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Database: PDB
Entry: 5ZJZ
LinkDB: 5ZJZ
Original site: 5ZJZ 
HEADER    RNA BINDING PROTEIN                     22-MAR-18   5ZJZ              
TITLE     STAPLED-PEPTIDES TAILORED AGAINST INITIATION OF TRANSLATION           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 4E;               
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 28-217;                                       
COMPND   5 SYNONYM: EIF4E,EIF-4F 25 KDA SUBUNIT;                                
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA 1;        
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: EIF-4G1;                                                    
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 OTHER_DETAILS: STAPLED PEPTIDE, N-TERMINAL ACETYLATION AND C-TERMINAL
COMPND  13 AMIDATION                                                            
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: EIF4E, EIF4EL1, EIF4F;                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET15B;                                   
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 SYNTHETIC: YES;                                                      
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606                                                 
KEYWDS    CAP DEPENDENT TRANSLATION, RNA BINDING PROTEIN                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.LAMA,A.LIBERATOR,Y.FROSI,J.NAKHLE,N.TSOMIA,T.BASHIR,D.P.LANE,       
AUTHOR   2 C.J.BROWN,C.S.VERMA,S.AUVIN,F.CIESIELSKI,M.UHRING                    
REVDAT   2   03-APR-19 5ZJZ    1       JRNL                                     
REVDAT   1   20-FEB-19 5ZJZ    0                                                
JRNL        AUTH   D.LAMA,A.M.LIBERATORE,Y.FROSI,J.NAKHLE,N.TSOMAIA,T.BASHIR,   
JRNL        AUTH 2 D.P.LANE,C.J.BROWN,C.S.VERMA,S.AUVIN                         
JRNL        TITL   STRUCTURAL INSIGHTS REVEAL A RECOGNITION FEATURE FOR         
JRNL        TITL 2 TAILORING HYDROCARBON STAPLED-PEPTIDES AGAINST THE           
JRNL        TITL 3 EUKARYOTIC TRANSLATION INITIATION FACTOR 4E PROTEIN.         
JRNL        REF    CHEM SCI                      V.  10  2489 2019              
JRNL        REFN                   ISSN 2041-6520                               
JRNL        PMID   30881679                                                     
JRNL        DOI    10.1039/C8SC03759K                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.67 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0189                                      
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) : 1.67                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.59                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 24882                          
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) : 0.191                           
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.212                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1310                            
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) : 1.67                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.72                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1686                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.83                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3820                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 89                           
REMARK   3   BIN FREE R VALUE                    : 0.4450                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1635                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 100                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.27                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.01000                                             
REMARK   3    B22 (A**2) : 0.02000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.02000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.103         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.098         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.069         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.140         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.950                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1738 ; 0.007 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1577 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2367 ; 1.496 ; 1.972       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3644 ; 0.916 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   196 ; 6.346 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    88 ;36.972 ;23.182       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   299 ;12.920 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;14.244 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   245 ; 0.081 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1889 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   393 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   788 ; 1.095 ; 1.904       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   786 ; 1.093 ; 1.903       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   982 ; 1.889 ; 2.838       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):   982 ; 1.891 ; 2.838       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   950 ; 1.362 ; 2.096       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):   951 ; 1.361 ; 2.096       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  1382 ; 2.234 ; 3.074       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  1978 ; 4.020 ;21.477       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  1947 ; 3.675 ;21.037       
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                                                           
REMARK   4                                                                      
REMARK   4 5ZJZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-MAR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1300007213.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-MAR-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 1                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.978570                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26192                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.670                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY                : 5.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.2800                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.67                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.78                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.62800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.260                              
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: 4TPW                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12.5%(W/V) PEG20000, 20%(W/V) PEG MME    
REMARK 280  550, 0.1M MES/IMIDAZOLE PH 6.5, VAPOR DIFFUSION, SITTING DROP,      
REMARK 280  TEMPERATURE 295K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       45.63500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       19.15000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       45.63500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       19.15000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2260 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 494  LIES ON A SPECIAL POSITION.                          
