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Database: PDB
Entry: 1FRT
LinkDB: 1FRT
Original site: 1FRT 
HEADER    COMPLEX (RECEPTOR/IMMUNOGLOBULIN)       11-NOV-94   1FRT              
TITLE     CRYSTAL STRUCTURE OF THE COMPLEX OF RAT NEONATAL FC RECEPTOR WITH FC  
CAVEAT     1FRT    FUC E 9 HAS WRONG CHIRALITY AT ATOM C1 FUC E 9 HAS WRONG     
CAVEAT   2 1FRT    CHIRALITY AT ATOM C5                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NEONATAL FC RECEPTOR;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: BETA 2-MICROGLOBULIN;                                      
COMPND   7 CHAIN: B;                                                            
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: IGG FC;                                                    
COMPND  11 CHAIN: C;                                                            
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 ORGAN: SERUM (MIXTURE OF SEVERAL SUBTYPES);                          
SOURCE   6 GENE: BETA-2-MICROGLOBULIN;                                          
SOURCE   7 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   8 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  10 EXPRESSION_SYSTEM_CELL_LINE: CHO;                                    
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PBJ5-GS;                                  
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  14 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE  15 ORGANISM_TAXID: 10116;                                               
SOURCE  16 ORGAN: SERUM (MIXTURE OF SEVERAL SUBTYPES);                          
SOURCE  17 GENE: BETA-2-MICROGLOBULIN;                                          
SOURCE  18 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  19 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  20 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  21 EXPRESSION_SYSTEM_CELL_LINE: CHO;                                    
SOURCE  22 EXPRESSION_SYSTEM_PLASMID: PBJ5-GS;                                  
SOURCE  23 MOL_ID: 3;                                                           
SOURCE  24 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  25 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE  26 ORGANISM_TAXID: 10116;                                               
SOURCE  27 ORGAN: SERUM (MIXTURE OF SEVERAL SUBTYPES);                          
SOURCE  28 GENE: BETA-2-MICROGLOBULIN;                                          
SOURCE  29 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  30 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  31 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  32 EXPRESSION_SYSTEM_CELL_LINE: CHO;                                    
SOURCE  33 EXPRESSION_SYSTEM_PLASMID: PBJ5-GS                                   
KEYWDS    COMPLEX (RECEPTOR-IMMUNOGLOBULIN), COMPLEX (RECEPTOR-IMMUNOGLOBULIN)  
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.P.BURMEISTER,P.J.BJORKMAN                                           
REVDAT   6   29-JUL-20 1FRT    1       CAVEAT COMPND REMARK HETNAM              
REVDAT   6 2                   1       LINK   SITE   ATOM                       
REVDAT   5   05-FEB-20 1FRT    1       CAVEAT REMARK SEQADV LINK                
REVDAT   4   13-JUL-11 1FRT    1       VERSN                                    
REVDAT   3   24-FEB-09 1FRT    1       VERSN                                    
REVDAT   2   15-MAY-95 1FRT    1       SOURCE REMARK                            
REVDAT   1   14-FEB-95 1FRT    0                                                
JRNL        AUTH   W.P.BURMEISTER,A.H.HUBER,P.J.BJORKMAN                        
JRNL        TITL   CRYSTAL STRUCTURE OF THE COMPLEX OF RAT NEONATAL FC RECEPTOR 
JRNL        TITL 2 WITH FC.                                                     
JRNL        REF    NATURE                        V. 372   379 1994              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   7969498                                                      
JRNL        DOI    10.1038/372379A0                                             
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   W.P.BURMEISTER,L.N.GASTINEL,N.E.SIMISTER,M.L.BLUM,           
REMARK   1  AUTH 2 P.J.BJORKMAN                                                 
REMARK   1  TITL   CRYSTAL STRUCTURE AT 2.2 ANGSTROMS RESOLUTION OF THE         
