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Database: PDB
Entry: 5NVK
LinkDB: 5NVK
Original site: 5NVK 
HEADER    TRANSLATION                             04-MAY-17   5NVK              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN 4EHP-GIGYF1 COMPLEX                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 4E TYPE 2;        
COMPND   3 CHAIN: A, C, E, G;                                                   
COMPND   4 SYNONYM: EIF4E TYPE 2,EUKARYOTIC TRANSLATION INITIATION FACTOR 4E    
COMPND   5 HOMOLOGOUS PROTEIN,EUKARYOTIC TRANSLATION INITIATION FACTOR 4E-LIKE  
COMPND   6 3,EIF4E-LIKE PROTEIN 4E-LP,MRNA CAP-BINDING PROTEIN 4EHP,H4EHP,MRNA  
COMPND   7 CAP-BINDING PROTEIN TYPE 3;                                          
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 OTHER_DETAILS: THE FIRST RESIDUE OF THE COORDINATE SEQUENCE OF CHAIN 
COMPND  10 G BELONGS TO THE EXPRESSION TAG;                                     
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: GRB10-INTERACTING GYF PROTEIN 1;                           
COMPND  13 CHAIN: B, D, F, H;                                                   
COMPND  14 SYNONYM: PERQ AMINO ACID-RICH WITH GYF DOMAIN-CONTAINING PROTEIN 1;  
COMPND  15 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: EIF4E2, EIF4EL3;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: STAR;                                     
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: GIGYF1, CDS2, PERQ1, PP3360;                                   
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  16 EXPRESSION_SYSTEM_VARIANT: STAR                                      
KEYWDS    TRANSLATIONAL REGULATION, CAP-BINDING PROTEIN, 4EHP-BINDING PROTEIN,  
KEYWDS   2 GRB10-INTERACTING GYF PROTEIN 1, TRANSLATION                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.PETER,E.VALKOV                                                      
REVDAT   2   24-JAN-18 5NVK    1       SOURCE                                   
REVDAT   1   26-JUL-17 5NVK    0                                                
JRNL        AUTH   D.PETER,R.WEBER,F.SANDMEIR,L.WOHLBOLD,S.HELMS,P.BAWANKAR,    
JRNL        AUTH 2 E.VALKOV,C.IGREJA,E.IZAURRALDE                               
JRNL        TITL   GIGYF1/2 PROTEINS USE AUXILIARY SEQUENCES TO SELECTIVELY     
JRNL        TITL 2 BIND TO 4EHP AND REPRESS TARGET MRNA EXPRESSION.             
JRNL        REF    GENES DEV.                    V.  31  1147 2017              
JRNL        REFN                   ISSN 1549-5477                               
JRNL        PMID   28698298                                                     
JRNL        DOI    10.1101/GAD.299420.117                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.84                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 24694                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.207                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.930                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1218                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 47.8493 -  6.0289    0.99     2722   123  0.1789 0.2230        
REMARK   3     2  6.0289 -  4.7868    1.00     2621   138  0.1750 0.2154        
REMARK   3     3  4.7868 -  4.1821    0.99     2625   132  0.1673 0.2028        
REMARK   3     4  4.1821 -  3.7999    1.00     2572   139  0.1960 0.2452        
REMARK   3     5  3.7999 -  3.5276    1.00     2607   139  0.2152 0.2712        
REMARK   3     6  3.5276 -  3.3197    1.00     2582   147  0.2380 0.2886        
REMARK   3     7  3.3197 -  3.1535    1.00     2555   142  0.2578 0.3282        
REMARK   3     8  3.1535 -  3.0162    1.00     2628   128  0.2598 0.3521        
REMARK   3     9  3.0162 -  2.9001    1.00     2564   130  0.2887 0.3206        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.410            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.070           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           8014                                  
REMARK   3   ANGLE     :  0.494          10834                                  
REMARK   3   CHIRALITY :  0.039           1152                                  
REMARK   3   PLANARITY :  0.003           1404                                  
REMARK   3   DIHEDRAL  : 16.455           4839                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN 'A' AND RESID 52 THROUGH 232)                   
REMARK   3    ORIGIN FOR THE GROUP (A): -10.9923  16.3599 -38.3102              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4310 T22:   0.4677                                     
REMARK   3      T33:   0.1218 T12:   0.0260                                     
REMARK   3      T13:  -0.0154 T23:   0.0190                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2925 L22:   1.5824                                     
