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Database: PDB
Entry: 3QD6
LinkDB: 3QD6
Original site: 3QD6 
HEADER    CYTOKINE/CYTOKINE RECEPTOR              18-JAN-11   3QD6              
TITLE     CRYSTAL STRUCTURE OF THE CD40 AND CD154 (CD40L) COMPLEX               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CD40 LIGAND;                                               
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 FRAGMENT: SECRETED FORM, SOLUBLE FORM;                               
COMPND   5 SYNONYM: CD40-L;                                                     
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 5;       
COMPND   9 CHAIN: R, S, T, U;                                                   
COMPND  10 FRAGMENT: EXTRACELLULAR DOMAIN;                                      
COMPND  11 SYNONYM: CD40L RECEPTOR;                                             
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CD154, CD40L;                                                  
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;                              
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PACGP67A;                                 
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 GENE: CD40;                                                          
SOURCE  17 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  18 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  21 EXPRESSION_SYSTEM_PLASMID: PVL1393                                   
KEYWDS    IMMUNE REGULATOR, RECEPTOR, CYTOKINE-CYTOKINE RECEPTOR COMPLEX        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.-O.LEE,Y.J.KIM,D.H.SONG,H.M.KIM,B.S.PARK                            
REVDAT   3   29-JUL-20 3QD6    1       COMPND REMARK SEQADV HETNAM              
REVDAT   3 2                   1       LINK   SITE                              
REVDAT   2   21-MAR-12 3QD6    1       JRNL   VERSN                             
REVDAT   1   02-FEB-11 3QD6    0                                                
JRNL        AUTH   H.-J.AN,Y.J.KIM,D.H.SONG,B.S.PARK,H.M.KIM,J.D.LEE,S.-G.PAIK, 
JRNL        AUTH 2 J.-O.LEE,H.LEE                                               
JRNL        TITL   CRYSTALLOGRAPHIC AND MUTATIONAL ANALYSIS OF THE CD40-CD154   
JRNL        TITL 2 COMPLEX AND ITS IMPLICATIONS FOR RECEPTOR ACTIVATION         
JRNL        REF    J.BIOL.CHEM.                  V. 286 11226 2011              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   21285457                                                     
JRNL        DOI    10.1074/JBC.M110.208215                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.3                                              
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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 114.96                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 3313622.000                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 24857                          
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) : 0.245                           
REMARK   3   FREE R VALUE                     : 0.298                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1209                            
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           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.72                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3962                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2650                       
REMARK   3   BIN FREE R VALUE                    : 0.3000                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.30                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 220                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.020                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9812                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 84                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 68.39                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.61000                                             
REMARK   3    B22 (A**2) : -2.61000                                             
REMARK   3    B33 (A**2) : 5.23000                                              
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) : 0.38                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.55                            
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) : 0.47                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.45                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.400                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.860                           
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  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.33                                                 
REMARK   3   BSOL        : 45.55                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : DNA-RNA_REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : CARBOHYDRATE.TOP                               
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 3QD6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-JAN-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000063495.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-JUL-06                          
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               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0050                             
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.2.25                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24906                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 114.961                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.7                               
REMARK 200  DATA REDUNDANCY                : 2.600                              
REMARK 200  R MERGE                    (I) : 0.10200                            
REMARK 200  R SYM                      (I) : 0.10200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.35100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.1.1                                          
REMARK 200 STARTING MODEL: 1ALY                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.27                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG6000, 0.1M MOPS, 10%              
REMARK 280  ISOPROPANOL, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE     
REMARK 280  295K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      140.76733            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       70.38367            
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      105.57550            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       35.19183            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      175.95917            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, R, S                         
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: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F, T, U                         
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   113                                                      
REMARK 465     ASP A   114                                                      
REMARK 465     PRO A   115                                                      
REMARK 465     GLY A   116                                                      
REMARK 465     ASP A   117                                                      
REMARK 465     GLN A   118                                                      
REMARK 465     ASN A   180                                                      
REMARK 465     ARG A   181                                                      
REMARK 465     GLU A   182                                                      
REMARK 465     ALA A   183                                                      
REMARK 465     SER A   184                                                      
REMARK 465     SER A   185                                                      
REMARK 465     GLN A   186                                                      
REMARK 465     ALA A   187                                                      
REMARK 465     ALA B   113                                                      
REMARK 465     ASP B   114                                                      
REMARK 465     PRO B   115                                                      
