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Database: PDB
Entry: 3FRU
LinkDB: 3FRU
Original site: 3FRU 
HEADER    COMPLEX (IMMUNOGLOBULIN/BINDING PROTEIN)22-DEC-97   3FRU              
TITLE     NEONATAL FC RECEPTOR, PH 6.5                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NEONATAL FC RECEPTOR;                                      
COMPND   3 CHAIN: A, C, E;                                                      
COMPND   4 FRAGMENT: EXTRACELLULAR LIGAND BINDING DOMAIN;                       
COMPND   5 SYNONYM: FCRN, BRAMBELL RECEPTOR;                                    
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: BETA-2-MICROGLOBULIN;                                      
COMPND   9 CHAIN: B, D, F;                                                      
COMPND  10 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 GENE: GLUTAMINE SYNTHETASE SELECTION;                                
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: CHO-K1;                                 
SOURCE  10 EXPRESSION_SYSTEM_CELLULAR_LOCATION: SECRETED;                       
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: STABLE;                               
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  14 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE  15 ORGANISM_TAXID: 10116;                                               
SOURCE  16 GENE: GLUTAMINE SYNTHETASE SELECTION;                                
SOURCE  17 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  18 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  20 EXPRESSION_SYSTEM_CELL_LINE: CHO-K1;                                 
SOURCE  21 EXPRESSION_SYSTEM_CELLULAR_LOCATION: SECRETED;                       
SOURCE  22 EXPRESSION_SYSTEM_VECTOR_TYPE: STABLE                                
KEYWDS    COMPLEX (IMMUNOGLOBULIN-BINDING PROTEIN), COMPLEX (IMMUNOGLOBULIN-    
KEYWDS   2 BINDING PROTEIN) COMPLEX                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.E.VAUGHN,W.P.BURMEISTER,P.J.BJORKMAN                                
REVDAT   4   29-JUL-20 3FRU    1       COMPND REMARK HETNAM LINK                
REVDAT   4 2                   1       SITE   ATOM                              
REVDAT   3   13-JUL-11 3FRU    1       VERSN                                    
REVDAT   2   24-FEB-09 3FRU    1       VERSN                                    
REVDAT   1   10-JUN-98 3FRU    0                                                
SPRSDE     10-JUN-98 3FRU      1FRU                                             
JRNL        AUTH   D.E.VAUGHN,P.J.BJORKMAN                                      
JRNL        TITL   STRUCTURAL BASIS OF PH-DEPENDENT ANTIBODY BINDING BY THE     
JRNL        TITL 2 NEONATAL FC RECEPTOR.                                        
JRNL        REF    STRUCTURE                     V.   6    63 1998              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   9493268                                                      
JRNL        DOI    10.1016/S0969-2126(98)00008-2                                
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 A RESOLUTION OF THE MHC-RELATED     
REMARK   1  TITL 2 NEONATAL FC RECEPTOR                                         
REMARK   1  REF    NATURE                        V. 372   336 1994              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS DEVELOPMENTAL                                    
REMARK   3   AUTHORS     : NULL                                                 
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
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)   (%) : 86.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 83821                          
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) : 0.232                           
REMARK   3   FREE R VALUE                     : 0.276                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
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            : 8877                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 220                                     
REMARK   3   SOLVENT ATOMS            : 620                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -7.40800                                             
REMARK   3    B22 (A**2) : 13.02200                                             
REMARK   3    B33 (A**2) : -5.61400                                             
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) : 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) : 0.013                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.600                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT                                                 
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 82.37                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : RESTRAINED                                              
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : 30.   ; 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  : PARAM3.CHO                                     
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3FRU 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_1000178966.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : JAN-92                             
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : F1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.918                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : FUJI                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM, CCP4                       
REMARK 200  DATA SCALING SOFTWARE          : CCP4                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 83821                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.0                               
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : 0.07200                            
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: MIR                          
REMARK 200 SOFTWARE USED: CCP4                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.5                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       74.80000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       74.80000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       63.25000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       95.85000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       63.25000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       95.85000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       74.80000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       63.25000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       95.85000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       74.80000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       63.25000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       95.85000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: THIS ENTRY CONSISTS OF THREE FCRN HETERODIMERS AS THEY       
REMARK 300 ARE ARRANGED IN THE ASYMMETRIC UNIT.  THE HEAVY CHAINS               
REMARK 300 COMPRISE RESIDUES A 1 - A 269, C 1 - C 269, AND E 5 -                
REMARK 300 E 269.  WITHIN EACH HEAVY CHAIN THERE ARE THREE DOMAINS:             
REMARK 300 ALPHA1 (1 - 87), ALPHA2 (88 - 179) AND ALPHA3 (179 - 269).           