REMARK   3      L33:   0.3805 L12:  -0.0402                                     
REMARK   3      L13:  -0.0740 L23:  -0.0665                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0366 S12:   0.0995 S13:   0.0666                       
REMARK   3      S21:  -0.1059 S22:  -0.0133 S23:   0.1934                       
REMARK   3      S31:   0.0238 S32:  -0.1134 S33:   0.0026                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN 'B' AND RESID 36 THROUGH 103)                   
REMARK   3    ORIGIN FOR THE GROUP (A): -14.0534  24.4844 -28.2380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5145 T22:   0.3997                                     
REMARK   3      T33:   0.1786 T12:  -0.0463                                     
REMARK   3      T13:   0.0451 T23:  -0.0186                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1754 L22:   1.8010                                     
REMARK   3      L33:   1.5434 L12:  -0.8313                                     
REMARK   3      L13:  -0.1835 L23:  -0.3312                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1559 S12:  -0.1338 S13:   0.0862                       
REMARK   3      S21:   0.2826 S22:   0.1166 S23:   0.1999                       
REMARK   3      S31:  -0.0965 S32:  -0.2711 S33:   0.0279                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN 'C' AND RESID 52 THROUGH 219)                   
REMARK   3    ORIGIN FOR THE GROUP (A):   5.8417  48.6068 -28.1842              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4549 T22:   0.3089                                     
REMARK   3      T33:   0.3164 T12:   0.0034                                     
REMARK   3      T13:   0.0881 T23:  -0.0458                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9998 L22:   2.3313                                     
REMARK   3      L33:   2.9829 L12:   0.0895                                     
REMARK   3      L13:  -0.5435 L23:   0.4329                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1877 S12:  -0.0607 S13:   0.4891                       
REMARK   3      S21:  -0.0437 S22:   0.0364 S23:  -0.3584                       
REMARK   3      S31:  -0.5157 S32:   0.1300 S33:  -0.1468                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN 'D' AND RESID 30 THROUGH 103)                   
REMARK   3    ORIGIN FOR THE GROUP (A):   7.7613  38.7647 -35.1999              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5794 T22:   0.4683                                     
REMARK   3      T33:   0.3171 T12:  -0.0491                                     
REMARK   3      T13:   0.0163 T23:  -0.0017                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7799 L22:   1.4646                                     
REMARK   3      L33:   1.5707 L12:  -0.0421                                     
REMARK   3      L13:   0.5039 L23:   0.6770                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2115 S12:   0.0498 S13:   0.2558                       
REMARK   3      S21:   0.2486 S22:   0.0391 S23:  -0.4911                       
REMARK   3      S31:  -0.0930 S32:   0.1150 S33:  -0.3035                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN 'E' AND RESID 52 THROUGH 219)                   
REMARK   3    ORIGIN FOR THE GROUP (A):  19.4290  76.7465  -1.2315              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5169 T22:   0.6521                                     
REMARK   3      T33:   0.1916 T12:   0.0962                                     
REMARK   3      T13:   0.0386 T23:  -0.0826                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4576 L22:   2.2894                                     
REMARK   3      L33:   1.5892 L12:  -0.1120                                     
REMARK   3      L13:  -0.1190 L23:   0.0383                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1440 S12:  -0.3586 S13:   0.0584                       
REMARK   3      S21:   0.4819 S22:   0.1859 S23:   0.3288                       
REMARK   3      S31:  -0.1073 S32:  -0.3006 S33:   0.0997                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN 'F' AND RESID 37 THROUGH 103)                   
REMARK   3    ORIGIN FOR THE GROUP (A):  30.3754  81.6680  -6.0963              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6678 T22:   0.5816                                     
REMARK   3      T33:   0.2656 T12:   0.0605                                     
REMARK   3      T13:  -0.0759 T23:  -0.1033                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0252 L22:   0.4051                                     
REMARK   3      L33:   0.9839 L12:  -0.1348                                     