REMARK 465     GLY B   116                                                      
REMARK 465     ASP B   117                                                      
REMARK 465     GLN B   118                                                      
REMARK 465     ASN B   180                                                      
REMARK 465     ARG B   181                                                      
REMARK 465     GLU B   182                                                      
REMARK 465     ALA B   183                                                      
REMARK 465     SER B   184                                                      
REMARK 465     SER B   185                                                      
REMARK 465     GLN B   186                                                      
REMARK 465     ALA B   187                                                      
REMARK 465     ALA C   113                                                      
REMARK 465     ASP C   114                                                      
REMARK 465     PRO C   115                                                      
REMARK 465     GLY C   116                                                      
REMARK 465     ASP C   117                                                      
REMARK 465     GLN C   118                                                      
REMARK 465     ASN C   180                                                      
REMARK 465     ARG C   181                                                      
REMARK 465     GLU C   182                                                      
REMARK 465     ALA C   183                                                      
REMARK 465     SER C   184                                                      
REMARK 465     SER C   185                                                      
REMARK 465     GLN C   186                                                      
REMARK 465     ALA C   187                                                      
REMARK 465     ALA D   113                                                      
REMARK 465     ASP D   114                                                      
REMARK 465     PRO D   115                                                      
REMARK 465     GLY D   116                                                      
REMARK 465     ASP D   117                                                      
REMARK 465     GLN D   118                                                      
REMARK 465     ASN D   180                                                      
REMARK 465     ARG D   181                                                      
REMARK 465     GLU D   182                                                      
REMARK 465     ALA D   183                                                      
REMARK 465     SER D   184                                                      
REMARK 465     SER D   185                                                      
REMARK 465     GLN D   186                                                      
REMARK 465     ALA D   187                                                      
REMARK 465     ALA E   113                                                      
REMARK 465     ASP E   114                                                      
REMARK 465     PRO E   115                                                      
REMARK 465     GLY E   116                                                      
REMARK 465     ASP E   117                                                      
REMARK 465     GLN E   118                                                      
REMARK 465     ASN E   180                                                      
REMARK 465     ARG E   181                                                      
REMARK 465     GLU E   182                                                      
REMARK 465     ALA E   183                                                      
REMARK 465     SER E   184                                                      
REMARK 465     SER E   185                                                      
REMARK 465     GLN E   186                                                      
REMARK 465     ALA E   187                                                      
REMARK 465     ALA F   113                                                      
REMARK 465     ASP F   114                                                      
REMARK 465     PRO F   115                                                      
REMARK 465     GLY F   116                                                      
REMARK 465     ASP F   117                                                      
REMARK 465     GLN F   118                                                      
REMARK 465     ASN F   180                                                      
REMARK 465     ARG F   181                                                      
REMARK 465     GLU F   182                                                      
REMARK 465     ALA F   183                                                      
REMARK 465     SER F   184                                                      
REMARK 465     SER F   185                                                      
REMARK 465     GLN F   186                                                      
REMARK 465     ALA F   187                                                      
REMARK 465     GLU R    21                                                      
REMARK 465     PRO R    22                                                      
REMARK 465     PRO R    23                                                      
REMARK 465     THR R    24                                                      
REMARK 465     ALA R    25                                                      
REMARK 465     SER R   126                                                      
REMARK 465     PRO R   127                                                      
REMARK 465     GLY R   128                                                      
REMARK 465     PHE R   129                                                      
REMARK 465     GLY R   130                                                      
REMARK 465     VAL R   131                                                      
REMARK 465     CYS R   146                                                      
REMARK 465     PRO R   147                                                      
REMARK 465     VAL R   148                                                      
REMARK 465     GLY R   149                                                      
REMARK 465     PHE R   150                                                      
REMARK 465     PHE R   151                                                      
REMARK 465     SER R   152                                                      
REMARK 465     ASN R   153                                                      
REMARK 465     VAL R   154                                                      
REMARK 465     SER R   155                                                      
REMARK 465     SER R   156                                                      
REMARK 465     ALA R   157                                                      
REMARK 465     PHE R   158                                                      
REMARK 465     GLU R   159                                                      
REMARK 465     LYS R   160                                                      
REMARK 465     CYS R   161                                                      
REMARK 465     HIS R   162                                                      
REMARK 465     PRO R   163                                                      
REMARK 465     TRP R   164                                                      
REMARK 465     THR R   165                                                      
REMARK 465     SER R   166                                                      
REMARK 465     CYS R   167                                                      
REMARK 465     GLU R   168                                                      
REMARK 465     THR R   169                                                      
REMARK 465     LYS R   170                                                      
REMARK 465     ASP R   171                                                      
REMARK 465     LEU R   172                                                      
REMARK 465     VAL R   173                                                      
REMARK 465     VAL R   174                                                      