REMARK   1  TITL 2 MHC-RELATED NEONATAL FC RECEPTOR                             
REMARK   1  REF    NATURE                        V. 372   336 1994              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   M.RAGHAVAN,M.Y.CHEN,L.N.GASTINEL,P.J.BJORKMAN                
REMARK   1  TITL   INVESTIGATION OF THE INTERACTION BETWEEN THE CLASS I         
REMARK   1  TITL 2 MHC-RELATED FC RECEPTOR AND ITS IMMUNOGLOBULIN G LIGAND      
REMARK   1  REF    IMMUNITY                      V.   1   303 1994              
REMARK   1  REFN                   ISSN 1074-7613                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   A.H.HUBER,R.F.KELLY,L.N.GASTINEL,P.J.BJORKMAN                
REMARK   1  TITL   CRYSTALLIZATION AND STOICHIOMETRY OF BINDING OF A COMPLEX    
REMARK   1  TITL 2 BETWEEN A RAT INTESTINAL FC RECEPTOR AND FC                  
REMARK   1  REF    J.MOL.BIOL.                   V. 230  1077 1993              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   J.DEISENHOFER                                                
REMARK   1  TITL   CRYSTALLOGRAPHIC REFINEMENT AND ATOMIC MODELS OF A HUMAN FC  
REMARK   1  TITL 2 FRAGMENT AND ITS COMPLEX WITH FRAGMENT B OF PROTEIN A FROM   
REMARK   1  TITL 3 STAPHYLOCOCCUS AUREUS AT 2.9-AND 2.8-ANGSTROMS RESOLUTION    
REMARK   1  REF    BIOCHEMISTRY                  V.  20  2361 1981              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    4.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 4.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 67.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 8433                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.423                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4608                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 148                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 199.0                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1FRT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000173395.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 8527                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 67.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X,-Y+1/2,Z                                             
REMARK 290       7555   -X+1/2,Y,-Z                                             
REMARK 290       8555   X,-Y,-Z+1/2                                             
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       62.50000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      108.25000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       72.50000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      108.25000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       62.50000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       72.50000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       62.50000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       72.50000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      108.25000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       72.50000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       62.50000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      108.25000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: MTRIX                                                        
REMARK 300  THE INFORMATION PRESENTED ON SYMMETRY RECORDS BELOW                 
REMARK 300  DESCRIBE TRANSFORMATIONS TO GENERATE CRYSTALLOGRAPHIC               
REMARK 300  RELATIONSHIPS AS DESCRIBED IN THE STATEMENT THAT FOLLOWS            
REMARK 300  EACH SYMMETRY OPERATOR.                                             
REMARK 300                                                                      
REMARK 300            APPLIED TO          TRANSFORMED TO                        
REMARK 300  MTRIX   CHAIN  RESIDUES       CHAIN  RESIDUES     RMSD              
REMARK 300    S1   C    1  -  C  443     ?    1  -  ?  443                      
REMARK 300                                                                      
REMARK 300  THIS TRANSFORMATION GENERATES THE SECOND CHAIN OF THE FC            
REMARK 300  MOLECULE.  IF THE SAME OPERATION IS ALSO APPLIED TO THE             
REMARK 300  FCRN MOLECULE, THE "STANDING UP" FCRNFC COMPLEX                     
REMARK 300  DISCUSSED IN THE ACCOMPANYING PAPER IS GENERATED.                   
