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Database: PDB
Entry: 1OSG
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Original site: 1OSG 
HEADER    IMMUNE SYSTEM                           19-MAR-03   1OSG              
TITLE     COMPLEX BETWEEN BAFF AND A BR3 DERIVED PEPTIDE PRESENTED IN           
TITLE    2 A BETA-HAIRPIN SCAFFOLD                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUMOR NECROSIS FACTOR LIGAND SUPERFAMILY MEMBER            
COMPND   3 13B;                                                                 
COMPND   4 CHAIN: A, B, C, D, E, F;                                             
COMPND   5 FRAGMENT: TNF DOMAIN;                                                
COMPND   6 SYNONYM: TNF-AND APOL- RELATED LEUKOCYTE EXPRESSED LIGAND            
COMPND   7 1, TALL-1, B LYMPHOCYTE STIMULATOR, BLYS, B CELL-                    
COMPND   8 ACTIVATING FACTOR, BAFF, DENDRITIC CELL- DERIVED TNF-LIKE            
COMPND   9 MOLECULE;                                                            
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: BR3 DERIVED PEPTIDE;                                       
COMPND  13 CHAIN: G, J, H, I, K, L;                                             
COMPND  14 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: BAFF;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL-21 (DE3);                               
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET15B;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 OTHER_DETAILS: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED.              
KEYWDS    JELLY-ROLL, BETA HAIRPIN, PROTEIN-PEPTIDE COMPLEX, IMMUNE             
KEYWDS   2 SYSTEM                                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.C.GORDON,B.PAN,S.G.HYMOWITZ,J.P.YIN,R.F.KELLEY,                     
AUTHOR   2 A.G.COCHRAN,M.YAN,V.M.DIXIT,W.J.FAIRBROTHER,M.A.STAROVASNIK          
REVDAT   2   24-FEB-09 1OSG    1       VERSN                                    
REVDAT   1   27-MAY-03 1OSG    0                                                
JRNL        AUTH   N.C.GORDON,B.PAN,S.G.HYMOWITZ,J.P.YIN,R.F.KELLEY,            
JRNL        AUTH 2 A.G.COCHRAN,M.YAN,V.M.DIXIT,W.J.FAIRBROTHER,                 
JRNL        AUTH 3 M.A.STAROVASNIK                                              
JRNL        TITL   BAFF/BLYS RECEPTOR 3 COMPRISES A MINIMAL TNF                 
JRNL        TITL 2 RECEPTOR-LIKE MODULE THAT ENCODES A HIGHLY FOCUSED           
JRNL        TITL 3 LIGAND-BINDING SITE                                          
JRNL        REF    BIOCHEMISTRY                  V.  42  5977 2003              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   12755599                                                     
JRNL        DOI    10.1021/BI034017G                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 23768                          
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 + TEST SET) : 0.220                           
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.286                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2536                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.08                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1609                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.80                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2400                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 308                          
REMARK   3   BIN FREE R VALUE                    : 0.3640                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7507                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 20                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.34                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.19000                                              
REMARK   3    B22 (A**2) : 0.19000                                              
REMARK   3    B33 (A**2) : -0.29000                                             
REMARK   3    B12 (A**2) : 0.10000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.500         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.348         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.975        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.900                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.836                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7686 ; 0.012 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  6946 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10414 ; 1.357 ; 1.962       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 16200 ; 0.775 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   924 ; 6.766 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1176 ; 0.077 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8382 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1534 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1309 ; 0.197 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  8004 ; 0.234 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  5331 ; 0.088 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   146 ; 0.154 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):     9 ; 0.109 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    48 ; 0.261 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.023 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4644 ; 0.931 ; 2.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7493 ; 1.678 ; 3.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3036 ; 1.042 ; 3.500       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2909 ; 1.722 ; 4.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D E F                     
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    142       A     214      4                      
REMARK   3           1     B    142       B     214      4                      
REMARK   3           1     C    142       C     214      4                      
REMARK   3           1     D    142       D     214      4                      
REMARK   3           1     E    142       E     214      4                      
REMARK   3           1     F    142       F     214      4                      
REMARK   3           2     A    227       A     285      4                      
REMARK   3           2     B    227       B     285      4                      
REMARK   3           2     C    227       C     285      4                      
REMARK   3           2     D    227       D     285      4                      
REMARK   3           2     E    227       E     285      4                      
REMARK   3           2     F    227       F     285      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   2017 ;  0.48 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   2017 ;  0.58 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   2017 ;  0.48 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):   2017 ;  0.57 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    E    (A):   2017 ;  0.52 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    F    (A):   2017 ;  0.47 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   2017 ;  0.38 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   2017 ;  0.36 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    C (A**2):   2017 ;  0.38 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    D (A**2):   2017 ;  0.44 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    E (A**2):   2017 ;  0.41 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    F (A**2):   2017 ;  0.45 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : G H I J K L                     