REMARK   3      L13:   0.4673 L23:   0.2768                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2550 S12:  -0.2716 S13:   0.3305                       
REMARK   3      S21:   0.6189 S22:   0.0819 S23:  -0.1172                       
REMARK   3      S31:  -0.2284 S32:   0.2730 S33:  -0.1017                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (CHAIN 'G' AND RESID 51 THROUGH 233)                   
REMARK   3    ORIGIN FOR THE GROUP (A):  50.5093  57.9738 -10.0165              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4384 T22:   0.3824                                     
REMARK   3      T33:   0.1826 T12:  -0.0043                                     
REMARK   3      T13:   0.0185 T23:  -0.0664                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7707 L22:   0.2239                                     
REMARK   3      L33:   1.1649 L12:  -0.0625                                     
REMARK   3      L13:   0.2948 L23:  -0.0475                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1067 S12:   0.1509 S13:  -0.2906                       
REMARK   3      S21:  -0.0565 S22:   0.1239 S23:  -0.0192                       
REMARK   3      S31:   0.1523 S32:   0.0526 S33:   0.0005                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (CHAIN 'H' AND RESID 38 THROUGH 103)                   
REMARK   3    ORIGIN FOR THE GROUP (A):  42.2549  55.2538   0.2461              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5198 T22:   0.5243                                     
REMARK   3      T33:   0.2328 T12:  -0.0353                                     
REMARK   3      T13:   0.0462 T23:   0.0514                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2787 L22:   0.4524                                     
REMARK   3      L33:   1.5026 L12:  -0.4414                                     
REMARK   3      L13:   0.2255 L23:  -0.0519                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0174 S12:  -0.4758 S13:  -0.5028                       
REMARK   3      S21:   0.0976 S22:  -0.0589 S23:   0.1580                       
REMARK   3      S31:   0.2921 S32:  -0.0429 S33:   0.0625                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5NVK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-MAY-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200004614.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-MAR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.999810                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24699                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.843                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.98                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.64700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.950                              
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: 5NVL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350 0.2 M KCL, VAPOR            
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42                             
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   -Y,X,Z+1/2                                              
REMARK 290       4555   Y,-X,Z+1/2                                              
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  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       30.45500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       30.45500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4350 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4260 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4160 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12530 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4350 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    46                                                      
REMARK 465     PRO A    47                                                      
REMARK 465     HIS A    48                                                      
REMARK 465     MET A    49                                                      
REMARK 465     LEU A    50                                                      
REMARK 465     GLU A    51                                                      
REMARK 465     GLY A    70                                                      
REMARK 465     ARG A    71                                                      
REMARK 465     PRO A    72                                                      
REMARK 465     THR A    73                                                      
REMARK 465     SER A    74                                                      
REMARK 465     SER A    75                                                      
REMARK 465     GLN A    76                                                      
