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Database: PDB
Entry: 1F6A
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HEADER    IMMUNE SYSTEM                           20-JUN-00   1F6A              
TITLE     STRUCTURE OF THE HUMAN IGE-FC BOUND TO ITS HIGH AFFINITY RECEPTOR     
TITLE    2 FC(EPSILON)RI(ALPHA)                                                 
CAVEAT     1F6A    MAN C 3 HAS WRONG CHIRALITY AT ATOM C1 MAN E 3 HAS WRONG     
CAVEAT   2 1F6A    CHIRALITY AT ATOM C1 MAN G 3 HAS WRONG CHIRALITY AT ATOM C1  
CAVEAT   3 1F6A    MAN H 3 HAS WRONG 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: HIGH AFFINITY IGE-FC RECEPTOR, FC(EPSILON)RI(ALPHA);        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: IG EPSILON CHAIN C REGION;                                 
COMPND  11 CHAIN: B, D;                                                         
COMPND  12 FRAGMENT: C(EPSILON)3-C(EPSILON)4 DOMAINS;                           
COMPND  13 SYNONYM: IGE-FC;                                                     
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 EXPRESSION_SYSTEM: HI-5 INSECT CELLS;                                
SOURCE   6 EXPRESSION_SYSTEM_COMMON: HI-5 INSECT CELLS;                         
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PVL1392;                                  
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: HI-5 INSECT CELLS;                                
SOURCE  14 EXPRESSION_SYSTEM_COMMON: HI-5 INSECT CELLS;                         
SOURCE  15 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PVL1392                                   
KEYWDS    IMMUNOGLOBULIN FOLD, GLYCOPROTEIN, RECEPTOR, IGE-BINDING PROTEIN, IGE 
KEYWDS   2 ANTIBODY, IGE-FC, IMMUNE SYSTEM                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.C.GARMAN,B.A.WURZBURG,S.S.TARCHEVSKAYA,J.P.KINET,T.S.JARDETZKY      
REVDAT   6   29-JUL-20 1F6A    1       CAVEAT COMPND REMARK SEQADV              
REVDAT   6 2                   1       HETNAM LINK   SITE   ATOM                
REVDAT   5   13-JUL-11 1F6A    1       VERSN                                    
REVDAT   4   24-FEB-09 1F6A    1       VERSN                                    
REVDAT   3   10-JAN-06 1F6A    1       REMARK SOURCE MASTER                     
REVDAT   2   01-APR-03 1F6A    1       JRNL                                     
REVDAT   1   20-JUL-00 1F6A    0                                                
JRNL        AUTH   S.C.GARMAN,B.A.WURZBURG,S.S.TARCHEVSKAYA,J.P.KINET,          
JRNL        AUTH 2 T.S.JARDETZKY                                                
JRNL        TITL   STRUCTURE OF THE FC FRAGMENT OF HUMAN IGE BOUND TO ITS       
JRNL        TITL 2 HIGH-AFFINITY RECEPTOR FC (EPSILON) RI (ALPHA).              
JRNL        REF    NATURE                        V. 406   259 2000              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   10917520                                                     
JRNL        DOI    10.1038/35018500                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.9                                              
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) : 3.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.87                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 5879235.760                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 27411                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : SHELLS                          
REMARK   3   R VALUE            (WORKING SET) : 0.254                           
REMARK   3   FREE R VALUE                     : 0.273                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1418                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
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) : 3.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.72                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4236                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3060                       
REMARK   3   BIN FREE R VALUE                    : 0.3490                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 265                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.021                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4821                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 430                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 100.5                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 89.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 12.20000                                             
REMARK   3    B22 (A**2) : 12.20000                                             
REMARK   3    B33 (A**2) : -24.40000                                            
REMARK   3    B12 (A**2) : 17.22000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.42                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.61                            
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) : 0.49                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.80                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.600                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.230                           
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) : 10.460; 4.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 15.790; 6.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 16.860; 6.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 23.320; 7.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.26                                                 
REMARK   3   BSOL        : 72.83                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : RESTRAINTS                                              
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : 0.04  ; 300                  
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; 2                    
REMARK   3   GROUP  2  POSITIONAL            (A) : 0.08  ; 300                  
REMARK   3   GROUP  2  B-FACTOR           (A**2) : NULL  ; 2                    
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  3  : ION.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   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1F6A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUN-00.                  
