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Database: PDB
Entry: 1I1A
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HEADER    IMMUNE SYSTEM                           31-JAN-01   1I1A              
TITLE     CRYSTAL STRUCTURE OF THE NEONATAL FC RECEPTOR COMPLEXED WITH A        
TITLE    2 HETERODIMERIC FC                                                     
CAVEAT     1I1A    NAG E 1 HAS WRONG CHIRALITY AT ATOM C1 FUC E 2 HAS WRONG     
CAVEAT   2 1I1A    CHIRALITY AT ATOM C1 NAG F 1 HAS WRONG CHIRALITY AT ATOM C1  
CAVEAT   3 1I1A    FUC F 6 HAS WRONG CHIRALITY AT ATOM C1 FUC H 8 HAS WRONG     
CAVEAT   4 1I1A    CHIRALITY AT ATOM C1 NAG A 601 HAS WRONG CHIRALITY AT ATOM   
CAVEAT   5 1I1A    C1                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NEONATAL FC RECEPTOR A;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAIN;                                      
COMPND   5 SYNONYM: IGG RECEPTOR FCRN LARGE SUBUNIT P51, FCRN;                  
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: BETA-2-MICROGLOBULIN;                                      
COMPND   9 CHAIN: B;                                                            
COMPND  10 FRAGMENT: FC FRAGMENT;                                               
COMPND  11 SYNONYM: HDFC;                                                       
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: IG GAMMA-2A CHAIN C REGION;                                
COMPND  15 CHAIN: C;                                                            
COMPND  16 FRAGMENT: WILD-TYPE FC FRAGMENT;                                     
COMPND  17 SYNONYM: WTFC;                                                       
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 MOL_ID: 4;                                                           
COMPND  20 MOLECULE: IG GAMMA-2A CHAIN C REGION;                                
COMPND  21 CHAIN: D;                                                            
COMPND  22 FRAGMENT: NON-FCRN-BINDING FC FRAGMENT;                              
COMPND  23 SYNONYM: NBFC;                                                       
COMPND  24 ENGINEERED: YES;                                                     
COMPND  25 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: CHO-K1;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PBJ-5GS;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  13 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE  14 ORGANISM_TAXID: 10116;                                               
SOURCE  15 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  16 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: CHO-K1;                                    
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PBJ-5GS;                                  
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  23 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE  24 ORGANISM_TAXID: 10116;                                               
SOURCE  25 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  26 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  27 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  28 EXPRESSION_SYSTEM_STRAIN: CHO-K1;                                    
SOURCE  29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  30 EXPRESSION_SYSTEM_PLASMID: PBJ-5GS;                                  
SOURCE  31 MOL_ID: 4;                                                           
SOURCE  32 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  33 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE  34 ORGANISM_TAXID: 10116;                                               
SOURCE  35 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  36 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  37 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  38 EXPRESSION_SYSTEM_STRAIN: CHO-K1;                                    
SOURCE  39 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  40 EXPRESSION_SYSTEM_PLASMID: PBJ-5GS                                   
KEYWDS    MHC CLASS I FOLD, IG CONSTANT DOMAINS, IMMUNE SYSTEM                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.L.MARTIN,A.P.WEST JR.,L.GAN,P.J.BJORKMAN                            
REVDAT   6   29-JUL-20 1I1A    1       CAVEAT COMPND REMARK SEQADV              
REVDAT   6 2                   1       HETNAM LINK   SITE   ATOM                
REVDAT   5   25-SEP-13 1I1A    1       REMARK                                   
REVDAT   4   13-JUL-11 1I1A    1       VERSN                                    
REVDAT   3   24-FEB-09 1I1A    1       VERSN                                    
REVDAT   2   09-MAY-01 1I1A    1       JRNL                                     
REVDAT   1   14-FEB-01 1I1A    0                                                
JRNL        AUTH   W.L.MARTIN,A.P.WEST JR.,L.GAN,P.J.BJORKMAN                   
JRNL        TITL   CRYSTAL STRUCTURE AT 2.8 A OF AN FCRN/HETERODIMERIC FC       
JRNL        TITL 2 COMPLEX: MECHANISM OF PH-DEPENDENT BINDING.                  
