55  3837 2012              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   22458568                                                     
JRNL        DOI    10.1021/JM300037X                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.24                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 5969                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.205                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 292                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.95                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.03                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 401                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.22                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2760                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 19                           
REMARK   3   BIN FREE R VALUE                    : 0.4010                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1547                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 14                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 58.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.34                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.08000                                             
REMARK   3    B22 (A**2) : 1.51000                                              
REMARK   3    B33 (A**2) : -1.43000                                             
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.425         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.317         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.910        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.918                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.852                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1641 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2222 ; 1.506 ; 1.953       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   189 ; 6.718 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    84 ;38.487 ;23.929       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   284 ;19.904 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;19.663 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   228 ; 0.100 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1255 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   935 ; 0.818 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1512 ; 1.581 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   706 ; 1.835 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   708 ; 3.215 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4DUM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-FEB-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB070802.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAY-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 90                                 
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E SUPERBRIGHT            
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : RIGAKU VARIMAX HR OPTICS           
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS HTC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6282                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 62.750                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.900                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : 0.11600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.04                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: THE PURIFIED PROTEIN WHICH CONTAINED     
REMARK 280  100 UM M7-GTP WAS THEN CONCENTRATED TO ABOUT 7 MG/ML IN 20 MM       
REMARK 280  HEPES, PH7.6, 100 MM KCL, 1MM DTT, 0.1 MM EDTA FOR                  
REMARK 280  CRYSTALLIZATION. THE M7-GTP-BOUND EIF4E PROTEIN WAS CRYSTALLIZED    
REMARK 280  WITH 1:1 RATIO OF PROTEIN SOLUTION TO RESERVOIR SOLUTION OF 17-     
REMARK 280  20% PEG-3350 AND 0.1-0.4M NA FORMATE, VAPOR DIFFUSION, SITTING      
REMARK 280  DROP, TEMPERATURE 289K                                              
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       19.11250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       62.72100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       29.38300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       62.72100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       19.11250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       29.38300            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -22                                                      
REMARK 465     ASP A   -21                                                      
REMARK 465     TYR A   -20                                                      
REMARK 465     LYS A   -19                                                      
REMARK 465     ASP A   -18                                                      