REMARK 100 THE DEPOSITION ID IS D_1000011295.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-NOV-99; 17-SEP-99               
REMARK 200  TEMPERATURE           (KELVIN) : 113; 113                           
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : APS; ALS                           
REMARK 200  BEAMLINE                       : 5ID-B; 5.0.2                       
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; NULL                            
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.034; 1.200                       
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH; ADSC QUANTUM 4        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27411                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.09100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.63                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL                        
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 80.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 7.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, TRIS, CHAPS, PH 8.5,   
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 296K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-Z                                              
REMARK 290       7555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       8555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       9555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290      10555   Y+2/3,X+1/3,-Z+1/3                                      
REMARK 290      11555   X-Y+2/3,-Y+1/3,-Z+1/3                                   
REMARK 290      12555   -X+2/3,-X+Y+1/3,-Z+1/3                                  
REMARK 290      13555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290      14555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290      15555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290      16555   Y+1/3,X+2/3,-Z+2/3                                      
REMARK 290      17555   X-Y+1/3,-Y+2/3,-Z+2/3                                   
REMARK 290      18555   -X+1/3,-X+Y+2/3,-Z+2/3                                  
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000       96.40000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       55.65657            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000      100.80000            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000       96.40000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       55.65657            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000      100.80000            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000       96.40000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       55.65657            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      100.80000            
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000       96.40000            
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       55.65657            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      100.80000            
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000       96.40000            
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       55.65657            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      100.80000            
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000       96.40000            
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       55.65657            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      100.80000            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000      111.31313            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000      201.60000            
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000      111.31313            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000      201.60000            
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000      111.31313            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000      201.60000            
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000      111.31313            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      201.60000            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000      111.31313            
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000      201.60000            
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000      111.31313            
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000      201.60000            