REMARK 300                                                                      
REMARK 300    S2   A    1  -  A  405     ?    1  -  ?  405                      
REMARK 300    S2   B    1  -  B   99     ?    1  -  ?   99                      
REMARK 300                                                                      
REMARK 300  THIS TRANSFORMATION GENERATES THE SECOND SUBUNIT FOR THE            
REMARK 300  "LYING DOWN" FC RECEPTOR DIMER PRESENTED IN THE                     
REMARK 300  ACCOMPANYING PAPER.                                                 
REMARK 300                                                                      
REMARK 300 SYMMETRY1   1  1.000000  0.000000  0.000000        0.00000           
REMARK 300 SYMMETRY2   1  0.000000 -1.000000  0.000000      145.00000           
REMARK 300 SYMMETRY3   1  0.000000  0.000000 -1.000000      108.25000           
REMARK 300 SYMMETRY1   2 -1.000000  0.000000  0.000000      250.00000           
REMARK 300 SYMMETRY2   2  0.000000 -1.000000  0.000000       72.50000           
REMARK 300 SYMMETRY3   2  0.000000  0.000000  1.000000        0.00000           
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: HEXAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E                         
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   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      145.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      108.25000            
REMARK 450                                                                      
REMARK 450 SOURCE                                                               
REMARK 450 SOURCE 1                                                             
REMARK 450  MOLECULE_NAME: FC (IGG) RECEPTOR, NEONATAL (FCRN) THE               
REMARK 450  CELL LINE SECRETES A SOLUBLE FCRN HETERODIMER COMPOSED              
REMARK 450  OF THE EXTRACELLULAR DOMAINS OF THE RAT FCRN HEAVY CHAIN            
REMARK 450  ASSOCIATED WITH RAT BETA-2-MICROGLOBULIN.                           
REMARK 450 SOURCE 2                                                             
REMARK 450  MOLECULE_NAME: FC FRAGMENT (IGG) OBTAINED FROM JACKSON              
REMARK 450  IMMUNORESEARCH LABS.  THE FC FRAGMENT IS A MIXTURE OF               
REMARK 450  SUBTYPES 1, 2A, 2B, AND 2C. THE N-TERMINUS IS NOT                   
REMARK 450  PRECISELY KNOWN, BUT THE CLEAVAGE SITE IS C-TERMINAL TO             
REMARK 450  THE DISULFIDE BONDS OF THE HINGE REGION. THE FRAGMENT IS,           
REMARK 450  THEREFORE, A NON-COVALENT DIMER.                                    
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: B1A                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR FC ON FCRN                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: B2A                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: POSSIBLE BINDING SITE FOR FC ON THE SECOND         
REMARK 800  MOLECULE OF THE FCRN DIMER                                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: B1B                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR FCRN ON FC                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: B2B                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: POSSIBLE BINDING SITE FOR FCRN ASSUMING THE        
REMARK 800  PRESENCE OF THE FCRN DIMER                                          
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THERE ARE A NUMBER OF CLOSE CONTACTS BETWEEN ATOMS IN THIS           