JRNL        REF    MOL.CELL                      V.   7   867 2001              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   11336709                                                     
JRNL        DOI    10.1016/S1097-2765(01)00230-1                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.95                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1843766.660                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 25005                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.292                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1195                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.009                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.90                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2122                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4280                       
REMARK   3   BIN FREE R VALUE                    : 0.4470                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.50                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 101                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.044                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6182                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 338                                     
REMARK   3   SOLVENT ATOMS            : 6                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 78.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 24.29000                                             
REMARK   3    B22 (A**2) : -6.04000                                             
REMARK   3    B33 (A**2) : -18.26000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.39                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.58                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.53                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.75                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.600                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.150                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ANISOTROPIC                               
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 11.220; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 17.520; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 14.600; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 20.740; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.28                                                 
REMARK   3   BSOL        : 44.40                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : CONSTRAINED                                             
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : CARBOHYDRATE.TOP                               
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1I1A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-FEB-01.                  
REMARK 100 THE DEPOSITION ID IS D_1000012780.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-DEC-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25005                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 1.000                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : 0.09900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.28400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 3FRU, PDB ENTRY 1FC1                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.66                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, AMMONIUM ACETATE, SODIUM       
REMARK 280  ACETATE, SODIUM CACODYLATE, PH 5.4, VAPOR DIFFUSION, HANGING        
REMARK 280  DROP, TEMPERATURE 298K                                              
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       34.17900            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       98.30200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.10650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       98.30200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       34.17900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.10650            
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 300 REMARK: THE GLYCOSYLATED HETERODIMER IS THE BIOLOGICAL UNIT.         
REMARK 300 THE CYSTEINES ATTACHED TO CYSTEINES 48 AND 226 ARE                   
REMARK 300 THE RESULT OF LONG TERM STORAGE IN THE                               
REMARK 300 GROWTH MEDIA.                                                        
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14550 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 37830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 70.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H                
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     ARG A     4                                                      
REMARK 465     VAL C   223                                                      
REMARK 465     PRO C   224                                                      
REMARK 465     ARG C   225                                                      