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    27                                                      
REMARK 465     VAL A    28                                                      
REMARK 465     ALA A    29                                                      
REMARK 465     ASN A    30                                                      
REMARK 465     PRO A    31                                                      
REMARK 465     SER A   207                                                      
REMARK 465     GLY A   208                                                      
REMARK 465     SER A   209                                                      
REMARK 465     THR A   210                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 159    CG   CD   CE   NZ                                   
REMARK 470     LYS A 212    CG   CD   CE   NZ                                   
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   CE   MK8 B     8     CE   MK8 B    12              1.34            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A  33      -57.02     77.40                                   
REMARK 500    ASP A  67       21.90   -143.27                                   
REMARK 500    ASP A 143     -115.67     38.98                                   
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 A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues MK8 B 8 and MK8 B 12     
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 AUTHORS STATE THAT THE CHAIN B IS A HYBRID SEQUENCE WHICH            
REMARK 999 CORRESPONDS APPROXIMATELY TO SEQUENCE 609-623 OF EIF4E (Q04637).     
REMARK 999 THE ACTUAL SEQUENCE IS: AC-KKRYSREQLL(S5)FQR(S5)-NH2 S5 CORRESPONDS  
REMARK 999 TO (S)-2-(4-PENTENYL) ALANINE. THIS ARE LINKED TOGETHER VIA          
REMARK 999 RCM(RING CLOSING METATHESIS) TO FORM A HYDROCARBON STAPLES.          
DBREF  5ZJZ A   28   217  UNP    P06730   IF4E_HUMAN      28    217             
DBREF  5ZJZ B    1    15  PDB    5ZJZ     5ZJZ             1     15             
SEQADV 5ZJZ MET A   27  UNP  P06730              INITIATING METHIONINE          
SEQRES   1 A  191  MET VAL ALA ASN PRO GLU HIS TYR ILE LYS HIS PRO LEU          
SEQRES   2 A  191  GLN ASN ARG TRP ALA LEU TRP PHE PHE LYS ASN ASP LYS          
SEQRES   3 A  191  SER LYS THR TRP GLN ALA ASN LEU ARG LEU ILE SER LYS          
SEQRES   4 A  191  PHE ASP THR VAL GLU ASP PHE TRP ALA LEU TYR ASN HIS          
SEQRES   5 A  191  ILE GLN LEU SER SER ASN LEU MET PRO GLY CYS ASP TYR          
SEQRES   6 A  191  SER LEU PHE LYS ASP GLY ILE GLU PRO MET TRP GLU ASP          
SEQRES   7 A  191  GLU LYS ASN LYS ARG GLY GLY ARG TRP LEU ILE THR LEU          
SEQRES   8 A  191  ASN LYS GLN GLN ARG ARG SER ASP LEU ASP ARG PHE TRP          
SEQRES   9 A  191  LEU GLU THR LEU LEU CYS LEU ILE GLY GLU SER PHE ASP          
SEQRES  10 A  191  ASP TYR SER ASP ASP VAL CYS GLY ALA VAL VAL ASN VAL          
SEQRES  11 A  191  ARG ALA LYS GLY ASP LYS ILE ALA ILE TRP THR THR GLU          
SEQRES  12 A  191  CYS GLU ASN ARG GLU ALA VAL THR HIS ILE GLY ARG VAL          
SEQRES  13 A  191  TYR LYS GLU ARG LEU GLY LEU PRO PRO LYS ILE VAL ILE          
SEQRES  14 A  191  GLY TYR GLN SER HIS ALA ASP THR ALA THR LYS SER GLY          
SEQRES  15 A  191  SER THR THR LYS ASN ARG PHE VAL VAL                          
SEQRES   1 B   15  ACE LYS LYS ARG TYR SER ARG MK8 GLN LEU LEU MK8 PHE          
SEQRES   2 B   15  TRP NH2                                                      
HET    ACE  B   1       3                                                       
HET    MK8  B   8       9                                                       