REMARK 300 THE LIGHT CHAINS ARE B 1 - B 99 (ASSOCIATED WITH HEAVY               
REMARK 300 CHAIN A), D 1 - D 99 (ASSOCIATED WITH HEAVY CHAIN C) AND             
REMARK 300 F 1 - F 99 (ASSOCIATED WITH HEAVY CHAIN E).                          
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4810 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20420 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, G                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 4.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3130 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
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 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    HOH E   422     O    HOH E   473              1.87            
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 108   C   -  N   -  CA  ANGL. DEV. =   9.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A   3      109.15    -42.04                                   
REMARK 500    ARG A  42      -17.89   -142.59                                   
REMARK 500    GLN A  43       18.30     57.28                                   
REMARK 500    SER A 221       21.76   -146.63                                   
REMARK 500    ASN B  21     -159.95   -156.46                                   
REMARK 500    HIS B  31      126.77   -176.62                                   
REMARK 500    SER B  55     -168.24   -123.78                                   
REMARK 500    TRP B  60       -8.27     77.68                                   
REMARK 500    ARG B  97      -12.07    -49.03                                   
REMARK 500    PRO C   3      116.41    -39.43                                   
REMARK 500    ASN C 104        4.59     81.79                                   
REMARK 500    THR C 159      -62.15   -120.48                                   
REMARK 500    SER C 193      109.78    -37.31                                   
REMARK 500    SER C 221       17.99   -147.78                                   
REMARK 500    HIS C 250       -8.72    -56.51                                   
REMARK 500    TRP D  60      -12.32     81.31                                   
REMARK 500    ARG D  97       -6.69    -57.64                                   
REMARK 500    PRO E   3      107.92    -39.17                                   
REMARK 500    TRP E  51       -9.27    -54.69                                   
REMARK 500    ALA E 110       96.50   -160.15                                   
REMARK 500    PHE E 119       -1.37   -142.17                                   
REMARK 500    ASN E 192     -175.56    -65.26                                   
REMARK 500    SER E 204       70.47     44.77                                   
REMARK 500    SER E 221       16.68   -150.26                                   
REMARK 500    PRO E 264      142.39    -39.12                                   
REMARK 500    SER F  52     -178.14    -69.35                                   
REMARK 500    SER F  55     -169.62   -123.41                                   
REMARK 500    TRP F  60       -7.21     75.39                                   
REMARK 500    ARG F  97       -0.12    -56.63                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3FRU A    1   269  UNP    P13599   FCGN_RAT        23    291             
DBREF  3FRU B    1    99  UNP    P07151   B2MG_RAT        21    119             
DBREF  3FRU C    1   269  UNP    P13599   FCGN_RAT        23    291             
DBREF  3FRU D    1    99  UNP    P07151   B2MG_RAT        21    119             
DBREF  3FRU E    1   269  UNP    P13599   FCGN_RAT        23    291             
DBREF  3FRU F    1    99  UNP    P07151   B2MG_RAT        21    119             