REMARK 465     GLU C   226                                                      
REMARK 465     CYS C   227                                                      
REMARK 465     ASN C   228                                                      
REMARK 465     PRO C   229                                                      
REMARK 465     CYS C   230                                                      
REMARK 465     GLY C   231                                                      
REMARK 465     CYS C   232                                                      
REMARK 465     THR C   233                                                      
REMARK 465     GLY C   234                                                      
REMARK 465     SER C   235                                                      
REMARK 465     GLU C   236                                                      
REMARK 465     VAL C   237                                                      
REMARK 465     SER C   238                                                      
REMARK 465     SER C   444                                                      
REMARK 465     PRO C   445                                                      
REMARK 465     GLY C   446                                                      
REMARK 465     LYS C   447                                                      
REMARK 465     VAL D   223                                                      
REMARK 465     PRO D   224                                                      
REMARK 465     ARG D   225                                                      
REMARK 465     GLU D   226                                                      
REMARK 465     CYS D   227                                                      
REMARK 465     ASN D   228                                                      
REMARK 465     PRO D   229                                                      
REMARK 465     CYS D   230                                                      
REMARK 465     GLY D   231                                                      
REMARK 465     CYS D   232                                                      
REMARK 465     THR D   233                                                      
REMARK 465     GLY D   234                                                      
REMARK 465     SER D   235                                                      
REMARK 465     GLU D   236                                                      
REMARK 465     VAL D   237                                                      
REMARK 465     SER D   238                                                      
REMARK 465     SER D   444                                                      
REMARK 465     PRO D   445                                                      
REMARK 465     GLY D   446                                                      
REMARK 465     LYS D   447                                                      
REMARK 465     GLY D   448                                                      
REMARK 465     ILE D   449                                                      
REMARK 465     GLU D   450                                                      
REMARK 465     GLY D   451                                                      
REMARK 465     ARG D   452                                                      
REMARK 465     GLY D   453                                                      
REMARK 465     SER D   454                                                      
REMARK 465     SER D   455                                                      
REMARK 465     HIS D   456                                                      
REMARK 465     HIS D   457                                                      
REMARK 465     HIS D   458                                                      
REMARK 465     HIS D   459                                                      
REMARK 465     HIS D   460                                                      
REMARK 465     HIS D   461                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS C  355   CG   CD                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ALA A   101     N    ASP A   103              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A  47   C   -  N   -  CA  ANGL. DEV. =  10.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  16       99.68    -59.96                                   
REMARK 500    PRO A  22     -168.82    -75.70                                   
REMARK 500    ALA A  50      -17.24    -40.65                                   
REMARK 500    THR A  89      156.93    -46.68                                   
REMARK 500    PRO A 102       47.94    -62.05                                   
REMARK 500    ASP A 103       51.54   -175.22                                   
REMARK 500    ASN A 104       98.03     36.46                                   
REMARK 500    SER A 105      169.95    170.70                                   
REMARK 500    ALA A 110       98.56   -163.83                                   
REMARK 500    LYS A 145       34.16    -90.25                                   
