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Database: PDB
Entry: 2Y7Q
LinkDB: 2Y7Q
Original site: 2Y7Q 
HEADER    IMMUNE SYSTEM                           01-FEB-11   2Y7Q              
TITLE     THE HIGH-AFFINITY COMPLEX BETWEEN IGE AND ITS RECEPTOR FC EPSILON RI  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HIGH AFFINITY IMMUNOGLOBULIN EPSILON RECEPTOR SUBUNIT      
COMPND   3 ALPHA;                                                               
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: SOLUBLE EXTRACELLULAR DOMAINS, RESIDUES 26-201;            
COMPND   6 SYNONYM: HIGH AFFINITY IGE RECEPTOR FC EPSILON RI, IGE FC RECEPTOR   
COMPND   7 SUBUNIT ALPHA, FC-EPSILON RI-ALPHA, FCERI;                           
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: IG EPSILON CHAIN C REGION;                                 
COMPND  12 CHAIN: B, D;                                                         
COMPND  13 FRAGMENT: FC FRAGMENT COMPRISING DOMAINS CEPSILON2-4, RESIDUES 104-  
COMPND  14 427;                                                                 
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MUTATION: 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: HOMO SAPIENS;                                     
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: HEK293S;                                
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PHLSEC;                                    
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 EXPRESSION_SYSTEM: MUS MUSCULUS;                                     
SOURCE  15 EXPRESSION_SYSTEM_COMMON: HOUSE MOUSE;                               
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 10090;                                      
SOURCE  17 EXPRESSION_SYSTEM_CELL_LINE: MOUSE MYELOMA NS0;                      
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  19 EXPRESSION_SYSTEM_VECTOR: PEE6                                       
KEYWDS    ALLERGY, ANTIBODY, IGE-BINDING PROTEIN, HIGH-AFFINITY RECEPTOR,       
KEYWDS   2 IMMUNOGLOBULIN C REGION, IMMUNE SYSTEM                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.M.DAVIES,M.D.HOLDOM,J.E.NETTLESHIP,A.J.BEAVIL,R.J.OWENS,B.J.SUTTON  
REVDAT   5   29-JUL-20 2Y7Q    1       COMPND REMARK HETNAM LINK                
REVDAT   5 2                   1       SITE   ATOM                              
REVDAT   4   08-MAY-19 2Y7Q    1       REMARK                                   
REVDAT   3   18-MAY-11 2Y7Q    1       JRNL                                     
REVDAT   2   27-APR-11 2Y7Q    1       JRNL                                     
REVDAT   1   20-APR-11 2Y7Q    0                                                
JRNL        AUTH   M.D.HOLDOM,A.M.DAVIES,J.E.NETTLESHIP,S.C.BAGBY,B.DHALIWAL,   
JRNL        AUTH 2 E.GIRARDI,J.HUNT,H.J.GOULD,A.J.BEAVIL,J.M.MCDONNELL,         
JRNL        AUTH 3 R.J.OWENS,B.J.SUTTON                                         
JRNL        TITL   CONFORMATIONAL CHANGES IN IGE CONTRIBUTE TO ITS UNIQUELY     
JRNL        TITL 2 SLOW DISSOCIATION RATE FROM RECEPTOR FCERI                   
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  18   571 2011              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   21516097                                                     
JRNL        DOI    10.1038/NSMB.2044                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   T.WAN,R.L.BEAVIL,S.M.FABIANE,A.J.BEAVIL,M.K.SOHI,M.KEOWN,    
REMARK   1  AUTH 2 R.J.YOUNG,A.J.HENRY,R.J.OWENS,H.J.GOULD,B.J.SUTTON           
REMARK   1  TITL   THE CRYSTAL STRUCTURE OF IGE FC REVEALS AN ASYMMETRICALLY    
REMARK   1  TITL 2 BENT CONFORMATION.                                           
REMARK   1  REF    NAT.IMMUNOL.                  V.   3   681 2002              
REMARK   1  REFN                   ISSN 1529-2908                               
REMARK   1  PMID   12068291                                                     
REMARK   1  DOI    10.1038/NI811                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.68                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 16116                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.248                           
REMARK   3   R VALUE            (WORKING SET) : 0.245                           
REMARK   3   FREE R VALUE                     : 0.292                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 812                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 37.6805 -  6.1707    0.99     2678   135  0.2730 0.3168        
REMARK   3     2  6.1707 -  4.9013    1.00     2578   126  0.2115 0.2715        
REMARK   3     3  4.9013 -  4.2827    1.00     2512   164  0.1867 0.2434        
REMARK   3     4  4.2827 -  3.8916    1.00     2521   136  0.2171 0.3013        
REMARK   3     5  3.8916 -  3.6129    1.00     2509   121  0.2323 0.3056        
REMARK   3     6  3.6129 -  3.4000    0.99     2506   130  0.2806 0.3299        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.35                                          
REMARK   3   B_SOL              : 91.81                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.450            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.550           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -5.97200                                             
REMARK   3    B22 (A**2) : 8.92480                                              
REMARK   3    B33 (A**2) : -2.95280                                             
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           5500                                  
REMARK   3   ANGLE     :  1.104           7497                                  
REMARK   3   CHIRALITY :  0.066            866                                  
REMARK   3   PLANARITY :  0.008            951                                  
REMARK   3   DIHEDRAL  : 20.103           1838                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 5                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN B AND RESID 337:364                   
REMARK   3     SELECTION          : CHAIN D AND RESID 337:364                   
REMARK   3     ATOM PAIRS NUMBER  : 206                                         
REMARK   3     RMSD               : 0.115                                       
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN B AND RESID 371:377                   
REMARK   3     SELECTION          : CHAIN D AND RESID 371:377                   
REMARK   3     ATOM PAIRS NUMBER  : 57                                          
REMARK   3     RMSD               : 0.079                                       
REMARK   3   NCS GROUP : 3                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN B AND RESID 391:437                   
REMARK   3     SELECTION          : CHAIN D AND RESID 391:437                   
REMARK   3     ATOM PAIRS NUMBER  : 331                                         
REMARK   3     RMSD               : 0.131                                       
REMARK   3   NCS GROUP : 4                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN B AND RESID 438:448                   
REMARK   3     SELECTION          : CHAIN D AND RESID 438:448                   
REMARK   3     ATOM PAIRS NUMBER  : 80                                          
REMARK   3     RMSD               : 0.081                                       
REMARK   3   NCS GROUP : 5                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN B AND RESID 462:544                   
REMARK   3     SELECTION          : CHAIN D AND RESID 462:544                   
REMARK   3     ATOM PAIRS NUMBER  : 395                                         
REMARK   3     RMSD               : 0.094                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: DISORDERED REGIONS WERE NOT MODELED.      