REMARK 999 THIS MOLECULE AND IN SYMMETRY-RELATED MOLECULES.                     
DBREF  1FRT A    1   269  UNP    P13599   FCGN_RAT        23    291             
DBREF  1FRT B    1    99  UNP    P07151   B2MG_RAT        21    119             
DBREF  1FRT C  239   443  GB     243866   AAB21181       262    466             
SEQADV 1FRT GLN C  272  GB   243866    GLU   295 CONFLICT                       
SEQADV 1FRT GLN C  283  GB   243866    GLU   306 CONFLICT                       
SEQADV 1FRT GLN C  294  GB   243866    GLU   317 CONFLICT                       
SEQADV 1FRT ASN C  312  GB   243866    ASP   335 CONFLICT                       
SEQADV 1FRT ASP C  315  GB   243866    ASN   338 CONFLICT                       
SEQADV 1FRT GLU C  356  GB   243866    ASP   379 CONFLICT                       
SEQADV 1FRT MET C  358  GB   243866    LEU   381 CONFLICT                       
SEQRES   1 A  269  ALA GLU PRO ARG LEU PRO LEU MET TYR HIS LEU ALA ALA          
SEQRES   2 A  269  VAL SER ASP LEU SER THR GLY LEU PRO SER PHE TRP ALA          
SEQRES   3 A  269  THR GLY TRP LEU GLY ALA GLN GLN TYR LEU THR TYR ASN          
SEQRES   4 A  269  ASN LEU ARG GLN GLU ALA ASP PRO CYS GLY ALA TRP ILE          
SEQRES   5 A  269  TRP GLU ASN GLN VAL SER TRP TYR TRP GLU LYS GLU THR          
SEQRES   6 A  269  THR ASP LEU LYS SER LYS GLU GLN LEU PHE LEU GLU ALA          
SEQRES   7 A  269  ILE ARG THR LEU GLU ASN GLN ILE ASN GLY THR PHE THR          
SEQRES   8 A  269  LEU GLN GLY LEU LEU GLY CYS GLU LEU ALA PRO ASP ASN          
SEQRES   9 A  269  SER SER LEU PRO THR ALA VAL PHE ALA LEU ASN GLY GLU          
SEQRES  10 A  269  GLU PHE MET ARG PHE ASN PRO ARG THR GLY ASN TRP SER          
SEQRES  11 A  269  GLY GLU TRP PRO GLU THR ASP ILE VAL GLY ASN LEU TRP          
SEQRES  12 A  269  MET LYS GLN PRO GLU ALA ALA ARG LYS GLU SER GLU PHE          
SEQRES  13 A  269  LEU LEU THR SER CYS PRO GLU ARG LEU LEU GLY HIS LEU          
SEQRES  14 A  269  GLU ARG GLY ARG GLN ASN LEU GLU TRP LYS GLU PRO PRO          
SEQRES  15 A  269  SER MET ARG LEU LYS ALA ARG PRO GLY ASN SER GLY SER          
SEQRES  16 A  269  SER VAL LEU THR CYS ALA ALA PHE SER PHE TYR PRO PRO          
SEQRES  17 A  269  GLU LEU LYS PHE ARG PHE LEU ARG ASN GLY LEU ALA SER          
SEQRES  18 A  269  GLY SER GLY ASN CYS SER THR GLY PRO ASN GLY ASP GLY          
SEQRES  19 A  269  SER PHE HIS ALA TRP SER LEU LEU GLU VAL LYS ARG GLY          
SEQRES  20 A  269  ASP GLU HIS HIS TYR GLN CYS GLN VAL GLU HIS GLU GLY          
SEQRES  21 A  269  LEU ALA GLN PRO LEU THR VAL ASP LEU                          
SEQRES   1 B   99  ILE GLN LYS THR PRO GLN ILE GLN VAL TYR SER ARG HIS          
SEQRES   2 B   99  PRO PRO GLU ASN GLY LYS PRO ASN PHE LEU ASN CYS TYR          
SEQRES   3 B   99  VAL SER GLN PHE HIS PRO PRO GLN ILE GLU ILE GLU LEU          
SEQRES   4 B   99  LEU LYS ASN GLY LYS LYS ILE PRO ASN ILE GLU MET SER          
SEQRES   5 B   99  ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR ILE LEU          
SEQRES   6 B   99  ALA HIS THR GLU PHE THR PRO THR GLU THR ASP VAL TYR          
SEQRES   7 B   99  ALA CYS ARG VAL LYS HIS VAL THR LEU LYS GLU PRO LYS          
SEQRES   8 B   99  THR VAL THR TRP ASP ARG ASP MET                              
SEQRES   1 C  205  SER VAL PHE LEU PHE PRO PRO LYS PRO LYS ASP THR LEU          
SEQRES   2 C  205  MET ILE SER ARG THR PRO GLU VAL THR CYS VAL VAL VAL          
SEQRES   3 C  205  ASP VAL SER HIS GLU ASP PRO GLN VAL LYS PHE ASN TRP          
SEQRES   4 C  205  TYR VAL ASP GLY VAL GLN VAL HIS ASN ALA LYS THR LYS          
SEQRES   5 C  205  PRO ARG GLU GLN GLN TYR ASN SER THR TYR ARG VAL VAL          
