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Database: PDB
Entry: 1KD7
LinkDB: 1KD7
Original site: 1KD7 
HEADER    MEMBRANE PROTEIN                        12-NOV-01   1KD7              
TITLE     CRYSTAL STRUCTURE OF AN EXTRACELLULAR DOMAIN FRAGMENT OF HUMAN BAFF   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUMOR NECROSIS FACTOR LIGAND SUPERFAMILY MEMBER 13B;       
COMPND   3 CHAIN: A, B, C, K, L, M;                                             
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAIN FRAGMENT;                             
COMPND   5 SYNONYM: BAFF, TALL-1, TNF-AND-APOL-RELATED LEUKOCYTE EXPRESSED      
COMPND   6 LIGAND 1;                                                            
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: PICHIA PASTORIS;                                  
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 4922                                        
KEYWDS    BETA-SHEET SHANDWICH, TNF, MEMBRANE PROTEIN                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.KARPUSAS,T.G.CACHERO,F.QIAN,A.BORIACK-SJODIN,C.MULLEN,K.STRAUCH,Y.- 
AUTHOR   2 M.HSU,S.L.KALLED                                                     
REVDAT   3   01-FEB-17 1KD7    1       AUTHOR VERSN                             
REVDAT   2   24-FEB-09 1KD7    1       VERSN                                    
REVDAT   1   12-NOV-02 1KD7    0                                                
JRNL        AUTH   M.KARPUSAS,T.G.CACHERO,F.QIAN,A.BORIACK-SJODIN,C.MULLEN,     
JRNL        AUTH 2 K.STRAUCH,Y.-M.HSU,S.L.KALLED                                
JRNL        TITL   CRYSTAL STRUCTURE OF EXTRACELLULAR HUMAN BAFF, A TNF FAMILY  
JRNL        TITL 2 MEMBER THAT STIMULATES B LYMPHOCYTES                         
JRNL        REF    J.MOL.BIOL.                   V. 315  1145 2002              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   11827482                                                     
JRNL        DOI    10.1006/JMBI.2001.5296                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 28918                          
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) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.250                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2861                            
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) : 2.80                         
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                    : 0.2500                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 2861                         
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            : 6858                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
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) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1KD7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-NOV-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB014832.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-DEC-00; 04-JUN-01               
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N; Y                               
REMARK 200  RADIATION SOURCE               : ROTATING ANODE; NSLS               
REMARK 200  BEAMLINE                       : NULL; X4A                          
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200; NULL                 
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; NULL                            
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418; 0.9464                     
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : OSMIC BLUE OPTICS; NULL            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE; CCD                   
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV; ADSC QUANTUM 4    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31743                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.07900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.26700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL                        
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 4000, 0.1 M SODIUM                
REMARK 280  ACETATESOLUTION OF 8% PEG 4000, 0.1 M SODIUM ACETATE PH 4.5,        
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                     
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      107.16000            
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       53.58000            
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       80.37000            
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       26.79000            
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      133.95000            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5530 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5560 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17400 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L, M                               