REMARK   4                                                                      
REMARK   4 2Y7Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-FEB-11.                  
REMARK 100 THE DEPOSITION ID IS D_1290045881.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97910                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16204                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 5.900                              
REMARK 200  R MERGE                    (I) : 0.25000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 1F6A AND 1O0V                            
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.78                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SITTING DROP VAPOR DIFFUSION.            
REMARK 280  RESERVOIR SOLUTION CONTAINED 2.8M SODIUM ACETATE PH 7., VAPOR       
REMARK 280  DIFFUSION, SITTING DROP                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       49.74550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.06100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       51.67050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       55.06100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       49.74550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       51.67050            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7560 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 35310 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.8 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, C                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN  99 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 160 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, THR 167 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, CYS 105 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, ASN 146 TO GLN                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, ASN 252 TO GLN                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, CYS 105 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, ASN 146 TO GLN                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, ASN 252 TO GLN                        
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     GLU A    -2                                                      
REMARK 465     THR A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     VAL A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     ASN A    27                                                      
REMARK 465     GLY A    28                                                      
REMARK 465     ASN A    29                                                      
REMARK 465     ASN A    30                                                      
REMARK 465     PHE A    31                                                      
REMARK 465     PHE A    32                                                      
REMARK 465     GLU A    33                                                      
REMARK 465     VAL A    34                                                      
REMARK 465     SER A    35                                                      
REMARK 465     GLN A    71                                                      
REMARK 465     GLN A    72                                                      
REMARK 465     VAL A    73                                                      
REMARK 465     ARG A   174                                                      
REMARK 465     GLU A   175                                                      
REMARK 465     LYS A   176                                                      
REMARK 465     GLY A   177                                                      
REMARK 465     THR A   178                                                      
REMARK 465     LYS A   179                                                      
REMARK 465     HIS A   180                                                      
REMARK 465     HIS A   181                                                      
REMARK 465     HIS A   182                                                      
REMARK 465     HIS A   183                                                      
REMARK 465     HIS A   184                                                      
REMARK 465     HIS A   185                                                      
REMARK 465     ASP B   222                                                      
REMARK 465     ILE B   223                                                      
REMARK 465     VAL B   224                                                      
REMARK 465     ALA B   225                                                      
REMARK 465     SER B   226                                                      
REMARK 465     ARG B   227                                                      
REMARK 465     ASP B   228                                                      
REMARK 465     ALA B   282                                                      
REMARK 465     SER B   283                                                      
REMARK 465     THR B   284                                                      
REMARK 465     THR B   285                                                      
REMARK 465     GLN B   286                                                      
REMARK 465     GLU B   287                                                      
REMARK 465     GLY B   288                                                      
REMARK 465     GLU B   289                                                      
REMARK 465     PRO B   454                                                      
REMARK 465     GLY B   455                                                      
REMARK 465     SER B   456                                                      
REMARK 465     HIS B   480                                                      
REMARK 465     ASN B   481                                                      
REMARK 465     GLU B   482                                                      
REMARK 465     VAL B   483                                                      
REMARK 465     GLN B   484                                                      
REMARK 465     SER B   501                                                      
REMARK 465     GLY B   502                                                      
REMARK 465     THR B   512                                                      
REMARK 465     ARG B   513                                                      
REMARK 465     ALA B   514                                                      
REMARK 465     GLU B   515                                                      
REMARK 465     TRP B   516                                                      
REMARK 465     GLU B   517                                                      
REMARK 465     GLN B   518                                                      
REMARK 465     LYS B   519                                                      
REMARK 465     ASP B   520                                                      
REMARK 465     GLU B   521                                                      
REMARK 465     VAL B   543                                                      
REMARK 465     ASN B   544                                                      
REMARK 465     PRO B   545                                                      
REMARK 465     GLY B   546                                                      
REMARK 465     LYS B   547                                                      
REMARK 465     ASP D   222                                                      
REMARK 465     ILE D   223                                                      
REMARK 465     VAL D   224                                                      
REMARK 465     ALA D   225                                                      
REMARK 465     SER D   226                                                      