REMARK 465     ASP A   -17                                                      
REMARK 465     ASP A   -16                                                      
REMARK 465     ASP A   -15                                                      
REMARK 465     LYS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     HIS A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     THR A    -7                                                      
REMARK 465     GLU A    -6                                                      
REMARK 465     ASN A    -5                                                      
REMARK 465     LEU A    -4                                                      
REMARK 465     TYR A    -3                                                      
REMARK 465     PHE A    -2                                                      
REMARK 465     GLN A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     GLU A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     GLU A     7                                                      
REMARK 465     THR A     8                                                      
REMARK 465     THR A     9                                                      
REMARK 465     PRO A    10                                                      
REMARK 465     THR A    11                                                      
REMARK 465     PRO A    12                                                      
REMARK 465     ASN A    13                                                      
REMARK 465     PRO A    14                                                      
REMARK 465     PRO A    15                                                      
REMARK 465     THR A    16                                                      
REMARK 465     THR A    17                                                      
REMARK 465     GLU A    18                                                      
REMARK 465     GLU A    19                                                      
REMARK 465     GLU A    20                                                      
REMARK 465     LYS A    21                                                      
REMARK 465     THR A    22                                                      
REMARK 465     GLU A    23                                                      
REMARK 465     SER A    24                                                      
REMARK 465     ASN A    25                                                      
REMARK 465     GLN A    26                                                      
REMARK 465     GLY A   208                                                      
REMARK 465     SER A   209                                                      
REMARK 465     THR A   210                                                      
REMARK 465     THR A   211                                                      
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    GLU A  32      -39.69    -38.66                                   
REMARK 500    ILE A  63      -70.76    -65.94                                   
REMARK 500    PRO A  87      140.02    -37.15                                   
REMARK 500    ASP A 143     -122.76     45.83                                   
REMARK 500    LYS A 206     -166.29   -119.36                                   
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 HLI A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1003                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4DT6   RELATED DB: PDB                                   
DBREF  4DUM A    1   217  UNP    P06730   IF4E_HUMAN       1    217             
SEQADV 4DUM MET A  -22  UNP  P06730              EXPRESSION TAG                 
SEQADV 4DUM ASP A  -21  UNP  P06730              EXPRESSION TAG                 
SEQADV 4DUM TYR A  -20  UNP  P06730              EXPRESSION TAG                 
SEQADV 4DUM LYS A  -19  UNP  P06730              EXPRESSION TAG                 
SEQADV 4DUM ASP A  -18  UNP  P06730              EXPRESSION TAG                 
SEQADV 4DUM ASP A  -17  UNP  P06730              EXPRESSION TAG                 
SEQADV 4DUM ASP A  -16  UNP  P06730              EXPRESSION TAG                 
SEQADV 4DUM ASP A  -15  UNP  P06730              EXPRESSION TAG                 
SEQADV 4DUM LYS A  -14  UNP  P06730              EXPRESSION TAG                 
SEQADV 4DUM HIS A  -13  UNP  P06730              EXPRESSION TAG                 
SEQADV 4DUM HIS A  -12  UNP  P06730              EXPRESSION TAG                 
SEQADV 4DUM HIS A  -11  UNP  P06730              EXPRESSION TAG                 
SEQADV 4DUM HIS A  -10  UNP  P06730              EXPRESSION TAG                 
SEQADV 4DUM HIS A   -9  UNP  P06730              EXPRESSION TAG                 
SEQADV 4DUM HIS A   -8  UNP  P06730              EXPRESSION TAG                 
SEQADV 4DUM THR A   -7  UNP  P06730              EXPRESSION TAG                 
