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Database: PDB
Entry: 3U7X
LinkDB: 3U7X
Original site: 3U7X 
HEADER    TRANSLATION                             14-OCT-11   3U7X              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN EIF4E-4EBP1 PEPTIDE COMPLEX WITHOUT CAP
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 4E;               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: EIF-4E, EIF4E, EIF-4F 25 KDA SUBUNIT, MRNA CAP-BINDING      
COMPND   5 PROTEIN;                                                             
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 4E-BINDING PROTEIN
COMPND   9 1;                                                                   
COMPND  10 CHAIN: C, D;                                                         
COMPND  11 FRAGMENT: UNP RESIDUES 46-66;                                        
COMPND  12 SYNONYM: 4E-BP1, EIF4E-BINDING PROTEIN 1, PHOSPHORYLATED HEAT- AND   
COMPND  13 ACID-STABLE PROTEIN REGULATED BY INSULIN 1, PHAS-I;                  
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: EIF4E, EIF4EL1, EIF4F;                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PT7;                                      
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 OTHER_DETAILS: FMOC SOLID-PHASE PEPTIDE SYNTHESIS (SHELDON           
SOURCE  17 BIOTECHNOLOGY CENTER)                                                
KEYWDS    EIF4E, 4EBP1, MRNA EXPORT, STRUCTURAL GENOMICS CONSORTIUM, SGC,       
KEYWDS   2 TRANSLATION                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.SIDDIQUI,W.TEMPEL,L.NEDYALKOVA,A.K.WERNIMONT,C.H.ARROWSMITH,        
AUTHOR   2 A.M.EDWARDS,C.BOUNTRA,J.WEIGELT,K.L.B.BORDEN,H.PARK,STRUCTURAL       
AUTHOR   3 GENOMICS CONSORTIUM (SGC)                                            
REVDAT   3   08-NOV-17 3U7X    1       REMARK                                   
REVDAT   2   08-FEB-12 3U7X    1       JRNL                                     
REVDAT   1   02-NOV-11 3U7X    0                                                
SPRSDE     02-NOV-11 3U7X      3SMU                                             
JRNL        AUTH   N.SIDDIQUI,W.TEMPEL,L.NEDYALKOVA,L.VOLPON,A.K.WERNIMONT,     
JRNL        AUTH 2 M.J.OSBORNE,H.W.PARK,K.L.BORDEN                              
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE ALLOSTERIC EFFECTS OF 4EBP1 ON  
JRNL        TITL 2 THE EUKARYOTIC TRANSLATION INITIATION FACTOR EIF4E.          
JRNL        REF    J.MOL.BIOL.                   V. 415   781 2012              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   22178476                                                     
JRNL        DOI    10.1016/J.JMB.2011.12.002                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 35692                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : THIN SHELLS (SFTOOLS)           
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.224                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.211                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1503                            
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2382                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.78                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2740                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 0                            
REMARK   3   BIN FREE R VALUE                    : 0.2940                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3205                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 123                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.17                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.74600                                              
REMARK   3    B22 (A**2) : -0.44100                                             
REMARK   3    B33 (A**2) : 0.29000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 2.14800                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.152         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.118         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.957         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.946                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.928                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3391 ; 0.014 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2319 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4615 ; 1.316 ; 1.936       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5588 ; 0.894 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   423 ; 6.494 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   165 ;35.033 ;22.848       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   562 ;12.499 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    31 ;17.783 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   494 ; 0.080 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3810 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   763 ; 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):  2043 ; 0.688 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   831 ; 0.147 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3278 ; 1.257 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1348 ; 1.902 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1326 ; 3.024 ; 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 : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : D C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     D     50       D      63      5                      
