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Database: PDB
Entry: 2W97
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Original site: 2W97 
HEADER    TRANSLATION                             22-JAN-09   2W97              
TITLE     CRYSTAL STRUCTURE OF EIF4E BOUND TO GLYCEROL AND EIF4G1 PEPTIDE       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 4E;               
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MRNA CAP-BINDING PROTEIN, EIF-4F 25 KDA SUBUNIT, EIF-4E,    
COMPND   5 EIF4E;                                                               
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 4E;               
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: MRNA CAP-BINDING PROTEIN, EIF-4F 25 KDA SUBUNIT, EIF-4E,    
COMPND  11 EIF4E;                                                               
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA 1;        
COMPND  15 CHAIN: E, F;                                                         
COMPND  16 FRAGMENT: EIF4GI BINDING MOTIF, RESIDUES 413-426;                    
COMPND  17 SYNONYM: P220, EIF-4-GAMMA 1, EIF-4G 1, EIF-4G1, EIF4GI;             
COMPND  18 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PET11D;                                    
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET11D;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  17 EXPRESSION_SYSTEM_VECTOR: PET11D;                                    
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PET11D;                                   
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 SYNTHETIC: YES;                                                      
SOURCE  21 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  22 ORGANISM_COMMON: HUMAN;                                              
SOURCE  23 ORGANISM_TAXID: 9606                                                 
KEYWDS    PROTEIN BIOSYNTHESIS, INITIATION FACTOR, TRANSLATION REGULATION,      
KEYWDS   2 TRANSLATION                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.J.BROWN,C.S.VERMA,M.D.WALKINSHAW,D.P.LANE                           
REVDAT   2   09-OCT-19 2W97    1       JRNL                                     
REVDAT   1   31-MAR-10 2W97    0                                                
JRNL        AUTH   C.J.BROWN,C.S.VERMA,M.D.WALKINSHAW,D.P.LANE                  
JRNL        TITL   CRYSTALLIZATION OF EIF4E COMPLEXED WITH EIF4GI PEPTIDE AND   
JRNL        TITL 2 GLYCEROL REVEALS DISTINCT STRUCTURAL DIFFERENCES AROUND THE  
JRNL        TITL 3 CAP-BINDING SITE.                                            
JRNL        REF    CELL CYCLE                    V.   8  1905 2009              
JRNL        REFN                   ESSN 1551-4005                               
JRNL        PMID   19440045                                                     
JRNL        DOI    10.4161/CC.8.12.8742                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.29 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.29                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.02                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 25283                          
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) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1341                            
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) : 2.29                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.35                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1602                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.39                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2220                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 103                          
REMARK   3   BIN FREE R VALUE                    : 0.3190                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3243                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 75                                      
REMARK   3   SOLVENT ATOMS            : 165                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.85                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
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): 0.255         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.207         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.137         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.455         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.936                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.907                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3393 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4581 ; 1.292 ; 1.959       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   383 ; 6.587 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   173 ;36.182 ;23.353       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   594 ;16.706 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;16.155 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   476 ; 0.091 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2543 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1518 ; 0.194 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2266 ; 0.302 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   246 ; 0.154 ; 0.200       
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):    71 ; 0.173 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    12 ; 0.140 ; 0.200       
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):  1979 ; 0.869 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3110 ; 1.531 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1650 ; 1.932 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1471 ; 3.235 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 2W97 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-JAN-09.                  
