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Database: PDB
Entry: 5EKV
LinkDB: 5EKV
Original site: 5EKV 
HEADER    TRANSLATION                             04-NOV-15   5EKV              
TITLE     CO-CRYSTAL STRUCTURE OF EIF4E WITH NUCLEOTIDE MIMETIC INHIBITOR.      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 4E;               
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: EIF4E,EIF-4F 25 KDA SUBUNIT,MRNA CAP-BINDING PROTEIN;       
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 4E-BINDING PROTEIN
COMPND   8 1;                                                                   
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 FRAGMENT: EIF4E BINDING SEQUENCE, UNP RESIDUES 51-64;                
COMPND  11 SYNONYM: EIF4E-BINDING PROTEIN 1,PHOSPHORYLATED HEAT- AND ACID-STABLE
COMPND  12 PROTEIN REGULATED BY INSULIN 1,PHAS-I;                               
COMPND  13 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: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VARIANT: ROSETTA PLYSS;                            
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET11D;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 OTHER_DETAILS: NATURAL SEQUENCE FROM 4EBP                            
KEYWDS    COMPLEX, INHIBITOR, TRANSLATION, EIF4E                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.W.NOWICKI,M.D.WALKINSHAW,P.M.FISCHER                                
REVDAT   2   14-SEP-16 5EKV    1       JRNL                                     
REVDAT   1   07-SEP-16 5EKV    0                                                
JRNL        AUTH   F.SOUKARIEH,M.W.NOWICKI,A.BASTIDE,T.POYRY,C.JONES,K.DUDEK,   
JRNL        AUTH 2 G.PATWARDHAN,F.MEULLENET,N.J.OLDHAM,M.D.WALKINSHAW,          
JRNL        AUTH 3 A.E.WILLIS,P.M.FISCHER                                       
JRNL        TITL   DESIGN OF NUCLEOTIDE-MIMETIC AND NON-NUCLEOTIDE INHIBITORS   
JRNL        TITL 2 OF THE TRANSLATION INITIATION FACTOR EIF4E: SYNTHESIS,       
JRNL        TITL 3 STRUCTURAL AND FUNCTIONAL CHARACTERISATION.                  
JRNL        REF    EUR.J.MED.CHEM.               V. 124   200 2016              
JRNL        REFN                   ISSN 0223-5234                               
JRNL        PMID   27592390                                                     
JRNL        DOI    10.1016/J.EJMECH.2016.08.047                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.61 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) : 3.61                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.39                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 6383                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.270                           
REMARK   3   R VALUE            (WORKING SET) : 0.267                           
REMARK   3   FREE R VALUE                     : 0.342                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.720                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 301                             
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 50.3949 -  4.5480    0.98     3151   157  0.2519 0.3353        
REMARK   3     2  4.5480 -  3.6102    0.96     2931   144  0.2812 0.3481        
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)     : 0.520            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.630           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.87                          
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      :  0.003           3348                                  
REMARK   3   ANGLE     :  0.764           4530                                  
REMARK   3   CHIRALITY :  0.047            471                                  
REMARK   3   PLANARITY :  0.004            567                                  
REMARK   3   DIHEDRAL  : 17.653           1243                                  
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 5EKV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-NOV-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000214984.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-JUL-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : PILATUS 6M                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.9                        
