GenomeNet

Database: PDB
Entry: 3TF2
LinkDB: 3TF2
Original site: 3TF2 
HEADER    TRANSLATION                             15-AUG-11   3TF2              
TITLE     CRYSTAL STRUCTURE OF THE CAP FREE HUMAN TRANSLATION INITIATION FACTOR 
TITLE    2 EIF4E                                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 4E;               
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: EIF-4E, EIF4E, EIF-4F 25 KDA SUBUNIT, MRNA CAP-BINDING      
COMPND   5 PROTEIN;                                                             
COMPND   6 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: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PT7                                       
KEYWDS    EIF4E, TRANSLATION, MRNA EXPORT, STRUCTURAL GENOMICS, STRUCTURAL      
KEYWDS   2 GENOMICS CONSORTIUM, SGC                                             
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   4   08-NOV-17 3TF2    1       REMARK                                   
REVDAT   3   18-APR-12 3TF2    1       JRNL                                     
REVDAT   2   28-DEC-11 3TF2    1       JRNL                                     
REVDAT   1   31-AUG-11 3TF2    0                                                
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        (%) : 97.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 44671                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : THINSHELLS (SFTOOLS)            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.217                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.004                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1342                            
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) : 3138                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.06                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2570                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 61                           
REMARK   3   BIN FREE R VALUE                    : 0.3430                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5581                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 14                                      
REMARK   3   SOLVENT ATOMS            : 169                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.85                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.60100                                              
REMARK   3    B22 (A**2) : -2.20900                                             
REMARK   3    B33 (A**2) : 1.79200                                              
REMARK   3    B12 (A**2) : -0.33900                                             
REMARK   3    B13 (A**2) : 0.47000                                              
REMARK   3    B23 (A**2) : 0.84000                                              
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): 0.204         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.166         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.260        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.943                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.919                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5808 ; 0.013 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  3877 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7910 ; 1.334 ; 1.925       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9373 ; 0.862 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   709 ; 6.858 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   287 ;34.303 ;23.763       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   935 ;14.044 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    39 ;15.283 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   853 ; 0.081 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6525 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1270 ; 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):  3499 ; 0.609 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1425 ; 0.153 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5617 ; 1.065 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2309 ; 1.722 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2283 ; 2.593 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    35        A   217                          
REMARK   3    RESIDUE RANGE :   A   218        A   267                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.1465 -26.7690  10.4988              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0999 T22:   0.0618                                     
REMARK   3      T33:   0.0734 T12:   0.0689                                     
REMARK   3      T13:  -0.0323 T23:  -0.0151                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7748 L22:   2.0235                                     
REMARK   3      L33:   5.6614 L12:  -0.4943                                     
REMARK   3      L13:   0.5543 L23:  -0.2922                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1427 S12:   0.0311 S13:   0.0321                       
REMARK   3      S21:   0.0726 S22:   0.0471 S23:   0.1301                       
REMARK   3      S31:  -0.5432 S32:  -0.3235 S33:   0.0956                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    35        B   217                          