REMARK 100 THE DEPOSITION ID IS D_1290036403.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-APR-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSRRC                              
REMARK 200  BEAMLINE                       : BL13B1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26638                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 4.400                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2V8W                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 60% AMMONIUM SULPHATE, 100MM TRIS-HCL    
REMARK 280  PH 8.0, 1% PEG400                                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       19.10050            
REMARK 290   SMTRY3   2  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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 5290 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.7 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F                            
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     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     THR B     3                                                      
REMARK 465     VAL B     4                                                      
REMARK 465     GLU B     5                                                      
REMARK 465     PRO B     6                                                      
REMARK 465     GLU B     7                                                      
REMARK 465     THR B     8                                                      
REMARK 465     THR B     9                                                      
REMARK 465     PRO B    10                                                      
REMARK 465     THR B    11                                                      
REMARK 465     PRO B    12                                                      
REMARK 465     ASN B    13                                                      
REMARK 465     PRO B    14                                                      
REMARK 465     PRO B    15                                                      
REMARK 465     THR B    16                                                      
REMARK 465     THR B    17                                                      
REMARK 465     GLU B    18                                                      
REMARK 465     GLU B    19                                                      
REMARK 465     GLU B    20                                                      
REMARK 465     LYS B    21                                                      
REMARK 465     THR B    22                                                      
REMARK 465     GLU B    23                                                      
REMARK 465     SER B    24                                                      
REMARK 465     ASN B    25                                                      
REMARK 465     GLN B    26                                                      
REMARK 465     GLU B    27                                                      
REMARK 465     VAL B    28                                                      
REMARK 465     ALA B    29                                                      
REMARK 465     ASP B    51                                                      
REMARK 465     LYS B    52                                                      
REMARK 465     SER B    53                                                      
REMARK 465     LYS B    54                                                      
REMARK 465     THR B    55                                                      
REMARK 465     TRP B    56                                                      
REMARK 465     GLN B    57                                                      
REMARK 465     ALA B    58                                                      
REMARK 465     SER B   207                                                      
REMARK 465     GLY B   208                                                      
REMARK 465     SER B   209                                                      
REMARK 465     PHE E   634                                                      
REMARK 465     LYS F   621                                                      
REMARK 465     PHE F   634                                                      
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    TYR A  34       -9.70   -143.16                                   
REMARK 500    ASP A  67       19.22   -145.51                                   
REMARK 500    ASP A 143     -132.39     54.02                                   
REMARK 500    LYS A 206     -124.29   -128.00                                   
REMARK 500    ASP B  67       20.98   -150.65                                   
REMARK 500    PRO B 100       47.15    -73.90                                   
REMARK 500    ASP B 104      140.17    -38.97                                   