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6413                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.610                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 81.068                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.28200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.61                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.81                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42300                            
REMARK 200  R SYM FOR SHELL            (I) : 0.42300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 2V8W                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 21-31% PEG 8000, 1-3% (NH4)2SO4, 100     
REMARK 280  MM HEPES, PH 7.5, 1 ROUND OF SEEDING, VAPOR DIFFUSION, HANGING      
REMARK 280  DROP, TEMPERATURE 291K                                              
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       19.24000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       68.23000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       50.39000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       68.23000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       19.24000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       50.39000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 1330 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10570 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 1400 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9920 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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     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     GLU A    27                                                      
REMARK 465     VAL A    28                                                      
REMARK 465     ALA A    29                                                      
REMARK 465     ASN A    30                                                      
REMARK 465     LYS A   206                                                      
REMARK 465     SER A   207                                                      
REMARK 465     GLY A   208                                                      
REMARK 465     SER A   209                                                      
REMARK 465     THR A   210                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     THR C     3                                                      
REMARK 465     VAL C     4                                                      
REMARK 465     GLU C     5                                                      
REMARK 465     PRO C     6                                                      
REMARK 465     GLU C     7                                                      
REMARK 465     THR C     8                                                      
REMARK 465     THR C     9                                                      
REMARK 465     PRO C    10                                                      
REMARK 465     THR C    11                                                      
REMARK 465     PRO C    12                                                      
REMARK 465     ASN C    13                                                      
REMARK 465     PRO C    14                                                      
REMARK 465     PRO C    15                                                      
REMARK 465     THR C    16                                                      
REMARK 465     THR C    17                                                      
REMARK 465     GLU C    18                                                      
REMARK 465     GLU C    19                                                      
REMARK 465     GLU C    20                                                      
REMARK 465     LYS C    21                                                      
REMARK 465     THR C    22                                                      
REMARK 465     GLU C    23                                                      
REMARK 465     SER C    24                                                      
REMARK 465     ASN C    25                                                      
REMARK 465     GLN C    26                                                      
REMARK 465     GLU C    27                                                      
REMARK 465     VAL C    28                                                      
REMARK 465     ALA C    29                                                      