REMARK 465     ARG D   227                                                      
REMARK 465     ALA D   282                                                      
REMARK 465     SER D   283                                                      
REMARK 465     THR D   284                                                      
REMARK 465     THR D   285                                                      
REMARK 465     GLN D   286                                                      
REMARK 465     GLU D   287                                                      
REMARK 465     GLY D   288                                                      
REMARK 465     GLU D   289                                                      
REMARK 465     TYR D   316                                                      
REMARK 465     GLN D   317                                                      
REMARK 465     GLY D   318                                                      
REMARK 465     ASP D   330                                                      
REMARK 465     SER D   331                                                      
REMARK 465     GLU D   452                                                      
REMARK 465     TRP D   453                                                      
REMARK 465     PRO D   454                                                      
REMARK 465     GLY D   455                                                      
REMARK 465     SER D   456                                                      
REMARK 465     ASN D   481                                                      
REMARK 465     GLU D   482                                                      
REMARK 465     VAL D   483                                                      
REMARK 465     LYS D   499                                                      
REMARK 465     GLY D   500                                                      
REMARK 465     SER D   501                                                      
REMARK 465     ASP D   520                                                      
REMARK 465     GLU D   521                                                      
REMARK 465     VAL D   543                                                      
REMARK 465     ASN D   544                                                      
REMARK 465     PRO D   545                                                      
REMARK 465     GLY D   546                                                      
REMARK 465     LYS D   547                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A   4    CG   CD   CE   NZ                                   
REMARK 470     LYS A   6    CD   CE   NZ                                        
REMARK 470     LYS A  18    CE   NZ                                             
REMARK 470     SER A  36    CB   OG                                             
REMARK 470     LYS A  38    CG   CD   CE   NZ                                   
REMARK 470     GLU A  47    CG   CD   OE1  OE2                                  
REMARK 470     VAL A  56    CG1  CG2                                            
REMARK 470     ASN A  57    OD1  ND2                                            
REMARK 470     LYS A  59    CG   CD   CE   NZ                                   
REMARK 470     LYS A  67    NZ                                                  
REMARK 470     GLN A  69    CG   CD   OE1  NE2                                  
REMARK 470     ALA A  74    CB                                                  
REMARK 470     GLU A  75    CB   CG   CD   OE1  OE2                             
REMARK 470     SER A  76    CB   OG                                             
REMARK 470     SER A  85    OG                                                  
REMARK 470     MET A  98    CG   SD   CE                                        
REMARK 470     GLU A  99    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 101    OE1  NE2                                            
REMARK 470     ARG A 111    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     ASN A 112    CG   OD1  ND2                                       
REMARK 470     LYS A 122    CG   CD   CE   NZ                                   
REMARK 470     GLU A 125    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 128    CE   NZ                                             
REMARK 470     ALA A 135    CB                                                  
REMARK 470     THR A 139    OG1  CG2                                            
REMARK 470     ASN A 140    CG   OD1  ND2                                       
REMARK 470     GLU A 144    CB   CG   CD   OE1  OE2                             
REMARK 470     LYS A 154    CE   NZ                                             
REMARK 470     GLN A 157    CD   OE1  NE2                                       
REMARK 470     GLU A 161    CD   OE1  OE2                                       
REMARK 470     GLU A 163    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 170    CD1                                                 
REMARK 470     LYS A 171    CG   CD   CE   NZ                                   
REMARK 470     PHE B 229    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     THR B 230    CB   OG1  CG2                                       
REMARK 470     LYS B 235    CE   NZ                                             
REMARK 470     ASP B 242    OD1  OD2                                            
REMARK 470     SER B 257    OG                                                  
REMARK 470     ILE B 264    CG1  CG2  CD1                                       
REMARK 470     GLN B 273    CG   CD   OE1  NE2                                  
REMARK 470     MET B 275    CE                                                  
REMARK 470     ASP B 278    OD1  OD2                                            
REMARK 470     LEU B 279    CD1  CD2                                            
REMARK 470     SER B 280    CB   OG                                             
REMARK 470     THR B 281    OG1  CG2                                            
REMARK 470     LEU B 290    CG   CD1  CD2                                       
REMARK 470     THR B 293    OG1  CG2                                            
REMARK 470     GLN B 294    OE1  NE2                                            
REMARK 470     GLU B 296    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 302    CG   CD   CE   NZ                                   
REMARK 470     SER B 306    OG                                                  
REMARK 470     GLN B 317    CD   OE1  NE2                                       
REMARK 470     HIS B 319    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS B 326    CE   NZ                                             
REMARK 470     LYS B 327    NZ                                                  
REMARK 470     ILE B 350    CD1                                                 
REMARK 470     ARG B 351    NH1  NH2                                            
REMARK 470     LYS B 352    CD   CE   NZ                                        
REMARK 470     SER B 353    OG                                                  
REMARK 470     SER B 366    OG                                                  
REMARK 470     THR B 369    OG1  CG2                                            
REMARK 470     LYS B 380    CB   CG   CD   CE   NZ                              
REMARK 470     VAL B 382    CG1  CG2                                            
REMARK 470     ASN B 383    CB   CG   OD1  ND2                                  
REMARK 470     LYS B 388    CD   CE   NZ                                        
REMARK 470     LYS B 391    CD   CE   NZ                                        
REMARK 470     GLN B 392    CD   OE1  NE2                                       
REMARK 470     ARG B 393    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG B 408    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 417    OE1  NE2                                            