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     GLU A   122                                                      
REMARK 465     GLN A   123                                                      
REMARK 465     LYS A   124                                                      
REMARK 465     LEU A   125                                                      
REMARK 465     ILE A   126                                                      
REMARK 465     SER A   127                                                      
REMARK 465     GLU A   128                                                      
REMARK 465     GLU A   129                                                      
REMARK 465     ASP A   130                                                      
REMARK 465     LEU A   131                                                      
REMARK 465     ASN A   132                                                      
REMARK 465     LYS A   133                                                      
REMARK 465     GLU A   134                                                      
REMARK 465     LEU A   135                                                      
REMARK 465     GLN A   136                                                      
REMARK 465     GLY A   137                                                      
REMARK 465     PRO A   138                                                      
REMARK 465     GLU A   139                                                      
REMARK 465     GLU A   140                                                      
REMARK 465     THR A   141                                                      
REMARK 465     GLU B   122                                                      
REMARK 465     GLN B   123                                                      
REMARK 465     LYS B   124                                                      
REMARK 465     LEU B   125                                                      
REMARK 465     ILE B   126                                                      
REMARK 465     SER B   127                                                      
REMARK 465     GLU B   128                                                      
REMARK 465     GLU B   129                                                      
REMARK 465     ASP B   130                                                      
REMARK 465     LEU B   131                                                      
REMARK 465     ASN B   132                                                      
REMARK 465     LYS B   133                                                      
REMARK 465     GLU B   134                                                      
REMARK 465     LEU B   135                                                      
REMARK 465     GLN B   136                                                      
REMARK 465     GLY B   137                                                      
REMARK 465     PRO B   138                                                      
REMARK 465     GLU B   139                                                      
REMARK 465     GLU B   140                                                      
REMARK 465     THR B   141                                                      
REMARK 465     GLU C   122                                                      
REMARK 465     GLN C   123                                                      
REMARK 465     LYS C   124                                                      
REMARK 465     LEU C   125                                                      
REMARK 465     ILE C   126                                                      
REMARK 465     SER C   127                                                      
REMARK 465     GLU C   128                                                      
REMARK 465     GLU C   129                                                      
REMARK 465     ASP C   130                                                      
REMARK 465     LEU C   131                                                      
REMARK 465     ASN C   132                                                      
REMARK 465     LYS C   133                                                      
REMARK 465     GLU C   134                                                      
REMARK 465     LEU C   135                                                      
REMARK 465     GLN C   136                                                      
REMARK 465     GLY C   137                                                      
REMARK 465     PRO C   138                                                      
REMARK 465     GLU C   139                                                      
REMARK 465     GLU C   140                                                      
REMARK 465     THR C   141                                                      
REMARK 465     GLU K   122                                                      
REMARK 465     GLN K   123                                                      