REMARK   3           1     C     50       C      63      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    D    (A):     81 ; 0.290 ; 0.500           
REMARK   3   LOOSE POSITIONAL   1    D    (A):     89 ; 0.220 ; 5.000           
REMARK   3   MEDIUM THERMAL     1    D (A**2):     81 ; 0.190 ; 2.000           
REMARK   3   LOOSE THERMAL      1    D (A**2):     89 ; 0.240 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     50       A      56      5                      
REMARK   3           1     B     50       B      56      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    A    (A):     42 ; 0.120 ; 0.500           
REMARK   3   LOOSE POSITIONAL   2    A    (A):     15 ; 0.210 ; 5.000           
REMARK   3   MEDIUM THERMAL     2    A (A**2):     42 ; 0.160 ; 2.000           
REMARK   3   LOOSE THERMAL      2    A (A**2):     15 ; 0.330 ;10.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    31        A   217                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.1223  -7.2829  18.1657              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0681 T22:   0.0112                                     
REMARK   3      T33:   0.0139 T12:  -0.0252                                     
REMARK   3      T13:  -0.0153 T23:  -0.0012                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0686 L22:   2.1662                                     
REMARK   3      L33:   5.0628 L12:   0.2282                                     
REMARK   3      L13:  -1.4839 L23:  -0.6502                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0068 S12:  -0.0791 S13:  -0.0832                       
REMARK   3      S21:  -0.0212 S22:   0.0138 S23:  -0.0917                       
REMARK   3      S31:   0.1495 S32:   0.0776 S33:  -0.0206                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    31        B   217                          
REMARK   3    ORIGIN FOR THE GROUP (A):  61.3098   0.4823  47.2028              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0204 T22:   0.0155                                     
REMARK   3      T33:   0.0596 T12:  -0.0012                                     
REMARK   3      T13:  -0.0265 T23:  -0.0243                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5964 L22:   2.3514                                     
REMARK   3      L33:   1.4817 L12:  -1.0078                                     
REMARK   3      L13:  -0.4728 L23:   0.4552                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0394 S12:   0.1048 S13:  -0.0225                       
REMARK   3      S21:  -0.1162 S22:  -0.0431 S23:   0.0613                       
REMARK   3      S31:  -0.0172 S32:  -0.1111 S33:   0.0825                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    50        C    63                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.4804  -2.1964   4.6319              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2401 T22:   0.4519                                     
REMARK   3      T33:   0.2478 T12:   0.0435                                     
REMARK   3      T13:  -0.0478 T23:   0.0796                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7394 L22:  14.2984                                     
REMARK   3      L33:   7.6677 L12:   5.3656                                     
REMARK   3      L13:   0.8119 L23:   2.9601                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1171 S12:   0.7830 S13:   0.1730                       
REMARK   3      S21:  -1.0067 S22:  -0.2905 S23:   0.2583                       
REMARK   3      S31:   0.0499 S32:  -0.3301 S33:   0.1733                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    50        D    63                          
REMARK   3    ORIGIN FOR THE GROUP (A):  72.6173  -4.1235  59.3549              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1614 T22:   0.3781                                     
REMARK   3      T33:   0.1954 T12:   0.0999                                     
REMARK   3      T13:  -0.0535 T23:   0.0635                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.7345 L22:  17.1965                                     
REMARK   3      L33:   8.7210 L12:   5.2802                                     
REMARK   3      L13:   0.4468 L23:   3.3278                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0609 S12:  -0.6796 S13:  -0.0342                       
REMARK   3      S21:   0.3767 S22:  -0.2368 S23:  -0.7951                       
REMARK   3      S31:  -0.1019 S32:   0.8658 S33:   0.2977                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL PLUS 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 U VALUES : WITH TLS ADDED. AMINO ACID RESIDUES 51         
REMARK   3  THROUGH 58 ARE POORLY DEFINED BY ELECTRON DENSITY. FO-FC DENSITY    
REMARK   3  SUGGESTS AN ALTERNATE CONFORMATION OF THIS REGION FOR CHAIN A.      
REMARK   3  AUTOBUSTER, PHENIX, COOT AND THE MOLPROBITY SERVER WERE ALSO        
REMARK   3  USED DURING REFINEMENT OF THE MODEL.                                