REMARK 470     ARG B 427    CZ   NH1  NH2                                       
REMARK 470     LYS B 435    NZ                                                  
REMARK 470     ALA B 441    CB                                                  
REMARK 470     ALA B 442    CB                                                  
REMARK 470     ALA B 447    CB                                                  
REMARK 470     THR B 450    CB   OG1  CG2                                       
REMARK 470     GLU B 452    CB   CG   CD   OE1  OE2                             
REMARK 470     TRP B 453    CD1  CD2  NE1  CE2  CE3  CZ2  CZ3                   
REMARK 470     TRP B 453    CH2                                                 
REMARK 470     ARG B 457    CZ   NH1  NH2                                       
REMARK 470     ASP B 458    CG   OD1  OD2                                       
REMARK 470     LYS B 459    CG   CD   CE   NZ                                   
REMARK 470     ARG B 460    CD   NE   CZ   NH1  NH2                             
REMARK 470     LEU B 462    CD1  CD2                                            
REMARK 470     GLN B 467    OE1  NE2                                            
REMARK 470     ILE B 474    CG1  CG2  CD1                                       
REMARK 470     VAL B 476    CG1  CG2                                            
REMARK 470     GLN B 477    OE1  NE2                                            
REMARK 470     LEU B 485    CD1  CD2                                            
REMARK 470     ARG B 489    CZ   NH1  NH2                                       
REMARK 470     GLN B 494    CD   OE1  NE2                                       
REMARK 470     LYS B 497    CG   CD   CE   NZ                                   
REMARK 470     THR B 498    CB   OG1  CG2                                       
REMARK 470     LYS B 499    CG   CD   CE   NZ                                   
REMARK 470     ARG B 508    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B 511    CB   CG1  CG2                                       
REMARK 470     PHE B 522    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE B 523    CD1                                                 
REMARK 470     ARG B 525    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ALA B 530    CB                                                  
REMARK 470     ALA B 531    CB                                                  
REMARK 470     SER B 532    CB   OG                                             
REMARK 470     PRO B 533    CB   CG   CD                                        
REMARK 470     SER B 534    OG                                                  
REMARK 470     VAL B 537    CG1  CG2                                            
REMARK 470     GLN B 538    OE1  NE2                                            
REMARK 470     VAL B 541    CG1  CG2                                            
REMARK 470     SER B 542    CB   OG                                             
REMARK 470     ASP D 228    CB   CG   OD1  OD2                                  
REMARK 470     THR D 230    OG1  CG2                                            
REMARK 470     LYS D 235    CE   NZ                                             
REMARK 470     ASP D 242    CG   OD1  OD2                                       
REMARK 470     THR D 250    OG1  CG2                                            
REMARK 470     GLN D 252    OE1  NE2                                            
REMARK 470     THR D 260    OG1  CG2                                            
REMARK 470     GLN D 265    CG   CD   OE1  NE2                                  
REMARK 470     GLN D 273    CG   CD   OE1  NE2                                  
REMARK 470     VAL D 274    CB   CG1  CG2                                       
REMARK 470     MET D 275    CB   CG   SD   CE                                   
REMARK 470     ASP D 278    CB   CG   OD1  OD2                                  
REMARK 470     LEU D 279    CD1  CD2                                            
REMARK 470     LEU D 290    CD1  CD2                                            
REMARK 470     SER D 292    OG                                                  
REMARK 470     GLN D 294    CG   CD   OE1  NE2                                  
REMARK 470     SER D 300    OG                                                  
REMARK 470     LYS D 302    CG   CD   CE   NZ                                   
REMARK 470     HIS D 319    CG   ND1  CD2  CE1  NE2                             
REMARK 470     THR D 325    OG1  CG2                                            
REMARK 470     LYS D 327    CE   NZ                                             
REMARK 470     ASN D 332    CB   CG   OD1  ND2                                  
REMARK 470     ARG D 334    CZ   NH1  NH2                                       
REMARK 470     VAL D 336    CG1  CG2                                            
REMARK 470     ARG D 342    CZ   NH1  NH2                                       
REMARK 470     ILE D 350    CD1                                                 
REMARK 470     ARG D 351    NE   CZ   NH1  NH2                                  
REMARK 470     SER D 353    OG                                                  
REMARK 470     LYS D 367    CB   CG   CD   CE   NZ                              
REMARK 470     THR D 369    OG1  CG2                                            
REMARK 470     GLN D 371    OE1  NE2                                            
REMARK 470     ALA D 377    CB                                                  
REMARK 470     LYS D 380    CB   CG   CD   CE   NZ                              
REMARK 470     ASN D 383    CG   OD1  ND2                                       
REMARK 470     SER D 385    OG                                                  
REMARK 470     GLU D 390    OE1  OE2                                            
REMARK 470     LYS D 391    CG   CD   CE   NZ                                   
REMARK 470     ARG D 393    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU D 397    CD1  CD2                                            
REMARK 470     ARG D 408    NE   CZ   NH1  NH2                                  
REMARK 470     ARG D 419    CZ   NH1  NH2                                       
REMARK 470     HIS D 424    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG D 427    CZ   NH1  NH2                                       
REMARK 470     MET D 430    CE                                                  
REMARK 470     THR D 434    OG1  CG2                                            
REMARK 470     LYS D 435    CG   CD   CE   NZ                                   
REMARK 470     ALA D 447    CB                                                  
REMARK 470     ASP D 458    OD1  OD2                                            
REMARK 470     LYS D 459    CG   CD   CE   NZ                                   
REMARK 470     ARG D 460    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     LEU D 462    CG   CD1  CD2                                       
REMARK 470     LEU D 465    CG   CD1  CD2                                       
REMARK 470     ILE D 466    CG1  CG2  CD1                                       
REMARK 470     ASN D 468    OD1  ND2                                            
REMARK 470     MET D 470    CE                                                  
REMARK 470     GLU D 472    CB   CG   CD   OE1  OE2                             
REMARK 470     GLN D 484    CG   CD   OE1  NE2                                  
REMARK 470     LEU D 485    CG   CD1  CD2                                       
REMARK 470     ARG D 489    CZ   NH1  NH2                                       
REMARK 470     SER D 491    OG                                                  
REMARK 470     ARG D 496    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 497    CG   CD   CE   NZ                                   
REMARK 470     THR D 498    CB   OG1  CG2                                       