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  269  ALA GLU PRO ARG LEU PRO LEU MET TYR HIS LEU ALA ALA          
SEQRES   2 C  269  VAL SER ASP LEU SER THR GLY LEU PRO SER PHE TRP ALA          
SEQRES   3 C  269  THR GLY TRP LEU GLY ALA GLN GLN TYR LEU THR TYR ASN          
SEQRES   4 C  269  ASN LEU ARG GLN GLU ALA ASP PRO CYS GLY ALA TRP ILE          
SEQRES   5 C  269  TRP GLU ASN GLN VAL SER TRP TYR TRP GLU LYS GLU THR          
SEQRES   6 C  269  THR ASP LEU LYS SER LYS GLU GLN LEU PHE LEU GLU ALA          
SEQRES   7 C  269  ILE ARG THR LEU GLU ASN GLN ILE ASN GLY THR PHE THR          
SEQRES   8 C  269  LEU GLN GLY LEU LEU GLY CYS GLU LEU ALA PRO ASP ASN          
SEQRES   9 C  269  SER SER LEU PRO THR ALA VAL PHE ALA LEU ASN GLY GLU          
SEQRES  10 C  269  GLU PHE MET ARG PHE ASN PRO ARG THR GLY ASN TRP SER          
SEQRES  11 C  269  GLY GLU TRP PRO GLU THR ASP ILE VAL GLY ASN LEU TRP          
SEQRES  12 C  269  MET LYS GLN PRO GLU ALA ALA ARG LYS GLU SER GLU PHE          
SEQRES  13 C  269  LEU LEU THR SER CYS PRO GLU ARG LEU LEU GLY HIS LEU          
SEQRES  14 C  269  GLU ARG GLY ARG GLN ASN LEU GLU TRP LYS GLU PRO PRO          
SEQRES  15 C  269  SER MET ARG LEU LYS ALA ARG PRO GLY ASN SER GLY SER          
SEQRES  16 C  269  SER VAL LEU THR CYS ALA ALA PHE SER PHE TYR PRO PRO          
SEQRES  17 C  269  GLU LEU LYS PHE ARG PHE LEU ARG ASN GLY LEU ALA SER          
SEQRES  18 C  269  GLY SER GLY ASN CYS SER THR GLY PRO ASN GLY ASP GLY          
SEQRES  19 C  269  SER PHE HIS ALA TRP SER LEU LEU GLU VAL LYS ARG GLY          
SEQRES  20 C  269  ASP GLU HIS HIS TYR GLN CYS GLN VAL GLU HIS GLU GLY          
SEQRES  21 C  269  LEU ALA GLN PRO LEU THR VAL ASP LEU                          
SEQRES   1 D   99  ILE GLN LYS THR PRO GLN ILE GLN VAL TYR SER ARG HIS          
SEQRES   2 D   99  PRO PRO GLU ASN GLY LYS PRO ASN PHE LEU ASN CYS TYR          
SEQRES   3 D   99  VAL SER GLN PHE HIS PRO PRO GLN ILE GLU ILE GLU LEU          
SEQRES   4 D   99  LEU LYS ASN GLY LYS LYS ILE PRO ASN ILE GLU MET SER          
SEQRES   5 D   99  ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR ILE LEU          
SEQRES   6 D   99  ALA HIS THR GLU PHE THR PRO THR GLU THR ASP VAL TYR          
SEQRES   7 D   99  ALA CYS ARG VAL LYS HIS VAL THR LEU LYS GLU PRO LYS          
SEQRES   8 D   99  THR VAL THR TRP ASP ARG ASP MET                              
SEQRES   1 E  269  ALA GLU PRO ARG LEU PRO LEU MET TYR HIS LEU ALA ALA          
SEQRES   2 E  269  VAL SER ASP LEU SER THR GLY LEU PRO SER PHE TRP ALA          
SEQRES   3 E  269  THR GLY TRP LEU GLY ALA GLN GLN TYR LEU THR TYR ASN          
SEQRES   4 E  269  ASN LEU ARG GLN GLU ALA ASP PRO CYS GLY ALA TRP ILE          
SEQRES   5 E  269  TRP GLU ASN GLN VAL SER TRP TYR TRP GLU LYS GLU THR          
SEQRES   6 E  269  THR ASP LEU LYS SER LYS GLU GLN LEU PHE LEU GLU ALA          
SEQRES   7 E  269  ILE ARG THR LEU GLU ASN GLN ILE ASN GLY THR PHE THR          
SEQRES   8 E  269  LEU GLN GLY LEU LEU GLY CYS GLU LEU ALA PRO ASP ASN          
SEQRES   9 E  269  SER SER LEU PRO THR ALA VAL PHE ALA LEU ASN GLY GLU          
SEQRES  10 E  269  GLU PHE MET ARG PHE ASN PRO ARG THR GLY ASN TRP SER          
SEQRES  11 E  269  GLY GLU TRP PRO GLU THR ASP ILE VAL GLY ASN LEU TRP          
SEQRES  12 E  269  MET LYS GLN PRO GLU ALA ALA ARG LYS GLU SER GLU PHE          
SEQRES  13 E  269  LEU LEU THR SER CYS PRO GLU ARG LEU LEU GLY HIS LEU          
SEQRES  14 E  269  GLU ARG GLY ARG GLN ASN LEU GLU TRP LYS GLU PRO PRO          
SEQRES  15 E  269  SER MET ARG LEU LYS ALA ARG PRO GLY ASN SER GLY SER          
SEQRES  16 E  269  SER VAL LEU THR CYS ALA ALA PHE SER PHE TYR PRO PRO          
SEQRES  17 E  269  GLU LEU LYS PHE ARG PHE LEU ARG ASN GLY LEU ALA SER          