REMARK   3    RESIDUE RANGE :   B   218        B   261                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.6393 -41.0687 -27.1996              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0752 T22:   0.0571                                     
REMARK   3      T33:   0.0977 T12:  -0.0576                                     
REMARK   3      T13:   0.0415 T23:  -0.0183                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6969 L22:   1.9495                                     
REMARK   3      L33:   5.5917 L12:   0.5092                                     
REMARK   3      L13:  -0.8704 L23:  -0.1906                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1830 S12:   0.0267 S13:  -0.1368                       
REMARK   3      S21:  -0.0283 S22:   0.0338 S23:   0.0762                       
REMARK   3      S31:   0.4700 S32:  -0.3691 S33:   0.1492                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    33        C   217                          
REMARK   3    RESIDUE RANGE :   C   218        C   258                          
REMARK   3    ORIGIN FOR THE GROUP (A):  39.9701 -15.6656 -37.4540              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0803 T22:   0.0588                                     
REMARK   3      T33:   0.1160 T12:  -0.0480                                     
REMARK   3      T13:   0.0055 T23:   0.0059                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7081 L22:   3.1382                                     
REMARK   3      L33:   5.2999 L12:   0.1293                                     
REMARK   3      L13:  -1.0590 L23:  -0.1778                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0825 S12:   0.1061 S13:   0.1806                       
REMARK   3      S21:  -0.1620 S22:   0.0240 S23:   0.2536                       
REMARK   3      S31:  -0.3712 S32:   0.0008 S33:  -0.1065                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    35        D   217                          
REMARK   3    RESIDUE RANGE :   D   218        D   251                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.0048 -52.3726  20.5936              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0882 T22:   0.0707                                     
REMARK   3      T33:   0.0986 T12:   0.0462                                     
REMARK   3      T13:  -0.0200 T23:   0.0083                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5960 L22:   4.2405                                     
REMARK   3      L33:   5.2502 L12:  -0.1111                                     
REMARK   3      L13:   1.0096 L23:  -0.1962                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1423 S12:  -0.1373 S13:  -0.2371                       
REMARK   3      S21:   0.1617 S22:   0.0456 S23:   0.1820                       
REMARK   3      S31:   0.4269 S32:   0.0260 S33:  -0.1878                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK BULK SOLVENT                                    
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:                                           
REMARK   3  HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES: WITH   
REMARK   3  TLS ADDED. SIGNIFICANT DIFFERENCE DENSITY IS OBSERVED AROUND GAPS   
REMARK   3  IN PROTEIN CHAINS C (RESIDUES 119-122) AND D (RESIDUES 118-125)     
REMARK   3  BUT IS NOT INTERPRETABLE IN TERMS OF PEPTIDE GEOMETRY. THE PROGRAM  
REMARK   3  COOT AND THE MOLPROBITY SERVER WERE ALSO USED IN THE                
REMARK   3  COURSE OF MODEL REFINEMENT.                                         
REMARK   4                                                                      
REMARK   4 3TF2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-AUG-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000067402.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-FEB-11                          
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               : 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) : 0.97929                            
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   : 44808                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 1.900                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.4000                             
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     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37400                            
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: MODIFIED COORDINATES OF PDB ENTRY 1IPB               
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG-3350, 0.2 M DIAMMONIUM           
REMARK 280  CITRATE, VAPOR DIFFUSION, TEMPERATURE 289K                          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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     PRO A    31                                                      
REMARK 465     GLU A    32                                                      
REMARK 465     HIS A    33                                                      
REMARK 465     TYR A    34                                                      
REMARK 465     ALA A   204                                                      
REMARK 465     THR A   205                                                      
REMARK 465     LYS A   206                                                      
REMARK 465     SER A   207                                                      
REMARK 465     GLY A   208                                                      
