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Database: PDB
Entry: 1RPQ
LinkDB: 1RPQ
Original site: 1RPQ 
HEADER    MEMBRANE PROTEIN                        03-DEC-03   1RPQ              
TITLE     HIGH AFFINITY IGE RECEPTOR (ALPHA CHAIN) COMPLEXED WITH TIGHT-BINDING 
TITLE    2 E131 'ZETA' PEPTIDE FROM PHAGE DISPLAY                               
CAVEAT     1RPQ    NAG A 340 HAS WRONG CHIRALITY AT ATOM C1 NAG B 340 HAS WRONG 
CAVEAT   2 1RPQ    CHIRALITY AT ATOM C1 NAG C 340 HAS WRONG CHIRALITY AT ATOM   
CAVEAT   3 1RPQ    C1 NAG D 340 HAS WRONG CHIRALITY AT ATOM C1                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HIGH AFFINITY IMMUNOGLOBULIN EPSILON RECEPTOR ALPHA-SUBUNIT
COMPND   3 PRECURSOR;                                                           
COMPND   4 CHAIN: A, B, C, D;                                                   
COMPND   5 FRAGMENT: ALPHA CHAIN EXTRACELLULAR DOMAINS;                         
COMPND   6 SYNONYM: FCERI, IGE FC RECEPTOR, ALPHA-SUBUNIT, FC-EPSILON RI-ALPHA; 
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: PEPTIDE E131;                                              
COMPND  10 CHAIN: W, X, Y, Z;                                                   
COMPND  11 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: FCER1A, FCE1A;                                                 
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PACGP67B;                                 
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 SYNTHETIC: YES;                                                      
SOURCE  14 OTHER_DETAILS: RANDOM PEPTIDE SEQUENCES DISPLAYED ON PHAGE, SELECTED 
SOURCE  15 FOR BINDING TO FC(EPSILON)RI(ALPHA)                                  
KEYWDS    RECEPTOR-PEPTIDE COMPLEX, MEMBRANE PROTEIN                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.STAMOS,C.EIGENBROT,G.R.NAKAMURA,M.E.REYNOLDS,J.P.YIN,H.B.LOWMAN,    
AUTHOR   2 W.J.FAIRBROTHER,M.A.STAROVASNIK                                      
REVDAT   4   29-JUL-20 1RPQ    1       CAVEAT COMPND REMARK HET                 
REVDAT   4 2                   1       HETNAM FORMUL LINK   SITE                
REVDAT   4 3                   1       ATOM                                     
REVDAT   3   13-JUL-11 1RPQ    1       VERSN                                    
REVDAT   2   24-FEB-09 1RPQ    1       VERSN                                    
REVDAT   1   20-JUL-04 1RPQ    0                                                
JRNL        AUTH   J.STAMOS,C.EIGENBROT,G.R.NAKAMURA,M.E.REYNOLDS,J.P.YIN,      
JRNL        AUTH 2 H.B.LOWMAN,W.J.FAIRBROTHER,M.A.STAROVASNIK                   
JRNL        TITL   CONVERGENT RECOGNITION OF THE IGE BINDING SITE ON THE        
JRNL        TITL 2 HIGH-AFFINITY IGE RECEPTOR.                                  
JRNL        REF    STRUCTURE                     V.  12  1289 2004              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   15242605                                                     
JRNL        DOI    10.1016/J.STR.2004.04.015                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   G.R.NAKAMURA,M.E.REYNOLDS,Y.M.CHEN,M.A.STAROVASNIK,          
REMARK   1  AUTH 2 H.B.LOWMAN                                                   
REMARK   1  TITL   STABLE "ZETA" PEPTIDES THAT ACT AS POTENT ANTAGONISTS OF THE 
REMARK   1  TITL 2 HIGH-AFFINITY IGE RECEPTOR                                   
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  99  1303 2002              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1  DOI    10.1073/PNAS.022635599                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 98.1                                          
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.200                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1000000.000                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 30473                          
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) : 0.294                           
REMARK   3   FREE R VALUE                     : 0.349                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 968                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.011                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.11                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 85.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2563                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3880                       
REMARK   3   BIN FREE R VALUE                    : 0.4330                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 3.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 81                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.048                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6125                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 632                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 85.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 70.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.25000                                              
REMARK   3    B22 (A**2) : -0.08000                                             
REMARK   3    B33 (A**2) : -2.17000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
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) : 0.48                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.65                            
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) : 0.56                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.76                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.00                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.110                           
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) : 2.530 ; 3.000                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 4.420 ; 3.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.440 ; 3.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.890 ; 3.000                
REMARK   3                                                                      
REMARK   3  NCS MODEL : RESTRAINED, PARTS OF CHAINS A, B, C, D                  
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : 0.00  ; 1000                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : 2.7   ; 3.0                  
REMARK   3   GROUP  2  POSITIONAL            (A) : 0.01  ; 1000                 
REMARK   3   GROUP  2  B-FACTOR           (A**2) : 2.7   ; 3.0                  
REMARK   3   GROUP  3  POSITIONAL            (A) : 0.01  ; 1000                 
REMARK   3   GROUP  3  B-FACTOR           (A**2) : 2.7   ; 3.0                  
REMARK   3   GROUP  4  POSITIONAL            (A) : 0.01  ; 1000                 
REMARK   3   GROUP  4  B-FACTOR           (A**2) : 2.7   ; 3.0                  
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : MSI_XPLOR_PARHCSDX.PRO                         
REMARK   3  PARAMETER FILE  2  : MSI_XPLOR_PARAM3.CHO                           
REMARK   3  PARAMETER FILE  3  : PARAM.SO4                                      
REMARK   3  PARAMETER FILE  4  : CIT.PAR                                        
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : MSI_XPLOR_TOPHCSDX.PRO                         
REMARK   3  TOPOLOGY FILE  2   : MSI_XPLOR_TOPH3.CHO                            
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 1RPQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-DEC-03.                  
