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Database: PDB
Entry: 2JGB
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HEADER    TRANSLATION                             12-FEB-07   2JGB              
TITLE     STRUCTURE OF HUMAN EIF4E HOMOLOGOUS PROTEIN 4EHP WITH M7GTP           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 4E TYPE 2;        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 45-234;                                           
COMPND   5 SYNONYM: EIF4E TYPE 2, EIF-4E TYPE 2, MRNA CAP-BINDING PROTEIN TYPE  
COMPND   6 3, EUKARYOTIC TRANSLATION INITIATION FACTOR 4E-LIKE 3, EUKARYOTIC    
COMPND   7 TRANSLATION INITIATION FACTOR 4E HOMOLOGOUS PROTEIN, MRNA CAP-BINDING
COMPND   8 PROTEIN 4EHP, EIF4E-LIKE PROTEIN 4E-LP, EUKARYOTIC INITITIATION      
COMPND   9 FACTOR 4E HOMOLOGOUS PROTEIN;                                        
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 4E-BINDING PROTEIN
COMPND  13 1;                                                                   
COMPND  14 CHAIN: B;                                                            
COMPND  15 FRAGMENT: RESIDUES 50-66;                                            
COMPND  16 SYNONYM: 4E-BP1, EIF4E-BINDING PROTEIN 1, PHOSPHORYLATED HEAT- AND   
COMPND  17 ACID-STABLE PROTEIN REGULATED BY INSULIN 1, PHAS-I, EIF4E BINDING    
COMPND  18 PROTEIN;                                                             
COMPND  19 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 BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PGEX-6P2;                                 
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606                                                 
KEYWDS    PHOSPHORYLATION, INITIATION FACTOR, 4EHP, EIF4E, RNA-BINDING,         
KEYWDS   2 ACETYLATION, CAP-BINDING, EUKARYOTIC INITIATION FACTOR, PROTEIN      
KEYWDS   3 SYNTHESIS INHIBITOR, TRANSLATION, PROTEIN BIOSYNTHESIS, TRANSLATION  
KEYWDS   4 REGULATION                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.D.CAMERON,P.ROSETTANI,S.KNAPP,M.G.VISMARA,L.RUSCONI                 
REVDAT   6   28-MAR-18 2JGB    1       SOURCE JRNL                              
REVDAT   5   24-FEB-09 2JGB    1       VERSN                                    
REVDAT   4   29-JAN-08 2JGB    1       JRNL   REMARK                            
REVDAT   3   17-APR-07 2JGB    1       JRNL                                     
REVDAT   2   03-APR-07 2JGB    1       AUTHOR JRNL                              
REVDAT   1   27-FEB-07 2JGB    0                                                
JRNL        AUTH   P.ROSETTANI,S.KNAPP,M.G.VISMARA,L.RUSCONI,A.D.CAMERON        
JRNL        TITL   STRUCTURES OF THE HUMAN EIF4E HOMOLOGOUS PROTEIN, H4EHP, IN  
JRNL        TITL 2 ITS M7GTP-BOUND AND UNLIGANDED FORMS.                        
JRNL        REF    J. MOL. BIOL.                 V. 368   691 2007              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   17368478                                                     
JRNL        DOI    10.1016/J.JMB.2007.02.019                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 51.92                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 23859                          
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) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1262                            
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) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1692                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3090                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 102                          
REMARK   3   BIN FREE R VALUE                    : 0.3560                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1665                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 193                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.37                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.53000                                              
REMARK   3    B22 (A**2) : -0.49000                                             
REMARK   3    B33 (A**2) : -0.04000                                             
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): 0.119         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.118         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.078         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.315         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.943                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.924                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1743 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2363 ; 1.494 ; 1.966       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   200 ; 5.991 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    84 ;32.425 ;22.619       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   299 ;13.642 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;19.504 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   244 ; 0.098 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1322 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   786 ; 0.209 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1164 ; 0.305 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   185 ; 0.143 ; 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):    50 ; 0.231 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    17 ; 0.106 ; 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):  1047 ; 1.153 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1640 ; 1.697 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   826 ; 2.492 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   723 ; 3.979 ; 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   : 1.20                                          
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. RESIDUES 225 TO 227 OF THE PROTEIN CANNOT BE OBSERVED.   
REMARK   4                                                                      
REMARK   4 2JGB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-FEB-07.                  
REMARK 100 THE DEPOSITION ID IS D_1290031412.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-JUN-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
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-D                        
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU IMAGE PLATE                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 111967                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 4.500                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.79                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.400                              
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: PDB ENTRY 1IPB                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG-3000, 0.1M SODIUM CITRATE PH     
REMARK 280  5.5 WITH 1MM M7GTP IN THE DROP                                      
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       21.74950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       51.88350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.64950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       51.88350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       21.74950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       24.64950            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 2670 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.2 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    40                                                      
REMARK 465     PRO A    41                                                      
REMARK 465     LEU A    42                                                      
REMARK 465     HIS A    43                                                      
REMARK 465     MET A    44                                                      
REMARK 465     GLY A   225                                                      
REMARK 465     ARG A   226                                                      
REMARK 465     LEU A   227                                                      
REMARK 465     VAL B    67                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ILE A   211     O    HOH A  2147              2.16            
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 MGT B1000                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE INITIAL GPLHM HAS BEEN INTRODUCED DURING THE CLONING.            