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS THE RECEPTOR CHAIN A BOUND TO     
REMARK 300 THE DIMERIC ANTIBODY CHAINS B AND D                                  
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, C, E, F, G, H                
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ARG A   174                                                      
REMARK 465     GLU A   175                                                      
REMARK 465     LYS A   176                                                      
REMARK 465     ALA B   326                                                      
REMARK 465     ASP B   327                                                      
REMARK 465     PRO B   545                                                      
REMARK 465     GLY B   546                                                      
REMARK 465     LYS B   547                                                      
REMARK 465     ALA D   326                                                      
REMARK 465     ASP D   327                                                      
REMARK 465     PRO D   328                                                      
REMARK 465     PRO D   545                                                      
REMARK 465     GLY D   546                                                      
REMARK 465     LYS D   547                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE1  GLN D   518     OE1  GLN D   518    11566     1.79            
REMARK 500   NH2  ARG B   351     NH2  ARG B   351     4556     2.12            
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    GLU B 529   CD    GLU B 529   OE1    -0.088                       
REMARK 500    GLU B 529   CD    GLU B 529   OE2    -0.085                       
REMARK 500    GLU D 529   CD    GLU D 529   OE1    -0.097                       
REMARK 500    GLU D 529   CD    GLU D 529   OE2    -0.082                       
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    PRO A  12   C   -  N   -  CA  ANGL. DEV. =  12.7 DEGREES          
REMARK 500    PRO A  12   C   -  N   -  CD  ANGL. DEV. = -14.4 DEGREES          
REMARK 500    GLU B 529   OE1 -  CD  -  OE2 ANGL. DEV. = -20.4 DEGREES          
REMARK 500    GLU D 529   OE1 -  CD  -  OE2 ANGL. DEV. = -20.1 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    PRO A  12      -49.04    -28.95                                   
REMARK 500    ASN A  27      151.56      4.53                                   
REMARK 500    ASN A  30       61.69   -160.12                                   
REMARK 500    GLU A  33       87.07     69.64                                   
REMARK 500    ASN A  42       -2.19     56.10                                   
REMARK 500    ASN A  57       54.04     37.29                                   
REMARK 500    HIS A  70     -113.18    -94.06                                   
REMARK 500    SER A  76      150.11    -45.88                                   
REMARK 500    SER A  85       82.98   -152.38                                   
REMARK 500    GLU A  99      134.84    -38.89                                   
REMARK 500    TRP A 110      144.96    -35.91                                   
REMARK 500    ARG A 111       24.36     42.29                                   
REMARK 500    ALA A 141      164.87    -49.91                                   
REMARK 500    GLN A 157       -8.58     70.59                                   
REMARK 500    ASP B 330       40.87    -84.57                                   
REMARK 500    PRO B 333      136.61    -33.77                                   
REMARK 500    ARG B 334       16.03     38.51                                   
REMARK 500    ILE B 350      -86.35    -74.43                                   
REMARK 500    ARG B 351      -18.16    -45.81                                   
REMARK 500    LYS B 352       25.42     44.92                                   
REMARK 500    PRO B 381      165.62    -45.98                                   
REMARK 500    ASN B 394       30.13    -76.58                                   
REMARK 500    THR B 396     -163.25    -70.90                                   
REMARK 500    GLU B 412       30.31    -83.09                                   
REMARK 500    PRO B 426      -77.15    -74.00                                   
REMARK 500    MET B 470      143.23   -176.02                                   
REMARK 500    PRO B 471     -176.93    -52.15                                   