REMARK 100 THE DEPOSITION ID IS D_1000020932.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-JAN-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.033                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30473                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.5                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : 0.06800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.69000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1F2Q                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 2000 MONOMETHYL ETHER, AMMONIUM      
REMARK 280  SULFATE, SODIUM CITRATE, PH 4.2, VAPOR DIFFUSION, HANGING DROP,     
REMARK 280  TEMPERATURE 292K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
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   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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       52.05000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       52.05000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  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       99.85000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       74.85000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       99.85000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       74.85000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       52.05000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       99.85000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       74.85000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       52.05000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       99.85000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       74.85000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
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: 3370 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12770 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 22.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, W, E, F, G                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3130 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12530 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 21.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, X, H, I, J                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3240 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12420 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 8.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, Y, K, L, M                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3650 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 12.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, Z, N, O, P                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8740 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23060 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 17.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, W, Y, E, F, G, K, L, M          
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8910 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23090 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 21.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, X, Z, H, I, J, N, O, P          
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    31                                                      
REMARK 465     PHE A    32                                                      
REMARK 465     GLU A    33                                                      
REMARK 465     ALA A   172                                                      
REMARK 465     PRO A   173                                                      
REMARK 465     ARG A   174                                                      
REMARK 465     GLU A   175                                                      
REMARK 465     LYS A   176                                                      
REMARK 465     VAL B     1                                                      
REMARK 465     PRO B     2                                                      
REMARK 465     GLN B     3                                                      
REMARK 465     ASN B    30                                                      
REMARK 465     PHE B    31                                                      
REMARK 465     PHE B    32                                                      
REMARK 465     GLU B    33                                                      
REMARK 465     ALA B   172                                                      
REMARK 465     PRO B   173                                                      
REMARK 465     ARG B   174                                                      
REMARK 465     GLU B   175                                                      
REMARK 465     LYS B   176                                                      
REMARK 465     VAL C     1                                                      
REMARK 465     PRO C     2                                                      
REMARK 465     GLN C     3                                                      
REMARK 465     PHE C    32                                                      
REMARK 465     GLU C    33                                                      
REMARK 465     ALA C   172                                                      
REMARK 465     PRO C   173                                                      