REMARK 465     LYS K   124                                                      
REMARK 465     LEU K   125                                                      
REMARK 465     ILE K   126                                                      
REMARK 465     SER K   127                                                      
REMARK 465     GLU K   128                                                      
REMARK 465     GLU K   129                                                      
REMARK 465     ASP K   130                                                      
REMARK 465     LEU K   131                                                      
REMARK 465     ASN K   132                                                      
REMARK 465     LYS K   133                                                      
REMARK 465     GLU K   134                                                      
REMARK 465     LEU K   135                                                      
REMARK 465     GLN K   136                                                      
REMARK 465     GLY K   137                                                      
REMARK 465     PRO K   138                                                      
REMARK 465     GLU K   139                                                      
REMARK 465     GLU K   140                                                      
REMARK 465     THR K   141                                                      
REMARK 465     GLU L   122                                                      
REMARK 465     GLN L   123                                                      
REMARK 465     LYS L   124                                                      
REMARK 465     LEU L   125                                                      
REMARK 465     ILE L   126                                                      
REMARK 465     SER L   127                                                      
REMARK 465     GLU L   128                                                      
REMARK 465     GLU L   129                                                      
REMARK 465     ASP L   130                                                      
REMARK 465     LEU L   131                                                      
REMARK 465     ASN L   132                                                      
REMARK 465     LYS L   133                                                      
REMARK 465     GLU L   134                                                      
REMARK 465     LEU L   135                                                      
REMARK 465     GLN L   136                                                      
REMARK 465     GLY L   137                                                      
REMARK 465     PRO L   138                                                      
REMARK 465     GLU L   139                                                      
REMARK 465     GLU L   140                                                      
REMARK 465     THR L   141                                                      
REMARK 465     GLU M   122                                                      
REMARK 465     GLN M   123                                                      
REMARK 465     LYS M   124                                                      
REMARK 465     LEU M   125                                                      
REMARK 465     ILE M   126                                                      
REMARK 465     SER M   127                                                      
REMARK 465     GLU M   128                                                      
REMARK 465     GLU M   129                                                      
REMARK 465     ASP M   130                                                      
REMARK 465     LEU M   131                                                      
REMARK 465     ASN M   132                                                      
REMARK 465     LYS M   133                                                      
REMARK 465     GLU M   134                                                      
REMARK 465     LEU M   135                                                      
REMARK 465     GLN M   136                                                      
REMARK 465     GLY M   137                                                      
REMARK 465     PRO M   138                                                      
REMARK 465     GLU M   139                                                      
REMARK 465     GLU M   140                                                      
REMARK 465     THR M   141                                                      
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    GLN A 144       81.10     55.33                                   
REMARK 500    SER A 153        0.68    -68.53                                   
REMARK 500    LYS A 160      118.67   -168.44                                   
REMARK 500    SER A 162       -4.72     68.16                                   