REMARK 465     GLN R   175                                                      
REMARK 465     GLN R   176                                                      
REMARK 465     ALA R   177                                                      
REMARK 465     GLY R   178                                                      
REMARK 465     THR R   179                                                      
REMARK 465     ASN R   180                                                      
REMARK 465     LYS R   181                                                      
REMARK 465     THR R   182                                                      
REMARK 465     ASP R   183                                                      
REMARK 465     VAL R   184                                                      
REMARK 465     VAL R   185                                                      
REMARK 465     CYS R   186                                                      
REMARK 465     GLY R   187                                                      
REMARK 465     PRO R   188                                                      
REMARK 465     GLN R   189                                                      
REMARK 465     ASP R   190                                                      
REMARK 465     SER R   191                                                      
REMARK 465     GLY R   192                                                      
REMARK 465     ARG R   193                                                      
REMARK 465     LEU R   194                                                      
REMARK 465     VAL R   195                                                      
REMARK 465     PRO R   196                                                      
REMARK 465     ARG R   197                                                      
REMARK 465     SER S   126                                                      
REMARK 465     PRO S   127                                                      
REMARK 465     GLY S   128                                                      
REMARK 465     PHE S   129                                                      
REMARK 465     GLY S   130                                                      
REMARK 465     VAL S   131                                                      
REMARK 465     CYS S   146                                                      
REMARK 465     PRO S   147                                                      
REMARK 465     VAL S   148                                                      
REMARK 465     GLY S   149                                                      
REMARK 465     PHE S   150                                                      
REMARK 465     PHE S   151                                                      
REMARK 465     SER S   152                                                      
REMARK 465     ASN S   153                                                      
REMARK 465     VAL S   154                                                      
REMARK 465     SER S   155                                                      
REMARK 465     SER S   156                                                      
REMARK 465     ALA S   157                                                      
REMARK 465     PHE S   158                                                      
REMARK 465     GLU S   159                                                      
REMARK 465     LYS S   160                                                      
REMARK 465     CYS S   161                                                      
REMARK 465     HIS S   162                                                      
REMARK 465     PRO S   163                                                      
REMARK 465     TRP S   164                                                      
REMARK 465     THR S   165                                                      
REMARK 465     SER S   166                                                      
REMARK 465     CYS S   167                                                      
REMARK 465     GLU S   168                                                      
REMARK 465     THR S   169                                                      
REMARK 465     LYS S   170                                                      
REMARK 465     ASP S   171                                                      
REMARK 465     LEU S   172                                                      
REMARK 465     VAL S   173                                                      
REMARK 465     VAL S   174                                                      
REMARK 465     GLN S   175                                                      
REMARK 465     GLN S   176                                                      
REMARK 465     ALA S   177                                                      
REMARK 465     GLY S   178                                                      
REMARK 465     THR S   179                                                      
REMARK 465     ASN S   180                                                      
REMARK 465     LYS S   181                                                      
REMARK 465     THR S   182                                                      
REMARK 465     ASP S   183                                                      
REMARK 465     VAL S   184                                                      
REMARK 465     VAL S   185                                                      
REMARK 465     CYS S   186                                                      
REMARK 465     GLY S   187                                                      
REMARK 465     PRO S   188                                                      
REMARK 465     GLN S   189                                                      
REMARK 465     ASP S   190                                                      
REMARK 465     SER S   191                                                      
REMARK 465     GLY S   192                                                      
REMARK 465     ARG S   193                                                      
REMARK 465     LEU S   194                                                      
REMARK 465     VAL S   195                                                      
REMARK 465     PRO S   196                                                      
REMARK 465     ARG S   197                                                      
REMARK 465     GLU T    21                                                      
REMARK 465     PRO T    22                                                      
REMARK 465     PRO T    23                                                      
REMARK 465     THR T    24                                                      
REMARK 465     ALA T    25                                                      
REMARK 465     SER T   126                                                      
REMARK 465     PRO T   127                                                      
REMARK 465     GLY T   128                                                      
REMARK 465     PHE T   129                                                      
REMARK 465     GLY T   130                                                      
REMARK 465     VAL T   131                                                      
REMARK 465     CYS T   146                                                      
REMARK 465     PRO T   147                                                      
REMARK 465     VAL T   148                                                      
REMARK 465     GLY T   149                                                      
REMARK 465     PHE T   150                                                      
REMARK 465     PHE T   151                                                      
REMARK 465     SER T   152                                                      
REMARK 465     ASN T   153                                                      
REMARK 465     VAL T   154                                                      
REMARK 465     SER T   155                                                      
REMARK 465     SER T   156                                                      
REMARK 465     ALA T   157                                                      
REMARK 465     PHE T   158                                                      
REMARK 465     GLU T   159                                                      
REMARK 465     LYS T   160                                                      