REMARK 465     SER A   209                                                      
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 B    31                                                      
REMARK 465     GLU B    32                                                      
REMARK 465     HIS B    33                                                      
REMARK 465     TYR B    34                                                      
REMARK 465     ASP B    51                                                      
REMARK 465     LYS B    52                                                      
REMARK 465     SER B    53                                                      
REMARK 465     LYS B   206                                                      
REMARK 465     SER B   207                                                      
REMARK 465     GLY B   208                                                      
REMARK 465     SER B   209                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     THR C     3                                                      
REMARK 465     VAL C     4                                                      
REMARK 465     GLU C     5                                                      
REMARK 465     PRO C     6                                                      
REMARK 465     GLU C     7                                                      
REMARK 465     THR C     8                                                      
REMARK 465     THR C     9                                                      
REMARK 465     PRO C    10                                                      
REMARK 465     THR C    11                                                      
REMARK 465     PRO C    12                                                      
REMARK 465     ASN C    13                                                      
REMARK 465     PRO C    14                                                      
REMARK 465     PRO C    15                                                      
REMARK 465     THR C    16                                                      
REMARK 465     THR C    17                                                      
REMARK 465     GLU C    18                                                      
REMARK 465     GLU C    19                                                      
REMARK 465     GLU C    20                                                      
REMARK 465     LYS C    21                                                      
REMARK 465     THR C    22                                                      
REMARK 465     GLU C    23                                                      
REMARK 465     SER C    24                                                      
REMARK 465     ASN C    25                                                      
REMARK 465     GLN C    26                                                      
REMARK 465     GLU C    27                                                      
REMARK 465     VAL C    28                                                      
REMARK 465     ALA C    29                                                      
REMARK 465     ASN C    30                                                      
REMARK 465     PRO C    31                                                      
REMARK 465     GLU C    32                                                      
REMARK 465     LYS C   119                                                      
REMARK 465     GLN C   120                                                      
REMARK 465     GLN C   121                                                      
REMARK 465     ARG C   122                                                      
REMARK 465     LYS C   206                                                      
REMARK 465     SER C   207                                                      
REMARK 465     GLY C   208                                                      
REMARK 465     SER C   209                                                      
REMARK 465     THR C   210                                                      
REMARK 465     THR C   211                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     THR D     3                                                      
REMARK 465     VAL D     4                                                      
REMARK 465     GLU D     5                                                      
REMARK 465     PRO D     6                                                      
REMARK 465     GLU D     7                                                      
REMARK 465     THR D     8                                                      
REMARK 465     THR D     9                                                      
REMARK 465     PRO D    10                                                      
REMARK 465     THR D    11                                                      
REMARK 465     PRO D    12                                                      
REMARK 465     ASN D    13                                                      
REMARK 465     PRO D    14                                                      
REMARK 465     PRO D    15                                                      
REMARK 465     THR D    16                                                      
REMARK 465     THR D    17                                                      
REMARK 465     GLU D    18                                                      
