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Database: PDB
Entry: 1F2Q
LinkDB: 1F2Q
Original site: 1F2Q 
HEADER    IMMUNE SYSTEM                           28-MAY-00   1F2Q              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN HIGH-AFFINITY IGE RECEPTOR             
CAVEAT     1F2Q    MAN B 3 HAS WRONG CHIRALITY AT ATOM C1 MAN C 3 HAS WRONG     
CAVEAT   2 1F2Q    CHIRALITY AT ATOM C1                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HIGH AFFINITY IMMUNOGLOBULIN EPSILON RECEPTOR ALPHA-       
COMPND   3 SUBUNIT;                                                             
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: EXTRACELLULAR DOMAIN;                                      
COMPND   6 SYNONYM: FC-EPSILON RI-ALPHA;                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HI-5;                                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PVL1392                                   
KEYWDS    IMMUNOGLOBULIN FOLD, GLYCOPROTEIN, RECEPTOR, IGE-BINDING PROTEIN,     
KEYWDS   2 IMMUNE SYSTEM                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.C.GARMAN,J.P.KINET,T.S.JARDETZKY                                    
REVDAT   4   29-JUL-20 1F2Q    1       CAVEAT COMPND REMARK HETNAM              
REVDAT   4 2                   1       LINK   SITE   ATOM                       
REVDAT   3   13-JUL-11 1F2Q    1       VERSN                                    
REVDAT   2   24-FEB-09 1F2Q    1       VERSN                                    
REVDAT   1   08-JUN-00 1F2Q    0                                                
JRNL        AUTH   S.C.GARMAN,J.P.KINET,T.S.JARDETZKY                           
JRNL        TITL   CRYSTAL STRUCTURE OF THE HUMAN HIGH-AFFINITY IGE RECEPTOR.   
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V.  95   951 1998              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   9875849                                                      
JRNL        DOI    10.1016/S0092-8674(00)81719-5                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.4                                              
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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 17.43                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 913683.660                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 10247                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.226                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 880                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.009                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.55                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1486                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3770                       
REMARK   3   BIN FREE R VALUE                    : 0.4530                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.60                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 158                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.036                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1371                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 92                                      
REMARK   3   SOLVENT ATOMS            : 73                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 46.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 67.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 30.48000                                             
REMARK   3    B22 (A**2) : -16.37000                                            
REMARK   3    B33 (A**2) : -14.11000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 18.52000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.34                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.48                            
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) : 0.41                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.59                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.500                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 27.00                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.810                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 4.350 ; 4.000                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 6.730 ; 6.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 6.600 ; 6.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 9.090 ; 8.000                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.34                                                 
REMARK   3   BSOL        : 53.15                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : CARBOHYDRATE.TOP                               
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: MAXIMUM LIKELIHOOD REFINEMENT AGAINST     
REMARK   3  HENDRICKSON-LATTMAN COEFFICIENT TARGETS                             
REMARK   4                                                                      
REMARK   4 1F2Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAY-00.                  
REMARK 100 THE DEPOSITION ID IS D_1000011171.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-JUN-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.08                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10247                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.05700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.22600                            
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: NULL                         
REMARK 200 SOFTWARE USED: DM                                                    
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, TRIS, SODIUM ACETATE, PH       
REMARK 280  8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 297K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       44.29500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.82000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       44.29500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.82000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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     VAL A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     PHE A    32                                                      