REMARK 465     SER A    77                                                      
REMARK 465     TYR A    78                                                      
REMARK 465     LEU A   233                                                      
REMARK 465     PHE A   234                                                      
REMARK 465     GLY B    29                                                      
REMARK 465     PRO B    30                                                      
REMARK 465     HIS B    31                                                      
REMARK 465     MET B    32                                                      
REMARK 465     LYS B    33                                                      
REMARK 465     TYR B    34                                                      
REMARK 465     LYS B    35                                                      
REMARK 465     GLY C    46                                                      
REMARK 465     PRO C    47                                                      
REMARK 465     HIS C    48                                                      
REMARK 465     MET C    49                                                      
REMARK 465     LEU C    50                                                      
REMARK 465     GLU C    51                                                      
REMARK 465     SER C   220                                                      
REMARK 465     ILE C   221                                                      
REMARK 465     LYS C   222                                                      
REMARK 465     MET C   223                                                      
REMARK 465     PRO C   224                                                      
REMARK 465     GLY C   225                                                      
REMARK 465     ARG C   226                                                      
REMARK 465     LEU C   227                                                      
REMARK 465     GLY C   228                                                      
REMARK 465     PRO C   229                                                      
REMARK 465     GLN C   230                                                      
REMARK 465     ARG C   231                                                      
REMARK 465     LEU C   232                                                      
REMARK 465     LEU C   233                                                      
REMARK 465     PHE C   234                                                      
REMARK 465     GLY D    29                                                      
REMARK 465     GLY E    46                                                      
REMARK 465     PRO E    47                                                      
REMARK 465     HIS E    48                                                      
REMARK 465     MET E    49                                                      
REMARK 465     LEU E    50                                                      
REMARK 465     GLU E    51                                                      
REMARK 465     SER E   220                                                      
REMARK 465     ILE E   221                                                      
REMARK 465     LYS E   222                                                      
REMARK 465     MET E   223                                                      
REMARK 465     PRO E   224                                                      
REMARK 465     GLY E   225                                                      
REMARK 465     ARG E   226                                                      
REMARK 465     LEU E   227                                                      
REMARK 465     GLY E   228                                                      
REMARK 465     PRO E   229                                                      
REMARK 465     GLN E   230                                                      
REMARK 465     ARG E   231                                                      
REMARK 465     LEU E   232                                                      
REMARK 465     LEU E   233                                                      
REMARK 465     PHE E   234                                                      
REMARK 465     GLY F    29                                                      
REMARK 465     PRO F    30                                                      
REMARK 465     HIS F    31                                                      
REMARK 465     MET F    32                                                      
REMARK 465     LYS F    33                                                      
REMARK 465     TYR F    34                                                      