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     G     23       G      34      4                      
REMARK   3           1     H     23       H      34      4                      
REMARK   3           1     I     23       I      34      4                      
REMARK   3           1     J     23       J      34      4                      
REMARK   3           1     K     23       K      34      4                      
REMARK   3           1     L     23       L      34      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    G    (A):    198 ;  0.66 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    H    (A):    198 ;  0.76 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    I    (A):    198 ;  0.88 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    J    (A):    198 ;  0.75 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    K    (A):    198 ;  0.67 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    L    (A):    198 ;  0.82 ;  0.50           
REMARK   3   MEDIUM THERMAL     2    G (A**2):    198 ;  0.29 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    H (A**2):    198 ;  0.23 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    I (A**2):    198 ;  0.29 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    J (A**2):    198 ;  0.25 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    K (A**2):    198 ;  0.32 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    L (A**2):    198 ;  0.29 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1OSG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-MAR-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB018624.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-NOV-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.08                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26356                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.41000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1KXG WITH THE WATERS REMOVED                         
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.07                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 1.0 M LICL, 0.1M           
REMARK 280  SODIUM CACODYLATE, PH 6.7, VAPOR DIFFUSION, HANGING DROP,           
REMARK 280  TEMPERATURE 292K                                                    
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      104.80933            
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       52.40467            
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       78.60700            
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       26.20233            
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      131.01167            
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 300 REMARK: THE BIOLOGICALLY RELEVANT ASSEMBLY OF BAFF IS A TRIMER.      
REMARK 300 THE CRYSTALLOGRAPHIC ASYMETRIC UNIT CONTAINS 2 TRIMERS.              
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, G, H, I                      
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: HEXAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F, J, K, L                      
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     GLY A    78                                                      
REMARK 465     SER A    79                                                      
REMARK 465     HIS A    80                                                      
REMARK 465     MET A    81                                                      
REMARK 465     GLU A    82                                                      
REMARK 465     LEU A    83                                                      
REMARK 465     GLN A    84                                                      
REMARK 465     GLY A    85                                                      
REMARK 465     HIS A    86                                                      
REMARK 465     HIS A    87                                                      
REMARK 465     ALA A    88                                                      
REMARK 465     GLU A    89                                                      
REMARK 465     LYS A    90                                                      
REMARK 465     LEU A    91                                                      
REMARK 465     PRO A    92                                                      
REMARK 465     ALA A    93                                                      
REMARK 465     GLY A    94                                                      
REMARK 465     ALA A    95                                                      
REMARK 465     GLY A    96                                                      
REMARK 465     ALA A    97                                                      
REMARK 465     PRO A    98                                                      
REMARK 465     LYS A    99                                                      
REMARK 465     ALA A   100                                                      
REMARK 465     GLY A   101                                                      
REMARK 465     LEU A   102                                                      
REMARK 465     GLU A   103                                                      
REMARK 465     GLU A   104                                                      
REMARK 465     ALA A   105                                                      
REMARK 465     PRO A   106                                                      
REMARK 465     ALA A   107                                                      
REMARK 465     VAL A   108                                                      
REMARK 465     THR A   109                                                      
REMARK 465     ALA A   110                                                      
REMARK 465     GLY A   111                                                      
REMARK 465     LEU A   112                                                      
REMARK 465     LYS A   113                                                      
REMARK 465     ILE A   114                                                      
REMARK 465     PHE A   115                                                      
REMARK 465     GLU A   116                                                      
REMARK 465     PRO A   117                                                      
REMARK 465     PRO A   118                                                      
REMARK 465     ALA A   119                                                      
REMARK 465     PRO A   120                                                      
REMARK 465     GLY A   121                                                      
REMARK 465     GLU A   122                                                      
REMARK 465     GLY A   123                                                      
REMARK 465     ASN A   124                                                      
REMARK 465     SER A   125                                                      
REMARK 465     SER A   126                                                      
REMARK 465     GLN A   127                                                      
REMARK 465     ASN A   128                                                      
REMARK 465     SER A   129                                                      