REMARK 465     GLU A    33                                                      
REMARK 465     VAL A    34                                                      
REMARK 465     SER A    35                                                      
REMARK 465     GLU A   175                                                      
REMARK 465     LYS A   176                                                      
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    ASN A  27      164.87    -24.74                                   
REMARK 500    ASN A  57       70.57     46.13                                   
REMARK 500    GLN A  71       21.95    -64.04                                   
REMARK 500    VAL A  73        7.77     44.79                                   
REMARK 500    TYR A 129      154.27    -42.72                                   
REMARK 500    HIS A 134        4.56     42.88                                   
REMARK 500    TRP A 156     -114.83     61.06                                   
REMARK 500    PRO A 173      156.09    -43.16                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1F2Q A    1   176  UNP    P12319   FCEA_HUMAN      26    201             
SEQRES   1 A  176  VAL PRO GLN LYS PRO LYS VAL SER LEU ASN PRO PRO TRP          
SEQRES   2 A  176  ASN ARG ILE PHE LYS GLY GLU ASN VAL THR LEU THR CYS          
SEQRES   3 A  176  ASN GLY ASN ASN PHE PHE GLU VAL SER SER THR LYS TRP          
SEQRES   4 A  176  PHE HIS ASN GLY SER LEU SER GLU GLU THR ASN SER SER          
SEQRES   5 A  176  LEU ASN ILE VAL ASN ALA LYS PHE GLU ASP SER GLY GLU          
SEQRES   6 A  176  TYR LYS CYS GLN HIS GLN GLN VAL ASN GLU SER GLU PRO          
SEQRES   7 A  176  VAL TYR LEU GLU VAL PHE SER ASP TRP LEU LEU LEU GLN          
SEQRES   8 A  176  ALA SER ALA GLU VAL VAL MET GLU GLY GLN PRO LEU PHE          
SEQRES   9 A  176  LEU ARG CYS HIS GLY TRP ARG ASN TRP ASP VAL TYR LYS          
SEQRES  10 A  176  VAL ILE TYR TYR LYS ASP GLY GLU ALA LEU LYS TYR TRP          
SEQRES  11 A  176  TYR GLU ASN HIS ASN ILE SER ILE THR ASN ALA THR VAL          
SEQRES  12 A  176  GLU ASP SER GLY THR TYR TYR CYS THR GLY LYS VAL TRP          
SEQRES  13 A  176  GLN LEU ASP TYR GLU SER GLU PRO LEU ASN ILE THR VAL          
SEQRES  14 A  176  ILE LYS ALA PRO ARG GLU LYS                                  
MODRES 1F2Q ASN A   42  ASN  GLYCOSYLATION SITE                                 
MODRES 1F2Q ASN A   21  ASN  GLYCOSYLATION SITE                                 
MODRES 1F2Q ASN A  166  ASN  GLYCOSYLATION SITE                                 
HET    NAG  B   1      14                                                       
HET    NAG  B   2      14                                                       
HET    MAN  B   3      11                                                       
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET    MAN  C   3      11                                                       
HET    NAG  A 221      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
FORMUL   2  NAG    5(C8 H15 N O6)                                               
FORMUL   2  MAN    2(C6 H12 O6)                                                 
FORMUL   5  HOH   *73(H2 O)                                                     
HELIX    1   1 LYS A   59  SER A   63  5                                   5    
HELIX    2   2 ARG A  111  TRP A  113  5                                   3    
HELIX    3   3 THR A  142  SER A  146  5                                   5    
SHEET    1   A 3 SER A   8  ASN A  10  0                                        
SHEET    2   A 3 VAL A  22  THR A  25 -1  N  THR A  23   O  ASN A  10           
SHEET    3   A 3 SER A  52  ILE A  55 -1  N  LEU A  53   O  LEU A  24           
SHEET    1   B 5 ARG A  15  PHE A  17  0                                        
SHEET    2   B 5 VAL A  79  PHE A  84  1  O  GLU A  82   N  ILE A  16           
SHEET    3   B 5 GLY A  64  GLN A  69 -1  N  GLY A  64   O  LEU A  81           
SHEET    4   B 5 LYS A  38  HIS A  41 -1  N  LYS A  38   O  GLN A  69           
SHEET    5   B 5 SER A  44  LEU A  45 -1  O  SER A  44   N  HIS A  41           
SHEET    1   C 3 LEU A  88  ALA A  92  0                                        
SHEET    2   C 3 LEU A 103  GLY A 109 -1  O  ARG A 106   N  GLN A  91           
SHEET    3   C 3 ASN A 135  ILE A 138 -1  O  ILE A 136   N  LEU A 105           
SHEET    1   D 4 GLU A 125  ALA A 126  0                                        
SHEET    2   D 4 VAL A 115  LYS A 122 -1  N  LYS A 122   O  GLU A 125           
SHEET    3   D 4 GLY A 147  VAL A 155 -1  O  TYR A 150   N  TYR A 121           
SHEET    4   D 4 LEU A 158  GLU A 161 -1  N  LEU A 158   O  VAL A 155           
SHEET    1   E 5 GLU A 125  ALA A 126  0                                        
SHEET    2   E 5 VAL A 115  LYS A 122 -1  N  LYS A 122   O  GLU A 125           
SHEET    3   E 5 GLY A 147  VAL A 155 -1  O  TYR A 150   N  TYR A 121           
SHEET    4   E 5 LEU A 165  ILE A 170 -1  N  LEU A 165   O  TYR A 149           
SHEET    5   E 5 VAL A  96  MET A  98  1  O  VAL A  97   N  ILE A 170           
SSBOND   1 CYS A   26    CYS A   68                          1555   1555  2.04  
SSBOND   2 CYS A  107    CYS A  151                          1555   1555  2.05  
LINK         ND2 ASN A  21                 C1  NAG A 221     1555   1555  1.45  
LINK         ND2 ASN A  42                 C1  NAG B   1     1555   1555  1.45  
LINK         ND2 ASN A 166                 C1  NAG C   1     1555   1555  1.47  
LINK         O4  NAG B   1                 C1  NAG B   2     1555   1555  1.39  
LINK         O4  NAG B   2                 C1  MAN B   3     1555   1555  1.39  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.40  
LINK         O4  NAG C   2                 C1  MAN C   3     1555   1555  1.40  
CISPEP   1 ASN A   10    PRO A   11          0        -0.28                     
CRYST1   88.590   69.640   49.360  90.00 116.69  90.00 C 1 2 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      0.011288  0.000000  0.005675        0.00000                         
SCALE2      0.000000  0.014360  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022675        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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