REMARK 500    ASP B 143     -134.26     62.70                                   
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 MGO A 1218                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 1219                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1220                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1221                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1218                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1219                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1220                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1222                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2V8X   RELATED DB: PDB                                   
REMARK 900 CRYSTALLOGRAPHIC AND MASS SPECTROMETRIC CHARACTERISATION OF EIF4E    
REMARK 900 WITH N7-CAP DERIVATIVES                                              
REMARK 900 RELATED ID: 1UG3   RELATED DB: PDB                                   
REMARK 900 C-TERMINAL PORTION OF HUMAN EIF4GI                                   
REMARK 900 RELATED ID: 1IPC   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF EUKARYOTIC INITIATION FACTOR 4ECOMPLEXED WITH   
REMARK 900 7-METHYL GTP                                                         
REMARK 900 RELATED ID: 2V8Y   RELATED DB: PDB                                   
REMARK 900 CRYSTALLOGRAPHIC AND MASS SPECTROMETRIC CHARACTERISATION OF EIF4E    
REMARK 900 WITH N7-CAP DERIVATIVES                                              
REMARK 900 RELATED ID: 1LJ2   RELATED DB: PDB                                   
REMARK 900 RECOGNITION OF EIF4G BY ROTAVIRUS NSP3 REVEALS A BASIS FORMRNA       
REMARK 900 CIRCULARIZATION                                                      
REMARK 900 RELATED ID: 1IPB   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF EUKARYOTIC INITIATION FACTOR 4ECOMPLEXED WITH   
REMARK 900 7-METHYL GPPPA                                                       
REMARK 900 RELATED ID: 2V8W   RELATED DB: PDB                                   
REMARK 900 CRYSTALLOGRAPHIC AND MASS SPECTROMETRIC CHARACTERISATION OF EIF4E    
REMARK 900 WITH N7-CAP DERIVATIVES                                              
DBREF  2W97 A    1   217  UNP    P06730   IF4E_HUMAN       1    217             
DBREF  2W97 B    1   217  UNP    P06730   IF4E_HUMAN       1    217             
DBREF  2W97 E  621   634  UNP    Q04637   IF4G1_HUMAN    413    426             
DBREF  2W97 F  621   634  UNP    Q04637   IF4G1_HUMAN    413    426             
SEQADV 2W97 LYS B   50  UNP  P06730    ASN    50 CONFLICT                       
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  217  MET ALA THR VAL GLU PRO GLU THR THR PRO THR PRO ASN          
SEQRES   2 B  217  PRO PRO THR THR GLU GLU GLU LYS THR GLU SER ASN GLN          
SEQRES   3 B  217  GLU VAL ALA ASN PRO GLU HIS TYR ILE LYS HIS PRO LEU          
SEQRES   4 B  217  GLN ASN ARG TRP ALA LEU TRP PHE PHE LYS LYS ASP LYS          
SEQRES   5 B  217  SER LYS THR TRP GLN ALA ASN LEU ARG LEU ILE SER LYS          
SEQRES   6 B  217  PHE ASP THR VAL GLU ASP PHE TRP ALA LEU TYR ASN HIS          
SEQRES   7 B  217  ILE GLN LEU SER SER ASN LEU MET PRO GLY CYS ASP TYR          
SEQRES   8 B  217  SER LEU PHE LYS ASP GLY ILE GLU PRO MET TRP GLU ASP          
SEQRES   9 B  217  GLU LYS ASN LYS ARG GLY GLY ARG TRP LEU ILE THR LEU          
SEQRES  10 B  217  ASN LYS GLN GLN ARG ARG SER ASP LEU ASP ARG PHE TRP          
SEQRES  11 B  217  LEU GLU THR LEU LEU CYS LEU ILE GLY GLU SER PHE ASP          
SEQRES  12 B  217  ASP TYR SER ASP ASP VAL CYS GLY ALA VAL VAL ASN VAL          
SEQRES  13 B  217  ARG ALA LYS GLY ASP LYS ILE ALA ILE TRP THR THR GLU          
SEQRES  14 B  217  CYS GLU ASN ARG GLU ALA VAL THR HIS ILE GLY ARG VAL          
SEQRES  15 B  217  TYR LYS GLU ARG LEU GLY LEU PRO PRO LYS ILE VAL ILE          
SEQRES  16 B  217  GLY TYR GLN SER HIS ALA ASP THR ALA THR LYS SER GLY          
SEQRES  17 B  217  SER THR THR LYS ASN ARG PHE VAL VAL                          
SEQRES   1 E   14  LYS LYS ARG TYR ASP ARG GLU PHE LEU LEU GLY PHE GLN          
SEQRES   2 E   14  PHE                                                          
SEQRES   1 F   14  LYS LYS ARG TYR ASP ARG GLU PHE LEU LEU GLY PHE GLN          
SEQRES   2 F   14  PHE                                                          
HET    MGO  A1218      33                                                       
HET    PGE  A1219      10                                                       
HET    SO4  A1220       5                                                       
HET    SO4  A1221       5                                                       
HET    GOL  A1222       6                                                       
HET    SO4  B1218       5                                                       
HET    SO4  B1219       5                                                       