REMARK 465     CYS T   161                                                      
REMARK 465     HIS T   162                                                      
REMARK 465     PRO T   163                                                      
REMARK 465     TRP T   164                                                      
REMARK 465     THR T   165                                                      
REMARK 465     SER T   166                                                      
REMARK 465     CYS T   167                                                      
REMARK 465     GLU T   168                                                      
REMARK 465     THR T   169                                                      
REMARK 465     LYS T   170                                                      
REMARK 465     ASP T   171                                                      
REMARK 465     LEU T   172                                                      
REMARK 465     VAL T   173                                                      
REMARK 465     VAL T   174                                                      
REMARK 465     GLN T   175                                                      
REMARK 465     GLN T   176                                                      
REMARK 465     ALA T   177                                                      
REMARK 465     GLY T   178                                                      
REMARK 465     THR T   179                                                      
REMARK 465     ASN T   180                                                      
REMARK 465     LYS T   181                                                      
REMARK 465     THR T   182                                                      
REMARK 465     ASP T   183                                                      
REMARK 465     VAL T   184                                                      
REMARK 465     VAL T   185                                                      
REMARK 465     CYS T   186                                                      
REMARK 465     GLY T   187                                                      
REMARK 465     PRO T   188                                                      
REMARK 465     GLN T   189                                                      
REMARK 465     ASP T   190                                                      
REMARK 465     SER T   191                                                      
REMARK 465     GLY T   192                                                      
REMARK 465     ARG T   193                                                      
REMARK 465     LEU T   194                                                      
REMARK 465     VAL T   195                                                      
REMARK 465     PRO T   196                                                      
REMARK 465     ARG T   197                                                      
REMARK 465     SER U   126                                                      
REMARK 465     PRO U   127                                                      
REMARK 465     GLY U   128                                                      
REMARK 465     PHE U   129                                                      
REMARK 465     GLY U   130                                                      
REMARK 465     VAL U   131                                                      
REMARK 465     CYS U   146                                                      
REMARK 465     PRO U   147                                                      
REMARK 465     VAL U   148                                                      
REMARK 465     GLY U   149                                                      
REMARK 465     PHE U   150                                                      
REMARK 465     PHE U   151                                                      
REMARK 465     SER U   152                                                      
REMARK 465     ASN U   153                                                      
REMARK 465     VAL U   154                                                      
REMARK 465     SER U   155                                                      
REMARK 465     SER U   156                                                      
REMARK 465     ALA U   157                                                      
REMARK 465     PHE U   158                                                      
REMARK 465     GLU U   159                                                      
REMARK 465     LYS U   160                                                      
REMARK 465     CYS U   161                                                      
REMARK 465     HIS U   162                                                      
REMARK 465     PRO U   163                                                      
REMARK 465     TRP U   164                                                      
REMARK 465     THR U   165                                                      
REMARK 465     SER U   166                                                      
REMARK 465     CYS U   167                                                      
REMARK 465     GLU U   168                                                      
REMARK 465     THR U   169                                                      
REMARK 465     LYS U   170                                                      
REMARK 465     ASP U   171                                                      
REMARK 465     LEU U   172                                                      
REMARK 465     VAL U   173                                                      
REMARK 465     VAL U   174                                                      
REMARK 465     GLN U   175                                                      
REMARK 465     GLN U   176                                                      
REMARK 465     ALA U   177                                                      
REMARK 465     GLY U   178                                                      
REMARK 465     THR U   179                                                      
REMARK 465     ASN U   180                                                      
REMARK 465     LYS U   181                                                      
REMARK 465     THR U   182                                                      
REMARK 465     ASP U   183                                                      
REMARK 465     VAL U   184                                                      
REMARK 465     VAL U   185                                                      
REMARK 465     CYS U   186                                                      
REMARK 465     GLY U   187                                                      
REMARK 465     PRO U   188                                                      
REMARK 465     GLN U   189                                                      
REMARK 465     ASP U   190                                                      
REMARK 465     SER U   191                                                      
REMARK 465     GLY U   192                                                      
REMARK 465     ARG U   193                                                      
REMARK 465     LEU U   194                                                      
REMARK 465     VAL U   195                                                      
REMARK 465     PRO U   196                                                      
REMARK 465     ARG U   197                                                      
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   SG   CYS F   194     O6   NAG F  1411              2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS A 194   CB    CYS A 194   SG      0.122                       
REMARK 500    CYS D 194   CB    CYS D 194   SG      0.111                       
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    CYS A 194   CA  -  CB  -  SG  ANGL. DEV. =   7.9 DEGREES          
REMARK 500    CYS B 194   CA  -  CB  -  SG  ANGL. DEV. =  11.2 DEGREES          
REMARK 500    CYS C 194   CA  -  CB  -  SG  ANGL. DEV. =   8.0 DEGREES          
REMARK 500    CYS D 194   CA  -  CB  -  SG  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    CYS E 194   CA  -  CB  -  SG  ANGL. DEV. =   6.7 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    ALA A 130       95.75    -49.51                                   
REMARK 500    SER A 132      -50.19    -16.55                                   