REMARK 470     SER D 507    OG                                                  
REMARK 470     ARG D 508    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 515    CB   CG   CD   OE1  OE2                             
REMARK 470     TRP D 516    CD1  CD2  NE1  CE2  CE3  CZ2  CZ3                   
REMARK 470     TRP D 516    CH2                                                 
REMARK 470     GLU D 517    CB   CG   CD   OE1  OE2                             
REMARK 470     GLN D 518    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 519    CD   CE   NZ                                        
REMARK 470     ALA D 530    CB                                                  
REMARK 470     SER D 532    CB   OG                                             
REMARK 470     PRO D 533    CB   CG   CD                                        
REMARK 470     SER D 534    CB   OG                                             
REMARK 470     GLN D 535    CD   OE1  NE2                                       
REMARK 470     THR D 536    OG1  CG2                                            
REMARK 470     GLN D 538    CB   CG   CD   OE1  NE2                             
REMARK 470     ARG D 539    NE   CZ   NH1  NH2                                  
REMARK 470     VAL D 541    CB   CG1  CG2                                       
REMARK 470     SER D 542    CB   OG                                             
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 B 533   C   -  N   -  CA  ANGL. DEV. =  20.8 DEGREES          
REMARK 500    PRO D 533   C   -  N   -  CA  ANGL. DEV. =  28.0 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  42      -14.42     65.94                                   
REMARK 500    GLU A  47       36.21    -78.81                                   
REMARK 500    ASN A  57       85.72     33.60                                   
REMARK 500    GLU A  77      173.57    -43.12                                   
REMARK 500    ASP A  86     -171.13   -175.37                                   
REMARK 500    GLU A  99      139.83    -25.35                                   
REMARK 500    ARG A 111     -136.16     63.71                                   
REMARK 500    LYS A 117       49.09     39.29                                   
REMARK 500    ALA A 141      104.40    -42.19                                   
REMARK 500    GLN A 157       -5.75     80.94                                   
REMARK 500    ASP B 242      156.10    -39.88                                   
REMARK 500    PRO B 261      113.38    -37.07                                   
REMARK 500    GLN B 317       49.84     36.65                                   
REMARK 500    ASN B 332       67.21   -113.68                                   
REMARK 500    ARG B 334        9.96     51.74                                   
REMARK 500    ASP B 347      -19.83    -48.26                                   
REMARK 500    ILE B 350      -83.05    -59.32                                   
REMARK 500    LYS B 367     -130.52   -109.85                                   
REMARK 500    HIS B 384       88.81     65.98                                   
REMARK 500    GLU B 389       78.77   -104.42                                   
REMARK 500    ARG B 427     -156.25   -137.49                                   
REMARK 500    THR B 450       83.89   -152.90                                   
REMARK 500    PRO B 451      140.51    -39.27                                   
REMARK 500    ASP B 458      120.04    -32.85                                   
REMARK 500    THR B 498     -141.96    -92.28                                   
REMARK 500    GLN B 535       39.12     76.84                                   
REMARK 500    PHE D 229     -131.31    -87.91                                   
REMARK 500    THR D 230      110.81    165.40                                   
REMARK 500    PRO D 261      109.92    -40.87                                   
REMARK 500    ILE D 350      -78.54    -64.38                                   
REMARK 500    ASN D 383     -145.27    -82.14                                   
REMARK 500    GLU D 390       80.60   -153.74                                   
REMARK 500    GLU D 412       30.90    -90.93                                   
REMARK 500    ARG D 427     -159.96   -141.35                                   
REMARK 500    SER D 437     -169.39    -65.57                                   
REMARK 500    ASP D 458       28.35     94.61                                   
REMARK 500    ARG D 513       -9.64    -57.52                                   
REMARK 500    PRO D 533     -106.00    106.17                                   
REMARK 500    GLN D 535       40.29     76.46                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 MET B  470     PRO B  471                  145.27                    
REMARK 500 MET D  470     PRO D  471                  142.83                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1FP5   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF THE HUMAN IGE-FC CEPSILON3-CEPSILON4   
REMARK 900 FRAGMENT.                                                            
REMARK 900 RELATED ID: 1F6A   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE HUMAN IGE-FC BOUND TO ITS HIGH AFFINITYRECEPTOR     
REMARK 900 FC(EPSILON)RI(ALPHA)                                                 
REMARK 900 RELATED ID: 1J87   RELATED DB: PDB                                   
REMARK 900 HUMAN HIGH AFFINITY FC RECEPTOR FC(EPSILON)RI(ALPHA), HEXAGONAL      
REMARK 900 CRYSTAL FORM 1                                                       
REMARK 900 RELATED ID: 1O0V   RELATED DB: PDB                                   
REMARK 900 THE CRYSTAL STRUCTURE OF IGE FC REVEALS AN ASYMMETRICALLYBENT        
REMARK 900 CONFORMATION                                                         
REMARK 900 RELATED ID: 1J88   RELATED DB: PDB                                   
REMARK 900 HUMAN HIGH AFFINITY FC RECEPTOR FC(EPSILON)RI(ALPHA), TETRAGONAL     
REMARK 900 CRYSTAL FORM 1                                                       
REMARK 900 RELATED ID: 1J86   RELATED DB: PDB                                   
REMARK 900 HUMAN HIGH AFFINITY FC RECEPTOR FC(EPSILON)RI(ALPHA), MONOCLINIC     
REMARK 900 CRYSTAL FORM 2                                                       
REMARK 900 RELATED ID: 1J89   RELATED DB: PDB                                   
REMARK 900 HUMAN HIGH AFFINITY FC RECEPTOR FC(EPSILON)RI(ALPHA), TETRAGONAL     
REMARK 900 CRYSTAL FORM 2                                                       
REMARK 900 RELATED ID: 1G84   RELATED DB: PDB                                   
REMARK 900 THE SOLUTION STRUCTURE OF THE C EPSILON2 DOMAIN FROM IGE             
REMARK 900 RELATED ID: 1IGE   RELATED DB: PDB                                   
REMARK 900 FC FRAGMENT (IGE'CL) (THEORETICAL MODEL)                             
REMARK 900 RELATED ID: 1RPQ   RELATED DB: PDB                                   
REMARK 900 HIGH AFFINITY IGE RECEPTOR (ALPHA CHAIN) COMPLEXED WITHTIGHT-        
REMARK 900 BINDING E131 'ZETA' PEPTIDE FROM PHAGE DISPLAY                       
REMARK 900 RELATED ID: 1F2Q   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN HIGH-AFFINITY IGE RECEPTOR            
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 CHAIN A RESIDUES -2 TO 0 ARTEFACT FROM PHLSEC VECTOR                 
REMARK 999 CHAIN A RESIDUES 177-179 ARTEFACT FROM PHLSEC VECTOR                 
REMARK 999 CHAIN A RESIDUES 180-185 C-TERMINAL HIS TAG                          
REMARK 999 CHAIN B RESIDUES 222-223 VECTOR LEADER SEQUENCE                      
REMARK 999 CHAIN D RESIDUES 222-223 VECTOR LEADER SEQUENCE                      
REMARK 999 SEQUENCE DISCREPANCIES ARE FOR THE SO-CALLED TRIPLE                  
REMARK 999 GLYCOSYLATION MUTANT.                                                
REMARK 999 SEQUENCE DISCREPANCIES ARE FOR GLYCOLSYLATION AND                    
REMARK 999 DISULPHIDE BOND MUTANTS. CHAIN A V143A CLONING ARTIFACT.             