HET    MK8  B  12       9                                                       
HET    NH2  B  15       1                                                       
HET    MGT  A 301      33                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     MK8 2-METHYL-L-NORLEUCINE                                            
HETNAM     NH2 AMINO GROUP                                                      
HETNAM     MGT 7N-METHYL-8-HYDROGUANOSINE-5'-TRIPHOSPHATE                       
FORMUL   2  ACE    C2 H4 O                                                      
FORMUL   2  MK8    2(C7 H15 N O2)                                               
FORMUL   2  NH2    H2 N                                                         
FORMUL   3  MGT    C11 H20 N5 O14 P3                                            
FORMUL   4  HOH   *100(H2 O)                                                    
HELIX    1 AA1 THR A   55  ALA A   58  5                                   4    
HELIX    2 AA2 VAL A   69  ILE A   79  1                                  11    
HELIX    3 AA3 LEU A   81  LEU A   85  5                                   5    
HELIX    4 AA4 GLN A  120  ASP A  125  1                                   6    
HELIX    5 AA5 ASP A  125  GLY A  139  1                                  15    
HELIX    6 AA6 PHE A  142  ASP A  147  5                                   6    
HELIX    7 AA7 ASN A  172  GLY A  188  1                                  17    
HELIX    8 AA8 HIS A  200  ALA A  204  1                                   5    
HELIX    9 AA9 SER B    6  TRP B   14  1                                   9    
SHEET    1 AA1 8 LEU A  60  THR A  68  0                                        
SHEET    2 AA1 8 PRO A  38  PHE A  48 -1  N  LEU A  45   O  ILE A  63           
SHEET    3 AA1 8 ASP A  90  LYS A  95 -1  O  SER A  92   N  TRP A  46           
SHEET    4 AA1 8 VAL A 149  ASN A 155 -1  O  VAL A 154   N  TYR A  91           
SHEET    5 AA1 8 LYS A 162  THR A 167 -1  O  TRP A 166   N  CYS A 150           
SHEET    6 AA1 8 GLY A 111  THR A 116 -1  N  ILE A 115   O  ILE A 163           
SHEET    7 AA1 8 GLY A 196  SER A 199 -1  O  GLY A 196   N  LEU A 114           
SHEET    8 AA1 8 PHE A 215  VAL A 216 -1  O  PHE A 215   N  TYR A 197           
LINK         C   ACE B   1                 N   LYS B   2     1555   1555  1.34  
LINK         C   ARG B   7                 N   MK8 B   8     1555   1555  1.34  
LINK         C   MK8 B   8                 N   GLN B   9     1555   1555  1.27  
LINK         C   LEU B  11                 N   MK8 B  12     1555   1555  1.35  
LINK         C   MK8 B  12                 N   PHE B  13     1555   1555  1.28  
LINK         C   TRP B  14                 N   NH2 B  15     1555   1555  1.43  
SITE     1 AC1 15 LYS A  54  THR A  55  TRP A  56  MET A 101                    
SITE     2 AC1 15 TRP A 102  GLU A 103  ARG A 157  LYS A 162                    
SITE     3 AC1 15 HOH A 401  HOH A 408  HOH A 409  HOH A 415                    
SITE     4 AC1 15 HOH A 429  HOH A 438  HOH A 444                               
SITE     1 AC2 12 HIS A 178  ARG A 181  VAL A 182  SER B   6                    
SITE     2 AC2 12 ARG B   7  GLN B   9  LEU B  10  LEU B  11                    
SITE     3 AC2 12 PHE B  13  TRP B  14  NH2 B  15  HOH B 104                    
CRYST1   91.270   38.300   78.930  90.00 122.74  90.00 C 1 2 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      0.010957  0.000000  0.007045        0.00000                         
SCALE2      0.000000  0.026110  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015062        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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