REMARK   4                                                                      
REMARK   4 3U7X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-OCT-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000068418.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-AUG-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97924                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-3000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-3000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35859                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
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     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.08900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.64000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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 1IPB                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1:1 OF (PROTEIN STOCK: 0.0004 M EIF4E,   
REMARK 280  0.001 M 4EPB1, 0.004 M RIBAVIRIN, 0.02 HEPES, 0.1 M POTASSIUM       
REMARK 280  CHLORIDE, 0.001 TCEP, PH 7.3):(RESERVOIR: 2 M AMMONIUM SULFATE,     
REMARK 280  2% PEG-400, 0.1 M SODIUM HEPES), VAPOR DIFFUSION, SITTING DROP,     
REMARK 280  TEMPERATURE 291K, PH 7.5                                            
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       19.13150            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: 1360 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1660 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4130 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -65.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       73.53122            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       19.13150            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       92.62955            
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     ASN B    30                                                      
REMARK 465     PRO C    47                                                      
REMARK 465     GLY C    48                                                      
REMARK 465     GLY C    49                                                      
REMARK 465     ASN C    64                                                      
REMARK 465     SER C    65                                                      
REMARK 465     PRO C    66                                                      
REMARK 465     PRO D    47                                                      
REMARK 465     GLY D    48                                                      
REMARK 465     GLY D    49                                                      
REMARK 465     ASN D    64                                                      
REMARK 465     SER D    65                                                      
REMARK 465     PRO D    66                                                      
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  49    CG   CD   CE   NZ                                   
REMARK 470     ASN A  50    OD1  ND2                                            
REMARK 470     LYS A  52    CG   CD   CE   NZ                                   
REMARK 470     SER A  53    OG                                                  
REMARK 470     LYS A  54    CG   CD   CE   NZ                                   
REMARK 470     THR A  55    OG1  CG2                                            
REMARK 470     TRP A  56    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A  56    CZ3  CH2                                            
REMARK 470     GLN A  57    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 106    NZ                                                  
REMARK 470     LYS A 159    CG   CD   CE   NZ                                   
REMARK 470     GLU A 185    CD   OE1  OE2                                       
REMARK 470     LYS A 206    CE   NZ                                             
REMARK 470     SER A 207    OG                                                  
REMARK 470     SER A 209    OG                                                  
REMARK 470     THR A 210    OG1  CG2                                            
REMARK 470     LYS A 212    NZ                                                  
REMARK 470     LYS B  49    CG   CD   CE   NZ                                   
REMARK 470     LYS B  52    CG   CD   CE   NZ                                   
REMARK 470     SER B  53    OG                                                  
REMARK 470     LYS B  54    CG   CD   CE   NZ                                   
REMARK 470     THR B  55    OG1  CG2                                            
REMARK 470     TRP B  56    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B  56    CZ3  CH2                                            
REMARK 470     GLN B  57    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 120    CG   CD   OE1  NE2                                  
REMARK 470     ASP B 144    OD1  OD2                                            
REMARK 470     LYS B 159    CG   CD   CE   NZ                                   
REMARK 470     GLU B 185    OE1  OE2                                            
REMARK 470     LYS B 206    NZ                                                  
REMARK 470     SER B 207    OG                                                  
REMARK 470     SER B 209    OG                                                  
REMARK 470     THR B 210    OG1  CG2                                            
REMARK 470     LYS B 212    CD   CE   NZ                                        
REMARK 470     THR C  50    OG1  CG2                                            
REMARK 470     ARG C  51    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C  57    CG   CD   CE   NZ                                   
REMARK 470     GLU C  61    CG   CD   OE1  OE2                                  
REMARK 470     ARG C  63    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR D  50    OG1  CG2                                            
REMARK 470     ARG D  51    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D  57    CG   CD   CE   NZ                                   
REMARK 470     GLU D  61    CG   CD   OE1  OE2                                  
REMARK 470     ARG D  63    NE   CZ   NH1  NH2                                  
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   OE1  GLU A   103     OE2  GLU B   103              2.17            
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    TYR A  34      -13.33   -145.13                                   
REMARK 500    ASN A  50       42.63    -74.44                                   