SEQADV 4DUM GLU A   -6  UNP  P06730              EXPRESSION TAG                 
SEQADV 4DUM ASN A   -5  UNP  P06730              EXPRESSION TAG                 
SEQADV 4DUM LEU A   -4  UNP  P06730              EXPRESSION TAG                 
SEQADV 4DUM TYR A   -3  UNP  P06730              EXPRESSION TAG                 
SEQADV 4DUM PHE A   -2  UNP  P06730              EXPRESSION TAG                 
SEQADV 4DUM GLN A   -1  UNP  P06730              EXPRESSION TAG                 
SEQADV 4DUM GLY A    0  UNP  P06730              EXPRESSION TAG                 
SEQRES   1 A  240  MET ASP TYR LYS ASP ASP ASP ASP LYS HIS HIS HIS HIS          
SEQRES   2 A  240  HIS HIS THR GLU ASN LEU TYR PHE GLN GLY MET ALA THR          
SEQRES   3 A  240  VAL GLU PRO GLU THR THR PRO THR PRO ASN PRO PRO THR          
SEQRES   4 A  240  THR GLU GLU GLU LYS THR GLU SER ASN GLN GLU VAL ALA          
SEQRES   5 A  240  ASN PRO GLU HIS TYR ILE LYS HIS PRO LEU GLN ASN ARG          
SEQRES   6 A  240  TRP ALA LEU TRP PHE PHE LYS ASN ASP LYS SER LYS THR          
SEQRES   7 A  240  TRP GLN ALA ASN LEU ARG LEU ILE SER LYS PHE ASP THR          
SEQRES   8 A  240  VAL GLU ASP PHE TRP ALA LEU TYR ASN HIS ILE GLN LEU          
SEQRES   9 A  240  SER SER ASN LEU MET PRO GLY CYS ASP TYR SER LEU PHE          
SEQRES  10 A  240  LYS ASP GLY ILE GLU PRO MET TRP GLU ASP GLU LYS ASN          
SEQRES  11 A  240  LYS ARG GLY GLY ARG TRP LEU ILE THR LEU ASN LYS GLN          
SEQRES  12 A  240  GLN ARG ARG SER ASP LEU ASP ARG PHE TRP LEU GLU THR          
SEQRES  13 A  240  LEU LEU CYS LEU ILE GLY GLU SER PHE ASP ASP TYR SER          
SEQRES  14 A  240  ASP ASP VAL CYS GLY ALA VAL VAL ASN VAL ARG ALA LYS          
SEQRES  15 A  240  GLY ASP LYS ILE ALA ILE TRP THR THR GLU CYS GLU ASN          
SEQRES  16 A  240  ARG GLU ALA VAL THR HIS ILE GLY ARG VAL TYR LYS GLU          
SEQRES  17 A  240  ARG LEU GLY LEU PRO PRO LYS ILE VAL ILE GLY TYR GLN          
SEQRES  18 A  240  SER HIS ALA ASP THR ALA THR LYS SER GLY SER THR THR          
SEQRES  19 A  240  LYS ASN ARG PHE VAL VAL                                      
HET    HLI  A1001      32                                                       
HET    EDO  A1002       4                                                       
HET    EDO  A1003       4                                                       
HETNAM     HLI (4-{7-[2-(4-CHLOROPHENOXY)ETHYL]-2-(METHYLAMINO)-6-OXO-          
HETNAM   2 HLI  6,7-DIHYDRO-1H-PURIN-8-YL}PHENYL)PHOSPHONIC ACID                
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  HLI    C20 H19 CL N5 O5 P                                           
FORMUL   3  EDO    2(C2 H6 O2)                                                  
FORMUL   5  HOH   *14(H2 O)                                                     
HELIX    1   1 ASN A   30  TYR A   34  5                                   5    
HELIX    2   2 THR A   55  ASN A   59  1                                   5    
HELIX    3   3 VAL A   69  ILE A   79  1                                  11    
HELIX    4   4 LEU A   81  LEU A   85  5                                   5    
HELIX    5   5 ASP A  104  ARG A  109  1                                   6    
HELIX    6   6 GLN A  120  ASP A  125  1                                   6    
HELIX    7   7 ASP A  125  GLY A  139  1                                  15    
HELIX    8   8 PHE A  142  ASP A  147  5                                   6    
HELIX    9   9 ASN A  172  GLY A  188  1                                  17    
HELIX   10  10 HIS A  200  ALA A  204  1                                   5    
SHEET    1   A 8 LEU A  60  THR A  68  0                                        
SHEET    2   A 8 PRO A  38  PHE A  48 -1  N  PHE A  47   O  ARG A  61           
SHEET    3   A 8 ASP A  90  LYS A  95 -1  O  PHE A  94   N  ALA A  44           
SHEET    4   A 8 VAL A 149  ASN A 155 -1  O  ALA A 152   N  LEU A  93           
SHEET    5   A 8 LYS A 162  THR A 167 -1  O  LYS A 162   N  ASN A 155           
SHEET    6   A 8 GLY A 111  THR A 116 -1  N  ILE A 115   O  ILE A 163           
SHEET    7   A 8 ILE A 195  SER A 199 -1  O  GLY A 196   N  LEU A 114           
SHEET    8   A 8 PHE A 215  VAL A 217 -1  O  PHE A 215   N  TYR A 197           
SITE     1 AC1 13 TRP A  56  LEU A  60  ASP A  90  SER A  92                    
SITE     2 AC1 13 PRO A 100  MET A 101  TRP A 102  GLU A 103                    
SITE     3 AC1 13 ARG A 157  LYS A 162  TRP A 166  ARG A 173                    
SITE     4 AC1 13 ARG A 181                                                     
SITE     1 AC2  1 TRP A  73                                                     
SITE     1 AC3  1 ASN A  77                                                     
CRYST1   38.225   58.766  125.442  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      0.026161  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.017017  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007972        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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