REMARK 500    LEU A 178      117.01     66.26                                   
REMARK 500    LYS A 181     -107.57    -91.33                                   
REMARK 500    GLU A 182       71.71   -110.51                                   
REMARK 500    ASN A 242       76.69   -157.31                                   
REMARK 500    GLN A 269       68.13     91.66                                   
REMARK 500    ILE A 270     -161.15   -112.19                                   
REMARK 500    GLN B 144       82.33     54.68                                   
REMARK 500    SER B 153        0.57    -68.92                                   
REMARK 500    LYS B 160      118.98   -168.44                                   
REMARK 500    SER B 162       -4.94     68.22                                   
REMARK 500    LEU B 178      116.93     65.66                                   
REMARK 500    LYS B 181     -107.81    -91.14                                   
REMARK 500    GLU B 182       71.11   -109.12                                   
REMARK 500    ASN B 242       76.95   -155.98                                   
REMARK 500    GLN B 269       68.45     91.19                                   
REMARK 500    ILE B 270     -161.50   -112.02                                   
REMARK 500    GLN C 144       83.48     54.68                                   
REMARK 500    SER C 153        0.61    -69.62                                   
REMARK 500    LYS C 160      118.65   -167.90                                   
REMARK 500    SER C 162       -5.09     68.38                                   
REMARK 500    LEU C 178      115.84     65.97                                   
REMARK 500    LYS C 181     -106.60    -91.63                                   
REMARK 500    GLU C 182       71.73   -111.03                                   
REMARK 500    PHE C 220      -90.74    -32.13                                   
REMARK 500    ASN C 242       76.30   -156.84                                   
REMARK 500    GLN C 269       68.24     92.86                                   
REMARK 500    ILE C 270     -162.06   -112.04                                   
REMARK 500    GLN K 144       82.18     54.88                                   
REMARK 500    LYS K 160      118.19   -169.42                                   
REMARK 500    SER K 162       -5.04     66.88                                   
REMARK 500    LEU K 178      117.30     65.76                                   
REMARK 500    LYS K 181     -107.08    -91.58                                   
REMARK 500    GLU K 182       71.11   -110.47                                   
REMARK 500    GLU K 223      147.08    -33.51                                   
REMARK 500    ASN K 242       76.30   -156.40                                   
REMARK 500    GLN K 269       68.34     92.94                                   
REMARK 500    ILE K 270     -161.40   -111.99                                   
REMARK 500    GLN L 144       82.17     54.98                                   
REMARK 500    SER L 153        0.26    -69.25                                   
REMARK 500    LYS L 160      119.12   -168.90                                   
REMARK 500    SER L 162       -4.56     67.69                                   
REMARK 500    LEU L 178      116.34     65.88                                   
REMARK 500    LYS L 181     -107.35    -91.22                                   
REMARK 500    GLU L 182       71.60   -109.69                                   
REMARK 500    ASN L 242       76.51   -156.63                                   
REMARK 500    GLN L 269       68.58     93.02                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      62 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 999                                                                      
REMARK 999 SEQUENCE AUTHOR STATES THE SEQUENCE EQKLISEEDLNKELQGPEET IS THE N-   
REMARK 999 TERMINUS (N122) CORRESPONDS TO RESIDUES THAT ARE NOT OBSERVED IN     
REMARK 999 THE ELECTRON DENSITY. AUTHOR ALSO STATES THAT THE MYC-TAG            
REMARK 999 (EQKLISEEDLNKEL) AND THE BAFF SEQUENCE FRAGMENT (QGPEET) THERE IS    
REMARK 999 NO SEQUENCE MATCH FOR THE MYC-TAG BECAUSE IT IS NOT RELATED TO THE   
REMARK 999 BAFF SEQUENCE, BUT IT IS A FRAGMENT OF ANOTHER PROTEIN.              
DBREF  1KD7 A  122   285  UNP    Q9Y275   TN13B_HUMAN    122    285             
DBREF  1KD7 B  122   285  UNP    Q9Y275   TN13B_HUMAN    122    285             
DBREF  1KD7 C  122   285  UNP    Q9Y275   TN13B_HUMAN    122    285             
DBREF  1KD7 K  122   285  UNP    Q9Y275   TN13B_HUMAN    122    285             
DBREF  1KD7 L  122   285  UNP    Q9Y275   TN13B_HUMAN    122    285             
DBREF  1KD7 M  122   285  UNP    Q9Y275   TN13B_HUMAN    122    285             
SEQADV 1KD7 GLN A  123  UNP  Q9Y275          123 SEE REMARK 999                 
SEQADV 1KD7 LYS A  124  UNP  Q9Y275          124 SEE REMARK 999                 