SEQRES   6 C  205  SER VAL LEU THR VAL LEU HIS GLN ASN TRP LEU ASP GLY          
SEQRES   7 C  205  LYS GLU TYR LYS CYS LYS VAL SER ASN LYS ALA LEU PRO          
SEQRES   8 C  205  ALA PRO ILE GLU LYS THR ILE SER LYS ALA LYS GLY GLN          
SEQRES   9 C  205  PRO ARG GLU PRO GLN VAL TYR THR LEU PRO PRO SER ARG          
SEQRES  10 C  205  GLU GLU MET THR LYS ASN GLN VAL SER LEU THR CYS LEU          
SEQRES  11 C  205  VAL LYS GLY PHE TYR PRO SER ASP ILE ALA VAL GLU TRP          
SEQRES  12 C  205  GLU SER ASN GLY GLN PRO GLU ASN ASN TYR LYS THR THR          
SEQRES  13 C  205  PRO PRO VAL LEU ASP SER ASP GLY SER PHE PHE LEU TYR          
SEQRES  14 C  205  SER LYS LEU THR VAL ASP LYS SER ARG TRP GLN GLN GLY          
SEQRES  15 C  205  ASN VAL PHE SER CYS SER VAL MET HIS GLU ALA LEU HIS          
SEQRES  16 C  205  ASN HIS TYR THR GLN LYS SER LEU SER LEU                      
MODRES 1FRT ASN A  104  ASN  GLYCOSYLATION SITE                                 
MODRES 1FRT ASN A  225  ASN  GLYCOSYLATION SITE                                 
MODRES 1FRT ASN C  297  ASN  GLYCOSYLATION SITE                                 
HET    NAG  D   1      14                                                       
HET    FUC  D   2      10                                                       
HET    NAG  E   1      14                                                       
HET    NAG  E   2      14                                                       
HET    BMA  E   3      11                                                       
HET    MAN  E   4      11                                                       
HET    NAG  E   5      14                                                       
HET    GAL  E   6      11                                                       
HET    MAN  E   7      11                                                       
HET    NAG  E   8      14                                                       
HET    FUC  E   9      10                                                       
HET    NAG  A 401      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     FUC ALPHA-L-FUCOPYRANOSE                                             
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
HETNAM     GAL BETA-D-GALACTOPYRANOSE                                           
FORMUL   4  NAG    6(C8 H15 N O6)                                               
FORMUL   4  FUC    2(C6 H12 O5)                                                 
FORMUL   5  BMA    C6 H12 O6                                                    
FORMUL   5  MAN    2(C6 H12 O6)                                                 
FORMUL   5  GAL    C6 H12 O6                                                    
HELIX    1   1 GLY A   49  GLU A   54  5                                   6    
HELIX    2   2 TRP A   59  ILE A   86  1                                  28    
HELIX    3   3 TRP A  133  LYS A  145  1                                  13    
HELIX    4   4 PRO A  147  THR A  159  1                                  13    
HELIX    5   5 THR A  159  GLY A  172  1                                  14    
HELIX    6   6 GLY A  172  GLU A  177  1                                   6    
HELIX    7   7 ASP A  248  HIS A  250  5                                   3    
HELIX    8   8 LYS C  246  MET C  252  1                                   7    
HELIX    9   9 LEU C  309  ASP C  315  1                                   7    
HELIX   10  10 SER C  354  MET C  358  5                                   5    