REMARK 500    ALA A 149      -90.93    -16.12                                   
REMARK 500    LYS A 152      -72.74    -45.88                                   
REMARK 500    GLU A 153      -38.04    -37.20                                   
REMARK 500    ARG A 185      116.29   -161.78                                   
REMARK 500    ASN A 192     -160.67    -63.11                                   
REMARK 500    SER A 195     -169.45   -128.96                                   
REMARK 500    SER A 204       72.16     39.14                                   
REMARK 500    TYR A 206      -92.32    -78.90                                   
REMARK 500    PRO A 207      110.96    -39.17                                   
REMARK 500    ASN A 217       20.06     47.97                                   
REMARK 500    SER A 221       14.72   -141.16                                   
REMARK 500    ARG A 246      152.06    -45.30                                   
REMARK 500    ASN B  17      127.16    -31.16                                   
REMARK 500    HIS B  31      135.30   -173.34                                   
REMARK 500    ASN B  42       15.78     59.04                                   
REMARK 500    THR B  73      142.08   -170.11                                   
REMARK 500    THR B  75      -62.81    -94.56                                   
REMARK 500    ARG B  97       -9.43    -44.07                                   
REMARK 500    ASP C 265       88.41     56.54                                   
REMARK 500    SER C 267       39.29    -74.49                                   
REMARK 500    GLN C 268       73.68     72.88                                   
REMARK 500    ASN C 269     -111.56   -100.67                                   
REMARK 500    ASP C 270       62.90   -118.14                                   
REMARK 500    PRO C 271       -1.12    -45.20                                   
REMARK 500    VAL C 273      102.79    -21.26                                   
REMARK 500    ALA C 287      169.72    -45.27                                   
REMARK 500    ALA C 291      130.17    -22.21                                   
REMARK 500    PRO C 292      163.30    -44.62                                   
REMARK 500    SER C 296       49.34    -85.43                                   
REMARK 500    ASN C 297        8.73   -156.26                                   
REMARK 500    SER C 325      145.86   -172.67                                   
REMARK 500    PRO C 329      -77.09    -63.53                                   
REMARK 500    MET C 358       34.41    -65.57                                   
REMARK 500    THR C 359      -35.77   -130.01                                   
REMARK 500    PRO C 375       25.44    -67.81                                   
REMARK 500    HIS C 435       12.39     57.49                                   
REMARK 500    SER C 442     -121.21   -146.08                                   
REMARK 500    VAL D 259       89.23    -68.56                                   
REMARK 500    THR D 260     -175.03    -67.45                                   
REMARK 500    CYS D 261       75.73   -178.66                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      75 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3FRU   RELATED DB: PDB                                   
REMARK 900 NEONATAL FC RECEPTOR                                                 
REMARK 900 RELATED ID: 1FC1   RELATED DB: PDB                                   
REMARK 900 FC FRAGMENT OF IGG                                                   
REMARK 900 RELATED ID: 1I1C   RELATED DB: PDB                                   
REMARK 900 NON-FCRN BINDING FC FRAGMENT OF RAT IGG2A                            
DBREF  1I1A A    1   269  UNP    P13599   FCGN_RAT        23    291             
DBREF  1I1A B    1    99  UNP    P07151   B2MG_RAT        21    119             
DBREF  1I1A C  223   447  UNP    P20760   GCA_RAT         98    322             
DBREF  1I1A D  223   447  UNP    P20760   GCA_RAT         98    322             
SEQADV 1I1A GLY D  252  UNP  P20760    THR   127 ENGINEERED                     
SEQADV 1I1A GLY D  253  UNP  P20760    ILE   128 ENGINEERED                     
SEQADV 1I1A GLY D  254  UNP  P20760    THR   129 ENGINEERED                     
SEQADV 1I1A GLU D  310  UNP  P20760    HIS   185 ENGINEERED                     
SEQADV 1I1A GLU D  433  UNP  P20760    HIS   308 ENGINEERED                     
SEQADV 1I1A GLU D  435  UNP  P20760    HIS   310 ENGINEERED                     
SEQADV 1I1A GLY D  448  UNP  P20760              CLONING ARTIFACT               
SEQADV 1I1A ILE D  449  UNP  P20760              CLONING ARTIFACT               
SEQADV 1I1A GLU D  450  UNP  P20760              CLONING ARTIFACT               
SEQADV 1I1A GLY D  451  UNP  P20760              CLONING ARTIFACT               
SEQADV 1I1A ARG D  452  UNP  P20760              CLONING ARTIFACT               
SEQADV 1I1A GLY D  453  UNP  P20760              CLONING ARTIFACT               
SEQADV 1I1A SER D  454  UNP  P20760              CLONING ARTIFACT               