REMARK 465     GLU D    19                                                      
REMARK 465     GLU D    20                                                      
REMARK 465     LYS D    21                                                      
REMARK 465     THR D    22                                                      
REMARK 465     GLU D    23                                                      
REMARK 465     SER D    24                                                      
REMARK 465     ASN D    25                                                      
REMARK 465     GLN D    26                                                      
REMARK 465     GLU D    27                                                      
REMARK 465     VAL D    28                                                      
REMARK 465     ALA D    29                                                      
REMARK 465     ASN D    30                                                      
REMARK 465     PRO D    31                                                      
REMARK 465     GLU D    32                                                      
REMARK 465     HIS D    33                                                      
REMARK 465     TYR D    34                                                      
REMARK 465     ASN D   118                                                      
REMARK 465     LYS D   119                                                      
REMARK 465     GLN D   120                                                      
REMARK 465     GLN D   121                                                      
REMARK 465     ARG D   122                                                      
REMARK 465     ARG D   123                                                      
REMARK 465     SER D   124                                                      
REMARK 465     ALA D   204                                                      
REMARK 465     THR D   205                                                      
REMARK 465     LYS D   206                                                      
REMARK 465     SER D   207                                                      
REMARK 465     GLY D   208                                                      
REMARK 465     SER D   209                                                      
REMARK 465     THR D   210                                                      
REMARK 465     THR D   211                                                      
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     ILE A  35    CG1  CG2  CD1                                       
REMARK 470     LYS A  49    CG   CD   CE   NZ                                   
REMARK 470     LYS A  54    CG   CD   CE   NZ                                   
REMARK 470     THR A  55    OG1  CG2                                            
REMARK 470     ARG A  61    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 119    CD   CE   NZ                                        
REMARK 470     GLN A 120    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 123    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 124    OG                                                  
REMARK 470     LYS A 159    CG   CD   CE   NZ                                   
REMARK 470     LYS A 162    CE   NZ                                             
REMARK 470     LYS A 192    CG   CD   CE   NZ                                   
REMARK 470     THR A 210    OG1  CG2                                            
REMARK 470     LYS A 212    CG   CD   CE   NZ                                   
REMARK 470     ILE B  35    CG2  CD1                                            
REMARK 470     LYS B  49    CD   CE   NZ                                        
REMARK 470     LYS B  54    CG   CD   CE   NZ                                   
REMARK 470     ARG B  61    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS B 106    CE   NZ                                             
REMARK 470     GLN B 120    CD   OE1  NE2                                       
REMARK 470     ARG B 122    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG B 123    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 159    CG   CD   CE   NZ                                   
REMARK 470     GLU B 171    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 173    CZ   NH1  NH2                                       
REMARK 470     GLU B 185    CD   OE1  OE2                                       
REMARK 470     THR B 210    OG1  CG2                                            
REMARK 470     LYS B 212    CG   CD   CE   NZ                                   
REMARK 470     HIS C  33    CG   ND1  CD2  CE1  NE2                             
REMARK 470     TYR C  34    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ILE C  35    CG1  CG2  CD1                                       
REMARK 470     LYS C  49    CD   CE   NZ                                        
REMARK 470     ASN C  50    OD1  ND2                                            
REMARK 470     LYS C  52    NZ                                                  
REMARK 470     LYS C  54    NZ                                                  
REMARK 470     GLN C  80    CG   CD   OE1  NE2                                  
REMARK 470     GLU C 105    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 106    CE   NZ                                             
REMARK 470     ASN C 118    CG   OD1  ND2                                       