REMARK 465     LYS F    35                                                      
REMARK 465     LEU F    36                                                      
REMARK 465     GLY G    46                                                      
REMARK 465     PRO G    47                                                      
REMARK 465     HIS G    48                                                      
REMARK 465     MET G    49                                                      
REMARK 465     LEU G    50                                                      
REMARK 465     GLY G    70                                                      
REMARK 465     ARG G    71                                                      
REMARK 465     PRO G    72                                                      
REMARK 465     THR G    73                                                      
REMARK 465     SER G    74                                                      
REMARK 465     SER G    75                                                      
REMARK 465     GLN G    76                                                      
REMARK 465     SER G    77                                                      
REMARK 465     TYR G    78                                                      
REMARK 465     GLU G    79                                                      
REMARK 465     GLN G    80                                                      
REMARK 465     PHE G   234                                                      
REMARK 465     GLY H    29                                                      
REMARK 465     PRO H    30                                                      
REMARK 465     HIS H    31                                                      
REMARK 465     MET H    32                                                      
REMARK 465     LYS H    33                                                      
REMARK 465     TYR H    34                                                      
REMARK 465     LYS H    35                                                      
REMARK 465     LEU H    36                                                      
REMARK 465     ALA H    37                                                      
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   HE   ARG B    40     OE2  GLU D    45              1.52            
REMARK 500   OD1  ASN C   184     HH   TYR C   214              1.57            
REMARK 500   O    ASN E    59     H    GLU E   118              1.58            
REMARK 500  HH22  ARG E   103     O    GLN F    75              1.58            
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    GLN A  80      102.51    -56.12                                   
REMARK 500    ILE A  85      -71.11    -89.03                                   
REMARK 500    PRO A 122       45.02    -71.16                                   
REMARK 500    MET A 161       52.96     70.08                                   
REMARK 500    ARG A 226       39.46   -142.12                                   
REMARK 500    THR C  73     -179.65    -63.07                                   
REMARK 500    ILE C  85      -71.00    -86.77                                   
REMARK 500    PRO C 122       55.08    -67.95                                   
REMARK 500    PHE D  65       43.16   -101.38                                   
REMARK 500    ASP D  71      -73.67    -65.03                                   
REMARK 500    PRO D  81     -178.07    -62.52                                   
REMARK 500    PRO E 122       58.23    -66.69                                   
REMARK 500    ASN E 209       32.22    -99.08                                   
REMARK 500    ASP F  71      -72.89    -57.81                                   
REMARK 500    ILE G  85      -72.39    -87.88                                   
REMARK 500    PRO G 122       52.56    -68.59                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5NVK A   52   234  UNP    O60573   IF4E2_HUMAN     52    234             
DBREF  5NVK B   33   103  UNP    O75420   GGYF1_HUMAN     33    103             
DBREF  5NVK C   52   234  UNP    O60573   IF4E2_HUMAN     52    234             
DBREF  5NVK D   33   103  UNP    O75420   GGYF1_HUMAN     33    103             
DBREF  5NVK E   52   234  UNP    O60573   IF4E2_HUMAN     52    234             
DBREF  5NVK F   33   103  UNP    O75420   GGYF1_HUMAN     33    103             
DBREF  5NVK G   52   234  UNP    O60573   IF4E2_HUMAN     52    234             
DBREF  5NVK H   33   103  UNP    O75420   GGYF1_HUMAN     33    103             
SEQADV 5NVK GLY A   46  UNP  O60573              EXPRESSION TAG                 
SEQADV 5NVK PRO A   47  UNP  O60573              EXPRESSION TAG                 
SEQADV 5NVK HIS A   48  UNP  O60573              EXPRESSION TAG                 