REMARK 500    LYS A 133      138.51    141.85                                   
REMARK 500    THR A 134       74.14     63.63                                   
REMARK 500    GLU A 142       44.74    -75.05                                   
REMARK 500    LYS A 143     -167.55   -108.63                                   
REMARK 500    ASN A 150     -176.12   -178.61                                   
REMARK 500    ASN A 151       20.98    -68.86                                   
REMARK 500    LEU A 155       78.67   -106.04                                   
REMARK 500    ALA A 173      140.25   -173.23                                   
REMARK 500    LEU A 193       59.59   -108.20                                   
REMARK 500    ARG A 203     -133.43   -130.63                                   
REMARK 500    LYS A 216      -90.17    -49.79                                   
REMARK 500    CYS A 218      -35.31   -173.69                                   
REMARK 500    ALA B 130      173.58    -56.47                                   
REMARK 500    THR B 135      155.63    -44.59                                   
REMARK 500    GLU B 142       36.20    -76.89                                   
REMARK 500    ASN B 150     -176.68   -179.71                                   
REMARK 500    ASN B 151       26.00    -68.63                                   
REMARK 500    LEU B 155       75.36   -109.37                                   
REMARK 500    ASN B 157       17.80     50.51                                   
REMARK 500    ALA B 173      137.35   -176.69                                   
REMARK 500    PHE B 189      117.73    -23.62                                   
REMARK 500    LEU B 193       52.15   -118.00                                   
REMARK 500    ARG B 203     -130.07   -134.86                                   
REMARK 500    LYS B 216      -95.23    -34.65                                   
REMARK 500    CYS B 218      -10.84   -154.47                                   
REMARK 500    ALA C 130      106.61    -57.00                                   
REMARK 500    THR C 134       68.78     31.54                                   
REMARK 500    GLU C 142       38.26    -75.03                                   
REMARK 500    SER C 149      -39.70    -37.91                                   
REMARK 500    ASN C 150     -174.28    177.69                                   
REMARK 500    ASN C 151       24.91    -69.91                                   
REMARK 500    LEU C 155       71.36   -108.14                                   
REMARK 500    ALA C 173      139.77   -171.59                                   
REMARK 500    CYS C 178      139.25   -171.84                                   
REMARK 500    ARG C 203     -131.88   -128.74                                   
REMARK 500    ASN C 210      161.73    179.18                                   
REMARK 500    SER C 214      104.53    -51.55                                   
REMARK 500    ALA C 215     -111.95   -100.62                                   
REMARK 500    LYS C 216      -73.85   -108.28                                   
REMARK 500    CYS C 218      -46.70   -148.27                                   
REMARK 500    THR C 251      114.68    -37.79                                   
REMARK 500    GLU D 142       38.13    -71.27                                   
REMARK 500    SER D 149      -38.03    -34.54                                   
REMARK 500    ASN D 150     -176.36    178.97                                   
REMARK 500    ASN D 151       22.61    -69.39                                   
REMARK 500    LEU D 155       69.43   -110.12                                   
REMARK 500    ASN D 157       17.80     54.61                                   
REMARK 500    PHE D 189      113.35     -7.63                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     173 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3QD6 A  116   261  UNP    P29965   CD40L_HUMAN    116    261             
DBREF  3QD6 B  116   261  UNP    P29965   CD40L_HUMAN    116    261             
DBREF  3QD6 C  116   261  UNP    P29965   CD40L_HUMAN    116    261             
DBREF  3QD6 D  116   261  UNP    P29965   CD40L_HUMAN    116    261             
DBREF  3QD6 E  116   261  UNP    P29965   CD40L_HUMAN    116    261             
DBREF  3QD6 F  116   261  UNP    P29965   CD40L_HUMAN    116    261             
DBREF  3QD6 R   21   190  UNP    P25942   TNR5_HUMAN      21    190             
DBREF  3QD6 S   21   190  UNP    P25942   TNR5_HUMAN      21    190             
DBREF  3QD6 T   21   190  UNP    P25942   TNR5_HUMAN      21    190             
DBREF  3QD6 U   21   190  UNP    P25942   TNR5_HUMAN      21    190             
SEQADV 3QD6 ALA A  113  UNP  P29965              EXPRESSION TAG                 
SEQADV 3QD6 ASP A  114  UNP  P29965              EXPRESSION TAG                 
SEQADV 3QD6 PRO A  115  UNP  P29965              EXPRESSION TAG                 
SEQADV 3QD6 ALA B  113  UNP  P29965              EXPRESSION TAG                 
SEQADV 3QD6 ASP B  114  UNP  P29965              EXPRESSION TAG                 
SEQADV 3QD6 PRO B  115  UNP  P29965              EXPRESSION TAG                 
SEQADV 3QD6 ALA C  113  UNP  P29965              EXPRESSION TAG                 
SEQADV 3QD6 ASP C  114  UNP  P29965              EXPRESSION TAG                 
SEQADV 3QD6 PRO C  115  UNP  P29965              EXPRESSION TAG                 
SEQADV 3QD6 ALA D  113  UNP  P29965              EXPRESSION TAG                 
SEQADV 3QD6 ASP D  114  UNP  P29965              EXPRESSION TAG                 
SEQADV 3QD6 PRO D  115  UNP  P29965              EXPRESSION TAG                 
SEQADV 3QD6 ALA E  113  UNP  P29965              EXPRESSION TAG                 
SEQADV 3QD6 ASP E  114  UNP  P29965              EXPRESSION TAG                 
SEQADV 3QD6 PRO E  115  UNP  P29965              EXPRESSION TAG                 
SEQADV 3QD6 ALA F  113  UNP  P29965              EXPRESSION TAG                 
SEQADV 3QD6 ASP F  114  UNP  P29965              EXPRESSION TAG                 
SEQADV 3QD6 PRO F  115  UNP  P29965              EXPRESSION TAG                 
SEQADV 3QD6 SER R  191  UNP  P25942              EXPRESSION TAG                 
SEQADV 3QD6 GLY R  192  UNP  P25942              EXPRESSION TAG                 
SEQADV 3QD6 ARG R  193  UNP  P25942              EXPRESSION TAG                 
SEQADV 3QD6 LEU R  194  UNP  P25942              EXPRESSION TAG                 
SEQADV 3QD6 VAL R  195  UNP  P25942              EXPRESSION TAG                 
SEQADV 3QD6 PRO R  196  UNP  P25942              EXPRESSION TAG                 
SEQADV 3QD6 ARG R  197  UNP  P25942              EXPRESSION TAG                 
SEQADV 3QD6 SER S  191  UNP  P25942              EXPRESSION TAG                 
SEQADV 3QD6 GLY S  192  UNP  P25942              EXPRESSION TAG                 
SEQADV 3QD6 ARG S  193  UNP  P25942              EXPRESSION TAG                 
SEQADV 3QD6 LEU S  194  UNP  P25942              EXPRESSION TAG                 
SEQADV 3QD6 VAL S  195  UNP  P25942              EXPRESSION TAG                 
SEQADV 3QD6 PRO S  196  UNP  P25942              EXPRESSION TAG                 
SEQADV 3QD6 ARG S  197  UNP  P25942              EXPRESSION TAG                 
SEQADV 3QD6 SER T  191  UNP  P25942              EXPRESSION TAG                 
SEQADV 3QD6 GLY T  192  UNP  P25942              EXPRESSION TAG                 
SEQADV 3QD6 ARG T  193  UNP  P25942              EXPRESSION TAG                 
SEQADV 3QD6 LEU T  194  UNP  P25942              EXPRESSION TAG                 
SEQADV 3QD6 VAL T  195  UNP  P25942              EXPRESSION TAG                 
SEQADV 3QD6 PRO T  196  UNP  P25942              EXPRESSION TAG                 
SEQADV 3QD6 ARG T  197  UNP  P25942              EXPRESSION TAG                 
SEQADV 3QD6 SER U  191  UNP  P25942              EXPRESSION TAG                 
SEQADV 3QD6 GLY U  192  UNP  P25942              EXPRESSION TAG                 
SEQADV 3QD6 ARG U  193  UNP  P25942              EXPRESSION TAG                 
SEQADV 3QD6 LEU U  194  UNP  P25942              EXPRESSION TAG                 
SEQADV 3QD6 VAL U  195  UNP  P25942              EXPRESSION TAG                 
SEQADV 3QD6 PRO U  196  UNP  P25942              EXPRESSION TAG                 
SEQADV 3QD6 ARG U  197  UNP  P25942              EXPRESSION TAG                 
SEQRES   1 A  149  ALA ASP PRO GLY ASP GLN ASN PRO GLN ILE ALA ALA HIS          