REMARK 500    HIS B 480       96.85   -164.24                                   
REMARK 500    LEU B 485      156.90    -45.11                                   
REMARK 500    LYS B 499       19.68    -69.18                                   
REMARK 500    SER B 501        7.16     58.40                                   
REMARK 500    GLU B 521      108.98    -59.02                                   
REMARK 500    ALA B 530      -92.29    -88.75                                   
REMARK 500    ALA B 531      132.92     -2.90                                   
REMARK 500    SER B 542      155.00    167.23                                   
REMARK 500    ASP D 330      -90.39   -131.47                                   
REMARK 500    ILE D 350      -85.86    -74.15                                   
REMARK 500    ARG D 351      -17.92    -46.53                                   
REMARK 500    LYS D 352       24.33     45.05                                   
REMARK 500    PRO D 365      102.37    -32.47                                   
REMARK 500    THR D 369     -171.64    -61.20                                   
REMARK 500    VAL D 370       36.81   -148.61                                   
REMARK 500    ASN D 371      123.11    -12.69                                   
REMARK 500    PRO D 381      165.29    -46.58                                   
REMARK 500    ASN D 394       31.18    -74.74                                   
REMARK 500    THR D 396     -164.20    -71.46                                   
REMARK 500    GLU D 412       30.71    -82.31                                   
REMARK 500    HIS D 424       28.90    -78.66                                   
REMARK 500    PRO D 426      -88.96    -61.59                                   
REMARK 500    MET D 470      141.89   -175.06                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      61 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     CPS A  370                                                       
REMARK 610     CPS D  103                                                       
REMARK 610     CPS D  104                                                       
REMARK 610     CPS D  105                                                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1F2Q   RELATED DB: PDB                                   
REMARK 900 1F2Q CONTAINS THE HUMAN HIGH-AFFINITY IGE RECEPTOR FC(EPSILON)       
REMARK 900 RI(ALPHA)                                                            
DBREF  1F6A A    1   176  UNP    P12319   FCEA_HUMAN      26    201             
DBREF  1F6A B  330   547  UNP    P01854   EPC_HUMAN      211    428             
DBREF  1F6A D  330   547  UNP    P01854   EPC_HUMAN      211    428             
SEQADV 1F6A ALA A   74  UNP  P12319    ASN    99 ENGINEERED                     
SEQADV 1F6A ALA A  135  UNP  P12319    ASN   160 ENGINEERED                     
SEQADV 1F6A ALA A  142  UNP  P12319    THR   167 ENGINEERED                     
SEQADV 1F6A ALA A  143  UNP  P12319    VAL   168 CLONING ARTIFACT               
SEQADV 1F6A ALA B  326  UNP  P01854              CLONING ARTIFACT               
SEQADV 1F6A ASP B  327  UNP  P01854              CLONING ARTIFACT               
SEQADV 1F6A PRO B  328  UNP  P01854              CLONING ARTIFACT               
SEQADV 1F6A CYS B  329  UNP  P01854              CLONING ARTIFACT               
SEQADV 1F6A ALA D  326  UNP  P01854              CLONING ARTIFACT               
SEQADV 1F6A ASP D  327  UNP  P01854              CLONING ARTIFACT               
SEQADV 1F6A PRO D  328  UNP  P01854              CLONING ARTIFACT               
SEQADV 1F6A CYS D  329  UNP  P01854              CLONING ARTIFACT               
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 ALA 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 ALA ILE SER ILE THR ASN ALA ALA ALA          
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                                  
SEQRES   1 B  222  ALA ASP PRO CYS ASP SER ASN PRO ARG GLY VAL SER ALA          
SEQRES   2 B  222  TYR LEU SER ARG PRO SER PRO PHE ASP LEU PHE ILE ARG          
SEQRES   3 B  222  LYS SER PRO THR ILE THR CYS LEU VAL VAL ASP LEU ALA          
SEQRES   4 B  222  PRO SER LYS GLY THR VAL ASN LEU THR TRP SER ARG ALA          
SEQRES   5 B  222  SER GLY LYS PRO VAL ASN HIS SER THR ARG LYS GLU GLU          
SEQRES   6 B  222  LYS GLN ARG ASN GLY THR LEU THR VAL THR SER THR LEU          
SEQRES   7 B  222  PRO VAL GLY THR ARG ASP TRP ILE GLU GLY GLU THR TYR          
SEQRES   8 B  222  GLN CYS ARG VAL THR HIS PRO HIS LEU PRO ARG ALA LEU          