REMARK 999 RESIDUES 44 TO 234                                                   
REMARK 999 RESIDUES 51 TO 67                                                    
DBREF  2JGB A   40    44  PDB    2JGB     2JGB            40     44             
DBREF  2JGB A   45   234  UNP    O60573   IF4E2_HUMAN     45    234             
DBREF  2JGB B   51    67  UNP    Q13541   4EBP1_HUMAN     50     66             
SEQRES   1 A  195  GLY PRO LEU HIS MET LYS ALA VAL VAL PRO GLY PRO ALA          
SEQRES   2 A  195  GLU HIS PRO LEU GLN TYR ASN TYR THR PHE TRP TYR SER          
SEQRES   3 A  195  ARG ARG THR PRO GLY ARG PRO THR SER SER GLN SER TYR          
SEQRES   4 A  195  GLU GLN ASN ILE LYS GLN ILE GLY THR PHE ALA SER VAL          
SEQRES   5 A  195  GLU GLN PHE TRP ARG PHE TYR SER HIS MET VAL ARG PRO          
SEQRES   6 A  195  GLY ASP LEU THR GLY HIS SER ASP PHE HIS LEU PHE LYS          
SEQRES   7 A  195  GLU GLY ILE LYS PRO MET TRP GLU ASP ASP ALA ASN LYS          
SEQRES   8 A  195  ASN GLY GLY LYS TRP ILE ILE ARG LEU ARG LYS GLY LEU          
SEQRES   9 A  195  ALA SER ARG CYS TRP GLU ASN LEU ILE LEU ALA MET LEU          
SEQRES  10 A  195  GLY GLU GLN PHE MET VAL GLY GLU GLU ILE CYS GLY ALA          
SEQRES  11 A  195  VAL VAL SER VAL ARG PHE GLN GLU ASP ILE ILE SER ILE          
SEQRES  12 A  195  TRP ASN LYS THR ALA SER ASP GLN ALA THR THR ALA ARG          
SEQRES  13 A  195  ILE ARG ASP THR LEU ARG ARG VAL LEU ASN LEU PRO PRO          
SEQRES  14 A  195  ASN THR ILE MET GLU TYR LYS THR HIS THR ASP SER ILE          
SEQRES  15 A  195  LYS MET PRO GLY ARG LEU GLY PRO GLN ARG LEU LEU PHE          
SEQRES   1 B   17  ARG ILE ILE TYR ASP ARG LYS PHE LEU MET GLU CYS ARG          
SEQRES   2 B   17  ASN SER PRO VAL                                              
HET    MGT  B1000      33                                                       
HETNAM     MGT 7N-METHYL-8-HYDROGUANOSINE-5'-TRIPHOSPHATE                       
FORMUL   3  MGT    C11 H20 N5 O14 P3                                            
FORMUL   4  HOH   *193(H2 O)                                                    
HELIX    1   1 SER A   74  ASN A   81  1                                   8    
HELIX    2   2 VAL A   91  SER A   99  1                                   9    
HELIX    3   3 ARG A  103  LEU A  107  5                                   5    
HELIX    4   4 LEU A  143  GLY A  157  1                                  15    
HELIX    5   5 ASP A  189  LEU A  204  1                                  16    
HELIX    6   6 HIS A  217  MET A  223  1                                   7    
HELIX    7   7 ASP B   55  CYS B   62  1                                   8    
HELIX    8   8 ARG B   63  SER B   65  5                                   3    
SHEET    1  AA 7 ILE A  82  SER A  90  0                                        
SHEET    2  AA 7 PRO A  55  ARG A  67 -1  N  LEU A  56   O  ALA A  89           
SHEET    3  AA 7 HIS A 110  LYS A 117 -1  O  HIS A 110   N  ARG A  67           
SHEET    4  AA 7 ILE A 166  VAL A 173 -1  O  CYS A 167   N  LYS A 117           
SHEET    5  AA 7 ASP A 178  ASN A 184 -1  O  ILE A 179   N  SER A 172           
SHEET    6  AA 7 GLY A 133  LEU A 139 -1  O  GLY A 133   N  ASN A 184           
SHEET    7  AA 7 MET A 212  THR A 216 -1  O  GLU A 213   N  ILE A 136           
SITE     1 AC1 16 ARG A  67  THR A  73  TYR A  78  HIS A 110                    
SITE     2 AC1 16 MET A 123  TRP A 124  GLU A 125  ARG A 174                    
SITE     3 AC1 16 PHE A 234  HOH A2018  HOH B2028  HOH B2029                    
SITE     4 AC1 16 HOH B2030  HOH B2031  HOH B2032  HOH B2033                    
CRYST1   43.499   49.299  103.767  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      0.022989  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.020284  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009637        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system