SEQRES   2 A  149  VAL ILE SER GLU ALA SER SER LYS THR THR SER VAL LEU          
SEQRES   3 A  149  GLN TRP ALA GLU LYS GLY TYR TYR THR MET SER ASN ASN          
SEQRES   4 A  149  LEU VAL THR LEU GLU ASN GLY LYS GLN LEU THR VAL LYS          
SEQRES   5 A  149  ARG GLN GLY LEU TYR TYR ILE TYR ALA GLN VAL THR PHE          
SEQRES   6 A  149  CYS SER ASN ARG GLU ALA SER SER GLN ALA PRO PHE ILE          
SEQRES   7 A  149  ALA SER LEU CYS LEU LYS SER PRO GLY ARG PHE GLU ARG          
SEQRES   8 A  149  ILE LEU LEU ARG ALA ALA ASN THR HIS SER SER ALA LYS          
SEQRES   9 A  149  PRO CYS GLY GLN GLN SER ILE HIS LEU GLY GLY VAL PHE          
SEQRES  10 A  149  GLU LEU GLN PRO GLY ALA SER VAL PHE VAL ASN VAL THR          
SEQRES  11 A  149  ASP PRO SER GLN VAL SER HIS GLY THR GLY PHE THR SER          
SEQRES  12 A  149  PHE GLY LEU LEU LYS LEU                                      
SEQRES   1 B  149  ALA ASP PRO GLY ASP GLN ASN PRO GLN ILE ALA ALA HIS          
SEQRES   2 B  149  VAL ILE SER GLU ALA SER SER LYS THR THR SER VAL LEU          
SEQRES   3 B  149  GLN TRP ALA GLU LYS GLY TYR TYR THR MET SER ASN ASN          
SEQRES   4 B  149  LEU VAL THR LEU GLU ASN GLY LYS GLN LEU THR VAL LYS          
SEQRES   5 B  149  ARG GLN GLY LEU TYR TYR ILE TYR ALA GLN VAL THR PHE          
SEQRES   6 B  149  CYS SER ASN ARG GLU ALA SER SER GLN ALA PRO PHE ILE          
SEQRES   7 B  149  ALA SER LEU CYS LEU LYS SER PRO GLY ARG PHE GLU ARG          
SEQRES   8 B  149  ILE LEU LEU ARG ALA ALA ASN THR HIS SER SER ALA LYS          
SEQRES   9 B  149  PRO CYS GLY GLN GLN SER ILE HIS LEU GLY GLY VAL PHE          
SEQRES  10 B  149  GLU LEU GLN PRO GLY ALA SER VAL PHE VAL ASN VAL THR          
SEQRES  11 B  149  ASP PRO SER GLN VAL SER HIS GLY THR GLY PHE THR SER          
SEQRES  12 B  149  PHE GLY LEU LEU LYS LEU                                      
SEQRES   1 C  149  ALA ASP PRO GLY ASP GLN ASN PRO GLN ILE ALA ALA HIS          
SEQRES   2 C  149  VAL ILE SER GLU ALA SER SER LYS THR THR SER VAL LEU          
SEQRES   3 C  149  GLN TRP ALA GLU LYS GLY TYR TYR THR MET SER ASN ASN          
SEQRES   4 C  149  LEU VAL THR LEU GLU ASN GLY LYS GLN LEU THR VAL LYS          
SEQRES   5 C  149  ARG GLN GLY LEU TYR TYR ILE TYR ALA GLN VAL THR PHE          
SEQRES   6 C  149  CYS SER ASN ARG GLU ALA SER SER GLN ALA PRO PHE ILE          
SEQRES   7 C  149  ALA SER LEU CYS LEU LYS SER PRO GLY ARG PHE GLU ARG          
SEQRES   8 C  149  ILE LEU LEU ARG ALA ALA ASN THR HIS SER SER ALA LYS          
SEQRES   9 C  149  PRO CYS GLY GLN GLN SER ILE HIS LEU GLY GLY VAL PHE          
SEQRES  10 C  149  GLU LEU GLN PRO GLY ALA SER VAL PHE VAL ASN VAL THR          
SEQRES  11 C  149  ASP PRO SER GLN VAL SER HIS GLY THR GLY PHE THR SER          
SEQRES  12 C  149  PHE GLY LEU LEU LYS LEU                                      
SEQRES   1 D  149  ALA ASP PRO GLY ASP GLN ASN PRO GLN ILE ALA ALA HIS          
SEQRES   2 D  149  VAL ILE SER GLU ALA SER SER LYS THR THR SER VAL LEU          
SEQRES   3 D  149  GLN TRP ALA GLU LYS GLY TYR TYR THR MET SER ASN ASN          
SEQRES   4 D  149  LEU VAL THR LEU GLU ASN GLY LYS GLN LEU THR VAL LYS          
SEQRES   5 D  149  ARG GLN GLY LEU TYR TYR ILE TYR ALA GLN VAL THR PHE          
SEQRES   6 D  149  CYS SER ASN ARG GLU ALA SER SER GLN ALA PRO PHE ILE          
SEQRES   7 D  149  ALA SER LEU CYS LEU LYS SER PRO GLY ARG PHE GLU ARG          
SEQRES   8 D  149  ILE LEU LEU ARG ALA ALA ASN THR HIS SER SER ALA LYS          
SEQRES   9 D  149  PRO CYS GLY GLN GLN SER ILE HIS LEU GLY GLY VAL PHE          
SEQRES  10 D  149  GLU LEU GLN PRO GLY ALA SER VAL PHE VAL ASN VAL THR          
SEQRES  11 D  149  ASP PRO SER GLN VAL SER HIS GLY THR GLY PHE THR SER          
SEQRES  12 D  149  PHE GLY LEU LEU LYS LEU                                      
SEQRES   1 E  149  ALA ASP PRO GLY ASP GLN ASN PRO GLN ILE ALA ALA HIS          
SEQRES   2 E  149  VAL ILE SER GLU ALA SER SER LYS THR THR SER VAL LEU          
SEQRES   3 E  149  GLN TRP ALA GLU LYS GLY TYR TYR THR MET SER ASN ASN          
SEQRES   4 E  149  LEU VAL THR LEU GLU ASN GLY LYS GLN LEU THR VAL LYS          
SEQRES   5 E  149  ARG GLN GLY LEU TYR TYR ILE TYR ALA GLN VAL THR PHE          
SEQRES   6 E  149  CYS SER ASN ARG GLU ALA SER SER GLN ALA PRO PHE ILE          
SEQRES   7 E  149  ALA SER LEU CYS LEU LYS SER PRO GLY ARG PHE GLU ARG          
SEQRES   8 E  149  ILE LEU LEU ARG ALA ALA ASN THR HIS SER SER ALA LYS          
SEQRES   9 E  149  PRO CYS GLY GLN GLN SER ILE HIS LEU GLY GLY VAL PHE          
SEQRES  10 E  149  GLU LEU GLN PRO GLY ALA SER VAL PHE VAL ASN VAL THR          
SEQRES  11 E  149  ASP PRO SER GLN VAL SER HIS GLY THR GLY PHE THR SER          
SEQRES  12 E  149  PHE GLY LEU LEU LYS LEU                                      
SEQRES   1 F  149  ALA ASP PRO GLY ASP GLN ASN PRO GLN ILE ALA ALA HIS          
SEQRES   2 F  149  VAL ILE SER GLU ALA SER SER LYS THR THR SER VAL LEU          
SEQRES   3 F  149  GLN TRP ALA GLU LYS GLY TYR TYR THR MET SER ASN ASN          
SEQRES   4 F  149  LEU VAL THR LEU GLU ASN GLY LYS GLN LEU THR VAL LYS          
SEQRES   5 F  149  ARG GLN GLY LEU TYR TYR ILE TYR ALA GLN VAL THR PHE          
SEQRES   6 F  149  CYS SER ASN ARG GLU ALA SER SER GLN ALA PRO PHE ILE          
SEQRES   7 F  149  ALA SER LEU CYS LEU LYS SER PRO GLY ARG PHE GLU ARG          
SEQRES   8 F  149  ILE LEU LEU ARG ALA ALA ASN THR HIS SER SER ALA LYS          
SEQRES   9 F  149  PRO CYS GLY GLN GLN SER ILE HIS LEU GLY GLY VAL PHE          
SEQRES  10 F  149  GLU LEU GLN PRO GLY ALA SER VAL PHE VAL ASN VAL THR          
SEQRES  11 F  149  ASP PRO SER GLN VAL SER HIS GLY THR GLY PHE THR SER          
SEQRES  12 F  149  PHE GLY LEU LEU LYS LEU                                      
SEQRES   1 R  177  GLU PRO PRO THR ALA CYS ARG GLU LYS GLN TYR LEU ILE          
SEQRES   2 R  177  ASN SER GLN CYS CYS SER LEU CYS GLN PRO GLY GLN LYS          
SEQRES   3 R  177  LEU VAL SER ASP CYS THR GLU PHE THR GLU THR GLU CYS          
SEQRES   4 R  177  LEU PRO CYS GLY GLU SER GLU PHE LEU ASP THR TRP ASN          
SEQRES   5 R  177  ARG GLU THR HIS CYS HIS GLN HIS LYS TYR CYS ASP PRO          
SEQRES   6 R  177  ASN LEU GLY LEU ARG VAL GLN GLN LYS GLY THR SER GLU          
SEQRES   7 R  177  THR ASP THR ILE CYS THR CYS GLU GLU GLY TRP HIS CYS          
SEQRES   8 R  177  THR SER GLU ALA CYS GLU SER CYS VAL LEU HIS ARG SER          
SEQRES   9 R  177  CYS SER PRO GLY PHE GLY VAL LYS GLN ILE ALA THR GLY          
SEQRES  10 R  177  VAL SER ASP THR ILE CYS GLU PRO CYS PRO VAL GLY PHE          
SEQRES  11 R  177  PHE SER ASN VAL SER SER ALA PHE GLU LYS CYS HIS PRO          
SEQRES  12 R  177  TRP THR SER CYS GLU THR LYS ASP LEU VAL VAL GLN GLN          
SEQRES  13 R  177  ALA GLY THR ASN LYS THR ASP VAL VAL CYS GLY PRO GLN          
SEQRES  14 R  177  ASP SER GLY ARG LEU VAL PRO ARG                              
SEQRES   1 S  177  GLU PRO PRO THR ALA CYS ARG GLU LYS GLN TYR LEU ILE          
SEQRES   2 S  177  ASN SER GLN CYS CYS SER LEU CYS GLN PRO GLY GLN LYS          
SEQRES   3 S  177  LEU VAL SER ASP CYS THR GLU PHE THR GLU THR GLU CYS          
SEQRES   4 S  177  LEU PRO CYS GLY GLU SER GLU PHE LEU ASP THR TRP ASN          
SEQRES   5 S  177  ARG GLU THR HIS CYS HIS GLN HIS LYS TYR CYS ASP PRO          
SEQRES   6 S  177  ASN LEU GLY LEU ARG VAL GLN GLN LYS GLY THR SER GLU          
SEQRES   7 S  177  THR ASP THR ILE CYS THR CYS GLU GLU GLY TRP HIS CYS          
SEQRES   8 S  177  THR SER GLU ALA CYS GLU SER CYS VAL LEU HIS ARG SER          
SEQRES   9 S  177  CYS SER PRO GLY PHE GLY VAL LYS GLN ILE ALA THR GLY          
SEQRES  10 S  177  VAL SER ASP THR ILE CYS GLU PRO CYS PRO VAL GLY PHE          
SEQRES  11 S  177  PHE SER ASN VAL SER SER ALA PHE GLU LYS CYS HIS PRO          
SEQRES  12 S  177  TRP THR SER CYS GLU THR LYS ASP LEU VAL VAL GLN GLN          
SEQRES  13 S  177  ALA GLY THR ASN LYS THR ASP VAL VAL CYS GLY PRO GLN          
SEQRES  14 S  177  ASP SER GLY ARG LEU VAL PRO ARG                              
SEQRES   1 T  177  GLU PRO PRO THR ALA CYS ARG GLU LYS GLN TYR LEU ILE          
SEQRES   2 T  177  ASN SER GLN CYS CYS SER LEU CYS GLN PRO GLY GLN LYS          
SEQRES   3 T  177  LEU VAL SER ASP CYS THR GLU PHE THR GLU THR GLU CYS          
SEQRES   4 T  177  LEU PRO CYS GLY GLU SER GLU PHE LEU ASP THR TRP ASN          
SEQRES   5 T  177  ARG GLU THR HIS CYS HIS GLN HIS LYS TYR CYS ASP PRO          
SEQRES   6 T  177  ASN LEU GLY LEU ARG VAL GLN GLN LYS GLY THR SER GLU          
SEQRES   7 T  177  THR ASP THR ILE CYS THR CYS GLU GLU GLY TRP HIS CYS          
SEQRES   8 T  177  THR SER GLU ALA CYS GLU SER CYS VAL LEU HIS ARG SER          