SEQADV 1KD7 LEU A  125  UNP  Q9Y275          125 SEE REMARK 999                 
SEQADV 1KD7 ILE A  126  UNP  Q9Y275          126 SEE REMARK 999                 
SEQADV 1KD7 SER A  127  UNP  Q9Y275          127 SEE REMARK 999                 
SEQADV 1KD7 GLU A  128  UNP  Q9Y275          128 SEE REMARK 999                 
SEQADV 1KD7 GLU A  129  UNP  Q9Y275          129 SEE REMARK 999                 
SEQADV 1KD7 ASP A  130  UNP  Q9Y275          130 SEE REMARK 999                 
SEQADV 1KD7 LEU A  131  UNP  Q9Y275          131 SEE REMARK 999                 
SEQADV 1KD7 ASN A  132  UNP  Q9Y275          132 SEE REMARK 999                 
SEQADV 1KD7 LYS A  133  UNP  Q9Y275          133 SEE REMARK 999                 
SEQADV 1KD7 GLU A  134  UNP  Q9Y275          134 SEE REMARK 999                 
SEQADV 1KD7 LEU A  135  UNP  Q9Y275          135 SEE REMARK 999                 
SEQADV 1KD7 GLN B  123  UNP  Q9Y275          123 SEE REMARK 999                 
SEQADV 1KD7 LYS B  124  UNP  Q9Y275          124 SEE REMARK 999                 
SEQADV 1KD7 LEU B  125  UNP  Q9Y275          125 SEE REMARK 999                 
SEQADV 1KD7 ILE B  126  UNP  Q9Y275          126 SEE REMARK 999                 
SEQADV 1KD7 SER B  127  UNP  Q9Y275          127 SEE REMARK 999                 
SEQADV 1KD7 GLU B  128  UNP  Q9Y275          128 SEE REMARK 999                 
SEQADV 1KD7 GLU B  129  UNP  Q9Y275          129 SEE REMARK 999                 
SEQADV 1KD7 ASP B  130  UNP  Q9Y275          130 SEE REMARK 999                 
SEQADV 1KD7 LEU B  131  UNP  Q9Y275          131 SEE REMARK 999                 
SEQADV 1KD7 ASN B  132  UNP  Q9Y275          132 SEE REMARK 999                 
SEQADV 1KD7 LYS B  133  UNP  Q9Y275          133 SEE REMARK 999                 
SEQADV 1KD7 GLU B  134  UNP  Q9Y275          134 SEE REMARK 999                 
SEQADV 1KD7 LEU B  135  UNP  Q9Y275          135 SEE REMARK 999                 
SEQADV 1KD7 GLN C  123  UNP  Q9Y275          123 SEE REMARK 999                 
SEQADV 1KD7 LYS C  124  UNP  Q9Y275          124 SEE REMARK 999                 
SEQADV 1KD7 LEU C  125  UNP  Q9Y275          125 SEE REMARK 999                 
SEQADV 1KD7 ILE C  126  UNP  Q9Y275          126 SEE REMARK 999                 
SEQADV 1KD7 SER C  127  UNP  Q9Y275          127 SEE REMARK 999                 
SEQADV 1KD7 GLU C  128  UNP  Q9Y275          128 SEE REMARK 999                 
SEQADV 1KD7 GLU C  129  UNP  Q9Y275          129 SEE REMARK 999                 
SEQADV 1KD7 ASP C  130  UNP  Q9Y275          130 SEE REMARK 999                 
SEQADV 1KD7 LEU C  131  UNP  Q9Y275          131 SEE REMARK 999                 
SEQADV 1KD7 ASN C  132  UNP  Q9Y275          132 SEE REMARK 999                 
SEQADV 1KD7 LYS C  133  UNP  Q9Y275          133 SEE REMARK 999                 
SEQADV 1KD7 GLU C  134  UNP  Q9Y275          134 SEE REMARK 999                 
SEQADV 1KD7 LEU C  135  UNP  Q9Y275          135 SEE REMARK 999                 
SEQADV 1KD7 GLN K  123  UNP  Q9Y275          123 SEE REMARK 999                 
SEQADV 1KD7 LYS K  124  UNP  Q9Y275          124 SEE REMARK 999                 
SEQADV 1KD7 LEU K  125  UNP  Q9Y275          125 SEE REMARK 999                 
SEQADV 1KD7 ILE K  126  UNP  Q9Y275          126 SEE REMARK 999                 
SEQADV 1KD7 SER K  127  UNP  Q9Y275          127 SEE REMARK 999                 
SEQADV 1KD7 GLU K  128  UNP  Q9Y275          128 SEE REMARK 999                 
SEQADV 1KD7 GLU K  129  UNP  Q9Y275          129 SEE REMARK 999                 
SEQADV 1KD7 ASP K  130  UNP  Q9Y275          130 SEE REMARK 999                 
SEQADV 1KD7 LEU K  131  UNP  Q9Y275          131 SEE REMARK 999                 
SEQADV 1KD7 ASN K  132  UNP  Q9Y275          132 SEE REMARK 999                 
SEQADV 1KD7 LYS K  133  UNP  Q9Y275          133 SEE REMARK 999                 
SEQADV 1KD7 GLU K  134  UNP  Q9Y275          134 SEE REMARK 999                 
SEQADV 1KD7 LEU K  135  UNP  Q9Y275          135 SEE REMARK 999                 
SEQADV 1KD7 GLN L  123  UNP  Q9Y275          123 SEE REMARK 999                 
SEQADV 1KD7 LYS L  124  UNP  Q9Y275          124 SEE REMARK 999                 
SEQADV 1KD7 LEU L  125  UNP  Q9Y275          125 SEE REMARK 999                 
SEQADV 1KD7 ILE L  126  UNP  Q9Y275          126 SEE REMARK 999                 
SEQADV 1KD7 SER L  127  UNP  Q9Y275          127 SEE REMARK 999                 
SEQADV 1KD7 GLU L  128  UNP  Q9Y275          128 SEE REMARK 999                 
SEQADV 1KD7 GLU L  129  UNP  Q9Y275          129 SEE REMARK 999                 
SEQADV 1KD7 ASP L  130  UNP  Q9Y275          130 SEE REMARK 999                 
SEQADV 1KD7 LEU L  131  UNP  Q9Y275          131 SEE REMARK 999                 
SEQADV 1KD7 ASN L  132  UNP  Q9Y275          132 SEE REMARK 999                 
SEQADV 1KD7 LYS L  133  UNP  Q9Y275          133 SEE REMARK 999                 
SEQADV 1KD7 GLU L  134  UNP  Q9Y275          134 SEE REMARK 999                 