SEQRES   9 B  222  MET ARG SER THR THR LYS THR SER GLY PRO ARG ALA ALA          
SEQRES  10 B  222  PRO GLU VAL TYR ALA PHE ALA THR PRO GLU TRP PRO GLY          
SEQRES  11 B  222  SER ARG ASP LYS ARG THR LEU ALA CYS LEU ILE GLN ASN          
SEQRES  12 B  222  PHE MET PRO GLU ASP ILE SER VAL GLN TRP LEU HIS ASN          
SEQRES  13 B  222  GLU VAL GLN LEU PRO ASP ALA ARG HIS SER THR THR GLN          
SEQRES  14 B  222  PRO ARG LYS THR LYS GLY SER GLY PHE PHE VAL PHE SER          
SEQRES  15 B  222  ARG LEU GLU VAL THR ARG ALA GLU TRP GLU GLN LYS ASP          
SEQRES  16 B  222  GLU PHE ILE CYS ARG ALA VAL HIS GLU ALA ALA SER PRO          
SEQRES  17 B  222  SER GLN THR VAL GLN ARG ALA VAL SER VAL ASN PRO GLY          
SEQRES  18 B  222  LYS                                                          
SEQRES   1 D  222  ALA ASP PRO CYS ASP SER ASN PRO ARG GLY VAL SER ALA          
SEQRES   2 D  222  TYR LEU SER ARG PRO SER PRO PHE ASP LEU PHE ILE ARG          
SEQRES   3 D  222  LYS SER PRO THR ILE THR CYS LEU VAL VAL ASP LEU ALA          
SEQRES   4 D  222  PRO SER LYS GLY THR VAL ASN LEU THR TRP SER ARG ALA          
SEQRES   5 D  222  SER GLY LYS PRO VAL ASN HIS SER THR ARG LYS GLU GLU          
SEQRES   6 D  222  LYS GLN ARG ASN GLY THR LEU THR VAL THR SER THR LEU          
SEQRES   7 D  222  PRO VAL GLY THR ARG ASP TRP ILE GLU GLY GLU THR TYR          
SEQRES   8 D  222  GLN CYS ARG VAL THR HIS PRO HIS LEU PRO ARG ALA LEU          
SEQRES   9 D  222  MET ARG SER THR THR LYS THR SER GLY PRO ARG ALA ALA          
SEQRES  10 D  222  PRO GLU VAL TYR ALA PHE ALA THR PRO GLU TRP PRO GLY          
SEQRES  11 D  222  SER ARG ASP LYS ARG THR LEU ALA CYS LEU ILE GLN ASN          
SEQRES  12 D  222  PHE MET PRO GLU ASP ILE SER VAL GLN TRP LEU HIS ASN          
SEQRES  13 D  222  GLU VAL GLN LEU PRO ASP ALA ARG HIS SER THR THR GLN          
SEQRES  14 D  222  PRO ARG LYS THR LYS GLY SER GLY PHE PHE VAL PHE SER          
SEQRES  15 D  222  ARG LEU GLU VAL THR ARG ALA GLU TRP GLU GLN LYS ASP          
SEQRES  16 D  222  GLU PHE ILE CYS ARG ALA VAL HIS GLU ALA ALA SER PRO          
SEQRES  17 D  222  SER GLN THR VAL GLN ARG ALA VAL SER VAL ASN PRO GLY          
SEQRES  18 D  222  LYS                                                          
MODRES 1F6A ASN B  394  ASN  GLYCOSYLATION SITE                                 
MODRES 1F6A ASN A  166  ASN  GLYCOSYLATION SITE                                 
MODRES 1F6A ASN A   42  ASN  GLYCOSYLATION SITE                                 
MODRES 1F6A ASN A   21  ASN  GLYCOSYLATION SITE                                 
MODRES 1F6A ASN D  394  ASN  GLYCOSYLATION SITE                                 
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET    MAN  C   3      11                                                       
HET    FUC  C   4      10                                                       
HET    NAG  E   1      14                                                       
HET    NAG  E   2      14                                                       
HET    MAN  E   3      11                                                       
HET    MAN  E   4      11                                                       
HET    MAN  E   5      11                                                       
HET    NAG  F   1      14                                                       
HET    NAG  F   2      14                                                       
HET    FUC  F   3      10                                                       
HET    NAG  G   1      14                                                       
HET    NAG  G   2      14                                                       
HET    MAN  G   3      11                                                       
HET    MAN  G   4      11                                                       
HET    MAN  G   5      11                                                       
HET    MAN  G   6      11                                                       
HET    NAG  H   1      14                                                       
HET    NAG  H   2      14                                                       
HET    MAN  H   3      11                                                       
HET    SO4  A 203       5                                                       
HET    CPS  A 370      26                                                       
HET    CPS  A 371      42                                                       