HELIX   11  11 LYS C  414  GLN C  419  1                                   6    
SHEET    1   A 8 ASP A  46  PRO A  47  0                                        
SHEET    2   A 8 GLN A  33  ASN A  39 -1  N  THR A  37   O  ASP A  46           
SHEET    3   A 8 PHE A  24  LEU A  30 -1  N  ALA A  26   O  TYR A  38           
SHEET    4   A 8 LEU A   7  VAL A  14 -1  O  MET A   8   N  TRP A  29           
SHEET    5   A 8 THR A  91  LEU A 100 -1  N  LEU A  92   O  ALA A  13           
SHEET    6   A 8 SER A 106  LEU A 114 -1  O  LEU A 107   N  GLU A  99           
SHEET    7   A 8 GLU A 117  PHE A 122 -1  O  GLU A 117   N  LEU A 114           
SHEET    8   A 8 TRP A 129  GLY A 131 -1  N  SER A 130   O  ARG A 121           
SHEET    1   B 4 SER A 183  PRO A 190  0                                        
SHEET    2   B 4 SER A 195  PHE A 205 -1  N  VAL A 197   O  ARG A 189           
SHEET    3   B 4 PHE A 236  LYS A 245 -1  N  PHE A 236   O  PHE A 205           
SHEET    4   B 4 ASN A 225  PRO A 230 -1  N  ASN A 225   O  LEU A 241           
SHEET    1   C 4 LEU A 219  ALA A 220  0                                        
SHEET    2   C 4 LYS A 211  ARG A 216 -1  N  ARG A 216   O  LEU A 219           
SHEET    3   C 4 TYR A 252  GLU A 257 -1  O  GLN A 253   N  LEU A 215           
SHEET    4   C 4 LEU A 265  VAL A 267 -1  N  LEU A 265   O  VAL A 256           
SHEET    1   D 4 GLN B   6  SER B  11  0                                        
SHEET    2   D 4 ASN B  21  PHE B  30 -1  N  ASN B  24   O  TYR B  10           
SHEET    3   D 4 PHE B  62  PHE B  70 -1  N  PHE B  62   O  PHE B  30           
SHEET    4   D 4 GLU B  50  MET B  51 -1  N  GLU B  50   O  HIS B  67           
SHEET    1   E 4 GLN B   6  SER B  11  0                                        
SHEET    2   E 4 ASN B  21  PHE B  30 -1  N  ASN B  24   O  TYR B  10           
SHEET    3   E 4 PHE B  62  PHE B  70 -1  N  PHE B  62   O  PHE B  30           
SHEET    4   E 4 SER B  55  PHE B  56 -1  N  SER B  55   O  TYR B  63           
SHEET    1   F 4 LYS B  44  LYS B  45  0                                        
SHEET    2   F 4 GLU B  36  LYS B  41 -1  N  LYS B  41   O  LYS B  44           
SHEET    3   F 4 TYR B  78  LYS B  83 -1  O  ALA B  79   N  LEU B  40           
SHEET    4   F 4 LYS B  91  THR B  94 -1  O  LYS B  91   N  VAL B  82           
SHEET    1   G 4 VAL C 240  PHE C 243  0                                        
SHEET    2   G 4 GLU C 258  ASP C 265 -1  O  THR C 260   N  PHE C 243           
SHEET    3   G 4 TYR C 300  THR C 307 -1  O  TYR C 300   N  ASP C 265           
SHEET    4   G 4 ARG C 292  GLN C 295 -1  N  ARG C 292   O  VAL C 303           
SHEET    1   H 4 VAL C 282  GLN C 283  0                                        
SHEET    2   H 4 PHE C 275  VAL C 279 -1  N  VAL C 279   O  VAL C 282           
SHEET    3   H 4 TYR C 319  VAL C 323 -1  N  LYS C 320   O  TYR C 278           
SHEET    4   H 4 ILE C 332  ILE C 336 -1  O  ILE C 332   N  VAL C 323           
SHEET    1   I 4 GLN C 347  LEU C 351  0                                        
SHEET    2   I 4 GLN C 362  PHE C 372 -1  O  THR C 366   N  LEU C 351           
SHEET    3   I 4 PHE C 404  ASP C 413 -1  N  PHE C 404   O  PHE C 372           
SHEET    4   I 4 TYR C 391  THR C 393 -1  O  LYS C 392   N  LYS C 409           
SHEET    1   J 4 GLN C 347  LEU C 351  0                                        
SHEET    2   J 4 GLN C 362  PHE C 372 -1  O  THR C 366   N  LEU C 351           
SHEET    3   J 4 PHE C 404  ASP C 413 -1  N  PHE C 404   O  PHE C 372           
SHEET    4   J 4 VAL C 397  LEU C 398 -1  N  VAL C 397   O  PHE C 405           