REMARK 465     ARG C   174                                                      
REMARK 465     GLU C   175                                                      
REMARK 465     LYS C   176                                                      
REMARK 465     VAL D     1                                                      
REMARK 465     PRO D     2                                                      
REMARK 465     GLN D     3                                                      
REMARK 465     GLU D    33                                                      
REMARK 465     ALA D   172                                                      
REMARK 465     PRO D   173                                                      
REMARK 465     ARG D   174                                                      
REMARK 465     GLU D   175                                                      
REMARK 465     LYS D   176                                                      
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C  SSEQI                                                     
REMARK 475     LYS A     4                                                      
REMARK 475     GLN A    71                                                      
REMARK 475     GLN A    72                                                      
REMARK 475     VAL A    73                                                      
REMARK 475     GLN B    71                                                      
REMARK 475     GLN B    72                                                      
REMARK 475     VAL B    73                                                      
REMARK 475     GLU B    75                                                      
REMARK 475     GLN C    71                                                      
REMARK 475     GLN C    72                                                      
REMARK 475     VAL C    73                                                      
REMARK 475     ASN C    74                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ASN A   27   CB   CG   OD1  ND2                                  
REMARK 480     HIS A   70   CB   CG   ND1  CD2  CE1  NE2                        
REMARK 480     PHE B   40   CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 480     HIS B   70   CB   CG   ND1  CD2  CE1  NE2                        
REMARK 480     PHE C   31   CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 480     THR C   37   CB   OG1  CG2                                       
REMARK 480     PHE C   40   CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 480     HIS C   70   CB   CG   ND1  CD2  CE1  NE2                        
REMARK 480     GLU C   75   CB   CG   CD   OE1  OE2                             
REMARK 480     PHE D   31   CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 480     ASP W   11   CB   CG   OD1  OD2                                  
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    PHE D  31   CB    PHE D  31   CG     -0.309                       
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    PHE D  31   CA  -  CB  -  CG  ANGL. DEV. =  21.8 DEGREES          
REMARK 500    PHE D  31   CB  -  CG  -  CD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    PHE D  31   CB  -  CG  -  CD1 ANGL. DEV. =  -6.5 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    ASN A  27       92.28    -27.65                                   
REMARK 500    SER A  35      -71.84   -165.61                                   
REMARK 500    ALA A  58      128.96    -26.95                                   
REMARK 500    HIS A  70     -152.98   -108.05                                   
REMARK 500    VAL A  73      -79.97     62.05                                   
REMARK 500    SER A  85       78.59   -151.80                                   
REMARK 500    ALA A  94      144.85   -172.20                                   
REMARK 500    ARG A 111       30.92     39.02                                   
REMARK 500    TRP A 113      152.72    -49.16                                   
REMARK 500    ASP A 145        0.37    -67.97                                   
REMARK 500    GLN A 157       -5.38     79.84                                   
REMARK 500    PRO B   5     -177.63    -61.37                                   
REMARK 500    LYS B   6      128.73   -170.27                                   
REMARK 500    ASN B  27      107.15    -44.07                                   
REMARK 500    SER B  35      -73.23   -131.04                                   
REMARK 500    ALA B  58      128.85    -26.80                                   
REMARK 500    HIS B  70     -154.35   -116.42                                   
REMARK 500    VAL B  73      -75.58     63.29                                   
REMARK 500    SER B  85       77.67   -151.37                                   
REMARK 500    ALA B  94      143.69   -172.42                                   
REMARK 500    ASN B 112        9.03     57.52                                   
REMARK 500    ASP B 145        0.40    -68.10                                   
REMARK 500    GLN B 157       -4.72     59.70                                   
REMARK 500    ASN C  29      -81.12   -168.88                                   
REMARK 500    ASN C  30      -76.06    -38.32                                   
REMARK 500    SER C  35      -71.26   -166.96                                   
