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Database: PDB
Entry: 3AM7
LinkDB: 3AM7
Original site: 3AM7 
HEADER    TRANSLATION/PROTEIN BINDING             17-AUG-10   3AM7              
TITLE     CRYSTAL STRUCTURE OF THE TERNARY COMPLEX OF EIF4E-M7GTP-4EBP2 PEPTIDE 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 4E;               
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 27-217;                                       
COMPND   5 SYNONYM: EIF-4E, EIF4E, MRNA CAP-BINDING PROTEIN, EIF-4F 25 KDA      
COMPND   6 SUBUNIT;                                                             
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 4E-BINDING PROTEIN
COMPND  10 2;                                                                   
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: UNP RESIDUES 47-65;                                        
COMPND  13 SYNONYM: EIF4E-BINDING PROTEIN 2, 4E-BP2;                            
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: EIF4E, EIF4EL1, EIF4F;                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: EIF4EBP2;                                                      
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CAP, TRANSLATION, PROTEIN-PROTEIN COMPLEX, TRANSLATION-PROTEIN        
KEYWDS   2 BINDING COMPLEX                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.TOMOO,A.FUKUYO,Y.IN,T.ISHIDA                                        
REVDAT   1   17-AUG-11 3AM7    0                                                
JRNL        AUTH   K.TOMOO,A.FUKUYO,Y.IN,T.ISHIDA                               
JRNL        TITL   CRYSTAL STRUCTURE OF THE TERNARY COMPLEX OF                  
JRNL        TITL 2 EIF4E-M7GTP-4EBP2 PEPTIDE                                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.30                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 14502                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.268                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 734                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1725                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 93                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.28                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.19                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.685                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.80                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.31                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3AM7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-SEP-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB029422.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E+ SUPERBRIGHT           
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS VII                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR                       
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16434                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.4                               
REMARK 200  DATA REDUNDANCY                : 3.810                              
REMARK 200  R MERGE                    (I) : 0.10100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.0000                             
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) : 43.90                    
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.81                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.10100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 8.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG-MME 2000, 0.1M MES, 0.2M         
REMARK 280  AMMONIUM SULFATE, PH 5.6, VAPOR DIFFUSION, HANGING DROP,            
REMARK 280  TEMPERATURE 291.0K                                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+3/4                                              
REMARK 290       4555   Y,-X,Z+1/4                                              
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       18.87500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       28.31250            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        9.43750            
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: 1510 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 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 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     LEU A    60                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A  34       -0.72   -140.27                                   
REMARK 500    LYS A  52      -37.97     63.45                                   
REMARK 500    LYS A  54      161.99    -49.98                                   
REMARK 500    ILE A  63      -68.08    -94.28                                   
REMARK 500    ASP A  67       27.68   -146.92                                   
REMARK 500    ASP A 143     -138.00     54.99                                   
REMARK 500    LYS A 206      -57.03   -168.56                                   
REMARK 500    SER A 207       10.58    172.39                                   
REMARK 500    SER A 209       49.37     17.83                                   
REMARK 500    THR A 210       93.34     37.14                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGP A 1000                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1WKW   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH 4EBP SUBTYPE                         
DBREF  3AM7 A   27   217  UNP    P06730   IF4E_HUMAN      27    217             
DBREF  3AM7 B   47    65  UNP    Q13542   4EBP2_HUMAN     47     65             
SEQRES   1 A  191  GLU VAL ALA ASN PRO GLU HIS TYR ILE LYS HIS PRO LEU          
SEQRES   2 A  191  GLN ASN ARG TRP ALA LEU TRP PHE PHE LYS ASN ASP LYS          
SEQRES   3 A  191  SER LYS THR TRP GLN ALA ASN LEU ARG LEU ILE SER LYS          
SEQRES   4 A  191  PHE ASP THR VAL GLU ASP PHE TRP ALA LEU TYR ASN HIS          
SEQRES   5 A  191  ILE GLN LEU SER SER ASN LEU MET PRO GLY CYS ASP TYR          
SEQRES   6 A  191  SER LEU PHE LYS ASP GLY ILE GLU PRO MET TRP GLU ASP          
SEQRES   7 A  191  GLU LYS ASN LYS ARG GLY GLY ARG TRP LEU ILE THR LEU          
SEQRES   8 A  191  ASN LYS GLN GLN ARG ARG SER ASP LEU ASP ARG PHE TRP          
SEQRES   9 A  191  LEU GLU THR LEU LEU CYS LEU ILE GLY GLU SER PHE ASP          
SEQRES  10 A  191  ASP TYR SER ASP ASP VAL CYS GLY ALA VAL VAL ASN VAL          
SEQRES  11 A  191  ARG ALA LYS GLY ASP LYS ILE ALA ILE TRP THR THR GLU          
SEQRES  12 A  191  CYS GLU ASN ARG GLU ALA VAL THR HIS ILE GLY ARG VAL          
SEQRES  13 A  191  TYR LYS GLU ARG LEU GLY LEU PRO PRO LYS ILE VAL ILE          
SEQRES  14 A  191  GLY TYR GLN SER HIS ALA ASP THR ALA THR LYS SER GLY          
SEQRES  15 A  191  SER THR THR LYS ASN ARG PHE VAL VAL                          
SEQRES   1 B   19  PRO GLY GLY THR ARG ILE ILE TYR ASP ARG LYS PHE LEU          
SEQRES   2 B   19  LEU ASP ARG ARG ASN SER                                      
HET    MGP  A1000      33                                                       
HETNAM     MGP 7-METHYL-GUANOSINE-5'-TRIPHOSPHATE                               
FORMUL   3  MGP    C11 H19 N5 O14 P3 1+                                         
FORMUL   4  HOH   *93(H2 O)                                                     
HELIX    1   1 ASN A   30  TYR A   34  5                                   5    
HELIX    2   2 VAL A   69  ILE A   79  1                                  11    
HELIX    3   3 LEU A   81  LEU A   85  5                                   5    
HELIX    4   4 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 ALA A  201  THR A  203  5                                   3    
HELIX    9   9 ASP B   55  ASP B   61  1                                   7    
SHEET    1   A 8 LEU A  62  THR A  68  0                                        
SHEET    2   A 8 PRO A  38  LYS A  49 -1  N  LEU A  45   O  ILE A  63           
SHEET    3   A 8 CYS A  89  LYS A  95 -1  O  SER A  92   N  TRP A  46           
SHEET    4   A 8 VAL A 149  ASN A 155 -1  O  VAL A 154   N  TYR A  91           
SHEET    5   A 8 LYS A 162  THR A 167 -1  O  LYS A 162   N  ASN A 155           
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  GLN A 198   N  ARG A 112           
SHEET    8   A 8 PHE A 215  VAL A 216 -1  O  PHE A 215   N  TYR A 197           
SITE     1 AC1 16 HOH A  18  HOH A  21  TRP A  56  MET A 101                    
SITE     2 AC1 16 TRP A 102  GLU A 103  ARG A 157  LYS A 159                    
SITE     3 AC1 16 LYS A 162  PRO A 191  LYS A 192  VAL A 194                    
SITE     4 AC1 16 VAL A 217  HOH A 234  HOH A 241  HOH A 271                    
CRYST1   87.840   87.840   37.750  90.00  90.00  90.00 P 43          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      0.011384  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011384  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.026490        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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