REMARK 465     ASN C    30                                                      
REMARK 465     PRO C    31                                                      
REMARK 465     GLU C    32                                                      
REMARK 465     HIS C    33                                                      
REMARK 465     TYR C    34                                                      
REMARK 465     ILE C    35                                                      
REMARK 465     THR C   205                                                      
REMARK 465     LYS C   206                                                      
REMARK 465     SER C   207                                                      
REMARK 465     GLY C   208                                                      
REMARK 465     SER C   209                                                      
REMARK 465     THR C   210                                                      
REMARK 465     THR C   211                                                      
REMARK 465     LYS C   212                                                      
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    ARG A 109      -58.58     64.71                                   
REMARK 500    ASP A 143     -130.38     62.21                                   
REMARK 500    GLU C 103        3.75    -69.42                                   
REMARK 500    SER C 124      -19.79   -145.81                                   
REMARK 500    ASP C 143     -131.23     62.57                                   
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 5PQ A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 5PQ C 301                 
DBREF  5EKV A    1   217  UNP    P06730   IF4E_HUMAN       1    217             
DBREF  5EKV B   51    64  UNP    Q13541   4EBP1_HUMAN     51     64             
DBREF  5EKV C    1   217  UNP    P06730   IF4E_HUMAN       1    217             
DBREF  5EKV D   51    64  UNP    Q13541   4EBP1_HUMAN     51     64             
SEQRES   1 A  217  MET ALA THR VAL GLU PRO GLU THR THR PRO THR PRO ASN          
SEQRES   2 A  217  PRO PRO THR THR GLU GLU GLU LYS THR GLU SER ASN GLN          
SEQRES   3 A  217  GLU VAL ALA ASN PRO GLU HIS TYR ILE LYS HIS PRO LEU          
SEQRES   4 A  217  GLN ASN ARG TRP ALA LEU TRP PHE PHE LYS ASN ASP LYS          
SEQRES   5 A  217  SER LYS THR TRP GLN ALA ASN LEU ARG LEU ILE SER LYS          
SEQRES   6 A  217  PHE ASP THR VAL GLU ASP PHE TRP ALA LEU TYR ASN HIS          
SEQRES   7 A  217  ILE GLN LEU SER SER ASN LEU MET PRO GLY CYS ASP TYR          
SEQRES   8 A  217  SER LEU PHE LYS ASP GLY ILE GLU PRO MET TRP GLU ASP          
SEQRES   9 A  217  GLU LYS ASN LYS ARG GLY GLY ARG TRP LEU ILE THR LEU          
SEQRES  10 A  217  ASN LYS GLN GLN ARG ARG SER ASP LEU ASP ARG PHE TRP          
SEQRES  11 A  217  LEU GLU THR LEU LEU CYS LEU ILE GLY GLU SER PHE ASP          
SEQRES  12 A  217  ASP TYR SER ASP ASP VAL CYS GLY ALA VAL VAL ASN VAL          
SEQRES  13 A  217  ARG ALA LYS GLY ASP LYS ILE ALA ILE TRP THR THR GLU          
SEQRES  14 A  217  CYS GLU ASN ARG GLU ALA VAL THR HIS ILE GLY ARG VAL          
SEQRES  15 A  217  TYR LYS GLU ARG LEU GLY LEU PRO PRO LYS ILE VAL ILE          
SEQRES  16 A  217  GLY TYR GLN SER HIS ALA ASP THR ALA THR LYS SER GLY          
SEQRES  17 A  217  SER THR THR LYS ASN ARG PHE VAL VAL                          
SEQRES   1 B   14  ARG ILE ILE TYR ASP ARG LYS PHE LEU MET GLU CYS ARG          
SEQRES   2 B   14  ASN                                                          
SEQRES   1 C  217  MET ALA THR VAL GLU PRO GLU THR THR PRO THR PRO ASN          
SEQRES   2 C  217  PRO PRO THR THR GLU GLU GLU LYS THR GLU SER ASN GLN          
SEQRES   3 C  217  GLU VAL ALA ASN PRO GLU HIS TYR ILE LYS HIS PRO LEU          
SEQRES   4 C  217  GLN ASN ARG TRP ALA LEU TRP PHE PHE LYS ASN ASP LYS          
SEQRES   5 C  217  SER LYS THR TRP GLN ALA ASN LEU ARG LEU ILE SER LYS          
SEQRES   6 C  217  PHE ASP THR VAL GLU ASP PHE TRP ALA LEU TYR ASN HIS          
SEQRES   7 C  217  ILE GLN LEU SER SER ASN LEU MET PRO GLY CYS ASP TYR          
SEQRES   8 C  217  SER LEU PHE LYS ASP GLY ILE GLU PRO MET TRP GLU ASP          
SEQRES   9 C  217  GLU LYS ASN LYS ARG GLY GLY ARG TRP LEU ILE THR LEU          
SEQRES  10 C  217  ASN LYS GLN GLN ARG ARG SER ASP LEU ASP ARG PHE TRP          
SEQRES  11 C  217  LEU GLU THR LEU LEU CYS LEU ILE GLY GLU SER PHE ASP          