REMARK 500    ALA C  58      128.70    -26.94                                   
REMARK 500    HIS C  70     -139.20   -110.81                                   
REMARK 500    VAL C  73      -73.86     63.75                                   
REMARK 500    SER C  85       74.65   -150.42                                   
REMARK 500    GLU C  99      107.89    -47.80                                   
REMARK 500    ARG C 111       19.71     59.60                                   
REMARK 500    ASP C 145        0.30    -67.78                                   
REMARK 500    ASN D  27      102.03      9.10                                   
REMARK 500    SER D  35      -70.94   -165.86                                   
REMARK 500    ALA D  58      128.63    -27.19                                   
REMARK 500    HIS D  70      -71.64   -104.44                                   
REMARK 500    GLN D  72       83.05    -67.01                                   
REMARK 500    VAL D  73      -63.10   -147.77                                   
REMARK 500    SER D  85       70.47   -150.59                                   
REMARK 500    ALA D  94      143.72   -172.33                                   
REMARK 500    PHE X   6       -7.00    -51.53                                   
REMARK 500    GLN Y   2      109.62     54.17                                   
REMARK 500    LEU Y  10      152.74     64.55                                   
REMARK 500    TYR Y  12      149.12   -178.35                                   
REMARK 500    VAL Y  18      -39.01    -39.75                                   
REMARK 500    TYR Y  20       10.58    -65.19                                   
REMARK 500    ASP Z  17        1.10    -56.26                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C  SSEQI                                                     
REMARK 615     SO4 A   401                                                      
REMARK 615     SO4 Z   402                                                      
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: OLIGOSACCHARIDE INHIBITOR                             
REMARK 630 MOLECULE NAME: 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE              
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                           
REMARK 630                                                                      
REMARK 630   M RES C SSSEQI                                                     
REMARK 630     NAG A   340                                                      
REMARK 630     NAG B   340                                                      
REMARK 630     NAG C   340                                                      
REMARK 630     NAG D   340                                                      
REMARK 630 SOURCE: NULL                                                         
REMARK 630 TAXONOMY: NULL                                                       
REMARK 630 SUBCOMP: NULL                                                        
REMARK 630 DETAILS: OLIGOSACCHARIDE                                             
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1KCO   RELATED DB: PDB                                   
REMARK 900 NMR STRUCTURE OF E131 PEPTIDE                                        
REMARK 900 RELATED ID: 1F2Q   RELATED DB: PDB                                   
REMARK 900 X-RAY STRUCTURE OF HIGH AFFINITY IGE RECEPTOR (ALPHA CHAIN)          
REMARK 900 RELATED ID: 1F6A   RELATED DB: PDB                                   
REMARK 900 X-RAY STRUCTURE OF HIGH AFFINITY IGE RECEPTOR (ALPHA CHAIN)          
REMARK 900 COMPLEXED WITH FC FROM IGE                                           
DBREF  1RPQ A    1   176  UNP    P12319   FCEA_HUMAN      26    201             
DBREF  1RPQ B    1   176  UNP    P12319   FCEA_HUMAN      26    201             
DBREF  1RPQ C    1   176  UNP    P12319   FCEA_HUMAN      26    201             
DBREF  1RPQ D    1   176  UNP    P12319   FCEA_HUMAN      26    201             
DBREF  1RPQ W    1    21  PDB    1RPQ     1RPQ             1     21             
DBREF  1RPQ X    1    21  PDB    1RPQ     1RPQ             1     21             
DBREF  1RPQ Y    1    21  PDB    1RPQ     1RPQ             1     21             
DBREF  1RPQ Z    1    21  PDB    1RPQ     1RPQ             1     21             
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                                  
SEQRES   1 B  176  VAL PRO GLN LYS PRO LYS VAL SER LEU ASN PRO PRO TRP          
SEQRES   2 B  176  ASN ARG ILE PHE LYS GLY GLU ASN VAL THR LEU THR CYS          
SEQRES   3 B  176  ASN GLY ASN ASN PHE PHE GLU VAL SER SER THR LYS TRP          
SEQRES   4 B  176  PHE HIS ASN GLY SER LEU SER GLU GLU THR ASN SER SER          
SEQRES   5 B  176  LEU ASN ILE VAL ASN ALA LYS PHE GLU ASP SER GLY GLU          
SEQRES   6 B  176  TYR LYS CYS GLN HIS GLN GLN VAL ASN GLU SER GLU PRO          
SEQRES   7 B  176  VAL TYR LEU GLU VAL PHE SER ASP TRP LEU LEU LEU GLN          
SEQRES   8 B  176  ALA SER ALA GLU VAL VAL MET GLU GLY GLN PRO LEU PHE          
SEQRES   9 B  176  LEU ARG CYS HIS GLY TRP ARG ASN TRP ASP VAL TYR LYS          
SEQRES  10 B  176  VAL ILE TYR TYR LYS ASP GLY GLU ALA LEU LYS TYR TRP          
SEQRES  11 B  176  TYR GLU ASN HIS ASN ILE SER ILE THR ASN ALA THR VAL          
SEQRES  12 B  176  GLU ASP SER GLY THR TYR TYR CYS THR GLY LYS VAL TRP          
SEQRES  13 B  176  GLN LEU ASP TYR GLU SER GLU PRO LEU ASN ILE THR VAL          