SEQRES  18 E  269  GLY SER GLY ASN CYS SER THR GLY PRO ASN GLY ASP GLY          
SEQRES  19 E  269  SER PHE HIS ALA TRP SER LEU LEU GLU VAL LYS ARG GLY          
SEQRES  20 E  269  ASP GLU HIS HIS TYR GLN CYS GLN VAL GLU HIS GLU GLY          
SEQRES  21 E  269  LEU ALA GLN PRO LEU THR VAL ASP LEU                          
SEQRES   1 F   99  ILE GLN LYS THR PRO GLN ILE GLN VAL TYR SER ARG HIS          
SEQRES   2 F   99  PRO PRO GLU ASN GLY LYS PRO ASN PHE LEU ASN CYS TYR          
SEQRES   3 F   99  VAL SER GLN PHE HIS PRO PRO GLN ILE GLU ILE GLU LEU          
SEQRES   4 F   99  LEU LYS ASN GLY LYS LYS ILE PRO ASN ILE GLU MET SER          
SEQRES   5 F   99  ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR ILE LEU          
SEQRES   6 F   99  ALA HIS THR GLU PHE THR PRO THR GLU THR ASP VAL TYR          
SEQRES   7 F   99  ALA CYS ARG VAL LYS HIS VAL THR LEU LYS GLU PRO LYS          
SEQRES   8 F   99  THR VAL THR TRP ASP ARG ASP MET                              
MODRES 3FRU ASN A  104  ASN  GLYCOSYLATION SITE                                 
MODRES 3FRU ASN A  225  ASN  GLYCOSYLATION SITE                                 
MODRES 3FRU ASN C  104  ASN  GLYCOSYLATION SITE                                 
MODRES 3FRU ASN C  225  ASN  GLYCOSYLATION SITE                                 
HET    NAG  G   1      14                                                       
HET    NDG  G   2      14                                                       
HET    BMA  G   3      11                                                       
HET    MAN  G   4      11                                                       
HET    NAG  G   5      14                                                       
HET    GAL  G   6      11                                                       
HET    FUL  G   7      10                                                       
HET    NAG  H   1      14                                                       
HET    NAG  H   2      14                                                       
HET    BMA  H   3      11                                                       
HET    MAN  H   4      11                                                       
HET    NDG  H   5      14                                                       
HET    GAL  H   6      11                                                       
HET    FUC  H   7      10                                                       
HET    NAG  A 401      14                                                       
HET    SO4  A 325       5                                                       
HET    SO4  A 326       5                                                       
HET    BME  B 420       4                                                       
HET    NAG  C 401      14                                                       
HET    BME  C 420       4                                                       
HET    BME  E 420       4                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     NDG 2-ACETAMIDO-2-DEOXY-ALPHA-D-GLUCOPYRANOSE                        
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
HETNAM     GAL BETA-D-GALACTOPYRANOSE                                           
HETNAM     FUL BETA-L-FUCOPYRANOSE                                              
HETNAM     FUC ALPHA-L-FUCOPYRANOSE                                             
HETNAM     SO4 SULFATE ION                                                      
HETNAM     BME BETA-MERCAPTOETHANOL                                             
HETSYN     FUL 6-DEOXY-BETA-L-GALACTOSE                                         
FORMUL   7  NAG    6(C8 H15 N O6)                                               
FORMUL   7  NDG    2(C8 H15 N O6)                                               