REMARK 470     ASP C 147    CG   OD1  OD2                                       
REMARK 470     LYS C 159    CG   CD   CE   NZ                                   
REMARK 470     LYS C 192    CG   CD   CE   NZ                                   
REMARK 470     GLN C 198    CD   OE1  NE2                                       
REMARK 470     THR C 205    OG1  CG2                                            
REMARK 470     LYS C 212    CG   CD   CE   NZ                                   
REMARK 470     ILE D  35    CG1  CG2  CD1                                       
REMARK 470     LYS D  49    CG   CD   CE   NZ                                   
REMARK 470     LYS D  52    CG   CD   CE   NZ                                   
REMARK 470     ARG D  61    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 159    CG   CD   CE   NZ                                   
REMARK 470     GLU D 174    CD   OE1  OE2                                       
REMARK 470     LYS D 192    CG   CD   CE   NZ                                   
REMARK 470     LYS D 212    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OH   TYR A   145     OE1  GLU A   174              2.10            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS B 136   CB    CYS B 136   SG     -0.129                       
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    ASP A  67       18.72   -142.73                                   
REMARK 500    PRO A 100       48.73    -80.63                                   
REMARK 500    ASP A 143     -113.31     60.80                                   
REMARK 500    LYS A 159       52.53   -105.95                                   
REMARK 500    PRO B 100       43.27    -82.69                                   
REMARK 500    ASP B 143     -114.25     57.75                                   
REMARK 500    ASN C  50       44.45    -92.47                                   
REMARK 500    ASP C  51       80.52    -69.01                                   
REMARK 500    ASP C 143     -118.43     66.89                                   
REMARK 500    ASP D  67       26.42   -141.61                                   
REMARK 500    ASP D 143     -114.84     61.45                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3TF2 A    1   217  UNP    P06730   IF4E_HUMAN       1    217             
DBREF  3TF2 B    1   217  UNP    P06730   IF4E_HUMAN       1    217             
DBREF  3TF2 C    1   217  UNP    P06730   IF4E_HUMAN       1    217             
DBREF  3TF2 D    1   217  UNP    P06730   IF4E_HUMAN       1    217             
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  217  MET ALA THR VAL GLU PRO GLU THR THR PRO THR PRO ASN          
SEQRES   2 C  217  PRO PRO THR THR GLU GLU GLU LYS THR GLU SER ASN GLN          
SEQRES   3 C  217  GLU VAL ALA ASN PRO GLU HIS TYR ILE LYS HIS PRO LEU          
SEQRES   4 C  217  GLN ASN ARG TRP ALA LEU TRP PHE PHE LYS ASN ASP LYS          
SEQRES   5 C  217  SER LYS THR TRP GLN ALA ASN LEU ARG LEU ILE SER LYS          
SEQRES   6 C  217  PHE ASP THR VAL GLU ASP PHE TRP ALA LEU TYR ASN HIS          
SEQRES   7 C  217  ILE GLN LEU SER SER ASN LEU MET PRO GLY CYS ASP TYR          
SEQRES   8 C  217  SER LEU PHE LYS ASP GLY ILE GLU PRO MET TRP GLU ASP          
SEQRES   9 C  217  GLU LYS ASN LYS ARG GLY GLY ARG TRP LEU ILE THR LEU          
SEQRES  10 C  217  ASN LYS GLN GLN ARG ARG SER ASP LEU ASP ARG PHE TRP          
SEQRES  11 C  217  LEU GLU THR LEU LEU CYS LEU ILE GLY GLU SER PHE ASP          
SEQRES  12 C  217  ASP TYR SER ASP ASP VAL CYS GLY ALA VAL VAL ASN VAL          
SEQRES  13 C  217  ARG ALA LYS GLY ASP LYS ILE ALA ILE TRP THR THR GLU          
SEQRES  14 C  217  CYS GLU ASN ARG GLU ALA VAL THR HIS ILE GLY ARG VAL          
SEQRES  15 C  217  TYR LYS GLU ARG LEU GLY LEU PRO PRO LYS ILE VAL ILE          
SEQRES  16 C  217  GLY TYR GLN SER HIS ALA ASP THR ALA THR LYS SER GLY          
SEQRES  17 C  217  SER THR THR LYS ASN ARG PHE VAL VAL                          
SEQRES   1 D  217  MET ALA THR VAL GLU PRO GLU THR THR PRO THR PRO ASN          
SEQRES   2 D  217  PRO PRO THR THR GLU GLU GLU LYS THR GLU SER ASN GLN          
SEQRES   3 D  217  GLU VAL ALA ASN PRO GLU HIS TYR ILE LYS HIS PRO LEU          
SEQRES   4 D  217  GLN ASN ARG TRP ALA LEU TRP PHE PHE LYS ASN ASP LYS          
SEQRES   5 D  217  SER LYS THR TRP GLN ALA ASN LEU ARG LEU ILE SER LYS          
SEQRES   6 D  217  PHE ASP THR VAL GLU ASP PHE TRP ALA LEU TYR ASN HIS          
SEQRES   7 D  217  ILE GLN LEU SER SER ASN LEU MET PRO GLY CYS ASP TYR          
SEQRES   8 D  217  SER LEU PHE LYS ASP GLY ILE GLU PRO MET TRP GLU ASP          
SEQRES   9 D  217  GLU LYS ASN LYS ARG GLY GLY ARG TRP LEU ILE THR LEU          
SEQRES  10 D  217  ASN LYS GLN GLN ARG ARG SER ASP LEU ASP ARG PHE TRP          
SEQRES  11 D  217  LEU GLU THR LEU LEU CYS LEU ILE GLY GLU SER PHE ASP          
SEQRES  12 D  217  ASP TYR SER ASP ASP VAL CYS GLY ALA VAL VAL ASN VAL          
SEQRES  13 D  217  ARG ALA LYS GLY ASP LYS ILE ALA ILE TRP THR THR GLU          
SEQRES  14 D  217  CYS GLU ASN ARG GLU ALA VAL THR HIS ILE GLY ARG VAL          
SEQRES  15 D  217  TYR LYS GLU ARG LEU GLY LEU PRO PRO LYS ILE VAL ILE          
SEQRES  16 D  217  GLY TYR GLN SER HIS ALA ASP THR ALA THR LYS SER GLY          
SEQRES  17 D  217  SER THR THR LYS ASN ARG PHE VAL VAL                          
HET    UNX  A5846       1                                                       
HET    UNX  A5848       1                                                       