SEQRES  14 B  176  ILE LYS ALA PRO ARG GLU LYS                                  
SEQRES   1 C  176  VAL PRO GLN LYS PRO LYS VAL SER LEU ASN PRO PRO TRP          
SEQRES   2 C  176  ASN ARG ILE PHE LYS GLY GLU ASN VAL THR LEU THR CYS          
SEQRES   3 C  176  ASN GLY ASN ASN PHE PHE GLU VAL SER SER THR LYS TRP          
SEQRES   4 C  176  PHE HIS ASN GLY SER LEU SER GLU GLU THR ASN SER SER          
SEQRES   5 C  176  LEU ASN ILE VAL ASN ALA LYS PHE GLU ASP SER GLY GLU          
SEQRES   6 C  176  TYR LYS CYS GLN HIS GLN GLN VAL ASN GLU SER GLU PRO          
SEQRES   7 C  176  VAL TYR LEU GLU VAL PHE SER ASP TRP LEU LEU LEU GLN          
SEQRES   8 C  176  ALA SER ALA GLU VAL VAL MET GLU GLY GLN PRO LEU PHE          
SEQRES   9 C  176  LEU ARG CYS HIS GLY TRP ARG ASN TRP ASP VAL TYR LYS          
SEQRES  10 C  176  VAL ILE TYR TYR LYS ASP GLY GLU ALA LEU LYS TYR TRP          
SEQRES  11 C  176  TYR GLU ASN HIS ASN ILE SER ILE THR ASN ALA THR VAL          
SEQRES  12 C  176  GLU ASP SER GLY THR TYR TYR CYS THR GLY LYS VAL TRP          
SEQRES  13 C  176  GLN LEU ASP TYR GLU SER GLU PRO LEU ASN ILE THR VAL          
SEQRES  14 C  176  ILE LYS ALA PRO ARG GLU LYS                                  
SEQRES   1 D  176  VAL PRO GLN LYS PRO LYS VAL SER LEU ASN PRO PRO TRP          
SEQRES   2 D  176  ASN ARG ILE PHE LYS GLY GLU ASN VAL THR LEU THR CYS          
SEQRES   3 D  176  ASN GLY ASN ASN PHE PHE GLU VAL SER SER THR LYS TRP          
SEQRES   4 D  176  PHE HIS ASN GLY SER LEU SER GLU GLU THR ASN SER SER          
SEQRES   5 D  176  LEU ASN ILE VAL ASN ALA LYS PHE GLU ASP SER GLY GLU          
SEQRES   6 D  176  TYR LYS CYS GLN HIS GLN GLN VAL ASN GLU SER GLU PRO          
SEQRES   7 D  176  VAL TYR LEU GLU VAL PHE SER ASP TRP LEU LEU LEU GLN          
SEQRES   8 D  176  ALA SER ALA GLU VAL VAL MET GLU GLY GLN PRO LEU PHE          
SEQRES   9 D  176  LEU ARG CYS HIS GLY TRP ARG ASN TRP ASP VAL TYR LYS          
SEQRES  10 D  176  VAL ILE TYR TYR LYS ASP GLY GLU ALA LEU LYS TYR TRP          
SEQRES  11 D  176  TYR GLU ASN HIS ASN ILE SER ILE THR ASN ALA THR VAL          
SEQRES  12 D  176  GLU ASP SER GLY THR TYR TYR CYS THR GLY LYS VAL TRP          
SEQRES  13 D  176  GLN LEU ASP TYR GLU SER GLU PRO LEU ASN ILE THR VAL          
SEQRES  14 D  176  ILE LYS ALA PRO ARG GLU LYS                                  
SEQRES   1 W   21  VAL GLN CYS PRO HIS PHE CYS TYR GLU LEU ASP TYR GLU          
SEQRES   2 W   21  LEU CYS PRO ASP VAL CYS TYR VAL                              
SEQRES   1 X   21  VAL GLN CYS PRO HIS PHE CYS TYR GLU LEU ASP TYR GLU          
SEQRES   2 X   21  LEU CYS PRO ASP VAL CYS TYR VAL                              
SEQRES   1 Y   21  VAL GLN CYS PRO HIS PHE CYS TYR GLU LEU ASP TYR GLU          
SEQRES   2 Y   21  LEU CYS PRO ASP VAL CYS TYR VAL                              
SEQRES   1 Z   21  VAL GLN CYS PRO HIS PHE CYS TYR GLU LEU ASP TYR GLU          
SEQRES   2 Z   21  LEU CYS PRO ASP VAL CYS TYR VAL                              
MODRES 1RPQ ASN A   21  ASN  GLYCOSYLATION SITE                                 
MODRES 1RPQ ASN A   42  ASN  GLYCOSYLATION SITE                                 
MODRES 1RPQ ASN A  140  ASN  GLYCOSYLATION SITE                                 
MODRES 1RPQ ASN A  166  ASN  GLYCOSYLATION SITE                                 
MODRES 1RPQ ASN B   21  ASN  GLYCOSYLATION SITE                                 
MODRES 1RPQ ASN B   42  ASN  GLYCOSYLATION SITE                                 
MODRES 1RPQ ASN B  140  ASN  GLYCOSYLATION SITE                                 
MODRES 1RPQ ASN B  166  ASN  GLYCOSYLATION SITE                                 
MODRES 1RPQ ASN C   21  ASN  GLYCOSYLATION SITE                                 
MODRES 1RPQ ASN C   42  ASN  GLYCOSYLATION SITE                                 
MODRES 1RPQ ASN C  140  ASN  GLYCOSYLATION SITE                                 
MODRES 1RPQ ASN C  166  ASN  GLYCOSYLATION SITE                                 
MODRES 1RPQ ASN D   21  ASN  GLYCOSYLATION SITE                                 
MODRES 1RPQ ASN D   42  ASN  GLYCOSYLATION SITE                                 
MODRES 1RPQ ASN D  140  ASN  GLYCOSYLATION SITE                                 
MODRES 1RPQ ASN D  166  ASN  GLYCOSYLATION SITE                                 
HET    NAG  E   1      14                                                       
HET    NAG  E   2      14                                                       
HET    NAG  E   3      14                                                       
HET    NAG  F   1      14                                                       
HET    NAG  F   2      14                                                       
HET    BMA  F   3      11                                                       
HET    BMA  F   4      11                                                       
HET    BMA  F   5      11                                                       
HET    NAG  G   1      14                                                       
HET    NAG  G   2      14                                                       
HET    BMA  G   3      11                                                       
HET    NAG  H   1      14                                                       
HET    NAG  H   2      14                                                       
HET    NAG  H   3      14                                                       
HET    NAG  I   1      14                                                       
