GenomeNet

Database: PDB
Entry: 5EIR
LinkDB: 5EIR
Original site: 5EIR 
HEADER    TRANSLATION                             30-OCT-15   5EIR              
TITLE     CO-CRYSTAL STRUCTURE OF EIF4E WITH NUCLEOTIDE MIMETIC INHIBITOR.      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 4E;               
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: EIF4E,EIF-4F 25 KDA SUBUNIT,MRNA CAP-BINDING PROTEIN;       
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA 1;        
COMPND   8 CHAIN: B;                                                            
COMPND   9 FRAGMENT: EIF4E BINDING SEQUENCE;                                    
COMPND  10 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 BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: ROSETTA PLYSS;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET11D;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  14 ORGANISM_TAXID: 32630;                                               
SOURCE  15 OTHER_DETAILS: COMMERCIAL SYNTHESIS                                  
KEYWDS    COMPLEX, INHIBITOR, TRANSLATION, EIF4E                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.W.NOWICKI,M.D.WALKINSHAW,P.M.FISCHER                                
REVDAT   2   14-SEP-16 5EIR    1       JRNL                                     
REVDAT   1   07-SEP-16 5EIR    0                                                
JRNL        AUTH   F.SOUKARIEH,M.W.NOWICKI,A.BASTIDE,T.POYRY,C.JONES,K.DUDEK,   
JRNL        AUTH 2 G.PATWARDHAN,F.MEULLENET,N.J.OLDHAM,M.D.WALKINSHAW,          
JRNL        AUTH 3 A.E.WILLIS,P.M.FISCHER                                       
JRNL        TITL   DESIGN OF NUCLEOTIDE-MIMETIC AND NON-NUCLEOTIDE INHIBITORS   
JRNL        TITL 2 OF THE TRANSLATION INITIATION FACTOR EIF4E: SYNTHESIS,       
JRNL        TITL 3 STRUCTURAL AND FUNCTIONAL CHARACTERISATION.                  
JRNL        REF    EUR.J.MED.CHEM.               V. 124   200 2016              
JRNL        REFN                   ISSN 0223-5234                               
JRNL        PMID   27592390                                                     
JRNL        DOI    10.1016/J.EJMECH.2016.08.047                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.69 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
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 : MLHL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.69                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.03                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.290                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 6738                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.249                           
REMARK   3   R VALUE            (WORKING SET) : 0.248                           
REMARK   3   FREE R VALUE                     : 0.272                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 310                             
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 48.0365 -  3.3891    0.92     3269   176  0.2300 0.2443        
REMARK   3     2  3.3891 -  2.6901    0.92     3159   134  0.2769 0.3327        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : 0.210            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.730           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.08                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.14                          
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      :  0.009           1809                                  
REMARK   3   ANGLE     :  1.245           2463                                  
REMARK   3   CHIRALITY :  0.060            253                                  
REMARK   3   PLANARITY :  0.007            304                                  
REMARK   3   DIHEDRAL  : 19.619            658                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 5EIR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-OCT-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000214958.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAY-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9173                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : PILATUS 6M                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 300K               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.16                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6814                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.690                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 123.670                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.8                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.16000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.69                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.84                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.35900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 2V8Y CHAIN A                                         
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 21-31% PEG 8000, 1???3% (NH4)2SO4, 100   
REMARK 280  MM HEPES, PH 7.5, 1 ROUND OF SEEDING. CRYSTALS REPLACED IN TO       
REMARK 280  ABOVE CONDITIONS WITHOUT (NH4)2SO4 PRIOR TO FREEZING., VAPOR        
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,-Y,-Z+1/2                                         
REMARK 290       4555   -X+1/2,-Y,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  1.000000  0.000000  0.000000       19.12500            