SEQADV 5NVK MET A   49  UNP  O60573              EXPRESSION TAG                 
SEQADV 5NVK LEU A   50  UNP  O60573              EXPRESSION TAG                 
SEQADV 5NVK GLU A   51  UNP  O60573              EXPRESSION TAG                 
SEQADV 5NVK GLY B   29  UNP  O75420              EXPRESSION TAG                 
SEQADV 5NVK PRO B   30  UNP  O75420              EXPRESSION TAG                 
SEQADV 5NVK HIS B   31  UNP  O75420              EXPRESSION TAG                 
SEQADV 5NVK MET B   32  UNP  O75420              EXPRESSION TAG                 
SEQADV 5NVK GLY C   46  UNP  O60573              EXPRESSION TAG                 
SEQADV 5NVK PRO C   47  UNP  O60573              EXPRESSION TAG                 
SEQADV 5NVK HIS C   48  UNP  O60573              EXPRESSION TAG                 
SEQADV 5NVK MET C   49  UNP  O60573              EXPRESSION TAG                 
SEQADV 5NVK LEU C   50  UNP  O60573              EXPRESSION TAG                 
SEQADV 5NVK GLU C   51  UNP  O60573              EXPRESSION TAG                 
SEQADV 5NVK GLY D   29  UNP  O75420              EXPRESSION TAG                 
SEQADV 5NVK PRO D   30  UNP  O75420              EXPRESSION TAG                 
SEQADV 5NVK HIS D   31  UNP  O75420              EXPRESSION TAG                 
SEQADV 5NVK MET D   32  UNP  O75420              EXPRESSION TAG                 
SEQADV 5NVK GLY E   46  UNP  O60573              EXPRESSION TAG                 
SEQADV 5NVK PRO E   47  UNP  O60573              EXPRESSION TAG                 
SEQADV 5NVK HIS E   48  UNP  O60573              EXPRESSION TAG                 
SEQADV 5NVK MET E   49  UNP  O60573              EXPRESSION TAG                 
SEQADV 5NVK LEU E   50  UNP  O60573              EXPRESSION TAG                 
SEQADV 5NVK GLU E   51  UNP  O60573              EXPRESSION TAG                 
SEQADV 5NVK GLY F   29  UNP  O75420              EXPRESSION TAG                 
SEQADV 5NVK PRO F   30  UNP  O75420              EXPRESSION TAG                 
SEQADV 5NVK HIS F   31  UNP  O75420              EXPRESSION TAG                 
SEQADV 5NVK MET F   32  UNP  O75420              EXPRESSION TAG                 
SEQADV 5NVK GLY G   46  UNP  O60573              EXPRESSION TAG                 
SEQADV 5NVK PRO G   47  UNP  O60573              EXPRESSION TAG                 
SEQADV 5NVK HIS G   48  UNP  O60573              EXPRESSION TAG                 
SEQADV 5NVK MET G   49  UNP  O60573              EXPRESSION TAG                 
SEQADV 5NVK LEU G   50  UNP  O60573              EXPRESSION TAG                 
SEQADV 5NVK GLU G   51  UNP  O60573              EXPRESSION TAG                 
SEQADV 5NVK GLY H   29  UNP  O75420              EXPRESSION TAG                 
SEQADV 5NVK PRO H   30  UNP  O75420              EXPRESSION TAG                 
SEQADV 5NVK HIS H   31  UNP  O75420              EXPRESSION TAG                 
SEQADV 5NVK MET H   32  UNP  O75420              EXPRESSION TAG                 
SEQRES   1 A  189  GLY PRO HIS MET LEU GLU ALA GLU HIS PRO LEU GLN TYR          
SEQRES   2 A  189  ASN TYR THR PHE TRP TYR SER ARG ARG THR PRO GLY ARG          
SEQRES   3 A  189  PRO THR SER SER GLN SER TYR GLU GLN ASN ILE LYS GLN          
SEQRES   4 A  189  ILE GLY THR PHE ALA SER VAL GLU GLN PHE TRP ARG PHE          
SEQRES   5 A  189  TYR SER HIS MET VAL ARG PRO GLY ASP LEU THR GLY HIS          
SEQRES   6 A  189  SER ASP PHE HIS LEU PHE LYS GLU GLY ILE LYS PRO MET          
SEQRES   7 A  189  TRP GLU ASP ASP ALA ASN LYS ASN GLY GLY LYS TRP ILE          
SEQRES   8 A  189  ILE ARG LEU ARG LYS GLY LEU ALA SER ARG CYS TRP GLU          
SEQRES   9 A  189  ASN LEU ILE LEU ALA MET LEU GLY GLU GLN PHE MET VAL          
SEQRES  10 A  189  GLY GLU GLU ILE CYS GLY ALA VAL VAL SER VAL ARG PHE          
SEQRES  11 A  189  GLN GLU ASP ILE ILE SER ILE TRP ASN LYS THR ALA SER          
SEQRES  12 A  189  ASP GLN ALA THR THR ALA ARG ILE ARG ASP THR LEU ARG          
SEQRES  13 A  189  ARG VAL LEU ASN LEU PRO PRO ASN THR ILE MET GLU TYR          
SEQRES  14 A  189  LYS THR HIS THR ASP SER ILE LYS MET PRO GLY ARG LEU          
SEQRES  15 A  189  GLY PRO GLN ARG LEU LEU PHE                                  
SEQRES   1 B   75  GLY PRO HIS MET LYS TYR LYS LEU ALA ASP TYR ARG TYR          
SEQRES   2 B   75  GLY ARG GLU GLU MET LEU ALA LEU TYR VAL LYS GLU ASN          
SEQRES   3 B   75  LYS VAL PRO GLU GLU LEU GLN ASP LYS GLU PHE ALA ALA          
SEQRES   4 B   75  VAL LEU GLN ASP GLU PRO LEU GLN PRO LEU ALA LEU GLU          
SEQRES   5 B   75  PRO LEU THR GLU GLU GLU GLN ARG ASN PHE SER LEU SER          
SEQRES   6 B   75  VAL ASN SER VAL ALA VAL LEU ARG LEU MET                      
SEQRES   1 C  189  GLY PRO HIS MET LEU GLU ALA GLU HIS PRO LEU GLN TYR          
SEQRES   2 C  189  ASN TYR THR PHE TRP TYR SER ARG ARG THR PRO GLY ARG          
SEQRES   3 C  189  PRO THR SER SER GLN SER TYR GLU GLN ASN ILE LYS GLN          