HET    NAG  I   2      14                                                       
HET    BMA  I   3      11                                                       
HET    BMA  I   4      11                                                       
HET    BMA  I   5      11                                                       
HET    NAG  J   1      14                                                       
HET    NAG  J   2      14                                                       
HET    BMA  J   3      11                                                       
HET    NAG  K   1      14                                                       
HET    NAG  K   2      14                                                       
HET    NAG  L   1      14                                                       
HET    NAG  L   2      14                                                       
HET    BMA  L   3      11                                                       
HET    BMA  L   4      11                                                       
HET    BMA  L   5      11                                                       
HET    NAG  M   1      14                                                       
HET    NAG  M   2      14                                                       
HET    BMA  M   3      11                                                       
HET    NAG  N   1      14                                                       
HET    NAG  N   2      14                                                       
HET    NAG  O   1      14                                                       
HET    NAG  O   2      14                                                       
HET    BMA  O   3      11                                                       
HET    BMA  O   4      11                                                       
HET    BMA  O   5      11                                                       
HET    NAG  P   1      14                                                       
HET    NAG  P   2      14                                                       
HET    BMA  P   3      11                                                       
HET    NAG  A 340      14                                                       
HET    SO4  A 401       5                                                       
HET    NAG  B 340      14                                                       
HET    NAG  C 340      14                                                       
HET    CIT  C 403      13                                                       
HET    NAG  D 340      14                                                       
HET    CIT  D 404      13                                                       
HET    SO4  Z 402       5                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM     SO4 SULFATE ION                                                      
HETNAM     CIT CITRIC ACID                                                      
FORMUL   9  NAG    30(C8 H15 N O6)                                              
FORMUL  10  BMA    16(C6 H12 O6)                                                
FORMUL  22  SO4    2(O4 S 2-)                                                   
FORMUL  25  CIT    2(C6 H8 O7)                                                  
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    
HELIX    4   4 LYS B   59  SER B   63  5                                   5    
HELIX    5   5 ARG B  111  TRP B  113  5                                   3    
HELIX    6   6 THR B  142  SER B  146  5                                   5    
HELIX    7   7 LYS C   59  SER C   63  5                                   5    
HELIX    8   8 ARG C  111  TRP C  113  5                                   3    
HELIX    9   9 THR C  142  SER C  146  5                                   5    
HELIX   10  10 LYS D   59  SER D   63  5                                   5    
HELIX   11  11 ARG D  111  TRP D  113  5                                   3    
HELIX   12  12 THR D  142  SER D  146  5                                   5    
HELIX   13  13 HIS W    5  LEU W   10  1                                   6    
HELIX   14  14 PRO W   16  TYR W   20  5                                   5    
HELIX   15  15 PRO X    4  TYR X    8  5                                   5    
HELIX   16  16 PRO X   16  TYR X   20  5                                   5    
HELIX   17  17 PRO Y    4  TYR Y    8  5                                   5    
HELIX   18  18 PRO Y   16  VAL Y   21  1                                   6    
HELIX   19  19 PRO Z    4  LEU Z   10  5                                   7    
HELIX   20  20 PRO Z   16  TYR Z   20  5                                   5    
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  25   N  SER A   8           
SHEET    3   A 3 SER A  52  ILE A  55 -1  O  ILE A  55   N  VAL A  22           
SHEET    1   B 5 ARG A  15  PHE A  17  0                                        
SHEET    2   B 5 VAL A  79  PHE A  84  1  O  PHE A  84   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  PHE A  40   O  LYS A  67           
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 ILE A 136  ILE A 138 -1  O  ILE A 138   N  LEU A 103           
SHEET    1   D 5 VAL A  96  MET A  98  0                                        
SHEET    2   D 5 LEU A 165  ILE A 170  1  O  THR A 168   N  VAL A  97           
SHEET    3   D 5 GLY A 147  VAL A 155 -1  N  TYR A 149   O  LEU A 165           