SEQADV 1I1A SER D  455  UNP  P20760              CLONING ARTIFACT               
SEQADV 1I1A HIS D  456  UNP  P20760              CLONING ARTIFACT               
SEQADV 1I1A HIS D  457  UNP  P20760              CLONING ARTIFACT               
SEQADV 1I1A HIS D  458  UNP  P20760              CLONING ARTIFACT               
SEQADV 1I1A HIS D  459  UNP  P20760              CLONING ARTIFACT               
SEQADV 1I1A HIS D  460  UNP  P20760              CLONING ARTIFACT               
SEQADV 1I1A HIS D  461  UNP  P20760              CLONING ARTIFACT               
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  225  VAL PRO ARG GLU CYS ASN PRO CYS GLY CYS THR GLY SER          
SEQRES   2 C  225  GLU VAL SER SER VAL PHE ILE PHE PRO PRO LYS THR LYS          
SEQRES   3 C  225  ASP VAL LEU THR ILE THR LEU THR PRO LYS VAL THR CYS          
SEQRES   4 C  225  VAL VAL VAL ASP ILE SER GLN ASN ASP PRO GLU VAL ARG          
SEQRES   5 C  225  PHE SER TRP PHE ILE ASP ASP VAL GLU VAL HIS THR ALA          
SEQRES   6 C  225  GLN THR HIS ALA PRO GLU LYS GLN SER ASN SER THR LEU          
SEQRES   7 C  225  ARG SER VAL SER GLU LEU PRO ILE VAL HIS ARG ASP TRP          
SEQRES   8 C  225  LEU ASN GLY LYS THR PHE LYS CYS LYS VAL ASN SER GLY          
SEQRES   9 C  225  ALA PHE PRO ALA PRO ILE GLU LYS SER ILE SER LYS PRO          
SEQRES  10 C  225  GLU GLY THR PRO ARG GLY PRO GLN VAL TYR THR MET ALA          
SEQRES  11 C  225  PRO PRO LYS GLU GLU MET THR GLN SER GLN VAL SER ILE          
SEQRES  12 C  225  THR CYS MET VAL LYS GLY PHE TYR PRO PRO ASP ILE TYR          
SEQRES  13 C  225  THR GLU TRP LYS MET ASN GLY GLN PRO GLN GLU ASN TYR          
SEQRES  14 C  225  LYS ASN THR PRO PRO THR MET ASP THR ASP GLY SER TYR          
SEQRES  15 C  225  PHE LEU TYR SER LYS LEU ASN VAL LYS LYS GLU THR TRP          
SEQRES  16 C  225  GLN GLN GLY ASN THR PHE THR CYS SER VAL LEU HIS GLU          
SEQRES  17 C  225  GLY LEU HIS ASN HIS HIS THR GLU LYS SER LEU SER HIS          
SEQRES  18 C  225  SER PRO GLY LYS                                              
SEQRES   1 D  239  VAL PRO ARG GLU CYS ASN PRO CYS GLY CYS THR GLY SER          
SEQRES   2 D  239  GLU VAL SER SER VAL PHE ILE PHE PRO PRO LYS THR LYS          
SEQRES   3 D  239  ASP VAL LEU GLY GLY GLY LEU THR PRO LYS VAL THR CYS          
SEQRES   4 D  239  VAL VAL VAL ASP ILE SER GLN ASN ASP PRO GLU VAL ARG          
SEQRES   5 D  239  PHE SER TRP PHE ILE ASP ASP VAL GLU VAL HIS THR ALA          
SEQRES   6 D  239  GLN THR HIS ALA PRO GLU LYS GLN SER ASN SER THR LEU          
SEQRES   7 D  239  ARG SER VAL SER GLU LEU PRO ILE VAL GLU ARG ASP TRP          
SEQRES   8 D  239  LEU ASN GLY LYS THR PHE LYS CYS LYS VAL ASN SER GLY          
SEQRES   9 D  239  ALA PHE PRO ALA PRO ILE GLU LYS SER ILE SER LYS PRO          
SEQRES  10 D  239  GLU GLY THR PRO ARG GLY PRO GLN VAL TYR THR MET ALA          
SEQRES  11 D  239  PRO PRO LYS GLU GLU MET THR GLN SER GLN VAL SER ILE          
SEQRES  12 D  239  THR CYS MET VAL LYS GLY PHE TYR PRO PRO ASP ILE TYR          
SEQRES  13 D  239  THR GLU TRP LYS MET ASN GLY GLN PRO GLN GLU ASN TYR          
SEQRES  14 D  239  LYS ASN THR PRO PRO THR MET ASP THR ASP GLY SER TYR          
SEQRES  15 D  239  PHE LEU TYR SER LYS LEU ASN VAL LYS LYS GLU THR TRP          
SEQRES  16 D  239  GLN GLN GLY ASN THR PHE THR CYS SER VAL LEU HIS GLU          
SEQRES  17 D  239  GLY LEU GLU ASN GLU HIS THR GLU LYS SER LEU SER HIS          
SEQRES  18 D  239  SER PRO GLY LYS GLY ILE GLU GLY ARG GLY SER SER HIS          
SEQRES  19 D  239  HIS HIS HIS HIS HIS                                          
MODRES 1I1A ASN C  297  ASN  GLYCOSYLATION SITE                                 
MODRES 1I1A ASN D  297  ASN  GLYCOSYLATION SITE                                 
MODRES 1I1A ASN A  104  ASN  GLYCOSYLATION SITE                                 
MODRES 1I1A ASN A  128  ASN  GLYCOSYLATION SITE                                 
MODRES 1I1A ASN A  225  ASN  GLYCOSYLATION SITE                                 
MODRES 1I1A ASN A   87  ASN  GLYCOSYLATION SITE                                 
HET    NAG  E   1      14                                                       
HET    FUC  E   2      10                                                       
HET    NAG  F   1      14                                                       
HET    NAG  F   2      14                                                       
HET    BMA  F   3      11                                                       
HET    MAN  F   4      11                                                       
HET    NDG  F   5      14                                                       
HET    FUC  F   6      10                                                       
HET    NAG  G   1      14                                                       
HET    NAG  G   2      14                                                       
HET    BMA  G   3      11                                                       
HET    MAN  G   4      11                                                       
HET    NAG  G   5      14                                                       
HET    MAN  G   6      11                                                       