REMARK 465     ARG A   130                                                      
REMARK 465     ASN A   131                                                      
REMARK 465     LYS A   132                                                      
REMARK 465     ARG A   133                                                      
REMARK 465     ALA A   134                                                      
REMARK 465     VAL 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     GLY B    78                                                      
REMARK 465     SER B    79                                                      
REMARK 465     HIS B    80                                                      
REMARK 465     MET B    81                                                      
REMARK 465     GLU B    82                                                      
REMARK 465     LEU B    83                                                      
REMARK 465     GLN B    84                                                      
REMARK 465     GLY B    85                                                      
REMARK 465     HIS B    86                                                      
REMARK 465     HIS B    87                                                      
REMARK 465     ALA B    88                                                      
REMARK 465     GLU B    89                                                      
REMARK 465     LYS B    90                                                      
REMARK 465     LEU B    91                                                      
REMARK 465     PRO B    92                                                      
REMARK 465     ALA B    93                                                      
REMARK 465     GLY B    94                                                      
REMARK 465     ALA B    95                                                      
REMARK 465     GLY B    96                                                      
REMARK 465     ALA B    97                                                      
REMARK 465     PRO B    98                                                      
REMARK 465     LYS B    99                                                      
REMARK 465     ALA B   100                                                      
REMARK 465     GLY B   101                                                      
REMARK 465     LEU B   102                                                      
REMARK 465     GLU B   103                                                      
REMARK 465     GLU B   104                                                      
REMARK 465     ALA B   105                                                      
REMARK 465     PRO B   106                                                      
REMARK 465     ALA B   107                                                      
REMARK 465     VAL B   108                                                      
REMARK 465     THR B   109                                                      
REMARK 465     ALA B   110                                                      
REMARK 465     GLY B   111                                                      
REMARK 465     LEU B   112                                                      
REMARK 465     LYS B   113                                                      
REMARK 465     ILE B   114                                                      
REMARK 465     PHE B   115                                                      
REMARK 465     GLU B   116                                                      
REMARK 465     PRO B   117                                                      
REMARK 465     PRO B   118                                                      
REMARK 465     ALA B   119                                                      
REMARK 465     PRO B   120                                                      
REMARK 465     GLY B   121                                                      
REMARK 465     GLU B   122                                                      
REMARK 465     GLY B   123                                                      
REMARK 465     ASN B   124                                                      
REMARK 465     SER B   125                                                      
REMARK 465     SER B   126                                                      
REMARK 465     GLN B   127                                                      
REMARK 465     ASN B   128                                                      
REMARK 465     SER B   129                                                      
REMARK 465     ARG B   130                                                      
REMARK 465     ASN B   131                                                      
REMARK 465     LYS B   132                                                      
REMARK 465     ARG B   133                                                      
REMARK 465     ALA B   134                                                      
REMARK 465     VAL 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     GLY C    78                                                      
REMARK 465     SER C    79                                                      
REMARK 465     HIS C    80                                                      
REMARK 465     MET C    81                                                      
REMARK 465     GLU C    82                                                      
REMARK 465     LEU C    83                                                      
REMARK 465     GLN C    84                                                      
REMARK 465     GLY C    85                                                      
REMARK 465     HIS C    86                                                      
REMARK 465     HIS C    87                                                      
REMARK 465     ALA C    88                                                      
REMARK 465     GLU C    89                                                      
REMARK 465     LYS C    90                                                      
REMARK 465     LEU C    91                                                      
REMARK 465     PRO C    92                                                      
REMARK 465     ALA C    93                                                      
REMARK 465     GLY C    94                                                      
REMARK 465     ALA C    95                                                      
REMARK 465     GLY C    96                                                      
REMARK 465     ALA C    97                                                      
REMARK 465     PRO C    98                                                      
REMARK 465     LYS C    99                                                      
REMARK 465     ALA C   100                                                      
REMARK 465     GLY C   101                                                      
REMARK 465     LEU C   102                                                      
REMARK 465     GLU C   103                                                      
REMARK 465     GLU C   104                                                      
REMARK 465     ALA C   105                                                      
REMARK 465     PRO C   106                                                      
REMARK 465     ALA C   107                                                      