SHEET    1   K 4 GLN C 386  PRO C 387  0                                        
SHEET    2   K 4 ALA C 378  SER C 383 -1  N  SER C 383   O  GLN C 386           
SHEET    3   K 4 PHE C 423  MET C 428 -1  O  SER C 424   N  GLU C 382           
SHEET    4   K 4 THR C 437  LEU C 441 -1  N  THR C 437   O  VAL C 427           
SSBOND   1 CYS A   98    CYS A  161                          1555   1555  2.03  
SSBOND   2 CYS A  200    CYS A  254                          1555   1555  2.04  
SSBOND   3 CYS B   25    CYS B   80                          1555   1555  2.03  
SSBOND   4 CYS C  261    CYS C  321                          1555   1555  2.06  
SSBOND   5 CYS C  367    CYS C  425                          1555   1555  2.03  
LINK         ND2 ASN A 104                 C1  NAG A 401     1555   1555  1.46  
LINK         N   SER A 193                 O7  NAG D   1     6755   1555  1.17  
LINK         ND2 ASN A 225                 C1  NAG D   1     1555   1555  1.46  
LINK         ND2 ASN C 297                 C1  NAG E   1     1555   1555  1.47  
LINK         O6  NAG D   1                 C1  FUC D   2     1555   1555  1.45  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.43  
LINK         O6  NAG E   1                 C1  FUC E   9     1555   1555  1.43  
LINK         O4  NAG E   2                 C1  BMA E   3     1555   1555  1.43  
LINK         O6  BMA E   3                 C1  MAN E   4     1555   1555  1.43  
LINK         O3  BMA E   3                 C1  MAN E   7     1555   1555  1.43  
LINK         O2  MAN E   4                 C1  NAG E   5     1555   1555  1.43  
LINK         O4  NAG E   5                 C1  GAL E   6     1555   1555  1.44  
LINK         O2  MAN E   7                 C1  NAG E   8     1555   1555  1.43  
CISPEP   1 TYR A  206    PRO A  207          0        -1.09                     
CISPEP   2 HIS B   31    PRO B   32          0         0.42                     
CISPEP   3 TYR C  373    PRO C  374          0        -5.15                     
SITE     1 B1A 24 ASN A  84  GLN A  85  ILE A  86  PHE A  90                    
SITE     2 B1A 24 ALA A 113  LEU A 114  ASN A 115  GLY A 116                    
SITE     3 B1A 24 GLU A 117  GLU A 118  PHE A 119  GLY A 131                    
SITE     4 B1A 24 GLU A 132  TRP A 133  PRO A 134  GLU A 135                    
SITE     5 B1A 24 THR A 136  ASP A 137  ILE B   1  GLN B   2                    
SITE     6 B1A 24 LYS B   3  THR B   4  THR B  86  LYS B  88                    
SITE     1 B2A  2 LEU A 219  LYS A 245                                          
SITE     1 B1B 25 LYS C 248  THR C 250  LEU C 251  MET C 252                    
SITE     2 B1B 25 ILE C 253  SER C 254  ARG C 255  THR C 256                    
SITE     3 B1B 25 PRO C 257  LYS C 288  LYS C 290  PRO C 291                    
SITE     4 B1B 25 VAL C 308  LEU C 309  HIS C 310  GLN C 311                    
SITE     5 B1B 25 LEU C 314  GLY C 385  GLN C 386  PRO C 387                    
SITE     6 B1B 25 MET C 428  HIS C 433  ASN C 434  HIS C 435                    
SITE     7 B1B 25 TYR C 436                                                     
SITE     1 B2B  2 GLN C 272  HIS C 285                                          
CRYST1  125.000  145.000  216.500  90.00  90.00  90.00 I 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      0.008000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006897  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004619        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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