HET    SO4  B 201       5                                                       
HET    SO4  B 202       5                                                       
HET    SO4  B 204       5                                                       
HET    SO4  D 205       5                                                       
HET    CPS  D 103      26                                                       
HET    CPS  D 104      26                                                       
HET    CPS  D 105      26                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
HETNAM     FUC ALPHA-L-FUCOPYRANOSE                                             
HETNAM     SO4 SULFATE ION                                                      
HETNAM     CPS 3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-                        
HETNAM   2 CPS  PROPANESULFONATE                                                
HETSYN     CPS CHAPS                                                            
FORMUL   4  NAG    10(C8 H15 N O6)                                              
FORMUL   4  MAN    9(C6 H12 O6)                                                 
FORMUL   4  FUC    2(C6 H12 O5)                                                 
FORMUL   9  SO4    5(O4 S 2-)                                                   
FORMUL  10  CPS    5(C32 H58 N2 O7 S)                                           
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 ASN B  332  VAL B  336  5                                   5    
HELIX    4   4 SER B  344  ILE B  350  1                                   7    
HELIX    5   5 GLY B  406  GLU B  412  1                                   7    
HELIX    6   6 PRO B  486  HIS B  490  5                                   5    
HELIX    7   7 ARG B  513  LYS B  519  1                                   7    
HELIX    8   8 SER D  344  ILE D  350  1                                   7    
HELIX    9   9 GLY D  406  GLU D  412  1                                   7    
HELIX   10  10 PRO D  486  HIS D  490  5                                   5    
HELIX   11  11 ARG D  513  LYS D  519  1                                   7    
SHEET    1   A 3 VAL A   7  ASN A  10  0                                        
SHEET    2   A 3 VAL A  22  CYS A  26 -1  O  THR A  23   N  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  O  GLY A  64   N  LEU A  81           
SHEET    4   B 5 LYS A  38  HIS A  41 -1  O  LYS A  38   N  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    1   D 4 GLU A 125  TRP A 130  0                                        
SHEET    2   D 4 TYR A 116  LYS A 122 -1  O  VAL A 118   N  TRP A 130           
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  O  LEU A 158   N  VAL A 155           
SHEET    1   E 5 GLU A 125  TRP A 130  0                                        
SHEET    2   E 5 TYR A 116  LYS A 122 -1  O  VAL A 118   N  TRP A 130           
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  VAL A 169 -1  O  LEU A 165   N  TYR A 149           
SHEET    5   E 5 VAL A  96  VAL A  97  1  N  VAL A  97   O  THR A 168           
SHEET    1   F 4 ALA B 338  SER B 341  0                                        
SHEET    2   F 4 THR B 355  LEU B 363 -1  O  THR B 357   N  SER B 341           
SHEET    3   F 4 LEU B 397  PRO B 404 -1  O  LEU B 397   N  LEU B 363           
SHEET    4   F 4 LYS B 388  LYS B 391 -1  N  LYS B 388   O  THR B 400           
SHEET    1   G 3 THR B 373  ARG B 376  0                                        
SHEET    2   G 3 THR B 415  VAL B 420 -1  N  GLN B 417   O  SER B 375           
SHEET    3   G 3 LEU B 429  THR B 434 -1  N  LEU B 429   O  VAL B 420           
SHEET    1   H 4 GLU B 444  ALA B 449  0                                        
SHEET    2   H 4 LYS B 459  PHE B 469 -1  O  ALA B 463   N  PHE B 448           
SHEET    3   H 4 PHE B 503  THR B 512 -1  N  PHE B 503   O  PHE B 469           
SHEET    4   H 4 SER B 491  THR B 492 -1  N  SER B 491   O  ARG B 508           
SHEET    1   I 4 GLU B 444  ALA B 449  0                                        
SHEET    2   I 4 LYS B 459  PHE B 469 -1  O  ALA B 463   N  PHE B 448           
SHEET    3   I 4 PHE B 503  THR B 512 -1  N  PHE B 503   O  PHE B 469           
SHEET    4   I 4 ARG B 496  LYS B 497 -1  O  ARG B 496   N  PHE B 504           
SHEET    1   J 3 SER B 475  VAL B 476  0                                        
SHEET    2   J 3 ALA B 526  VAL B 527 -1  N  VAL B 527   O  SER B 475           
SHEET    3   J 3 THR B 536  VAL B 537 -1  N  VAL B 537   O  ALA B 526           