FORMUL   7  BMA    2(C6 H12 O6)                                                 
FORMUL   7  MAN    2(C6 H12 O6)                                                 
FORMUL   7  GAL    2(C6 H12 O6)                                                 
FORMUL   7  FUL    C6 H12 O5                                                    
FORMUL   8  FUC    C6 H12 O5                                                    
FORMUL  10  SO4    2(O4 S 2-)                                                   
FORMUL  12  BME    3(C2 H6 O S)                                                 
FORMUL  16  HOH   *620(H2 O)                                                    
HELIX    1   1 GLY A   49  TRP A   53  5                                   5    
HELIX    2   2 TYR A   60  GLN A   85  1                                  26    
HELIX    3   3 PRO A  134  MET A  144  1                                  11    
HELIX    4   4 PRO A  147  LEU A  176  1                                  30    
HELIX    5   5 GLU A  249  HIS A  251  5                                   3    
HELIX    6   6 GLY C   49  TRP C   53  5                                   5    
HELIX    7   7 TYR C   60  GLN C   85  1                                  26    
HELIX    8   8 PRO C  134  LYS C  145  1                                  12    
HELIX    9   9 PRO C  147  LEU C  176  1                                  30    
HELIX   10  10 GLU C  249  HIS C  251  5                                   3    
HELIX   11  11 GLY E   49  ILE E   52  5                                   4    
HELIX   12  12 TYR E   60  GLN E   85  1                                  26    
HELIX   13  13 PRO E  134  MET E  144  1                                  11    
HELIX   14  14 PRO E  147  LEU E  176  1                                  30    
HELIX   15  15 GLU E  249  HIS E  251  5                                   3    
SHEET    1  AA 8 ASN A 128  SER A 130  0                                        
SHEET    2  AA 8 GLU A 117  ASN A 123 -1  N  ASN A 123   O  ASN A 128           
SHEET    3  AA 8 SER A 106  LEU A 114 -1  N  LEU A 114   O  GLU A 117           
SHEET    4  AA 8 THR A  91  LEU A 100 -1  N  GLU A  99   O  LEU A 107           
SHEET    5  AA 8 LEU A   7  VAL A  14 -1  N  ALA A  13   O  LEU A  92           
SHEET    6  AA 8 PHE A  24  LEU A  30 -1  N  TRP A  29   O  MET A   8           
SHEET    7  AA 8 GLN A  33  ASN A  39 -1  N  TYR A  38   O  ALA A  26           
SHEET    8  AA 8 ALA A  45  CYS A  48 -1  N  ASP A  46   O  THR A  37           
SHEET    1  AB 4 SER A 183  PRO A 190  0                                        
SHEET    2  AB 4 SER A 195  PHE A 205 -1  N  PHE A 203   O  SER A 183           
SHEET    3  AB 4 PHE A 236  LYS A 245 -1  N  VAL A 244   O  SER A 196           
SHEET    4  AB 4 ASN A 225  PRO A 230 -1  N  GLY A 229   O  HIS A 237           
SHEET    1  AC 4 LEU A 219  SER A 221  0                                        
SHEET    2  AC 4 LYS A 211  ARG A 216 -1  N  ARG A 216   O  LEU A 219           
SHEET    3  AC 4 TYR A 252  GLU A 257 -1  N  GLU A 257   O  LYS A 211           
SHEET    4  AC 4 LEU A 265  VAL A 267 -1  N  VAL A 267   O  CYS A 254           
SHEET    1 AD1 4 GLN B   6  SER B  11  0                                        
SHEET    2 AD1 4 PRO B  20  PHE B  30 -1  N  SER B  28   O  GLN B   6           
SHEET    3 AD1 4 PHE B  62  THR B  71 -1  N  PHE B  70   O  ASN B  21           
SHEET    4 AD1 4 ILE B  49  SER B  52 -1  N  GLU B  50   O  HIS B  67           
SHEET    1 AD2 4 GLN B   6  SER B  11  0                                        
SHEET    2 AD2 4 PRO B  20  PHE B  30 -1  N  SER B  28   O  GLN B   6           
SHEET    3 AD2 4 PHE B  62  THR B  71 -1  N  PHE B  70   O  ASN B  21           