SEQRES   4 C  189  ILE GLY THR PHE ALA SER VAL GLU GLN PHE TRP ARG PHE          
SEQRES   5 C  189  TYR SER HIS MET VAL ARG PRO GLY ASP LEU THR GLY HIS          
SEQRES   6 C  189  SER ASP PHE HIS LEU PHE LYS GLU GLY ILE LYS PRO MET          
SEQRES   7 C  189  TRP GLU ASP ASP ALA ASN LYS ASN GLY GLY LYS TRP ILE          
SEQRES   8 C  189  ILE ARG LEU ARG LYS GLY LEU ALA SER ARG CYS TRP GLU          
SEQRES   9 C  189  ASN LEU ILE LEU ALA MET LEU GLY GLU GLN PHE MET VAL          
SEQRES  10 C  189  GLY GLU GLU ILE CYS GLY ALA VAL VAL SER VAL ARG PHE          
SEQRES  11 C  189  GLN GLU ASP ILE ILE SER ILE TRP ASN LYS THR ALA SER          
SEQRES  12 C  189  ASP GLN ALA THR THR ALA ARG ILE ARG ASP THR LEU ARG          
SEQRES  13 C  189  ARG VAL LEU ASN LEU PRO PRO ASN THR ILE MET GLU TYR          
SEQRES  14 C  189  LYS THR HIS THR ASP SER ILE LYS MET PRO GLY ARG LEU          
SEQRES  15 C  189  GLY PRO GLN ARG LEU LEU PHE                                  
SEQRES   1 D   75  GLY PRO HIS MET LYS TYR LYS LEU ALA ASP TYR ARG TYR          
SEQRES   2 D   75  GLY ARG GLU GLU MET LEU ALA LEU TYR VAL LYS GLU ASN          
SEQRES   3 D   75  LYS VAL PRO GLU GLU LEU GLN ASP LYS GLU PHE ALA ALA          
SEQRES   4 D   75  VAL LEU GLN ASP GLU PRO LEU GLN PRO LEU ALA LEU GLU          
SEQRES   5 D   75  PRO LEU THR GLU GLU GLU GLN ARG ASN PHE SER LEU SER          
SEQRES   6 D   75  VAL ASN SER VAL ALA VAL LEU ARG LEU MET                      
SEQRES   1 E  189  GLY PRO HIS MET LEU GLU ALA GLU HIS PRO LEU GLN TYR          
SEQRES   2 E  189  ASN TYR THR PHE TRP TYR SER ARG ARG THR PRO GLY ARG          
SEQRES   3 E  189  PRO THR SER SER GLN SER TYR GLU GLN ASN ILE LYS GLN          
SEQRES   4 E  189  ILE GLY THR PHE ALA SER VAL GLU GLN PHE TRP ARG PHE          
SEQRES   5 E  189  TYR SER HIS MET VAL ARG PRO GLY ASP LEU THR GLY HIS          
SEQRES   6 E  189  SER ASP PHE HIS LEU PHE LYS GLU GLY ILE LYS PRO MET          
SEQRES   7 E  189  TRP GLU ASP ASP ALA ASN LYS ASN GLY GLY LYS TRP ILE          
SEQRES   8 E  189  ILE ARG LEU ARG LYS GLY LEU ALA SER ARG CYS TRP GLU          
SEQRES   9 E  189  ASN LEU ILE LEU ALA MET LEU GLY GLU GLN PHE MET VAL          
SEQRES  10 E  189  GLY GLU GLU ILE CYS GLY ALA VAL VAL SER VAL ARG PHE          
SEQRES  11 E  189  GLN GLU ASP ILE ILE SER ILE TRP ASN LYS THR ALA SER          
SEQRES  12 E  189  ASP GLN ALA THR THR ALA ARG ILE ARG ASP THR LEU ARG          
SEQRES  13 E  189  ARG VAL LEU ASN LEU PRO PRO ASN THR ILE MET GLU TYR          
SEQRES  14 E  189  LYS THR HIS THR ASP SER ILE LYS MET PRO GLY ARG LEU          
SEQRES  15 E  189  GLY PRO GLN ARG LEU LEU PHE                                  
SEQRES   1 F   75  GLY PRO HIS MET LYS TYR LYS LEU ALA ASP TYR ARG TYR          
SEQRES   2 F   75  GLY ARG GLU GLU MET LEU ALA LEU TYR VAL LYS GLU ASN          
SEQRES   3 F   75  LYS VAL PRO GLU GLU LEU GLN ASP LYS GLU PHE ALA ALA          
SEQRES   4 F   75  VAL LEU GLN ASP GLU PRO LEU GLN PRO LEU ALA LEU GLU          
SEQRES   5 F   75  PRO LEU THR GLU GLU GLU GLN ARG ASN PHE SER LEU SER          
SEQRES   6 F   75  VAL ASN SER VAL ALA VAL LEU ARG LEU MET                      
SEQRES   1 G  189  GLY PRO HIS MET LEU GLU ALA GLU HIS PRO LEU GLN TYR          
SEQRES   2 G  189  ASN TYR THR PHE TRP TYR SER ARG ARG THR PRO GLY ARG          
SEQRES   3 G  189  PRO THR SER SER GLN SER TYR GLU GLN ASN ILE LYS GLN          
SEQRES   4 G  189  ILE GLY THR PHE ALA SER VAL GLU GLN PHE TRP ARG PHE          
SEQRES   5 G  189  TYR SER HIS MET VAL ARG PRO GLY ASP LEU THR GLY HIS          
SEQRES   6 G  189  SER ASP PHE HIS LEU PHE LYS GLU GLY ILE LYS PRO MET          
SEQRES   7 G  189  TRP GLU ASP ASP ALA ASN LYS ASN GLY GLY LYS TRP ILE          
SEQRES   8 G  189  ILE ARG LEU ARG LYS GLY LEU ALA SER ARG CYS TRP GLU          
SEQRES   9 G  189  ASN LEU ILE LEU ALA MET LEU GLY GLU GLN PHE MET VAL          
SEQRES  10 G  189  GLY GLU GLU ILE CYS GLY ALA VAL VAL SER VAL ARG PHE          
SEQRES  11 G  189  GLN GLU ASP ILE ILE SER ILE TRP ASN LYS THR ALA SER          
SEQRES  12 G  189  ASP GLN ALA THR THR ALA ARG ILE ARG ASP THR LEU ARG          
SEQRES  13 G  189  ARG VAL LEU ASN LEU PRO PRO ASN THR ILE MET GLU TYR          
SEQRES  14 G  189  LYS THR HIS THR ASP SER ILE LYS MET PRO GLY ARG LEU          
SEQRES  15 G  189  GLY PRO GLN ARG LEU LEU PHE                                  
SEQRES   1 H   75  GLY PRO HIS MET LYS TYR LYS LEU ALA ASP TYR ARG TYR          
SEQRES   2 H   75  GLY ARG GLU GLU MET LEU ALA LEU TYR VAL LYS GLU ASN          
SEQRES   3 H   75  LYS VAL PRO GLU GLU LEU GLN ASP LYS GLU PHE ALA ALA          
SEQRES   4 H   75  VAL LEU GLN ASP GLU PRO LEU GLN PRO LEU ALA LEU GLU          
SEQRES   5 H   75  PRO LEU THR GLU GLU GLU GLN ARG ASN PHE SER LEU SER          
SEQRES   6 H   75  VAL ASN SER VAL ALA VAL LEU ARG LEU MET                      