DBREF  2Y7Q A    1   176  UNP    P12319   FCERA_HUMAN     26    201             
DBREF  2Y7Q B  224   547  UNP    P01854   IGHE_HUMAN     104    428             
DBREF  2Y7Q D  224   547  UNP    P01854   IGHE_HUMAN     104    428             
SEQADV 2Y7Q GLU A   -2  UNP  P12319              CLONING ARTIFACT               
SEQADV 2Y7Q THR A   -1  UNP  P12319              CLONING ARTIFACT               
SEQADV 2Y7Q GLY A    0  UNP  P12319              CLONING ARTIFACT               
SEQADV 2Y7Q ALA A   74  UNP  P12319    ASN    99 ENGINEERED MUTATION            
SEQADV 2Y7Q ALA A  135  UNP  P12319    ASN   160 ENGINEERED MUTATION            
SEQADV 2Y7Q ALA A  142  UNP  P12319    THR   167 ENGINEERED MUTATION            
SEQADV 2Y7Q ALA A  143  UNP  P12319    VAL   168 CLONING ARTIFACT               
SEQADV 2Y7Q GLY A  177  UNP  P12319              CLONING ARTIFACT               
SEQADV 2Y7Q THR A  178  UNP  P12319              CLONING ARTIFACT               
SEQADV 2Y7Q LYS A  179  UNP  P12319              CLONING ARTIFACT               
SEQADV 2Y7Q HIS A  180  UNP  P12319              EXPRESSION TAG                 
SEQADV 2Y7Q HIS A  181  UNP  P12319              EXPRESSION TAG                 
SEQADV 2Y7Q HIS A  182  UNP  P12319              EXPRESSION TAG                 
SEQADV 2Y7Q HIS A  183  UNP  P12319              EXPRESSION TAG                 
SEQADV 2Y7Q HIS A  184  UNP  P12319              EXPRESSION TAG                 
SEQADV 2Y7Q HIS A  185  UNP  P12319              EXPRESSION TAG                 
SEQADV 2Y7Q ASP B  222  UNP  P01854              EXPRESSION TAG                 
SEQADV 2Y7Q ILE B  223  UNP  P01854              EXPRESSION TAG                 
SEQADV 2Y7Q ALA B  225  UNP  P01854    CYS   105 ENGINEERED MUTATION            
SEQADV 2Y7Q GLN B  265  UNP  P01854    ASN   146 ENGINEERED MUTATION            
SEQADV 2Y7Q GLN B  371  UNP  P01854    ASN   252 ENGINEERED MUTATION            
SEQADV 2Y7Q ASP D  222  UNP  P01854              EXPRESSION TAG                 
SEQADV 2Y7Q ILE D  223  UNP  P01854              EXPRESSION TAG                 
SEQADV 2Y7Q ALA D  225  UNP  P01854    CYS   105 ENGINEERED MUTATION            
SEQADV 2Y7Q GLN D  265  UNP  P01854    ASN   146 ENGINEERED MUTATION            
SEQADV 2Y7Q GLN D  371  UNP  P01854    ASN   252 ENGINEERED MUTATION            
SEQRES   1 A  188  GLU THR GLY VAL PRO GLN LYS PRO LYS VAL SER LEU ASN          
SEQRES   2 A  188  PRO PRO TRP ASN ARG ILE PHE LYS GLY GLU ASN VAL THR          
SEQRES   3 A  188  LEU THR CYS ASN GLY ASN ASN PHE PHE GLU VAL SER SER          
SEQRES   4 A  188  THR LYS TRP PHE HIS ASN GLY SER LEU SER GLU GLU THR          
SEQRES   5 A  188  ASN SER SER LEU ASN ILE VAL ASN ALA LYS PHE GLU ASP          
SEQRES   6 A  188  SER GLY GLU TYR LYS CYS GLN HIS GLN GLN VAL ALA GLU          
SEQRES   7 A  188  SER GLU PRO VAL TYR LEU GLU VAL PHE SER ASP TRP LEU          
SEQRES   8 A  188  LEU LEU GLN ALA SER ALA GLU VAL VAL MET GLU GLY GLN          
SEQRES   9 A  188  PRO LEU PHE LEU ARG CYS HIS GLY TRP ARG ASN TRP ASP          
SEQRES  10 A  188  VAL TYR LYS VAL ILE TYR TYR LYS ASP GLY GLU ALA LEU          
SEQRES  11 A  188  LYS TYR TRP TYR GLU ASN HIS ALA ILE SER ILE THR ASN          
SEQRES  12 A  188  ALA ALA ALA GLU ASP SER GLY THR TYR TYR CYS THR GLY          
SEQRES  13 A  188  LYS VAL TRP GLN LEU ASP TYR GLU SER GLU PRO LEU ASN          
SEQRES  14 A  188  ILE THR VAL ILE LYS ALA PRO ARG GLU LYS GLY THR LYS          
SEQRES  15 A  188  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 B  327  ASP ILE VAL ALA SER ARG ASP PHE THR PRO PRO THR VAL          
SEQRES   2 B  327  LYS ILE LEU GLN SER SER CYS ASP GLY GLY GLY HIS PHE          
SEQRES   3 B  327  PRO PRO THR ILE GLN LEU LEU CYS LEU VAL SER GLY TYR          
SEQRES   4 B  327  THR PRO GLY THR ILE GLN ILE THR TRP LEU GLU ASP GLY          
SEQRES   5 B  327  GLN VAL MET ASP VAL ASP LEU SER THR ALA SER THR THR          
SEQRES   6 B  327  GLN GLU GLY GLU LEU ALA SER THR GLN SER GLU LEU THR          
SEQRES   7 B  327  LEU SER GLN LYS HIS TRP LEU SER ASP ARG THR TYR THR          
SEQRES   8 B  327  CYS GLN VAL THR TYR GLN GLY HIS THR PHE GLU ASP SER          
SEQRES   9 B  327  THR LYS LYS CYS ALA ASP SER ASN PRO ARG GLY VAL SER          
SEQRES  10 B  327  ALA TYR LEU SER ARG PRO SER PRO PHE ASP LEU PHE ILE          
SEQRES  11 B  327  ARG LYS SER PRO THR ILE THR CYS LEU VAL VAL ASP LEU          
SEQRES  12 B  327  ALA PRO SER LYS GLY THR VAL GLN LEU THR TRP SER ARG          
SEQRES  13 B  327  ALA SER GLY LYS PRO VAL ASN HIS SER THR ARG LYS GLU          
SEQRES  14 B  327  GLU LYS GLN ARG ASN GLY THR LEU THR VAL THR SER THR          
SEQRES  15 B  327  LEU PRO VAL GLY THR ARG ASP TRP ILE GLU GLY GLU THR          
SEQRES  16 B  327  TYR GLN CYS ARG VAL THR HIS PRO HIS LEU PRO ARG ALA          
SEQRES  17 B  327  LEU MET ARG SER THR THR LYS THR SER GLY PRO ARG ALA          
SEQRES  18 B  327  ALA PRO GLU VAL TYR ALA PHE ALA THR PRO GLU TRP PRO          
SEQRES  19 B  327  GLY SER ARG ASP LYS ARG THR LEU ALA CYS LEU ILE GLN          
SEQRES  20 B  327  ASN PHE MET PRO GLU ASP ILE SER VAL GLN TRP LEU HIS          
SEQRES  21 B  327  ASN GLU VAL GLN LEU PRO ASP ALA ARG HIS SER THR THR          
SEQRES  22 B  327  GLN PRO ARG LYS THR LYS GLY SER GLY PHE PHE VAL PHE          
SEQRES  23 B  327  SER ARG LEU GLU VAL THR ARG ALA GLU TRP GLU GLN LYS          
SEQRES  24 B  327  ASP GLU PHE ILE CYS ARG ALA VAL HIS GLU ALA ALA SER          