SEQRES   9 T  177  CYS SER PRO GLY PHE GLY VAL LYS GLN ILE ALA THR GLY          
SEQRES  10 T  177  VAL SER ASP THR ILE CYS GLU PRO CYS PRO VAL GLY PHE          
SEQRES  11 T  177  PHE SER ASN VAL SER SER ALA PHE GLU LYS CYS HIS PRO          
SEQRES  12 T  177  TRP THR SER CYS GLU THR LYS ASP LEU VAL VAL GLN GLN          
SEQRES  13 T  177  ALA GLY THR ASN LYS THR ASP VAL VAL CYS GLY PRO GLN          
SEQRES  14 T  177  ASP SER GLY ARG LEU VAL PRO ARG                              
SEQRES   1 U  177  GLU PRO PRO THR ALA CYS ARG GLU LYS GLN TYR LEU ILE          
SEQRES   2 U  177  ASN SER GLN CYS CYS SER LEU CYS GLN PRO GLY GLN LYS          
SEQRES   3 U  177  LEU VAL SER ASP CYS THR GLU PHE THR GLU THR GLU CYS          
SEQRES   4 U  177  LEU PRO CYS GLY GLU SER GLU PHE LEU ASP THR TRP ASN          
SEQRES   5 U  177  ARG GLU THR HIS CYS HIS GLN HIS LYS TYR CYS ASP PRO          
SEQRES   6 U  177  ASN LEU GLY LEU ARG VAL GLN GLN LYS GLY THR SER GLU          
SEQRES   7 U  177  THR ASP THR ILE CYS THR CYS GLU GLU GLY TRP HIS CYS          
SEQRES   8 U  177  THR SER GLU ALA CYS GLU SER CYS VAL LEU HIS ARG SER          
SEQRES   9 U  177  CYS SER PRO GLY PHE GLY VAL LYS GLN ILE ALA THR GLY          
SEQRES  10 U  177  VAL SER ASP THR ILE CYS GLU PRO CYS PRO VAL GLY PHE          
SEQRES  11 U  177  PHE SER ASN VAL SER SER ALA PHE GLU LYS CYS HIS PRO          
SEQRES  12 U  177  TRP THR SER CYS GLU THR LYS ASP LEU VAL VAL GLN GLN          
SEQRES  13 U  177  ALA GLY THR ASN LYS THR ASP VAL VAL CYS GLY PRO GLN          
SEQRES  14 U  177  ASP SER GLY ARG LEU VAL PRO ARG                              
MODRES 3QD6 ASN A  240  ASN  GLYCOSYLATION SITE                                 
MODRES 3QD6 ASN E  240  ASN  GLYCOSYLATION SITE                                 
MODRES 3QD6 ASN C  240  ASN  GLYCOSYLATION SITE                                 
MODRES 3QD6 ASN B  240  ASN  GLYCOSYLATION SITE                                 
MODRES 3QD6 ASN F  240  ASN  GLYCOSYLATION SITE                                 
MODRES 3QD6 ASN D  240  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A1411      14                                                       
HET    NAG  B1411      14                                                       
HET    NAG  C1411      14                                                       
HET    NAG  D1411      14                                                       
HET    NAG  E1411      14                                                       
HET    NAG  F1411      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
FORMUL  11  NAG    6(C8 H15 N O6)                                               
HELIX    1   1 ASN A  157  LYS A  159  5                                   3    
HELIX    2   2 LEU B  155  LYS B  159  5                                   5    
HELIX    3   3 LEU C  155  LYS C  159  5                                   5    
HELIX    4   4 LEU D  155  LYS D  159  5                                   5    
HELIX    5   5 LEU E  155  LYS E  159  5                                   5    
HELIX    6   6 LEU F  155  LYS F  159  5                                   5    
HELIX    7   7 ASP R   84  LEU R   87  5                                   4    
HELIX    8   8 ASP S   84  LEU S   87  5                                   4    
HELIX    9   9 ASP T   84  LEU T   87  5                                   4    
HELIX   10  10 ASP U   84  LEU U   87  5                                   4    
SHEET    1   A 3 TRP A 140  ALA A 141  0                                        
SHEET    2   A 3 ALA A 123  SER A 128 -1  N  ILE A 127   O  ALA A 141           
SHEET    3   A 3 THR A 147  MET A 148 -1  O  THR A 147   N  HIS A 125           
SHEET    1   B 5 TRP A 140  ALA A 141  0                                        
SHEET    2   B 5 ALA A 123  SER A 128 -1  N  ILE A 127   O  ALA A 141           
SHEET    3   B 5 SER A 255  LYS A 260 -1  O  PHE A 256   N  VAL A 126           
SHEET    4   B 5 GLY A 167  CYS A 178 -1  N  TYR A 172   O  GLY A 257           
SHEET    5   B 5 GLN A 220  LEU A 231 -1  O  LEU A 231   N  GLY A 167           
SHEET    1   C 4 VAL A 153  GLU A 156  0                                        
SHEET    2   C 4 GLN A 160  VAL A 163 -1  O  THR A 162   N  THR A 154           
SHEET    3   C 4 SER A 236  VAL A 237 -1  O  VAL A 237   N  LEU A 161           
SHEET    4   C 4 LEU A 195  LYS A 196 -1  N  LYS A 196   O  SER A 236           
SHEET    1   D 3 ARG A 207  ALA A 209  0                                        
SHEET    2   D 3 ILE A 190  SER A 192 -1  N  ALA A 191   O  ALA A 208           
SHEET    3   D 3 ASN A 240  VAL A 241 -1  O  ASN A 240   N  SER A 192           
SHEET    1   E 3 GLN B 139  ALA B 141  0                                        
SHEET    2   E 3 ALA B 123  GLU B 129 -1  N  ILE B 127   O  ALA B 141           
SHEET    3   E 3 THR B 147  MET B 148 -1  O  THR B 147   N  HIS B 125           
SHEET    1   F 5 GLN B 139  ALA B 141  0                                        
SHEET    2   F 5 ALA B 123  GLU B 129 -1  N  ILE B 127   O  ALA B 141           
SHEET    3   F 5 SER B 255  LEU B 261 -1  O  PHE B 256   N  VAL B 126           
SHEET    4   F 5 GLY B 167  CYS B 178 -1  N  TYR B 172   O  GLY B 257           
SHEET    5   F 5 GLN B 220  LEU B 231 -1  O  LEU B 231   N  GLY B 167           
SHEET    1   G 4 VAL B 153  THR B 154  0                                        
SHEET    2   G 4 LEU B 161  VAL B 163 -1  O  THR B 162   N  THR B 154           
SHEET    3   G 4 SER B 236  VAL B 237 -1  O  VAL B 237   N  LEU B 161           
SHEET    4   G 4 LEU B 195  LYS B 196 -1  N  LYS B 196   O  SER B 236           
SHEET    1   H 2 ILE B 190  SER B 192  0                                        
SHEET    2   H 2 ARG B 207  ALA B 209 -1  O  ALA B 208   N  ALA B 191           
SHEET    1   I 3 GLN C 139  ALA C 141  0                                        
SHEET    2   I 3 ALA C 123  GLU C 129 -1  N  ILE C 127   O  ALA C 141           
SHEET    3   I 3 THR C 147  MET C 148 -1  O  THR C 147   N  HIS C 125           
SHEET    1   J 5 GLN C 139  ALA C 141  0                                        
SHEET    2   J 5 ALA C 123  GLU C 129 -1  N  ILE C 127   O  ALA C 141           
SHEET    3   J 5 SER C 255  LYS C 260 -1  O  PHE C 256   N  VAL C 126           
SHEET    4   J 5 GLY C 167  CYS C 178 -1  N  TYR C 170   O  LEU C 259           
SHEET    5   J 5 GLN C 220  LEU C 231 -1  O  LEU C 231   N  GLY C 167           
SHEET    1   K 4 VAL C 153  THR C 154  0                                        
SHEET    2   K 4 LEU C 161  VAL C 163 -1  O  THR C 162   N  THR C 154           
SHEET    3   K 4 SER C 236  VAL C 237 -1  O  VAL C 237   N  LEU C 161           
SHEET    4   K 4 LEU C 195  LYS C 196 -1  N  LYS C 196   O  SER C 236           
SHEET    1   L 2 ALA C 191  SER C 192  0                                        
SHEET    2   L 2 ARG C 207  ALA C 208 -1  O  ALA C 208   N  ALA C 191           
SHEET    1   M 3 GLN D 139  ALA D 141  0                                        
SHEET    2   M 3 ALA D 123  GLU D 129 -1  N  ILE D 127   O  ALA D 141           
SHEET    3   M 3 THR D 147  MET D 148 -1  O  THR D 147   N  HIS D 125           
SHEET    1   N 5 GLN D 139  ALA D 141  0                                        
SHEET    2   N 5 ALA D 123  GLU D 129 -1  N  ILE D 127   O  ALA D 141           
SHEET    3   N 5 SER D 255  LYS D 260 -1  O  PHE D 256   N  VAL D 126           
SHEET    4   N 5 GLY D 167  THR D 176 -1  N  TYR D 170   O  LEU D 259           
SHEET    5   N 5 SER D 222  LEU D 231 -1  O  LEU D 231   N  GLY D 167           
SHEET    1   O 4 VAL D 153  THR D 154  0                                        
SHEET    2   O 4 LEU D 161  VAL D 163 -1  O  THR D 162   N  THR D 154           
SHEET    3   O 4 SER D 236  VAL D 237 -1  O  VAL D 237   N  LEU D 161           
SHEET    4   O 4 LEU D 195  LYS D 196 -1  N  LYS D 196   O  SER D 236           
SHEET    1   P 2 ILE D 190  SER D 192  0                                        
SHEET    2   P 2 ARG D 207  ALA D 209 -1  O  ALA D 208   N  ALA D 191           
SHEET    1   Q 3 GLN E 139  ALA E 141  0                                        
SHEET    2   Q 3 ALA E 123  GLU E 129 -1  N  ILE E 127   O  ALA E 141           
SHEET    3   Q 3 THR E 147  MET E 148 -1  O  THR E 147   N  HIS E 125           
SHEET    1   R 5 GLN E 139  ALA E 141  0                                        
SHEET    2   R 5 ALA E 123  GLU E 129 -1  N  ILE E 127   O  ALA E 141           
SHEET    3   R 5 SER E 255  LYS E 260 -1  O  PHE E 256   N  VAL E 126           
SHEET    4   R 5 GLY E 167  CYS E 178 -1  N  TYR E 172   O  GLY E 257           