REMARK 465     VAL C   108                                                      
REMARK 465     THR C   109                                                      
REMARK 465     ALA C   110                                                      
REMARK 465     GLY C   111                                                      
REMARK 465     LEU C   112                                                      
REMARK 465     LYS C   113                                                      
REMARK 465     ILE C   114                                                      
REMARK 465     PHE C   115                                                      
REMARK 465     GLU C   116                                                      
REMARK 465     PRO C   117                                                      
REMARK 465     PRO C   118                                                      
REMARK 465     ALA C   119                                                      
REMARK 465     PRO C   120                                                      
REMARK 465     GLY C   121                                                      
REMARK 465     GLU C   122                                                      
REMARK 465     GLY C   123                                                      
REMARK 465     ASN C   124                                                      
REMARK 465     SER C   125                                                      
REMARK 465     SER C   126                                                      
REMARK 465     GLN C   127                                                      
REMARK 465     ASN C   128                                                      
REMARK 465     SER C   129                                                      
REMARK 465     ARG C   130                                                      
REMARK 465     ASN C   131                                                      
REMARK 465     LYS C   132                                                      
REMARK 465     ARG C   133                                                      
REMARK 465     ALA C   134                                                      
REMARK 465     VAL 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     GLY D    78                                                      
REMARK 465     SER D    79                                                      
REMARK 465     HIS D    80                                                      
REMARK 465     MET D    81                                                      
REMARK 465     GLU D    82                                                      
REMARK 465     LEU D    83                                                      
REMARK 465     GLN D    84                                                      
REMARK 465     GLY D    85                                                      
REMARK 465     HIS D    86                                                      
REMARK 465     HIS D    87                                                      
REMARK 465     ALA D    88                                                      
REMARK 465     GLU D    89                                                      
REMARK 465     LYS D    90                                                      
REMARK 465     LEU D    91                                                      
REMARK 465     PRO D    92                                                      
REMARK 465     ALA D    93                                                      
REMARK 465     GLY D    94                                                      
REMARK 465     ALA D    95                                                      
REMARK 465     GLY D    96                                                      
REMARK 465     ALA D    97                                                      
REMARK 465     PRO D    98                                                      
REMARK 465     LYS D    99                                                      
REMARK 465     ALA D   100                                                      
REMARK 465     GLY D   101                                                      
REMARK 465     LEU D   102                                                      
REMARK 465     GLU D   103                                                      
REMARK 465     GLU D   104                                                      
REMARK 465     ALA D   105                                                      
REMARK 465     PRO D   106                                                      
REMARK 465     ALA D   107                                                      
REMARK 465     VAL D   108                                                      
REMARK 465     THR D   109                                                      
REMARK 465     ALA D   110                                                      
REMARK 465     GLY D   111                                                      
REMARK 465     LEU D   112                                                      
REMARK 465     LYS D   113                                                      
REMARK 465     ILE D   114                                                      
REMARK 465     PHE D   115                                                      
REMARK 465     GLU D   116                                                      
REMARK 465     PRO D   117                                                      
REMARK 465     PRO D   118                                                      
REMARK 465     ALA D   119                                                      
REMARK 465     PRO D   120                                                      
REMARK 465     GLY D   121                                                      
REMARK 465     GLU D   122                                                      
REMARK 465     GLY D   123                                                      
REMARK 465     ASN D   124                                                      
REMARK 465     SER D   125                                                      
REMARK 465     SER D   126                                                      
REMARK 465     GLN D   127                                                      
REMARK 465     ASN D   128                                                      
REMARK 465     SER D   129                                                      
REMARK 465     ARG D   130                                                      
REMARK 465     ASN D   131                                                      
REMARK 465     LYS D   132                                                      
REMARK 465     ARG D   133                                                      
REMARK 465     ALA D   134                                                      
REMARK 465     VAL D   135                                                      
REMARK 465     GLN D   136                                                      
REMARK 465     GLY D   137                                                      
REMARK 465     PRO D   138                                                      
REMARK 465     GLU D   139                                                      
REMARK 465     GLU D   140                                                      
REMARK 465     THR D   141                                                      
REMARK 465     GLY E    78                                                      
REMARK 465     SER E    79                                                      