SHEET    4 AD2 4 LEU B  54  SER B  57 -1  N  SER B  55   O  TYR B  63           
SHEET    1  AE 4 LYS B  44  ILE B  46  0                                        
SHEET    2  AE 4 GLU B  36  LYS B  41 -1  N  LYS B  41   O  LYS B  44           
SHEET    3  AE 4 TYR B  78  LYS B  83 -1  N  LYS B  83   O  GLU B  36           
SHEET    4  AE 4 LYS B  91  THR B  94 -1  N  VAL B  93   O  CYS B  80           
SHEET    1  BA 8 ASN C 128  SER C 130  0                                        
SHEET    2  BA 8 GLU C 117  ASN C 123 -1  N  ASN C 123   O  ASN C 128           
SHEET    3  BA 8 SER C 106  LEU C 114 -1  N  LEU C 114   O  GLU C 117           
SHEET    4  BA 8 THR C  91  LEU C 100 -1  N  GLU C  99   O  LEU C 107           
SHEET    5  BA 8 LEU C   7  VAL C  14 -1  N  ALA C  13   O  LEU C  92           
SHEET    6  BA 8 PHE C  24  LEU C  30 -1  N  TRP C  29   O  MET C   8           
SHEET    7  BA 8 GLN C  33  ASN C  39 -1  N  TYR C  38   O  ALA C  26           
SHEET    8  BA 8 ALA C  45  CYS C  48 -1  N  ASP C  46   O  THR C  37           
SHEET    1  BB 4 SER C 183  PRO C 190  0                                        
SHEET    2  BB 4 SER C 195  PHE C 205 -1  N  PHE C 203   O  SER C 183           
SHEET    3  BB 4 PHE C 236  LYS C 245 -1  N  VAL C 244   O  SER C 196           
SHEET    4  BB 4 ASN C 225  PRO C 230 -1  N  GLY C 229   O  HIS C 237           
SHEET    1  BC 4 LEU C 219  SER C 221  0                                        
SHEET    2  BC 4 LYS C 211  ARG C 216 -1  N  ARG C 216   O  LEU C 219           
SHEET    3  BC 4 TYR C 252  GLU C 257 -1  N  GLU C 257   O  LYS C 211           
SHEET    4  BC 4 LEU C 265  VAL C 267 -1  N  VAL C 267   O  CYS C 254           
SHEET    1 BD1 4 GLN D   6  SER D  11  0                                        
SHEET    2 BD1 4 PRO D  20  PHE D  30 -1  N  SER D  28   O  GLN D   6           
SHEET    3 BD1 4 PHE D  62  THR D  71 -1  N  PHE D  70   O  ASN D  21           
SHEET    4 BD1 4 ILE D  49  SER D  52 -1  N  GLU D  50   O  HIS D  67           
SHEET    1 BD2 4 GLN D   6  SER D  11  0                                        
SHEET    2 BD2 4 PRO D  20  PHE D  30 -1  N  SER D  28   O  GLN D   6           
SHEET    3 BD2 4 PHE D  62  THR D  71 -1  N  PHE D  70   O  ASN D  21           
SHEET    4 BD2 4 LEU D  54  SER D  57 -1  N  SER D  55   O  TYR D  63           
SHEET    1  BE 4 LYS D  44  ILE D  46  0                                        
SHEET    2  BE 4 GLU D  36  LYS D  41 -1  N  LYS D  41   O  LYS D  44           
SHEET    3  BE 4 TYR D  78  LYS D  83 -1  N  LYS D  83   O  GLU D  36           
SHEET    4  BE 4 LYS D  91  THR D  94 -1  N  VAL D  93   O  CYS D  80           
SHEET    1  CA 8 ASN E 128  SER E 130  0                                        
SHEET    2  CA 8 GLU E 117  ASN E 123 -1  N  ASN E 123   O  ASN E 128           
SHEET    3  CA 8 SER E 106  LEU E 114 -1  N  LEU E 114   O  GLU E 117           
SHEET    4  CA 8 THR E  91  LEU E 100 -1  N  GLU E  99   O  LEU E 107           
SHEET    5  CA 8 LEU E   7  VAL E  14 -1  N  ALA E  13   O  LEU E  92           
SHEET    6  CA 8 PHE E  24  LEU E  30 -1  N  TRP E  29   O  MET E   8           
SHEET    7  CA 8 GLN E  33  ASN E  39 -1  N  TYR E  38   O  ALA E  26           
SHEET    8  CA 8 ALA E  45  CYS E  48 -1  N  ASP E  46   O  THR E  37           
SHEET    1  CB 4 SER E 183  PRO E 190  0                                        
SHEET    2  CB 4 SER E 195  PHE E 205 -1  N  PHE E 203   O  SER E 183           
SHEET    3  CB 4 PHE E 236  LYS E 245 -1  N  VAL E 244   O  SER E 196           
SHEET    4  CB 4 ASN E 225  PRO E 230 -1  N  GLY E 229   O  HIS E 237           
SHEET    1  CC 4 LEU E 219  SER E 221  0                                        
SHEET    2  CC 4 LYS E 211  ARG E 216 -1  N  ARG E 216   O  LEU E 219           