REMARK 290   SMTRY2   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       61.83500            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       19.12500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       61.83500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1550 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10950 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 404  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     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     LYS A   206                                                      
REMARK 465     SER A   207                                                      
REMARK 465     GLY A   208                                                      
REMARK 465     SER A   209                                                      
REMARK 465     THR A   210                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   402     O    HOH A   431              1.99            
REMARK 500   CB   ALA A   204     FAI  5O8 A   301              2.05            
REMARK 500   CB   ALA A   204     FAG  5O8 A   301              2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
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   ATM2   ATM3                                     
REMARK 500    MET A 101   O   -  C   -  N   ANGL. DEV. =  -9.8 DEGREES          
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 143     -135.68     57.46                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues 5O8 A 301 and SO4 A      
REMARK 800  302                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues 5O8 A 301 and SO4 A      
REMARK 800  302                                                                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2V8W   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2W97   RELATED DB: PDB                                   
DBREF  5EIR A    1   217  UNP    P06730   IF4E_HUMAN       1    217             
DBREF  5EIR B  621   634  PDB    5EIR     5EIR           621    634             
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   14  LYS LYS ARG TYR ASP ARG GLU PHE LEU LEU GLY PHE GLN          
SEQRES   2 B   14  PHE                                                          
HET    5O8  A 301      68                                                       
HET    SO4  A 302       5                                                       
HETNAM     5O8 ~{N}-[[(2~{R},3~{S},4~{R},5~{R})-5-[2-AZANYL-6-                  
HETNAM   2 5O8  OXIDANYLIDENE-7-(PHENYLMETHYL)-1~{H}-PURIN-7-IUM-9-             
HETNAM   3 5O8  YL]-3,4-BIS(OXIDANYL)OXOLAN-2-YL]METHYL]-1,1,1-                 
HETNAM   4 5O8  TRIS(FLUORANYL)METHANESULFONAMIDE                               
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  5O8    C18 H20 F3 N6 O6 S 1+                                        
FORMUL   4  SO4    O4 S 2-                                                      
FORMUL   5  HOH   *32(H2 O)                                                     
HELIX    1 AA1 ASN A   30  TYR A   34  5                                   5    
HELIX    2 AA2 THR A   55  ASN A   59  1                                   5    
HELIX    3 AA3 VAL A   69  ASN A   77  1                                   9    
HELIX    4 AA4 ASP A  104  ARG A  109  1                                   6    
HELIX    5 AA5 GLN A  120  ASP A  125  1                                   6    
HELIX    6 AA6 ASP A  125  GLY A  139  1                                  15    
HELIX    7 AA7 PHE A  142  ASP A  147  5                                   6    
HELIX    8 AA8 ASN A  172  GLY A  188  1                                  17    
HELIX    9 AA9 HIS A  200  ALA A  204  1                                   5    
HELIX   10 AB1 ASP B  625  LEU B  630  1                                   6    
HELIX   11 AB2 GLY B  631  GLN B  633  5                                   3    
SHEET    1 AA1 8 LEU A  60  THR A  68  0                                        
SHEET    2 AA1 8 PRO A  38  PHE A  48 -1  N  TRP A  43   O  PHE A  66           
SHEET    3 AA1 8 CYS A  89  LYS A  95 -1  O  PHE A  94   N  ALA A  44           
SHEET    4 AA1 8 VAL A 149  VAL A 156 -1  O  ALA A 152   N  LEU A  93           
SHEET    5 AA1 8 LYS A 162  THR A 167 -1  O  LYS A 162   N  ASN A 155           
SHEET    6 AA1 8 GLY A 111  THR A 116 -1  N  GLY A 111   O  THR A 167           
SHEET    7 AA1 8 ILE A 195  SER A 199 -1  O  GLN A 198   N  ARG A 112           
SHEET    8 AA1 8 PHE A 215  VAL A 217 -1  O  PHE A 215   N  TYR A 197           
SSBOND   1 5O8 A  301    SO4 A  302                          1555   1555  2.01  
LINK         CBGA5O8 A 301                 O3  SO4 A 302     1555   1555  1.21  
LINK         CBGA5O8 A 301                 O4  SO4 A 302     1555   1555  1.45  
SITE     1 AC1 12 TRP A  56  MET A 101  TRP A 102  GLU A 103                    
SITE     2 AC1 12 ARG A 112  ARG A 157  TRP A 166  HIS A 200                    
SITE     3 AC1 12 THR A 203  ALA A 204  HOH A 413  HOH A 416                    
SITE     1 AC2 12 TRP A  56  MET A 101  TRP A 102  GLU A 103                    
SITE     2 AC2 12 ARG A 112  ARG A 157  TRP A 166  HIS A 200                    
SITE     3 AC2 12 THR A 203  ALA A 204  HOH A 413  HOH A 416                    
CRYST1   38.250   52.120  123.670  90.00  90.00  90.00 P 21 2 21     4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.026144  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.019186  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008086        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system