SEQRES  25 B  327  PRO SER GLN THR VAL GLN ARG ALA VAL SER VAL ASN PRO          
SEQRES  26 B  327  GLY LYS                                                      
SEQRES   1 D  327  ASP ILE VAL ALA SER ARG ASP PHE THR PRO PRO THR VAL          
SEQRES   2 D  327  LYS ILE LEU GLN SER SER CYS ASP GLY GLY GLY HIS PHE          
SEQRES   3 D  327  PRO PRO THR ILE GLN LEU LEU CYS LEU VAL SER GLY TYR          
SEQRES   4 D  327  THR PRO GLY THR ILE GLN ILE THR TRP LEU GLU ASP GLY          
SEQRES   5 D  327  GLN VAL MET ASP VAL ASP LEU SER THR ALA SER THR THR          
SEQRES   6 D  327  GLN GLU GLY GLU LEU ALA SER THR GLN SER GLU LEU THR          
SEQRES   7 D  327  LEU SER GLN LYS HIS TRP LEU SER ASP ARG THR TYR THR          
SEQRES   8 D  327  CYS GLN VAL THR TYR GLN GLY HIS THR PHE GLU ASP SER          
SEQRES   9 D  327  THR LYS LYS CYS ALA ASP SER ASN PRO ARG GLY VAL SER          
SEQRES  10 D  327  ALA TYR LEU SER ARG PRO SER PRO PHE ASP LEU PHE ILE          
SEQRES  11 D  327  ARG LYS SER PRO THR ILE THR CYS LEU VAL VAL ASP LEU          
SEQRES  12 D  327  ALA PRO SER LYS GLY THR VAL GLN LEU THR TRP SER ARG          
SEQRES  13 D  327  ALA SER GLY LYS PRO VAL ASN HIS SER THR ARG LYS GLU          
SEQRES  14 D  327  GLU LYS GLN ARG ASN GLY THR LEU THR VAL THR SER THR          
SEQRES  15 D  327  LEU PRO VAL GLY THR ARG ASP TRP ILE GLU GLY GLU THR          
SEQRES  16 D  327  TYR GLN CYS ARG VAL THR HIS PRO HIS LEU PRO ARG ALA          
SEQRES  17 D  327  LEU MET ARG SER THR THR LYS THR SER GLY PRO ARG ALA          
SEQRES  18 D  327  ALA PRO GLU VAL TYR ALA PHE ALA THR PRO GLU TRP PRO          
SEQRES  19 D  327  GLY SER ARG ASP LYS ARG THR LEU ALA CYS LEU ILE GLN          
SEQRES  20 D  327  ASN PHE MET PRO GLU ASP ILE SER VAL GLN TRP LEU HIS          
SEQRES  21 D  327  ASN GLU VAL GLN LEU PRO ASP ALA ARG HIS SER THR THR          
SEQRES  22 D  327  GLN PRO ARG LYS THR LYS GLY SER GLY PHE PHE VAL PHE          
SEQRES  23 D  327  SER ARG LEU GLU VAL THR ARG ALA GLU TRP GLU GLN LYS          
SEQRES  24 D  327  ASP GLU PHE ILE CYS ARG ALA VAL HIS GLU ALA ALA SER          
SEQRES  25 D  327  PRO SER GLN THR VAL GLN ARG ALA VAL SER VAL ASN PRO          
SEQRES  26 D  327  GLY LYS                                                      
MODRES 2Y7Q ASN A   21  ASN  GLYCOSYLATION SITE                                 
MODRES 2Y7Q ASN A   42  ASN  GLYCOSYLATION SITE                                 
MODRES 2Y7Q ASN B  394  ASN  GLYCOSYLATION SITE                                 
MODRES 2Y7Q ASN D  394  ASN  GLYCOSYLATION SITE                                 
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET    BMA  C   3      11                                                       
HET    MAN  C   4      11                                                       
HET    NAG  A 201      14                                                       
HET    NAG  B 601      14                                                       
HET    NAG  D 601      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
FORMUL   4  NAG    5(C8 H15 N O6)                                               
FORMUL   4  BMA    C6 H12 O6                                                    
FORMUL   4  MAN    C6 H12 O6                                                    
HELIX    1 AA1 LYS A   59  SER A   63  5                                   5    
HELIX    2 AA2 ALA A  142  SER A  146  5                                   5    
HELIX    3 AA3 GLN B  301  LEU B  305  1                                   5    
HELIX    4 AA4 ASN B  332  VAL B  336  5                                   5    
HELIX    5 AA5 SER B  344  PHE B  349  1                                   6    
HELIX    6 AA6 GLY B  406  GLU B  412  1                                   7    
HELIX    7 AA7 GLN D  301  SER D  306  1                                   6    
HELIX    8 AA8 SER D  344  PHE D  349  1                                   6    
HELIX    9 AA9 GLY D  406  GLU D  412  1                                   7    
SHEET    1 AA1 3 SER A   8  ASN A  10  0                                        
SHEET    2 AA1 3 VAL A  22  THR A  25 -1  O  THR A  25   N  SER A   8           
SHEET    3 AA1 3 SER A  52  ILE A  55 -1  O  LEU A  53   N  LEU A  24           
SHEET    1 AA2 5 ARG A  15  PHE A  17  0                                        
SHEET    2 AA2 5 SER A  76  PHE A  84  1  O  PHE A  84   N  ILE A  16           
SHEET    3 AA2 5 GLY A  64  GLN A  69 -1  N  CYS A  68   O  SER A  76           
SHEET    4 AA2 5 LYS A  38  HIS A  41 -1  N  PHE A  40   O  LYS A  67           
SHEET    5 AA2 5 SER A  44  SER A  46 -1  O  SER A  46   N  TRP A  39           
SHEET    1 AA3 3 LEU A  88  ALA A  92  0                                        
SHEET    2 AA3 3 LEU A 103  GLY A 109 -1  O  HIS A 108   N  LEU A  89           
SHEET    3 AA3 3 ALA A 135  ILE A 138 -1  O  ILE A 138   N  LEU A 103           
SHEET    1 AA4 5 VAL A  96  VAL A  97  0                                        
SHEET    2 AA4 5 LEU A 165  VAL A 169  1  O  THR A 168   N  VAL A  97           
SHEET    3 AA4 5 GLY A 147  VAL A 155 -1  N  TYR A 149   O  LEU A 165           
SHEET    4 AA4 5 VAL A 115  LYS A 122 -1  N  TYR A 121   O  TYR A 150           
SHEET    5 AA4 5 GLU A 125  TRP A 130 -1  O  LEU A 127   N  TYR A 120           
SHEET    1 AA5 4 VAL A  96  VAL A  97  0                                        