HELIX    1 AA1 VAL A   91  HIS A  100  1                                  10    
HELIX    2 AA2 ALA A  144  LEU A  156  1                                  13    
HELIX    3 AA3 GLN A  190  VAL A  203  1                                  14    
HELIX    4 AA4 ARG B   43  LEU B   49  1                                   7    
HELIX    5 AA5 GLU B   84  LEU B   92  1                                   9    
HELIX    6 AA6 VAL B   97  ARG B  101  1                                   5    
HELIX    7 AA7 VAL C   91  HIS C  100  1                                  10    
HELIX    8 AA8 ASP C  127  LYS C  130  5                                   4    
HELIX    9 AA9 ALA C  144  LEU C  156  1                                  13    
HELIX   10 AB1 GLN C  190  VAL C  203  1                                  14    
HELIX   11 AB2 ARG D   43  LEU D   49  1                                   7    
HELIX   12 AB3 GLU D   84  SER D   91  1                                   8    
HELIX   13 AB4 VAL D   97  ARG D  101  1                                   5    
HELIX   14 AB5 SER E   75  ASN E   81  1                                   7    
HELIX   15 AB6 VAL E   91  HIS E  100  1                                  10    
HELIX   16 AB7 ASP E  127  LYS E  130  5                                   4    
HELIX   17 AB8 ALA E  144  LEU E  156  1                                  13    
HELIX   18 AB9 GLN E  190  VAL E  203  1                                  14    
HELIX   19 AC1 ARG F   43  LEU F   49  1                                   7    
HELIX   20 AC2 GLU F   84  PHE F   90  1                                   7    
HELIX   21 AC3 VAL F   97  ARG F  101  1                                   5    
HELIX   22 AC4 VAL G   91  HIS G  100  1                                  10    
HELIX   23 AC5 ASP G  127  LYS G  130  5                                   4    
HELIX   24 AC6 ALA G  144  LEU G  156  1                                  13    
HELIX   25 AC7 GLN G  190  VAL G  203  1                                  14    
HELIX   26 AC8 ARG H   43  LEU H   49  1                                   7    
HELIX   27 AC9 GLU H   84  LEU H   92  1                                   9    
HELIX   28 AD1 VAL H   97  ARG H  101  1                                   5    
SHEET    1 AA1 7 LYS A  83  SER A  90  0                                        
SHEET    2 AA1 7 LEU A  56  ARG A  66 -1  N  PHE A  62   O  ILE A  85           
SHEET    3 AA1 7 SER A 111  LYS A 117 -1  O  PHE A 116   N  THR A  61           
SHEET    4 AA1 7 ILE A 166  VAL A 173 -1  O  ALA A 169   N  LEU A 115           
SHEET    5 AA1 7 ASP A 178  ASN A 184 -1  O  TRP A 183   N  GLY A 168           
SHEET    6 AA1 7 GLY A 133  LEU A 139 -1  N  LEU A 139   O  ASP A 178           
SHEET    7 AA1 7 MET A 212  THR A 216 -1  O  GLU A 213   N  ILE A 136           
SHEET    1 AA2 7 LYS C  83  SER C  90  0                                        
SHEET    2 AA2 7 LEU C  56  ARG C  66 -1  N  LEU C  56   O  ALA C  89           
SHEET    3 AA2 7 SER C 111  LYS C 117 -1  O  PHE C 116   N  THR C  61           
SHEET    4 AA2 7 ILE C 166  VAL C 173 -1  O  ALA C 169   N  LEU C 115           
SHEET    5 AA2 7 ASP C 178  ASN C 184 -1  O  ILE C 179   N  SER C 172           
SHEET    6 AA2 7 GLY C 133  LEU C 139 -1  N  LEU C 139   O  ASP C 178           
SHEET    7 AA2 7 MET C 212  THR C 216 -1  O  GLU C 213   N  ILE C 136           
SHEET    1 AA3 7 LYS E  83  SER E  90  0                                        
SHEET    2 AA3 7 LEU E  56  ARG E  66 -1  N  TYR E  64   O  LYS E  83           
SHEET    3 AA3 7 SER E 111  LYS E 117 -1  O  PHE E 116   N  THR E  61           
SHEET    4 AA3 7 ILE E 166  VAL E 173 -1  O  VAL E 173   N  SER E 111           
SHEET    5 AA3 7 ASP E 178  ASN E 184 -1  O  TRP E 183   N  GLY E 168           
SHEET    6 AA3 7 GLY E 133  LEU E 139 -1  N  LEU E 139   O  ASP E 178           
SHEET    7 AA3 7 MET E 212  THR E 216 -1  O  GLU E 213   N  ILE E 136           
SHEET    1 AA4 7 LYS G  83  SER G  90  0                                        
SHEET    2 AA4 7 LEU G  56  ARG G  66 -1  N  PHE G  62   O  ILE G  85           
SHEET    3 AA4 7 SER G 111  LYS G 117 -1  O  PHE G 116   N  THR G  61           
SHEET    4 AA4 7 ILE G 166  VAL G 173 -1  O  ALA G 169   N  LEU G 115           
SHEET    5 AA4 7 ASP G 178  ASN G 184 -1  O  ILE G 179   N  SER G 172           
SHEET    6 AA4 7 GLY G 133  LEU G 139 -1  N  LEU G 139   O  ASP G 178           
SHEET    7 AA4 7 MET G 212  THR G 216 -1  O  GLU G 213   N  ILE G 136           
CRYST1  135.320  135.320   60.910  90.00  90.00  90.00 P 42         16          
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      0.007390  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007390  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016418        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system