HET    GOL  B1220       6                                                       
HETNAM     MGO [[(2R,3S,4R,5R)-5-(6-AMINO-3-METHYL-4-OXO-5H-IMIDAZO[4,          
HETNAM   2 MGO  5-C]PYRIDIN-1-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHOXY-            
HETNAM   3 MGO  HYDROXY-PHOSPHORYL] PHOSPHONO HYDROGEN PHOSPHATE                
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  MGO    C12 H20 N4 O14 P3 1+                                         
FORMUL   6  PGE    C6 H14 O4                                                    
FORMUL   7  SO4    4(O4 S 2-)                                                   
FORMUL   9  GOL    2(C3 H8 O3)                                                  
FORMUL  13  HOH   *165(H2 O)                                                    
HELIX    1   1 TRP A   56  ALA A   58  5                                   3    
HELIX    2   2 VAL A   69  ILE A   79  1                                  11    
HELIX    3   3 LEU A   81  LEU A   85  5                                   5    
HELIX    4   4 ASN A  118  ASP A  125  1                                   8    
HELIX    5   5 ASP A  125  GLY A  139  1                                  15    
HELIX    6   6 PHE A  142  ASP A  147  5                                   6    
HELIX    7   7 ASN A  172  GLY A  188  1                                  17    
HELIX    8   8 HIS A  200  THR A  205  1                                   6    
HELIX    9   9 ASN B   30  TYR B   34  5                                   5    
HELIX   10  10 VAL B   69  ILE B   79  1                                  11    
HELIX   11  11 LEU B   81  LEU B   85  5                                   5    
HELIX   12  12 ASN B  118  ASP B  125  1                                   8    
HELIX   13  13 ASP B  125  GLY B  139  1                                  15    
HELIX   14  14 PHE B  142  ASP B  147  5                                   6    
HELIX   15  15 ASN B  172  LEU B  187  1                                  16    
HELIX   16  16 HIS B  200  LYS B  206  1                                   7    
HELIX   17  17 ASP E  625  PHE E  632  1                                   8    
HELIX   18  18 ASP F  625  GLY F  631  1                                   7    
SHEET    1  AA 8 LEU A  60  THR A  68  0                                        
SHEET    2  AA 8 PRO A  38  PHE A  48 -1  N  LEU A  39   O  ASP A  67           
SHEET    3  AA 8 ASP A  90  LYS A  95 -1  O  ASP A  90   N  PHE A  48           
SHEET    4  AA 8 VAL A 149  ASN A 155 -1  O  CYS A 150   N  LYS A  95           
SHEET    5  AA 8 LYS A 162  THR A 167 -1  O  LYS A 162   N  ASN A 155           
SHEET    6  AA 8 GLY A 111  THR A 116 -1  O  GLY A 111   N  THR A 167           
SHEET    7  AA 8 GLY A 196  SER A 199 -1  O  GLY A 196   N  LEU A 114           
SHEET    8  AA 8 PHE A 215  VAL A 216 -1  O  PHE A 215   N  TYR A 197           
SHEET    1  BA 8 LEU B  60  THR B  68  0                                        
SHEET    2  BA 8 PRO B  38  LYS B  49 -1  N  LEU B  39   O  ASP B  67           
SHEET    3  BA 8 CYS B  89  LYS B  95 -1  O  ASP B  90   N  PHE B  48           
SHEET    4  BA 8 VAL B 149  ASN B 155 -1  O  CYS B 150   N  LYS B  95           
SHEET    5  BA 8 LYS B 162  THR B 167 -1  O  LYS B 162   N  ASN B 155           
SHEET    6  BA 8 GLY B 111  THR B 116 -1  O  GLY B 111   N  THR B 167           
SHEET    7  BA 8 ILE B 195  SER B 199 -1  O  GLY B 196   N  LEU B 114           
SHEET    8  BA 8 PHE B 215  VAL B 217 -1  O  PHE B 215   N  TYR B 197           
SITE     1 AC1 17 TRP A  56  MET A 101  TRP A 102  GLU A 103                    
SITE     2 AC1 17 ARG A 157  LYS A 162  SER A 207  GLY A 208                    
SITE     3 AC1 17 HOH A2022  HOH A2040  HOH A2076  HOH A2077                    
SITE     4 AC1 17 HOH A2078  HOH A2079  HOH A2080  HOH A2081                    
SITE     5 AC1 17 GLU B 103                                                     
SITE     1 AC2  8 ASP A  96  GLY A  97  ASN A 118  LYS A 119                    
SITE     2 AC2  8 GLN A 120  ASP A 147  VAL A 149  HOH A2082                    
SITE     1 AC3  3 ARG A  42  LYS A  65  LYS A 119                               
SITE     1 AC4  3 GLU A 171  ARG A 173  GLU A 174                               
SITE     1 AC5  3 ARG B  42  LYS B  65  LYS B 119                               
SITE     1 AC6  4 GLU B 171  ARG B 173  GLU B 174  HOH B2061                    
SITE     1 AC7  3 ARG B 112  HIS B 200  THR B 203                               
SITE     1 AC8  3 THR A 116  GLN A 121  ILE A 195                               
CRYST1   84.106   38.201   93.687  90.00 101.51  90.00 P 1 21 1      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      0.011890  0.000000  0.002421        0.00000                         
SCALE2      0.000000  0.026177  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010893        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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