SHEET    2 AA5 4 LEU A 165  VAL A 169  1  O  THR A 168   N  VAL A  97           
SHEET    3 AA5 4 GLY A 147  VAL A 155 -1  N  TYR A 149   O  LEU A 165           
SHEET    4 AA5 4 LEU A 158  GLU A 161 -1  O  TYR A 160   N  GLY A 153           
SHEET    1 AA6 6 ALA B 291  SER B 300  0                                        
SHEET    2 AA6 6 THR B 250  TYR B 259 -1  N  LEU B 253   O  LEU B 297           
SHEET    3 AA6 6 THR B 233  SER B 239 -1  N  LYS B 235   O  LEU B 255           
SHEET    4 AA6 6 THR D 233  SER D 239 -1  O  GLN D 238   N  GLN B 238           
SHEET    5 AA6 6 THR D 250  TYR D 259 -1  O  LEU D 253A  N  LEU D 237           
SHEET    6 AA6 6 ALA D 291  SER D 300 -1  O  THR D 293   N  VAL D 256           
SHEET    1 AA7 4 GLN B 273  SER B 280  0                                        
SHEET    2 AA7 4 ILE B 264  GLU B 270 -1  N  TRP B 268   O  MET B 275           
SHEET    3 AA7 4 TYR B 310  TYR B 316 -1  O  GLN B 313   N  THR B 267           
SHEET    4 AA7 4 THR B 320  THR B 325 -1  O  PHE B 321   N  VAL B 314           
SHEET    1 AA8 4 SER B 337  LEU B 340  0                                        
SHEET    2 AA8 4 THR B 355  LEU B 363 -1  O  LEU B 359   N  TYR B 339           
SHEET    3 AA8 4 LEU B 397  PRO B 404 -1  O  LEU B 397   N  LEU B 363           
SHEET    4 AA8 4 LYS B 388  LYS B 391 -1  N  LYS B 388   O  THR B 400           
SHEET    1 AA9 3 GLN B 371  ARG B 376  0                                        
SHEET    2 AA9 3 TYR B 416  THR B 421 -1  O  GLN B 417   N  SER B 375           
SHEET    3 AA9 3 LEU B 429  ARG B 431 -1  O  ARG B 431   N  CYS B 418           
SHEET    1 AB1 4 ALA B 447  ALA B 449  0                                        
SHEET    2 AB1 4 ARG B 460  GLN B 467 -1  O  ALA B 463   N  PHE B 448           
SHEET    3 AB1 4 PHE B 504  VAL B 511 -1  O  LEU B 509   N  LEU B 462           
SHEET    4 AB1 4 HIS B 490  THR B 492 -1  N  SER B 491   O  ARG B 508           
SHEET    1 AB2 3 ILE B 474  LEU B 479  0                                        
SHEET    2 AB2 3 ILE B 523  HIS B 528 -1  O  VAL B 527   N  SER B 475           
SHEET    3 AB2 3 VAL B 537  ALA B 540 -1  O  VAL B 537   N  ALA B 526           
SHEET    1 AB3 4 GLN D 273  SER D 280  0                                        
SHEET    2 AB3 4 ILE D 264  GLU D 270 -1  N  ILE D 264   O  SER D 280           
SHEET    3 AB3 4 TYR D 310  THR D 315 -1  O  GLN D 313   N  THR D 267           
SHEET    4 AB3 4 PHE D 321  THR D 325 -1  O  PHE D 321   N  VAL D 314           
SHEET    1 AB4 3 SER D 337  LEU D 340  0                                        
SHEET    2 AB4 3 THR D 355  LEU D 363 -1  O  LEU D 359   N  TYR D 339           
SHEET    3 AB4 3 LEU D 397  PRO D 404 -1  O  VAL D 399   N  VAL D 360           
SHEET    1 AB5 3 GLN D 371  ARG D 376  0                                        
SHEET    2 AB5 3 THR D 415  THR D 421 -1  O  GLN D 417   N  SER D 375           
SHEET    3 AB5 3 LEU D 429  THR D 434 -1  O  LEU D 429   N  VAL D 420           
SHEET    1 AB6 4 ALA D 447  ALA D 449  0                                        
SHEET    2 AB6 4 LEU D 462  PHE D 469 -1  O  ALA D 463   N  PHE D 448           
SHEET    3 AB6 4 PHE D 503  LEU D 509 -1  O  LEU D 509   N  LEU D 462           
SHEET    4 AB6 4 HIS D 490  THR D 492 -1  N  SER D 491   O  ARG D 508           
SHEET    1 AB7 3 ILE D 474  LEU D 479  0                                        
SHEET    2 AB7 3 ILE D 523  HIS D 528 -1  O  VAL D 527   N  SER D 475           
SHEET    3 AB7 3 VAL D 537  ALA D 540 -1  O  ARG D 539   N  CYS D 524           
SSBOND   1 CYS A   26    CYS A   68                          1555   1555  2.04  
SSBOND   2 CYS A  107    CYS A  151                          1555   1555  2.02  
SSBOND   3 CYS B  241    CYS D  328                          1555   1555  2.02  
SSBOND   4 CYS B  254    CYS B  312                          1555   1555  2.03  
SSBOND   5 CYS B  328    CYS D  241                          1555   1555  2.03  
SSBOND   6 CYS B  358    CYS B  418                          1555   1555  2.04  
SSBOND   7 CYS B  464    CYS B  524                          1555   1555  2.04  
SSBOND   8 CYS D  254    CYS D  312                          1555   1555  2.02  
SSBOND   9 CYS D  358    CYS D  418                          1555   1555  2.03  
SSBOND  10 CYS D  464    CYS D  524                          1555   1555  2.04  
LINK         ND2 ASN A  21                 C1  NAG A 201     1555   1555  1.45  
LINK         ND2 ASN A  42                 C1  NAG C   1     1555   1555  1.44  
LINK         ND2 ASN B 394                 C1  NAG B 601     1555   1555  1.44  
LINK         ND2 ASN D 394                 C1  NAG D 601     1555   1555  1.45  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.44  
LINK         O4  NAG C   2                 C1  BMA C   3     1555   1555  1.47  
LINK         O3  BMA C   3                 C1  MAN C   4     1555   1555  1.44  
CISPEP   1 ASN A   10    PRO A   11          0        -1.99                     
CISPEP   2 SER B  532    PRO B  533          0         0.29                     
CRYST1   99.491  103.341  110.122  90.00  90.00  90.00 P 21 21 21    8          
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      0.010051  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009677  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009081        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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