SEQADV 1KD7 LEU L  135  UNP  Q9Y275          135 SEE REMARK 999                 
SEQADV 1KD7 GLN M  123  UNP  Q9Y275          123 SEE REMARK 999                 
SEQADV 1KD7 LYS M  124  UNP  Q9Y275          124 SEE REMARK 999                 
SEQADV 1KD7 LEU M  125  UNP  Q9Y275          125 SEE REMARK 999                 
SEQADV 1KD7 ILE M  126  UNP  Q9Y275          126 SEE REMARK 999                 
SEQADV 1KD7 SER M  127  UNP  Q9Y275          127 SEE REMARK 999                 
SEQADV 1KD7 GLU M  128  UNP  Q9Y275          128 SEE REMARK 999                 
SEQADV 1KD7 GLU M  129  UNP  Q9Y275          129 SEE REMARK 999                 
SEQADV 1KD7 ASP M  130  UNP  Q9Y275          130 SEE REMARK 999                 
SEQADV 1KD7 LEU M  131  UNP  Q9Y275          131 SEE REMARK 999                 
SEQADV 1KD7 ASN M  132  UNP  Q9Y275          132 SEE REMARK 999                 
SEQADV 1KD7 LYS M  133  UNP  Q9Y275          133 SEE REMARK 999                 
SEQADV 1KD7 GLU M  134  UNP  Q9Y275          134 SEE REMARK 999                 
SEQADV 1KD7 LEU M  135  UNP  Q9Y275          135 SEE REMARK 999                 
SEQRES   1 A  164  GLU GLN LYS LEU ILE SER GLU GLU ASP LEU ASN LYS GLU          
SEQRES   2 A  164  LEU GLN GLY PRO GLU GLU THR VAL THR GLN ASP CYS LEU          
SEQRES   3 A  164  GLN LEU ILE ALA ASP SER GLU THR PRO THR ILE GLN LYS          
SEQRES   4 A  164  GLY SER TYR THR PHE VAL PRO TRP LEU LEU SER PHE LYS          
SEQRES   5 A  164  ARG GLY SER ALA LEU GLU GLU LYS GLU ASN LYS ILE LEU          
SEQRES   6 A  164  VAL LYS GLU THR GLY TYR PHE PHE ILE TYR GLY GLN VAL          
SEQRES   7 A  164  LEU TYR THR ASP LYS THR TYR ALA MET GLY HIS LEU ILE          
SEQRES   8 A  164  GLN ARG LYS LYS VAL HIS VAL PHE GLY ASP GLU LEU SER          
SEQRES   9 A  164  LEU VAL THR LEU PHE ARG CYS ILE GLN ASN MET PRO GLU          
SEQRES  10 A  164  THR LEU PRO ASN ASN SER CYS TYR SER ALA GLY ILE ALA          
SEQRES  11 A  164  LYS LEU GLU GLU GLY ASP GLU LEU GLN LEU ALA ILE PRO          
SEQRES  12 A  164  ARG GLU ASN ALA GLN ILE SER LEU ASP GLY ASP VAL THR          
SEQRES  13 A  164  PHE PHE GLY ALA LEU LYS LEU LEU                              
SEQRES   1 B  164  GLU GLN LYS LEU ILE SER GLU GLU ASP LEU ASN LYS GLU          
SEQRES   2 B  164  LEU GLN GLY PRO GLU GLU THR VAL THR GLN ASP CYS LEU          
SEQRES   3 B  164  GLN LEU ILE ALA ASP SER GLU THR PRO THR ILE GLN LYS          
SEQRES   4 B  164  GLY SER TYR THR PHE VAL PRO TRP LEU LEU SER PHE LYS          
SEQRES   5 B  164  ARG GLY SER ALA LEU GLU GLU LYS GLU ASN LYS ILE LEU          
SEQRES   6 B  164  VAL LYS GLU THR GLY TYR PHE PHE ILE TYR GLY GLN VAL          
SEQRES   7 B  164  LEU TYR THR ASP LYS THR TYR ALA MET GLY HIS LEU ILE          
SEQRES   8 B  164  GLN ARG LYS LYS VAL HIS VAL PHE GLY ASP GLU LEU SER          
SEQRES   9 B  164  LEU VAL THR LEU PHE ARG CYS ILE GLN ASN MET PRO GLU          
SEQRES  10 B  164  THR LEU PRO ASN ASN SER CYS TYR SER ALA GLY ILE ALA          
SEQRES  11 B  164  LYS LEU GLU GLU GLY ASP GLU LEU GLN LEU ALA ILE PRO          
SEQRES  12 B  164  ARG GLU ASN ALA GLN ILE SER LEU ASP GLY ASP VAL THR          
SEQRES  13 B  164  PHE PHE GLY ALA LEU LYS LEU LEU                              
SEQRES   1 C  164  GLU GLN LYS LEU ILE SER GLU GLU ASP LEU ASN LYS GLU          
SEQRES   2 C  164  LEU GLN GLY PRO GLU GLU THR VAL THR GLN ASP CYS LEU          
SEQRES   3 C  164  GLN LEU ILE ALA ASP SER GLU THR PRO THR ILE GLN LYS          
SEQRES   4 C  164  GLY SER TYR THR PHE VAL PRO TRP LEU LEU SER PHE LYS          
SEQRES   5 C  164  ARG GLY SER ALA LEU GLU GLU LYS GLU ASN LYS ILE LEU          
SEQRES   6 C  164  VAL LYS GLU THR GLY TYR PHE PHE ILE TYR GLY GLN VAL          
SEQRES   7 C  164  LEU TYR THR ASP LYS THR TYR ALA MET GLY HIS LEU ILE          
SEQRES   8 C  164  GLN ARG LYS LYS VAL HIS VAL PHE GLY ASP GLU LEU SER          
SEQRES   9 C  164  LEU VAL THR LEU PHE ARG CYS ILE GLN ASN MET PRO GLU          
SEQRES  10 C  164  THR LEU PRO ASN ASN SER CYS TYR SER ALA GLY ILE ALA          
SEQRES  11 C  164  LYS LEU GLU GLU GLY ASP GLU LEU GLN LEU ALA ILE PRO          
SEQRES  12 C  164  ARG GLU ASN ALA GLN ILE SER LEU ASP GLY ASP VAL THR          
SEQRES  13 C  164  PHE PHE GLY ALA LEU LYS LEU LEU                              
SEQRES   1 K  164  GLU GLN LYS LEU ILE SER GLU GLU ASP LEU ASN LYS GLU          
SEQRES   2 K  164  LEU GLN GLY PRO GLU GLU THR VAL THR GLN ASP CYS LEU          
SEQRES   3 K  164  GLN LEU ILE ALA ASP SER GLU THR PRO THR ILE GLN LYS          
SEQRES   4 K  164  GLY SER TYR THR PHE VAL PRO TRP LEU LEU SER PHE LYS          
SEQRES   5 K  164  ARG GLY SER ALA LEU GLU GLU LYS GLU ASN LYS ILE LEU          
SEQRES   6 K  164  VAL LYS GLU THR GLY TYR PHE PHE ILE TYR GLY GLN VAL          
SEQRES   7 K  164  LEU TYR THR ASP LYS THR TYR ALA MET GLY HIS LEU ILE          
SEQRES   8 K  164  GLN ARG LYS LYS VAL HIS VAL PHE GLY ASP GLU LEU SER          
SEQRES   9 K  164  LEU VAL THR LEU PHE ARG CYS ILE GLN ASN MET PRO GLU          