HET    UNX  A5851       1                                                       
HET    UNX  A5853       1                                                       
HET    UNX  A5855       1                                                       
HET    UNX  A5859       1                                                       
HET    UNX  B5849       1                                                       
HET    UNX  B5856       1                                                       
HET    UNX  B5858       1                                                       
HET    UNX  B5861       1                                                       
HET    UNX  C5845       1                                                       
HET    UNX  C5850       1                                                       
HET    UNX  C5860       1                                                       
HET    UNX  D5862       1                                                       
HETNAM     UNX UNKNOWN ATOM OR ION                                              
FORMUL   5  UNX    14(X)                                                        
FORMUL  19  HOH   *169(H2 O)                                                    
HELIX    1   1 THR A   55  ASN A   59  1                                   5    
HELIX    2   2 VAL A   69  HIS A   78  1                                  10    
HELIX    3   3 LEU A   81  LEU A   85  5                                   5    
HELIX    4   4 GLN A  120  ASP A  125  1                                   6    
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 THR B   55  ASN B   59  1                                   5    
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  ARG B  122  5                                   5    
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  LEU B  187  1                                  16    
HELIX   15  15 HIS B  200  THR B  205  1                                   6    
HELIX   16  16 THR C   55  ASN C   59  1                                   5    
HELIX   17  17 VAL C   69  ILE C   79  1                                  11    
HELIX   18  18 LEU C   81  LEU C   85  5                                   5    
HELIX   19  19 SER C  124  GLY C  139  1                                  16    
HELIX   20  20 PHE C  142  ASP C  147  5                                   6    
HELIX   21  21 ASN C  172  GLY C  188  1                                  17    
HELIX   22  22 HIS C  200  ALA C  204  1                                   5    
HELIX   23  23 THR D   55  ASN D   59  1                                   5    
HELIX   24  24 VAL D   69  ILE D   79  1                                  11    
HELIX   25  25 LEU D   81  LEU D   85  5                                   5    
HELIX   26  26 LEU D  126  GLY D  139  1                                  14    
HELIX   27  27 PHE D  142  ASP D  147  5                                   6    
HELIX   28  28 ASN D  172  LEU D  187  1                                  16    
SHEET    1   A 8 LEU A  60  THR A  68  0                                        
SHEET    2   A 8 PRO A  38  PHE A  48 -1  N  LEU A  39   O  ASP A  67           
SHEET    3   A 8 ASP A  90  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 LYS A 162  THR A 167 -1  O  TRP A 166   N  CYS A 150           
SHEET    6   A 8 GLY A 111  THR A 116 -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  PHE B  48 -1  N  LEU B  39   O  ASP B  67           
SHEET    3   B 8 CYS B  89  LYS B  95 -1  O  PHE B  94   N  ALA B  44           
SHEET    4   B 8 VAL B 149  VAL B 156 -1  O  VAL B 156   N  CYS B  89           
SHEET    5   B 8 LYS B 162  THR B 167 -1  O  TRP B 166   N  CYS B 150           
SHEET    6   B 8 GLY B 111  THR B 116 -1  N  ILE B 115   O  ILE B 163           
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           
SHEET    1   C 8 LEU C  60  THR C  68  0                                        
SHEET    2   C 8 PRO C  38  PHE C  48 -1  N  TRP C  43   O  PHE C  66           
SHEET    3   C 8 ASP C  90  LYS C  95 -1  O  SER C  92   N  TRP C  46           
SHEET    4   C 8 VAL C 149  ASN C 155 -1  O  ALA C 152   N  LEU C  93           
SHEET    5   C 8 LYS C 162  THR C 167 -1  O  TRP C 166   N  GLY C 151           
SHEET    6   C 8 GLY C 111  THR C 116 -1  N  ILE C 115   O  ILE C 163           
SHEET    7   C 8 GLY C 196  SER C 199 -1  O  GLY C 196   N  LEU C 114           
SHEET    8   C 8 PHE C 215  VAL C 216 -1  O  PHE C 215   N  TYR C 197           
SHEET    1   D 8 LEU D  60  THR D  68  0                                        
SHEET    2   D 8 PRO D  38  PHE D  48 -1  N  TRP D  43   O  PHE D  66           
SHEET    3   D 8 ASP D  90  LYS D  95 -1  O  SER D  92   N  TRP D  46           
SHEET    4   D 8 VAL D 149  ASN D 155 -1  O  VAL D 154   N  TYR D  91           
SHEET    5   D 8 LYS D 162  THR D 167 -1  O  TRP D 166   N  CYS D 150           
SHEET    6   D 8 GLY D 111  THR D 116 -1  N  ILE D 115   O  ILE D 163           
SHEET    7   D 8 GLY D 196  SER D 199 -1  O  GLY D 196   N  LEU D 114           
SHEET    8   D 8 PHE D 215  VAL D 216 -1  O  PHE D 215   N  TYR D 197           
CRYST1   39.236   56.739  100.310 103.61  91.36 110.14 P 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      0.025487  0.009345  0.003134        0.00000                         
SCALE2      0.000000  0.018772  0.005041        0.00000                         
SCALE3      0.000000  0.000000  0.010325        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system