HET    NAG  G   7      14                                                       
HET    FUL  G   8      10                                                       
HET    NAG  H   1      14                                                       
HET    NAG  H   2      14                                                       
HET    BMA  H   3      11                                                       
HET    MAN  H   4      11                                                       
HET    NAG  H   5      14                                                       
HET    MAN  H   6      11                                                       
HET    NAG  H   7      14                                                       
HET    FUC  H   8      10                                                       
HET    NAG  A 601      14                                                       
HET    NAG  A 751      14                                                       
HET    CYS  A 901       7                                                       
HET    CYS  A 951       7                                                       
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     NDG 2-ACETAMIDO-2-DEOXY-ALPHA-D-GLUCOPYRANOSE                        
HETNAM     FUL BETA-L-FUCOPYRANOSE                                              
HETNAM     CYS CYSTEINE                                                         
HETSYN     FUL 6-DEOXY-BETA-L-GALACTOSE                                         
FORMUL   5  NAG    13(C8 H15 N O6)                                              
FORMUL   5  FUC    3(C6 H12 O5)                                                 
FORMUL   6  BMA    3(C6 H12 O6)                                                 
FORMUL   6  MAN    5(C6 H12 O6)                                                 
FORMUL   6  NDG    C8 H15 N O6                                                  
FORMUL   7  FUL    C6 H12 O5                                                    
FORMUL  11  CYS    2(C3 H7 N O2 S)                                              
FORMUL  13  HOH   *6(H2 O)                                                      
HELIX    1   1 GLY A   49  ILE A   52  5                                   4    
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 GLN A  146  THR A  159  1                                  14    
HELIX    5   5 THR A  159  ARG A  173  1                                  15    
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  THR C  252  1                                   7    
HELIX    9   9 VAL C  309  ASN C  315  1                                   7    
HELIX   10  10 PRO C  354  MET C  358  5                                   5    
HELIX   11  11 LYS C  414  GLN C  419  1                                   6    
HELIX   12  12 LEU C  432  ASN C  434  5                                   3    
HELIX   13  13 LYS D  246  LEU D  251  1                                   6    
HELIX   14  14 VAL D  309  LEU D  314  1                                   6    
HELIX   15  15 LYS D  414  GLN D  419  1                                   6    
HELIX   16  16 LEU D  432  ASN D  434  5                                   3    
SHEET    1   A 8 ASP A  46  PRO A  47  0                                        
SHEET    2   A 8 GLN A  33  ASN A  39 -1  O  THR A  37   N  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  N  MET A   8   O  TRP A  29           
SHEET    5   A 8 THR A  91  LEU A 100 -1  O  LEU A  92   N  ALA A  13           
SHEET    6   A 8 SER A 106  LEU A 114 -1  N  LEU A 107   O  GLU A  99           
SHEET    7   A 8 GLU A 117  ASN A 123 -1  O  GLU A 117   N  LEU A 114           
SHEET    8   A 8 ASN A 128  SER A 130 -1  O  ASN A 128   N  ASN A 123           
SHEET    1   B 4 SER A 183  ARG A 189  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 CYS A 226  PRO A 230 -1  O  SER A 227   N  TRP A 239           
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  N  GLN A 253   O  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  O  SER B  55   N  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  O  LYS B  41   N  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 LYS C 258  VAL C 263 -1  O  THR C 260   N  PHE C 243           
SHEET    3   G 4 LEU C 300  PRO C 307 -1  N  SER C 302   O  VAL C 263           
SHEET    4   G 4 GLN C 288  LYS C 294 -1  O  GLN C 288   N  GLU C 305           
SHEET    1   H 4 GLU C 283  VAL C 284  0                                        
SHEET    2   H 4 ARG C 274  ILE C 279 -1  O  TRP C 277   N  VAL C 284           
SHEET    3   H 4 PHE C 319  ASN C 324 -1  N  LYS C 320   O  PHE 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  MET C 351  0                                        
SHEET    2   I 4 GLN C 362  PHE C 372 -1  O  THR C 366   N  MET C 351           
SHEET    3   I 4 TYR C 404  LYS C 413 -1  N  TYR C 404   O  PHE C 372           
SHEET    4   I 4 TYR C 391  ASN C 393 -1  O  LYS C 392   N  LYS C 409           
SHEET    1   J 4 GLN C 347  MET C 351  0                                        
SHEET    2   J 4 GLN C 362  PHE C 372 -1  O  THR C 366   N  MET C 351           