SHEET    4   D 5 TYR A 116  LYS A 122 -1  N  TYR A 121   O  TYR A 150           
SHEET    5   D 5 GLU A 125  GLU A 132 -1  O  LEU A 127   N  TYR A 120           
SHEET    1   E 4 VAL A  96  MET A  98  0                                        
SHEET    2   E 4 LEU A 165  ILE A 170  1  O  THR A 168   N  VAL A  97           
SHEET    3   E 4 GLY A 147  VAL A 155 -1  N  TYR A 149   O  LEU A 165           
SHEET    4   E 4 LEU A 158  GLU A 161 -1  O  TYR A 160   N  GLY A 153           
SHEET    1   F 3 VAL B   7  ASN B  10  0                                        
SHEET    2   F 3 VAL B  22  CYS B  26 -1  O  THR B  25   N  SER B   8           
SHEET    3   F 3 SER B  52  ILE B  55 -1  O  ILE B  55   N  VAL B  22           
SHEET    1   G 5 ARG B  15  PHE B  17  0                                        
SHEET    2   G 5 VAL B  79  PHE B  84  1  O  PHE B  84   N  ILE B  16           
SHEET    3   G 5 GLY B  64  GLN B  69 -1  N  GLY B  64   O  LEU B  81           
SHEET    4   G 5 LYS B  38  HIS B  41 -1  N  PHE B  40   O  LYS B  67           
SHEET    5   G 5 SER B  44  LEU B  45 -1  O  SER B  44   N  HIS B  41           
SHEET    1   H 3 LEU B  88  ALA B  92  0                                        
SHEET    2   H 3 LEU B 103  GLY B 109 -1  O  ARG B 106   N  GLN B  91           
SHEET    3   H 3 ILE B 136  ILE B 138 -1  O  ILE B 138   N  LEU B 103           
SHEET    1   I 5 VAL B  96  MET B  98  0                                        
SHEET    2   I 5 LEU B 165  ILE B 170  1  O  THR B 168   N  VAL B  97           
SHEET    3   I 5 GLY B 147  VAL B 155 -1  N  TYR B 149   O  LEU B 165           
SHEET    4   I 5 TYR B 116  LYS B 122 -1  N  TYR B 121   O  TYR B 150           
SHEET    5   I 5 GLU B 125  GLU B 132 -1  O  LEU B 127   N  TYR B 120           
SHEET    1   J 4 VAL B  96  MET B  98  0                                        
SHEET    2   J 4 LEU B 165  ILE B 170  1  O  THR B 168   N  VAL B  97           
SHEET    3   J 4 GLY B 147  VAL B 155 -1  N  TYR B 149   O  LEU B 165           
SHEET    4   J 4 LEU B 158  GLU B 161 -1  O  TYR B 160   N  GLY B 153           
SHEET    1   K 3 VAL C   7  ASN C  10  0                                        
SHEET    2   K 3 VAL C  22  CYS C  26 -1  O  THR C  25   N  SER C   8           
SHEET    3   K 3 SER C  52  ILE C  55 -1  O  ILE C  55   N  VAL C  22           
SHEET    1   L 5 ARG C  15  PHE C  17  0                                        
SHEET    2   L 5 VAL C  79  PHE C  84  1  O  PHE C  84   N  ILE C  16           
SHEET    3   L 5 GLY C  64  GLN C  69 -1  N  GLY C  64   O  LEU C  81           
SHEET    4   L 5 LYS C  38  HIS C  41 -1  N  PHE C  40   O  LYS C  67           
SHEET    5   L 5 SER C  44  LEU C  45 -1  O  SER C  44   N  HIS C  41           
SHEET    1   M 3 LEU C  88  ALA C  92  0                                        
SHEET    2   M 3 LEU C 103  GLY C 109 -1  O  ARG C 106   N  GLN C  91           
SHEET    3   M 3 ILE C 136  ILE C 138 -1  O  ILE C 138   N  LEU C 103           
SHEET    1   N 5 VAL C  96  MET C  98  0                                        
SHEET    2   N 5 LEU C 165  ILE C 170  1  O  THR C 168   N  VAL C  97           
SHEET    3   N 5 GLY C 147  VAL C 155 -1  N  TYR C 149   O  LEU C 165           
SHEET    4   N 5 VAL C 115  LYS C 122 -1  N  TYR C 121   O  TYR C 150           
SHEET    5   N 5 GLU C 125  GLU C 132 -1  O  LEU C 127   N  TYR C 120           
SHEET    1   O 4 VAL C  96  MET C  98  0                                        
SHEET    2   O 4 LEU C 165  ILE C 170  1  O  THR C 168   N  VAL C  97           
SHEET    3   O 4 GLY C 147  VAL C 155 -1  N  TYR C 149   O  LEU C 165           
SHEET    4   O 4 LEU C 158  GLU C 161 -1  O  LEU C 158   N  VAL C 155           
SHEET    1   P 3 VAL D   7  ASN D  10  0                                        
SHEET    2   P 3 VAL D  22  CYS D  26 -1  O  THR D  25   N  SER D   8           
SHEET    3   P 3 SER D  52  ILE D  55 -1  O  ILE D  55   N  VAL D  22           
SHEET    1   Q 5 ARG D  15  PHE D  17  0                                        
SHEET    2   Q 5 VAL D  79  PHE D  84  1  O  PHE D  84   N  ILE D  16           
SHEET    3   Q 5 GLY D  64  GLN D  69 -1  N  GLY D  64   O  LEU D  81           
SHEET    4   Q 5 LYS D  38  HIS D  41 -1  N  PHE D  40   O  LYS D  67           
SHEET    5   Q 5 SER D  44  LEU D  45 -1  O  SER D  44   N  HIS D  41           
SHEET    1   R 3 LEU D  88  ALA D  92  0                                        
SHEET    2   R 3 LEU D 103  GLY D 109 -1  O  ARG D 106   N  GLN D  91           
SHEET    3   R 3 ILE D 136  ILE D 138 -1  O  ILE D 138   N  LEU D 103           
SHEET    1   S 5 VAL D  96  MET D  98  0                                        
SHEET    2   S 5 LEU D 165  ILE D 170  1  O  THR D 168   N  VAL D  97           
SHEET    3   S 5 GLY D 147  VAL D 155 -1  N  TYR D 149   O  LEU D 165           
SHEET    4   S 5 TYR D 116  LYS D 122 -1  N  TYR D 121   O  TYR D 150           
SHEET    5   S 5 GLU D 125  GLU D 132 -1  O  LEU D 127   N  TYR D 120           
SHEET    1   T 4 VAL D  96  MET D  98  0                                        
SHEET    2   T 4 LEU D 165  ILE D 170  1  O  THR D 168   N  VAL D  97           
SHEET    3   T 4 GLY D 147  VAL D 155 -1  N  TYR D 149   O  LEU D 165           
SHEET    4   T 4 LEU D 158  GLU D 161 -1  O  LEU D 158   N  VAL D 155           
SSBOND   1 CYS A   26    CYS A   68                          1555   1555  2.03  
SSBOND   2 CYS A  107    CYS A  151                          1555   1555  2.03  