SHEET    1   K 2 PHE B 522  ILE B 523  0                                        
SHEET    2   K 2 ALA B 540  VAL B 541 -1  O  VAL B 541   N  PHE B 522           
SHEET    1   L 4 SER D 337  SER D 341  0                                        
SHEET    2   L 4 THR D 355  LEU D 363 -1  O  THR D 357   N  SER D 341           
SHEET    3   L 4 LEU D 397  PRO D 404 -1  O  LEU D 397   N  LEU D 363           
SHEET    4   L 4 LYS D 388  LYS D 391 -1  N  LYS D 388   O  THR D 400           
SHEET    1   M 3 LEU D 372  ARG D 376  0                                        
SHEET    2   M 3 THR D 415  VAL D 420 -1  N  GLN D 417   O  SER D 375           
SHEET    3   M 3 LEU D 429  THR D 434 -1  O  LEU D 429   N  VAL D 420           
SHEET    1   N 4 GLU D 444  ALA D 449  0                                        
SHEET    2   N 4 LYS D 459  PHE D 469 -1  O  ALA D 463   N  PHE D 448           
SHEET    3   N 4 PHE D 503  THR D 512 -1  N  PHE D 503   O  PHE D 469           
SHEET    4   N 4 SER D 491  THR D 492 -1  N  SER D 491   O  ARG D 508           
SHEET    1   O 4 GLU D 444  ALA D 449  0                                        
SHEET    2   O 4 LYS D 459  PHE D 469 -1  O  ALA D 463   N  PHE D 448           
SHEET    3   O 4 PHE D 503  THR D 512 -1  N  PHE D 503   O  PHE D 469           
SHEET    4   O 4 ARG D 496  LYS D 497 -1  O  ARG D 496   N  PHE D 504           
SHEET    1   P 3 SER D 475  VAL D 476  0                                        
SHEET    2   P 3 PHE D 522  VAL D 527 -1  N  VAL D 527   O  SER D 475           
SHEET    3   P 3 THR D 536  VAL D 541 -1  N  VAL D 537   O  ALA D 526           
SSBOND   1 CYS A   26    CYS A   68                          1555   1555  2.05  
SSBOND   2 CYS A  107    CYS A  151                          1555   1555  2.05  
SSBOND   3 CYS B  329    CYS D  329                          1555   1555  2.03  
SSBOND   4 CYS B  358    CYS B  418                          1555   1555  2.04  
SSBOND   5 CYS B  464    CYS B  524                          1555   1555  2.04  
SSBOND   6 CYS D  358    CYS D  418                          1555   1555  2.04  
SSBOND   7 CYS D  464    CYS D  524                          1555   1555  2.04  
LINK         ND2 ASN A  21                 C1  NAG C   1     1555   1555  1.45  
LINK         ND2 ASN A  42                 C1  NAG E   1     1555   1555  1.45  
LINK         ND2 ASN A 166                 C1  NAG F   1     1555   1555  1.45  
LINK         ND2 ASN B 394                 C1  NAG G   1     1555   1555  1.45  
LINK         ND2 ASN D 394                 C1  NAG H   1     1555   1555  1.46  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.38  
LINK         O6  NAG C   1                 C1  FUC C   4     1555   1555  1.41  
LINK         O4  NAG C   2                 C1  MAN C   3     1555   1555  1.38  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.39  
LINK         O4  NAG E   2                 C1  MAN E   3     1555   1555  1.38  
LINK         O3  MAN E   3                 C1  MAN E   4     1555   1555  1.41  
LINK         O6  MAN E   3                 C1  MAN E   5     1555   1555  1.41  
LINK         O4  NAG F   1                 C1  NAG F   2     1555   1555  1.39  
LINK         O6  NAG F   1                 C1  FUC F   3     1555   1555  1.40  
LINK         O4  NAG G   1                 C1  NAG G   2     1555   1555  1.38  
LINK         O4  NAG G   2                 C1  MAN G   3     1555   1555  1.38  
LINK         O6  MAN G   3                 C1  MAN G   4     1555   1555  1.42  
LINK         O3  MAN G   3                 C1  MAN G   6     1555   1555  1.40  
LINK         O2  MAN G   4                 C1  MAN G   5     1555   1555  1.41  
LINK         O4  NAG H   1                 C1  NAG H   2     1555   1555  1.40  
LINK         O4  NAG H   2                 C1  MAN H   3     1555   1555  1.39  
CISPEP   1 ASN A   10    PRO A   11          0        -0.08                     
CISPEP   2 MET B  470    PRO B  471          0        -2.45                     
CISPEP   3 SER B  532    PRO B  533          0         0.16                     
CISPEP   4 MET D  470    PRO D  471          0        -0.11                     
CISPEP   5 SER D  532    PRO D  533          0        -0.24                     
CRYST1  192.800  192.800  302.400  90.00  90.00 120.00 H 3 2        36          
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      0.005187  0.002995  0.000000        0.00000                         
SCALE2      0.000000  0.005989  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003307        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system