SHEET    3  CC 4 TYR E 252  GLU E 257 -1  N  GLU E 257   O  LYS E 211           
SHEET    4  CC 4 LEU E 265  VAL E 267 -1  N  VAL E 267   O  CYS E 254           
SHEET    1 CD1 4 GLN F   6  SER F  11  0                                        
SHEET    2 CD1 4 PRO F  20  PHE F  30 -1  N  SER F  28   O  GLN F   6           
SHEET    3 CD1 4 PHE F  62  THR F  71 -1  N  PHE F  70   O  ASN F  21           
SHEET    4 CD1 4 ILE F  49  SER F  52 -1  N  GLU F  50   O  HIS F  67           
SHEET    1 CD2 4 GLN F   6  SER F  11  0                                        
SHEET    2 CD2 4 PRO F  20  PHE F  30 -1  N  SER F  28   O  GLN F   6           
SHEET    3 CD2 4 PHE F  62  THR F  71 -1  N  PHE F  70   O  ASN F  21           
SHEET    4 CD2 4 LEU F  54  SER F  57 -1  N  SER F  55   O  TYR F  63           
SHEET    1  CE 4 LYS F  44  ILE F  46  0                                        
SHEET    2  CE 4 GLU F  36  LYS F  41 -1  N  LYS F  41   O  LYS F  44           
SHEET    3  CE 4 TYR F  78  LYS F  83 -1  N  LYS F  83   O  GLU F  36           
SHEET    4  CE 4 LYS F  91  THR F  94 -1  N  VAL F  93   O  CYS F  80           
SSBOND   1 CYS A  200    CYS A  254                          1555   1555  2.05  
SSBOND   2 CYS B   25    CYS B   80                          1555   1555  2.05  
SSBOND   3 CYS C  200    CYS C  254                          1555   1555  2.04  
SSBOND   4 CYS D   25    CYS D   80                          1555   1555  2.05  
SSBOND   5 CYS E  200    CYS E  254                          1555   1555  2.04  
SSBOND   6 CYS F   25    CYS F   80                          1555   1555  2.04  
LINK         ND2 ASN A 104                 C1  NAG A 401     1555   1555  1.45  
LINK         ND2 ASN A 225                 C1  NAG G   1     1555   1555  1.45  
LINK         ND2 ASN C 104                 C1  NAG C 401     1555   1555  1.45  
LINK         ND2 ASN C 225                 C1  NAG H   1     1555   1555  1.50  
LINK         O4  NAG G   1                 C1  NDG G   2     1555   1555  1.39  
LINK         O6  NAG G   1                 C1  FUL G   7     1555   1555  1.40  
LINK         O4  NDG G   2                 C1  BMA G   3     1555   1555  1.39  
LINK         O6  BMA G   3                 C1  MAN G   4     1555   1555  1.42  
LINK         O2  MAN G   4                 C1  NAG G   5     1555   1555  1.38  
LINK         O4  NAG G   5                 C1  GAL G   6     1555   1555  1.39  
LINK         O4  NAG H   1                 C1  NAG H   2     1555   1555  1.41  
LINK         O6  NAG H   1                 C1  FUC H   7     1555   1555  1.41  
LINK         O4  NAG H   2                 C1  BMA H   3     1555   1555  1.40  
LINK         O6  BMA H   3                 C1  MAN H   4     1555   1555  1.41  
LINK         O2  MAN H   4                 C1  NDG H   5     1555   1555  1.40  
LINK         O4  NDG H   5                 C1  GAL H   6     1555   1555  1.39  
CISPEP   1 TYR A  206    PRO A  207          0        -0.07                     
CISPEP   2 HIS B   31    PRO B   32          0         1.01                     
CISPEP   3 TYR C  206    PRO C  207          0        -0.02                     
CISPEP   4 HIS D   31    PRO D   32          0         0.59                     
CISPEP   5 TYR E  206    PRO E  207          0        -0.10                     
CISPEP   6 HIS F   31    PRO F   32          0         0.44                     
CRYST1  126.500  191.700  149.600  90.00  90.00  90.00 C 2 2 21     24          
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      0.007905  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005216  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006684        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system