SEQRES  10 K  164  THR LEU PRO ASN ASN SER CYS TYR SER ALA GLY ILE ALA          
SEQRES  11 K  164  LYS LEU GLU GLU GLY ASP GLU LEU GLN LEU ALA ILE PRO          
SEQRES  12 K  164  ARG GLU ASN ALA GLN ILE SER LEU ASP GLY ASP VAL THR          
SEQRES  13 K  164  PHE PHE GLY ALA LEU LYS LEU LEU                              
SEQRES   1 L  164  GLU GLN LYS LEU ILE SER GLU GLU ASP LEU ASN LYS GLU          
SEQRES   2 L  164  LEU GLN GLY PRO GLU GLU THR VAL THR GLN ASP CYS LEU          
SEQRES   3 L  164  GLN LEU ILE ALA ASP SER GLU THR PRO THR ILE GLN LYS          
SEQRES   4 L  164  GLY SER TYR THR PHE VAL PRO TRP LEU LEU SER PHE LYS          
SEQRES   5 L  164  ARG GLY SER ALA LEU GLU GLU LYS GLU ASN LYS ILE LEU          
SEQRES   6 L  164  VAL LYS GLU THR GLY TYR PHE PHE ILE TYR GLY GLN VAL          
SEQRES   7 L  164  LEU TYR THR ASP LYS THR TYR ALA MET GLY HIS LEU ILE          
SEQRES   8 L  164  GLN ARG LYS LYS VAL HIS VAL PHE GLY ASP GLU LEU SER          
SEQRES   9 L  164  LEU VAL THR LEU PHE ARG CYS ILE GLN ASN MET PRO GLU          
SEQRES  10 L  164  THR LEU PRO ASN ASN SER CYS TYR SER ALA GLY ILE ALA          
SEQRES  11 L  164  LYS LEU GLU GLU GLY ASP GLU LEU GLN LEU ALA ILE PRO          
SEQRES  12 L  164  ARG GLU ASN ALA GLN ILE SER LEU ASP GLY ASP VAL THR          
SEQRES  13 L  164  PHE PHE GLY ALA LEU LYS LEU LEU                              
SEQRES   1 M  164  GLU GLN LYS LEU ILE SER GLU GLU ASP LEU ASN LYS GLU          
SEQRES   2 M  164  LEU GLN GLY PRO GLU GLU THR VAL THR GLN ASP CYS LEU          
SEQRES   3 M  164  GLN LEU ILE ALA ASP SER GLU THR PRO THR ILE GLN LYS          
SEQRES   4 M  164  GLY SER TYR THR PHE VAL PRO TRP LEU LEU SER PHE LYS          
SEQRES   5 M  164  ARG GLY SER ALA LEU GLU GLU LYS GLU ASN LYS ILE LEU          
SEQRES   6 M  164  VAL LYS GLU THR GLY TYR PHE PHE ILE TYR GLY GLN VAL          
SEQRES   7 M  164  LEU TYR THR ASP LYS THR TYR ALA MET GLY HIS LEU ILE          
SEQRES   8 M  164  GLN ARG LYS LYS VAL HIS VAL PHE GLY ASP GLU LEU SER          
SEQRES   9 M  164  LEU VAL THR LEU PHE ARG CYS ILE GLN ASN MET PRO GLU          
SEQRES  10 M  164  THR LEU PRO ASN ASN SER CYS TYR SER ALA GLY ILE ALA          
SEQRES  11 M  164  LYS LEU GLU GLU GLY ASP GLU LEU GLN LEU ALA ILE PRO          
SEQRES  12 M  164  ARG GLU ASN ALA GLN ILE SER LEU ASP GLY ASP VAL THR          
SEQRES  13 M  164  PHE PHE GLY ALA LEU LYS LEU LEU                              
SHEET    1   A 5 TRP A 168  ARG A 174  0                                        
SHEET    2   A 5 CYS A 146  ALA A 151 -1  N  ILE A 150   O  LEU A 169           
SHEET    3   A 5 PHE A 278  LYS A 283 -1  O  PHE A 279   N  LEU A 149           
SHEET    4   A 5 GLY A 191  TYR A 201 -1  N  PHE A 194   O  LEU A 282           
SHEET    5   A 5 ASN A 243  LEU A 253 -1  O  GLY A 249   N  ILE A 195           
SHEET    1   B 2 ILE A 158  LYS A 160  0                                        
SHEET    2   B 2 TYR A 163  PHE A 165 -1  O  PHE A 165   N  ILE A 158           
SHEET    1   C 5 GLU A 179  GLU A 180  0                                        
SHEET    2   C 5 ILE A 185  LEU A 186 -1  O  LEU A 186   N  GLU A 179           
SHEET    3   C 5 GLU A 258  ALA A 262 -1  O  LEU A 259   N  ILE A 185           
SHEET    4   C 5 ALA A 207  LYS A 215 -1  N  LYS A 215   O  GLU A 258           
SHEET    5   C 5 LEU A 226  ASN A 235 -1  O  VAL A 227   N  ARG A 214           
SHEET    1   D 5 TRP B 168  ARG B 174  0                                        
SHEET    2   D 5 CYS B 146  ALA B 151 -1  N  GLN B 148   O  PHE B 172           
SHEET    3   D 5 PHE B 278  LYS B 283 -1  O  PHE B 279   N  LEU B 149           
SHEET    4   D 5 GLY B 191  TYR B 201 -1  N  PHE B 194   O  LEU B 282           
SHEET    5   D 5 ASN B 243  LEU B 253 -1  O  ASN B 243   N  TYR B 201           
SHEET    1   E 2 ILE B 158  LYS B 160  0                                        
SHEET    2   E 2 TYR B 163  PHE B 165 -1  O  PHE B 165   N  ILE B 158           
SHEET    1   F 5 GLU B 179  GLU B 180  0                                        
SHEET    2   F 5 ILE B 185  LEU B 186 -1  O  LEU B 186   N  GLU B 179           
SHEET    3   F 5 GLU B 258  ALA B 262 -1  O  LEU B 259   N  ILE B 185           
SHEET    4   F 5 ALA B 207  LYS B 215 -1  N  LYS B 215   O  GLU B 258           
SHEET    5   F 5 LEU B 226  ASN B 235 -1  O  VAL B 227   N  ARG B 214           
SHEET    1   G 5 TRP C 168  ARG C 174  0                                        
SHEET    2   G 5 CYS C 146  ALA C 151 -1  N  ILE C 150   O  LEU C 169           
SHEET    3   G 5 PHE C 278  LYS C 283 -1  O  PHE C 279   N  LEU C 149           
SHEET    4   G 5 GLY C 191  TYR C 201 -1  N  PHE C 194   O  LEU C 282           
SHEET    5   G 5 ASN C 243  LEU C 253 -1  O  GLY C 249   N  ILE C 195           
SHEET    1   H 5 LEU C 226  ASN C 235  0                                        
SHEET    2   H 5 ALA C 207  LYS C 215 -1  N  ARG C 214   O  VAL C 227           
SHEET    3   H 5 GLU C 258  ILE C 263 -1  O  GLU C 258   N  LYS C 215           