SSBOND   3 CYS B   26    CYS B   68                          1555   1555  2.03  
SSBOND   4 CYS B  107    CYS B  151                          1555   1555  2.04  
SSBOND   5 CYS C   26    CYS C   68                          1555   1555  2.03  
SSBOND   6 CYS C  107    CYS C  151                          1555   1555  2.04  
SSBOND   7 CYS D   26    CYS D   68                          1555   1555  2.03  
SSBOND   8 CYS D  107    CYS D  151                          1555   1555  2.05  
SSBOND   9 CYS W    3    CYS W   19                          1555   1555  2.03  
SSBOND  10 CYS W    7    CYS W   15                          1555   1555  2.03  
SSBOND  11 CYS X    3    CYS X   19                          1555   1555  2.03  
SSBOND  12 CYS X    7    CYS X   15                          1555   1555  2.01  
SSBOND  13 CYS Y    3    CYS Y   19                          1555   1555  2.01  
SSBOND  14 CYS Y    7    CYS Y   15                          1555   1555  2.02  
SSBOND  15 CYS Z    3    CYS Z   19                          1555   1555  2.02  
SSBOND  16 CYS Z    7    CYS Z   15                          1555   1555  2.01  
LINK         ND2 ASN A  21                 C1  NAG E   1     1555   1555  1.44  
LINK         ND2 ASN A  42                 C1  NAG F   1     1555   1555  1.46  
LINK         ND2 ASN A 140                 C1  NAG A 340     1555   1555  1.45  
LINK         ND2 ASN A 166                 C1  NAG G   1     1555   1555  1.45  
LINK         ND2 ASN B  21                 C1  NAG H   1     1555   1555  1.46  
LINK         ND2 ASN B  42                 C1  NAG I   1     1555   1555  1.45  
LINK         ND2 ASN B 140                 C1  NAG B 340     1555   1555  1.45  
LINK         ND2 ASN B 166                 C1  NAG J   1     1555   1555  1.45  
LINK         ND2 ASN C  21                 C1  NAG K   1     1555   1555  1.45  
LINK         ND2 ASN C  42                 C1  NAG L   1     1555   1555  1.45  
LINK         ND2 ASN C 140                 C1  NAG C 340     1555   1555  1.46  
LINK         ND2 ASN C 166                 C1  NAG M   1     1555   1555  1.45  
LINK         ND2 ASN D  21                 C1  NAG N   1     1555   1555  1.45  
LINK         ND2 ASN D  42                 C1  NAG O   1     1555   1555  1.44  
LINK         ND2 ASN D 140                 C1  NAG D 340     1555   1555  1.46  
LINK         ND2 ASN D 166                 C1  NAG P   1     1555   1555  1.46  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.38  
LINK         O4  NAG E   2                 C1  NAG E   3     1555   1555  1.40  
LINK         O4  NAG F   1                 C1  NAG F   2     1555   1555  1.38  
LINK         O4  NAG F   2                 C1  BMA F   3     1555   1555  1.38  
LINK         O3  BMA F   3                 C1  BMA F   4     1555   1555  1.40  
LINK         O4  BMA F   3                 C1  BMA F   5     1555   1555  1.40  
LINK         O4  NAG G   1                 C1  NAG G   2     1555   1555  1.39  
LINK         O4  NAG G   2                 C1  BMA G   3     1555   1555  1.39  
LINK         O4  NAG H   1                 C1  NAG H   2     1555   1555  1.39  
LINK         O4  NAG H   2                 C1  NAG H   3     1555   1555  1.40  
LINK         O4  NAG I   1                 C1  NAG I   2     1555   1555  1.38  
LINK         O4  NAG I   2                 C1  BMA I   3     1555   1555  1.38  
LINK         O3  BMA I   3                 C1  BMA I   4     1555   1555  1.40  
LINK         O4  BMA I   3                 C1  BMA I   5     1555   1555  1.39  
LINK         O4  NAG J   1                 C1  NAG J   2     1555   1555  1.39  
LINK         O4  NAG J   2                 C1  BMA J   3     1555   1555  1.39  
LINK         O4  NAG K   1                 C1  NAG K   2     1555   1555  1.39  
LINK         O4  NAG L   1                 C1  NAG L   2     1555   1555  1.39  
LINK         O4  NAG L   2                 C1  BMA L   3     1555   1555  1.38  
LINK         O3  BMA L   3                 C1  BMA L   4     1555   1555  1.41  
LINK         O4  BMA L   3                 C1  BMA L   5     1555   1555  1.39  
LINK         O4  NAG M   1                 C1  NAG M   2     1555   1555  1.39  
LINK         O4  NAG M   2                 C1  BMA M   3     1555   1555  1.39  
LINK         O4  NAG N   1                 C1  NAG N   2     1555   1555  1.39  
LINK         O4  NAG O   1                 C1  NAG O   2     1555   1555  1.39  
LINK         O4  NAG O   2                 C1  BMA O   3     1555   1555  1.38  
LINK         O3  BMA O   3                 C1  BMA O   4     1555   1555  1.40  
LINK         O4  BMA O   3                 C1  BMA O   5     1555   1555  1.39  
LINK         O4  NAG P   1                 C1  NAG P   2     1555   1555  1.40  
LINK         O4  NAG P   2                 C1  BMA P   3     1555   1555  1.39  
CISPEP   1 ASN A   10    PRO A   11          0        -0.12                     
CISPEP   2 ASN B   10    PRO B   11          0         0.06                     
CISPEP   3 ASN C   10    PRO C   11          0        -0.42                     
CISPEP   4 ASN D   10    PRO D   11          0        -0.18                     
CRYST1  199.700  149.700  104.100  90.00  90.00  90.00 C 2 2 21     32          
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      0.005008  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006680  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009606        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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