SEQRES  12 C  217  ASP TYR SER ASP ASP VAL CYS GLY ALA VAL VAL ASN VAL          
SEQRES  13 C  217  ARG ALA LYS GLY ASP LYS ILE ALA ILE TRP THR THR GLU          
SEQRES  14 C  217  CYS GLU ASN ARG GLU ALA VAL THR HIS ILE GLY ARG VAL          
SEQRES  15 C  217  TYR LYS GLU ARG LEU GLY LEU PRO PRO LYS ILE VAL ILE          
SEQRES  16 C  217  GLY TYR GLN SER HIS ALA ASP THR ALA THR LYS SER GLY          
SEQRES  17 C  217  SER THR THR LYS ASN ARG PHE VAL VAL                          
SEQRES   1 D   14  ARG ILE ILE TYR ASP ARG LYS PHE LEU MET GLU CYS ARG          
SEQRES   2 D   14  ASN                                                          
HET    5PQ  A 301      28                                                       
HET    5PQ  C 301      28                                                       
HETNAM     5PQ 3-[[(2~{R},3~{S},4~{R},5~{R})-5-(2-AZANYL-7-METHYL-6-            
HETNAM   2 5PQ  OXIDANYLIDENE-1~{H}-PURIN-7-IUM-9-YL)-3,4-                      
HETNAM   3 5PQ  BIS(OXIDANYL)OXOLAN-2-YL]METHYLAMINO]-4-OXIDANYL-               
HETNAM   4 5PQ  CYCLOBUT-3-ENE-1,2-DIONE                                        
FORMUL   5  5PQ    2(C15 H17 N6 O7 1+)                                          
HELIX    1 AA1 THR A   55  ASN A   59  1                                   5    
HELIX    2 AA2 VAL A   69  ASN A   77  1                                   9    
HELIX    3 AA3 LYS A  119  ARG A  123  5                                   5    
HELIX    4 AA4 SER A  124  GLY A  139  1                                  16    
HELIX    5 AA5 PHE A  142  ASP A  147  5                                   6    
HELIX    6 AA6 ASN A  172  GLY A  188  1                                  17    
HELIX    7 AA7 SER A  199  ALA A  204  1                                   6    
HELIX    8 AA8 ASP B   55  GLU B   61  1                                   7    
HELIX    9 AA9 CYS B   62  ASN B   64  5                                   3    
HELIX   10 AB1 THR C   55  LEU C   60  1                                   6    
HELIX   11 AB2 VAL C   69  ILE C   79  1                                  11    
HELIX   12 AB3 SER C  124  GLY C  139  1                                  16    
HELIX   13 AB4 PHE C  142  ASP C  147  5                                   6    
HELIX   14 AB5 ASN C  172  GLY C  188  1                                  17    
HELIX   15 AB6 HIS C  200  ALA C  204  1                                   5    
HELIX   16 AB7 ASP D   55  GLU D   61  1                                   7    
SHEET    1 AA1 8 LEU A  60  THR A  68  0                                        
SHEET    2 AA1 8 PRO A  38  LYS A  49 -1  N  PHE A  47   O  ARG A  61           
SHEET    3 AA1 8 CYS A  89  LYS A  95 -1  O  PHE A  94   N  ALA A  44           
SHEET    4 AA1 8 VAL A 149  VAL A 156 -1  O  ALA A 152   N  LEU A  93           
SHEET    5 AA1 8 ASP A 161  THR A 167 -1  O  LYS A 162   N  ASN A 155           
SHEET    6 AA1 8 ARG A 112  LEU A 117 -1  N  LEU A 117   O  ASP A 161           
SHEET    7 AA1 8 ILE A 195  TYR A 197 -1  O  GLY A 196   N  LEU A 114           
SHEET    8 AA1 8 PHE A 215  VAL A 217 -1  O  VAL A 217   N  ILE A 195           
SHEET    1 AA2 8 ARG C  61  THR C  68  0                                        
SHEET    2 AA2 8 PRO C  38  PHE C  47 -1  N  PHE C  47   O  ARG C  61           
SHEET    3 AA2 8 CYS C  89  LYS C  95 -1  O  SER C  92   N  TRP C  46           
SHEET    4 AA2 8 VAL C 149  VAL C 156 -1  O  VAL C 156   N  CYS C  89           
SHEET    5 AA2 8 ASP C 161  THR C 167 -1  O  LYS C 162   N  ASN C 155           
SHEET    6 AA2 8 GLY C 111  LEU C 117 -1  N  LEU C 117   O  ASP C 161           
SHEET    7 AA2 8 ILE C 195  SER C 199 -1  O  GLY C 196   N  LEU C 114           
SHEET    8 AA2 8 PHE C 215  VAL C 217 -1  O  VAL C 217   N  ILE C 195           
SITE     1 AC1  5 TRP A  56  MET A 101  TRP A 102  GLU A 103                    
SITE     2 AC1  5 ARG A 157                                                     
SITE     1 AC2  6 TRP C  56  GLN C  57  MET C 101  TRP C 102                    
SITE     2 AC2  6 GLU C 103  ARG C 157                                          
CRYST1   38.480  100.780  136.460  90.00  90.00  90.00 P 21 21 21    8          
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      0.025988  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009923  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007328        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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