REMARK 500    ASP A  67       16.52   -143.28                                   
REMARK 500    ASP A 143     -136.52     57.22                                   
REMARK 500    ASP B  67       20.29   -141.89                                   
REMARK 500    ASP B 143     -136.80     58.85                                   
REMARK 500    GLU D  61       31.73    -76.00                                   
REMARK 500    CYS D  62      -61.25   -142.86                                   
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 SO4 A 218                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 218                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 219                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 220                 
DBREF  3U7X A    1   217  UNP    P06730   IF4E_HUMAN       1    217             
DBREF  3U7X B    1   217  UNP    P06730   IF4E_HUMAN       1    217             
DBREF  3U7X C   47    66  UNP    Q13541   4EBP1_HUMAN     47     66             
DBREF  3U7X D   47    66  UNP    Q13541   4EBP1_HUMAN     47     66             
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 ASN 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 C   20  PRO GLY GLY THR ARG ILE ILE TYR ASP ARG LYS PHE LEU          
SEQRES   2 C   20  MET GLU CYS ARG ASN SER PRO                                  
SEQRES   1 D   20  PRO GLY GLY THR ARG ILE ILE TYR ASP ARG LYS PHE LEU          
SEQRES   2 D   20  MET GLU CYS ARG ASN SER PRO                                  
HET    SO4  A 218       5                                                       
HET    UNX  A 219       1                                                       
HET    UNX  A 220       1                                                       
HET    UNX  A 221       1                                                       
HET    UNX  A 222       1                                                       
HET    UNX  A 223       1                                                       
HET    UNX  A 224       1                                                       
HET    UNX  A 225       1                                                       
HET    UNX  A 226       1                                                       
HET    UNX  A 227       1                                                       
HET    SO4  B 218       5                                                       
HET    SO4  B 219       5                                                       
HET    SO4  B 220       5                                                       
HET    UNX  B 222       1                                                       
HET    UNX  B 223       1                                                       
HET    UNX  B 224       1                                                       
HET    UNX  B 225       1                                                       
HET    UNX  B 226       1                                                       
HET    UNX  B 227       1                                                       
HET    UNX  B 228       1                                                       
HET    UNX  B 229       1                                                       
HET    UNX  B 230       1                                                       
HET    UNX  B 231       1                                                       
HET    UNX  B 232       1                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     UNX UNKNOWN ATOM OR ION                                              
FORMUL   5  SO4    4(O4 S 2-)                                                   
FORMUL   6  UNX    20(X)                                                        
FORMUL  29  HOH   *123(H2 O)                                                    
HELIX    1   1 THR A   55  ASN A   59  1                                   5    
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  LYS A  206  1                                   7    
HELIX    9   9 VAL B   69  ILE B   79  1                                  11    
HELIX   10  10 LEU B   81  LEU B   85  5                                   5    
HELIX   11  11 ASN B  118  ASP B  125  1                                   8    
HELIX   12  12 ASP B  125  GLY B  139  1                                  15    
HELIX   13  13 PHE B  142  ASP B  147  5                                   6    
HELIX   14  14 ASN B  172  GLY B  188  1                                  17    
HELIX   15  15 HIS B  200  LYS B  206  1                                   7    
HELIX   16  16 ASP C   55  CYS C   62  1                                   8    
HELIX   17  17 ASP D   55  GLU D   61  1                                   7    
SHEET    1   A 8 LEU A  60  THR A  68  0                                        
SHEET    2   A 8 PRO A  38  LYS A  49 -1  N  LEU A  45   O  ILE A  63           
SHEET    3   A 8 CYS A  89  LYS A  95 -1  O  SER A  92   N  TRP A  46           
SHEET    4   A 8 VAL A 149  ASN A 155 -1  O  VAL A 154   N  TYR A  91           
SHEET    5   A 8 ASP A 161  THR A 167 -1  O  TRP A 166   N  CYS A 150           
SHEET    6   A 8 GLY A 111  LEU A 117 -1  N  ILE A 115   O  ILE A 163           
SHEET    7   A 8 GLY A 196  SER A 199 -1  O  GLY A 196   N  LEU A 114           
SHEET    8   A 8 PHE A 215  VAL A 216 -1  O  PHE A 215   N  TYR A 197           
SHEET    1   B 8 LEU B  60  THR B  68  0                                        
SHEET    2   B 8 PRO B  38  LYS B  49 -1  N  LEU B  45   O  ILE B  63           
SHEET    3   B 8 CYS B  89  LYS B  95 -1  O  SER B  92   N  TRP B  46           
SHEET    4   B 8 VAL B 149  ASN B 155 -1  O  CYS B 150   N  LYS B  95           
SHEET    5   B 8 ASP B 161  THR B 167 -1  O  TRP B 166   N  GLY B 151           
SHEET    6   B 8 GLY B 111  LEU B 117 -1  N  LEU B 117   O  ASP B 161           
SHEET    7   B 8 GLY B 196  SER B 199 -1  O  GLY B 196   N  LEU B 114           
SHEET    8   B 8 PHE B 215  VAL B 216 -1  O  PHE B 215   N  TYR B 197           
SITE     1 AC1  4 GLU A 171  ARG A 173  GLU A 174  HOH A 249                    
SITE     1 AC2  2 ARG B  42  LYS B  65                                          
SITE     1 AC3  2 ARG B 157  LYS B 162                                          
SITE     1 AC4  3 GLU B 171  ARG B 173  GLU B 174                               
CRYST1   86.500   38.263   93.533  90.00  97.97  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      0.011561  0.000000  0.001618        0.00000                         
SCALE2      0.000000  0.026135  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010796        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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