SHEET    4   H 5 TYR C 163  PHE C 165 -1  N  THR C 164   O  ILE C 263           
SHEET    5   H 5 ILE C 158  LYS C 160 -1  N  ILE C 158   O  PHE C 165           
SHEET    1   I 5 LEU C 226  ASN C 235  0                                        
SHEET    2   I 5 ALA C 207  LYS C 215 -1  N  ARG C 214   O  VAL C 227           
SHEET    3   I 5 GLU C 258  ILE C 263 -1  O  GLU C 258   N  LYS C 215           
SHEET    4   I 5 ILE C 185  LEU C 186 -1  N  ILE C 185   O  LEU C 259           
SHEET    5   I 5 GLU C 179  GLU C 180 -1  N  GLU C 179   O  LEU C 186           
SHEET    1   J 5 TRP K 168  ARG K 174  0                                        
SHEET    2   J 5 CYS K 146  ALA K 151 -1  N  GLN K 148   O  PHE K 172           
SHEET    3   J 5 PHE K 278  LYS K 283 -1  O  PHE K 279   N  LEU K 149           
SHEET    4   J 5 GLY K 191  TYR K 201 -1  N  PHE K 194   O  LEU K 282           
SHEET    5   J 5 ASN K 243  LEU K 253 -1  O  GLY K 249   N  ILE K 195           
SHEET    1   K 5 LEU K 226  ASN K 235  0                                        
SHEET    2   K 5 ALA K 207  LYS K 215 -1  N  ARG K 214   O  VAL K 227           
SHEET    3   K 5 GLU K 258  ILE K 263 -1  O  GLU K 258   N  LYS K 215           
SHEET    4   K 5 TYR K 163  PHE K 165 -1  N  THR K 164   O  ILE K 263           
SHEET    5   K 5 ILE K 158  LYS K 160 -1  N  ILE K 158   O  PHE K 165           
SHEET    1   L 5 LEU K 226  ASN K 235  0                                        
SHEET    2   L 5 ALA K 207  LYS K 215 -1  N  ARG K 214   O  VAL K 227           
SHEET    3   L 5 GLU K 258  ILE K 263 -1  O  GLU K 258   N  LYS K 215           
SHEET    4   L 5 ILE K 185  LEU K 186 -1  N  ILE K 185   O  LEU K 259           
SHEET    5   L 5 GLU K 179  GLU K 180 -1  N  GLU K 179   O  LEU K 186           
SHEET    1   M 5 TRP L 168  ARG L 174  0                                        
SHEET    2   M 5 CYS L 146  ALA L 151 -1  N  GLN L 148   O  PHE L 172           
SHEET    3   M 5 PHE L 278  LYS L 283 -1  O  PHE L 279   N  LEU L 149           
SHEET    4   M 5 GLY L 191  TYR L 201 -1  N  PHE L 194   O  LEU L 282           
SHEET    5   M 5 ASN L 243  LEU L 253 -1  O  GLY L 249   N  ILE L 195           
SHEET    1   N 5 LEU L 226  ASN L 235  0                                        
SHEET    2   N 5 ALA L 207  LYS L 215 -1  N  ARG L 214   O  VAL L 227           
SHEET    3   N 5 GLU L 258  ILE L 263 -1  O  GLU L 258   N  LYS L 215           
SHEET    4   N 5 TYR L 163  PHE L 165 -1  N  THR L 164   O  ILE L 263           
SHEET    5   N 5 ILE L 158  LYS L 160 -1  N  ILE L 158   O  PHE L 165           
SHEET    1   O 5 LEU L 226  ASN L 235  0                                        
SHEET    2   O 5 ALA L 207  LYS L 215 -1  N  ARG L 214   O  VAL L 227           
SHEET    3   O 5 GLU L 258  ILE L 263 -1  O  GLU L 258   N  LYS L 215           
SHEET    4   O 5 ILE L 185  LEU L 186 -1  N  ILE L 185   O  LEU L 259           
SHEET    5   O 5 GLU L 179  GLU L 180 -1  N  GLU L 179   O  LEU L 186           
SHEET    1   P 5 TRP M 168  ARG M 174  0                                        
SHEET    2   P 5 CYS M 146  ALA M 151 -1  N  GLN M 148   O  PHE M 172           
SHEET    3   P 5 PHE M 278  LYS M 283 -1  O  PHE M 279   N  LEU M 149           
SHEET    4   P 5 GLY M 191  TYR M 201 -1  N  PHE M 194   O  LEU M 282           
SHEET    5   P 5 ASN M 243  LEU M 253 -1  O  GLY M 249   N  ILE M 195           
SHEET    1   Q 5 LEU M 226  ASN M 235  0                                        
SHEET    2   Q 5 ALA M 207  LYS M 215 -1  N  ARG M 214   O  VAL M 227           
SHEET    3   Q 5 GLU M 258  ILE M 263 -1  O  GLU M 258   N  LYS M 215           
SHEET    4   Q 5 TYR M 163  PHE M 165 -1  N  THR M 164   O  ILE M 263           
SHEET    5   Q 5 ILE M 158  LYS M 160 -1  N  ILE M 158   O  PHE M 165           
SHEET    1   R 5 LEU M 226  ASN M 235  0                                        
SHEET    2   R 5 ALA M 207  LYS M 215 -1  N  ARG M 214   O  VAL M 227           
SHEET    3   R 5 GLU M 258  ILE M 263 -1  O  GLU M 258   N  LYS M 215           
SHEET    4   R 5 ILE M 185  LEU M 186 -1  N  ILE M 185   O  LEU M 259           
SHEET    5   R 5 GLU M 179  GLU M 180 -1  N  GLU M 179   O  LEU M 186           
SSBOND   1 CYS A  232    CYS A  245                          1555   1555  2.03  
SSBOND   2 CYS B  232    CYS B  245                          1555   1555  2.03  
SSBOND   3 CYS C  232    CYS C  245                          1555   1555  2.03  
SSBOND   4 CYS K  232    CYS K  245                          1555   1555  2.03  
SSBOND   5 CYS L  232    CYS L  245                          1555   1555  2.04  
SSBOND   6 CYS M  232    CYS M  245                          1555   1555  2.03  
CRYST1  121.720  121.720  160.740  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      0.008216  0.004743  0.000000        0.00000                         
SCALE2      0.000000  0.009487  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006221        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system