SHEET    5   R 5 GLN E 220  LEU E 231 -1  O  LEU E 231   N  GLY E 167           
SHEET    1   S 4 VAL E 153  THR E 154  0                                        
SHEET    2   S 4 LEU E 161  VAL E 163 -1  O  THR E 162   N  THR E 154           
SHEET    3   S 4 SER E 236  VAL E 237 -1  O  VAL E 237   N  LEU E 161           
SHEET    4   S 4 LEU E 195  LYS E 196 -1  N  LYS E 196   O  SER E 236           
SHEET    1   T 2 PHE E 189  SER E 192  0                                        
SHEET    2   T 2 ARG E 207  ASN E 210 -1  O  ALA E 208   N  ALA E 191           
SHEET    1   U 3 TRP F 140  ALA F 141  0                                        
SHEET    2   U 3 ALA F 123  SER F 128 -1  N  ILE F 127   O  ALA F 141           
SHEET    3   U 3 THR F 147  MET F 148 -1  O  THR F 147   N  HIS F 125           
SHEET    1   V 5 TRP F 140  ALA F 141  0                                        
SHEET    2   V 5 ALA F 123  SER F 128 -1  N  ILE F 127   O  ALA F 141           
SHEET    3   V 5 SER F 255  LYS F 260 -1  O  PHE F 256   N  VAL F 126           
SHEET    4   V 5 GLY F 167  CYS F 178 -1  N  TYR F 172   O  GLY F 257           
SHEET    5   V 5 GLN F 220  LEU F 231 -1  O  LEU F 225   N  ALA F 173           
SHEET    1   W 4 VAL F 153  THR F 154  0                                        
SHEET    2   W 4 LEU F 161  VAL F 163 -1  O  THR F 162   N  THR F 154           
SHEET    3   W 4 SER F 236  VAL F 237 -1  O  VAL F 237   N  LEU F 161           
SHEET    4   W 4 LEU F 195  LYS F 196 -1  N  LYS F 196   O  SER F 236           
SHEET    1   X 3 ARG F 207  ALA F 208  0                                        
SHEET    2   X 3 ALA F 191  SER F 192 -1  N  ALA F 191   O  ALA F 208           
SHEET    3   X 3 ASN F 240  VAL F 241 -1  O  ASN F 240   N  SER F 192           
SHEET    1   Y 2 TYR R  31  LEU R  32  0                                        
SHEET    2   Y 2 CYS R  37  CYS R  38 -1  O  CYS R  38   N  TYR R  31           
SHEET    1   Z 2 GLU R  66  PHE R  67  0                                        
SHEET    2   Z 2 HIS R  78  GLN R  79 -1  O  HIS R  78   N  PHE R  67           
SHEET    1  AA 2 LEU R  89  GLN R  93  0                                        
SHEET    2  AA 2 ILE R 102  CYS R 105 -1  O  ILE R 102   N  GLN R  93           
SHEET    1  AB 2 TRP R 109  CYS R 111  0                                        
SHEET    2  AB 2 CYS R 119  LEU R 121 -1  O  VAL R 120   N  HIS R 110           
SHEET    1  AC 2 GLN S  30  LEU S  32  0                                        
SHEET    2  AC 2 CYS S  37  SER S  39 -1  O  CYS S  38   N  TYR S  31           
SHEET    1  AD 2 GLN S  45  SER S  49  0                                        
SHEET    2  AD 2 GLU S  58  PRO S  61 -1  O  LEU S  60   N  LYS S  46           
SHEET    1  AE 2 GLU S  66  PHE S  67  0                                        
SHEET    2  AE 2 HIS S  78  GLN S  79 -1  O  HIS S  78   N  PHE S  67           
SHEET    1  AF 2 LEU S  89  GLN S  93  0                                        
SHEET    2  AF 2 ILE S 102  CYS S 105 -1  O  ILE S 102   N  GLN S  93           
SHEET    1  AG 2 GLN T  30  ILE T  33  0                                        
SHEET    2  AG 2 GLN T  36  SER T  39 -1  O  GLN T  36   N  ILE T  33           
SHEET    1  AH 2 GLN T  45  SER T  49  0                                        
SHEET    2  AH 2 GLU T  58  PRO T  61 -1  O  LEU T  60   N  LYS T  46           
SHEET    1  AI 2 GLU T  66  PHE T  67  0                                        
SHEET    2  AI 2 HIS T  78  GLN T  79 -1  O  HIS T  78   N  PHE T  67           
SHEET    1  AJ 2 LEU T  89  GLN T  93  0                                        
SHEET    2  AJ 2 ILE T 102  CYS T 105 -1  O  ILE T 102   N  GLN T  93           
SHEET    1  AK 2 TRP T 109  CYS T 111  0                                        
SHEET    2  AK 2 CYS T 119  LEU T 121 -1  O  VAL T 120   N  HIS T 110           
SHEET    1  AL 2 GLN U  30  ILE U  33  0                                        
SHEET    2  AL 2 GLN U  36  SER U  39 -1  O  GLN U  36   N  ILE U  33           
SHEET    1  AM 2 GLN U  45  SER U  49  0                                        
SHEET    2  AM 2 GLU U  58  PRO U  61 -1  O  GLU U  58   N  VAL U  48           
SHEET    1  AN 2 GLU U  66  PHE U  67  0                                        
SHEET    2  AN 2 HIS U  78  GLN U  79 -1  O  HIS U  78   N  PHE U  67           
SHEET    1  AO 2 LEU U  89  GLN U  93  0                                        
SHEET    2  AO 2 ILE U 102  CYS U 105 -1  O  ILE U 102   N  GLN U  93           
SHEET    1  AP 2 TRP U 109  CYS U 111  0                                        
SHEET    2  AP 2 CYS U 119  LEU U 121 -1  O  VAL U 120   N  HIS U 110           
SSBOND   1 CYS A  178    CYS A  218                          1555   1555  2.03  
SSBOND   2 CYS B  178    CYS B  218                          1555   1555  2.03  
SSBOND   3 CYS C  178    CYS C  218                          1555   1555  2.04  
SSBOND   4 CYS D  178    CYS D  218                          1555   1555  2.03  
SSBOND   5 CYS E  178    CYS E  218                          1555   1555  2.04  
SSBOND   6 CYS F  178    CYS F  218                          1555   1555  2.03  
SSBOND   7 CYS R   26    CYS R   37                          1555   1555  2.02  
SSBOND   8 CYS R   38    CYS R   51                          1555   1555  2.03  
SSBOND   9 CYS R   41    CYS R   59                          1555   1555  2.03  
SSBOND  10 CYS R   62    CYS R   77                          1555   1555  2.03  
SSBOND  11 CYS R   83    CYS R  103                          1555   1555  2.04  
SSBOND  12 CYS R  105    CYS R  119                          1555   1555  2.03  
SSBOND  13 CYS R  111    CYS R  116                          1555   1555  2.03  
SSBOND  14 CYS R  125    CYS R  143                          1555   1555  2.03  
SSBOND  15 CYS S   26    CYS S   37                          1555   1555  2.03  
SSBOND  16 CYS S   38    CYS S   51                          1555   1555  2.02  
SSBOND  17 CYS S   41    CYS S   59                          1555   1555  2.02  
SSBOND  18 CYS S   62    CYS S   77                          1555   1555  2.05  
SSBOND  19 CYS S   83    CYS S  103                          1555   1555  2.03  
SSBOND  20 CYS S  105    CYS S  119                          1555   1555  2.03  
SSBOND  21 CYS S  111    CYS S  116                          1555   1555  2.03  
SSBOND  22 CYS S  125    CYS S  143                          1555   1555  2.03  
SSBOND  23 CYS T   26    CYS T   37                          1555   1555  2.03  
SSBOND  24 CYS T   38    CYS T   51                          1555   1555  2.03  
SSBOND  25 CYS T   41    CYS T   59                          1555   1555  2.03  
SSBOND  26 CYS T   62    CYS T   77                          1555   1555  2.04  
SSBOND  27 CYS T   83    CYS T  103                          1555   1555  2.02  
SSBOND  28 CYS T  105    CYS T  119                          1555   1555  2.03  
SSBOND  29 CYS T  111    CYS T  116                          1555   1555  2.03  
SSBOND  30 CYS T  125    CYS T  143                          1555   1555  2.05  
SSBOND  31 CYS U   26    CYS U   37                          1555   1555  2.03  
SSBOND  32 CYS U   38    CYS U   51                          1555   1555  2.03  
SSBOND  33 CYS U   41    CYS U   59                          1555   1555  2.02  
SSBOND  34 CYS U   62    CYS U   77                          1555   1555  2.04  
SSBOND  35 CYS U   83    CYS U  103                          1555   1555  2.03  
SSBOND  36 CYS U  105    CYS U  119                          1555   1555  2.04  
SSBOND  37 CYS U  111    CYS U  116                          1555   1555  2.03  
SSBOND  38 CYS U  125    CYS U  143                          1555   1555  2.03  
LINK         ND2 ASN A 240                 C1  NAG A1411     1555   1555  1.45  
LINK         ND2 ASN B 240                 C1  NAG B1411     1555   1555  1.46  
LINK         ND2 ASN C 240                 C1  NAG C1411     1555   1555  1.45  
LINK         ND2 ASN D 240                 C1  NAG D1411     1555   1555  1.46  
LINK         ND2 ASN E 240                 C1  NAG E1411     1555   1555  1.45  
LINK         ND2 ASN F 240                 C1  NAG F1411     1555   1555  1.46  
CRYST1  133.212  133.212  211.151  90.00  90.00 120.00 P 65         36          
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      0.007507  0.004334  0.000000        0.00000                         
SCALE2      0.000000  0.008668  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004736        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system