SHEET    3   J 4 TYR C 404  LYS C 413 -1  N  TYR C 404   O  PHE C 372           
SHEET    4   J 4 THR C 397  MET C 398 -1  N  THR C 397   O  PHE C 405           
SHEET    1   K 4 GLN C 386  PRO C 387  0                                        
SHEET    2   K 4 TYR C 378  MET C 383 -1  O  MET C 383   N  GLN C 386           
SHEET    3   K 4 PHE C 423  LEU C 428 -1  N  THR C 424   O  LYS C 382           
SHEET    4   K 4 HIS C 436  LEU C 441 -1  O  THR C 437   N  VAL C 427           
SHEET    1   L 3 LYS D 258  VAL D 259  0                                        
SHEET    2   L 3 VAL D 303  PRO D 307 -1  O  LEU D 306   N  VAL D 259           
SHEET    3   L 3 GLN D 288  HIS D 290 -1  O  GLN D 288   N  GLU D 305           
SHEET    1   M 2 SER D 276  PHE D 278  0                                        
SHEET    2   M 2 LYS D 320  LYS D 322 -1  O  LYS D 320   N  PHE D 278           
SHEET    1   N 4 GLN D 347  MET D 351  0                                        
SHEET    2   N 4 GLN D 362  PHE D 372 -1  O  THR D 366   N  MET D 351           
SHEET    3   N 4 TYR D 404  LYS D 413 -1  O  TYR D 404   N  PHE D 372           
SHEET    4   N 4 TYR D 391  ASN D 393 -1  N  LYS D 392   O  LYS D 409           
SHEET    1   O 4 GLN D 347  MET D 351  0                                        
SHEET    2   O 4 GLN D 362  PHE D 372 -1  O  THR D 366   N  MET D 351           
SHEET    3   O 4 TYR D 404  LYS D 413 -1  O  TYR D 404   N  PHE D 372           
SHEET    4   O 4 THR D 397  MET D 398 -1  N  THR D 397   O  PHE D 405           
SHEET    1   P 4 GLN D 386  PRO D 387  0                                        
SHEET    2   P 4 THR D 379  MET D 383 -1  O  MET D 383   N  GLN D 386           
SHEET    3   P 4 PHE D 423  LEU D 428 -1  N  THR D 424   O  LYS D 382           
SHEET    4   P 4 HIS D 436  LEU D 441 -1  O  THR D 437   N  VAL D 427           
SSBOND   1 CYS A   98    CYS A  161                          1555   1555  2.06  
SSBOND   2 CYS A  200    CYS A  254                          1555   1555  2.03  
SSBOND   3 CYS B   25    CYS B   80                          1555   1555  2.03  
SSBOND   4 CYS C  261    CYS C  321                          1555   1555  2.03  
SSBOND   5 CYS C  367    CYS C  425                          1555   1555  2.03  
SSBOND   6 CYS D  261    CYS D  321                          1555   1555  2.03  
SSBOND   7 CYS D  367    CYS D  425                          1555   1555  2.03  
LINK         SG  CYS A  48                 SG  CYS A 901     1555   1555  2.04  
LINK         ND2 ASN A  87                 C1  NAG A 601     1555   1555  1.46  
LINK         ND2 ASN A 104                 C1  NAG E   1     1555   1555  1.45  
LINK         ND2 ASN A 128                 C1  NAG F   1     1555   1555  1.45  
LINK         ND2 ASN A 225                 C1  NAG A 751     1555   1555  1.45  
LINK         SG  CYS A 226                 SG  CYS A 951     1555   1555  2.03  
LINK         ND2 ASN C 297                 C1  NAG G   1     1555   1555  1.45  
LINK         ND2 ASN D 297                 C1  NAG H   1     1555   1555  1.45  
LINK         O6  NAG E   1                 C1  FUC E   2     1555   1555  1.40  
LINK         O4  NAG F   1                 C1  NAG F   2     1555   1555  1.39  
LINK         O6  NAG F   1                 C1  FUC F   6     1555   1555  1.40  
LINK         O4  NAG F   2                 C1  BMA F   3     1555   1555  1.39  
LINK         O3  BMA F   3                 C1  MAN F   4     1555   1555  1.41  
LINK         O2  MAN F   4                 C1  NDG F   5     1555   1555  1.40  
LINK         O4  NAG G   1                 C1  NAG G   2     1555   1555  1.39  
LINK         O6  NAG G   1                 C1  FUL G   8     1555   1555  1.40  
LINK         O4  NAG G   2                 C1  BMA G   3     1555   1555  1.39  
LINK         O3  BMA G   3                 C1  MAN G   4     1555   1555  1.40  
LINK         O6  BMA G   3                 C1  MAN G   6     1555   1555  1.39  
LINK         O2  MAN G   4                 C1  NAG G   5     1555   1555  1.39  
LINK         O2  MAN G   6                 C1  NAG G   7     1555   1555  1.39  
LINK         O4  NAG H   1                 C1  NAG H   2     1555   1555  1.39  
LINK         O6  NAG H   1                 C1  FUC H   8     1555   1555  1.40  
LINK         O4  NAG H   2                 C1  BMA H   3     1555   1555  1.39  
LINK         O3  BMA H   3                 C1  MAN H   4     1555   1555  1.40  
LINK         O6  BMA H   3                 C1  MAN H   6     1555   1555  1.40  
LINK         O2  MAN H   4                 C1  NAG H   5     1555   1555  1.39  
LINK         O2  MAN H   6                 C1  NAG H   7     1555   1555  1.39  
CISPEP   1 HIS B   31    PRO B   32          0         0.17                     
CISPEP   2 TYR C  373    PRO C  374          0        -0.03                     
CISPEP   3 TYR D  373    PRO D  374          0        -0.27                     
CRYST1   68.358   74.213  196.604  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014629  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013475  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005086        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system