REMARK 465     HIS E    80                                                      
REMARK 465     MET E    81                                                      
REMARK 465     GLU E    82                                                      
REMARK 465     LEU E    83                                                      
REMARK 465     GLN E    84                                                      
REMARK 465     GLY E    85                                                      
REMARK 465     HIS E    86                                                      
REMARK 465     HIS E    87                                                      
REMARK 465     ALA E    88                                                      
REMARK 465     GLU E    89                                                      
REMARK 465     LYS E    90                                                      
REMARK 465     LEU E    91                                                      
REMARK 465     PRO E    92                                                      
REMARK 465     ALA E    93                                                      
REMARK 465     GLY E    94                                                      
REMARK 465     ALA E    95                                                      
REMARK 465     GLY E    96                                                      
REMARK 465     ALA E    97                                                      
REMARK 465     PRO E    98                                                      
REMARK 465     LYS E    99                                                      
REMARK 465     ALA E   100                                                      
REMARK 465     GLY E   101                                                      
REMARK 465     LEU E   102                                                      
REMARK 465     GLU E   103                                                      
REMARK 465     GLU E   104                                                      
REMARK 465     ALA E   105                                                      
REMARK 465     PRO E   106                                                      
REMARK 465     ALA E   107                                                      
REMARK 465     VAL E   108                                                      
REMARK 465     THR E   109                                                      
REMARK 465     ALA E   110                                                      
REMARK 465     GLY E   111                                                      
REMARK 465     LEU E   112                                                      
REMARK 465     LYS E   113                                                      
REMARK 465     ILE E   114                                                      
REMARK 465     PHE E   115                                                      
REMARK 465     GLU E   116                                                      
REMARK 465     PRO E   117                                                      
REMARK 465     PRO E   118                                                      
REMARK 465     ALA E   119                                                      
REMARK 465     PRO E   120                                                      
REMARK 465     GLY E   121                                                      
REMARK 465     GLU E   122                                                      
REMARK 465     GLY E   123                                                      
REMARK 465     ASN E   124                                                      
REMARK 465     SER E   125                                                      
REMARK 465     SER E   126                                                      
REMARK 465     GLN E   127                                                      
REMARK 465     ASN E   128                                                      
REMARK 465     SER E   129                                                      
REMARK 465     ARG E   130                                                      
REMARK 465     ASN E   131                                                      
REMARK 465     LYS E   132                                                      
REMARK 465     ARG E   133                                                      
REMARK 465     ALA E   134                                                      
REMARK 465     VAL E   135                                                      
REMARK 465     GLN E   136                                                      
REMARK 465     GLY E   137                                                      
REMARK 465     PRO E   138                                                      
REMARK 465     GLU E   139                                                      
REMARK 465     GLU E   140                                                      
REMARK 465     THR E   141                                                      
REMARK 465     GLY F    78                                                      
REMARK 465     SER F    79                                                      
REMARK 465     HIS F    80                                                      
REMARK 465     MET F    81                                                      
REMARK 465     GLU F    82                                                      
REMARK 465     LEU F    83                                                      
REMARK 465     GLN F    84                                                      
REMARK 465     GLY F    85                                                      
REMARK 465     HIS F    86                                                      
REMARK 465     HIS F    87                                                      
REMARK 465     ALA F    88                                                      
REMARK 465     GLU F    89                                                      
REMARK 465     LYS F    90                                                      
REMARK 465     LEU F    91                                                      
REMARK 465     PRO F    92                                                      
REMARK 465     ALA F    93                                                      
REMARK 465     GLY F    94                                                      
REMARK 465     ALA F    95                                                      
REMARK 465     GLY F    96                                                      
REMARK 465     ALA F    97                                                      
REMARK 465     PRO F    98                                                      
REMARK 465     LYS F    99                                                      
REMARK 465     ALA F   100                                                      
REMARK 465     GLY F   101                                                      
REMARK 465     LEU F   102                                                      
REMARK 465     GLU F   103                                                      
REMARK 465     GLU F   104                                                      
REMARK 465     ALA F   105                                                      
REMARK 465     PRO F   106                                                      
REMARK 465     ALA F   107                                                      
REMARK 465     VAL F   108                                                      
REMARK 465     THR F   109                                                      
REMARK 465     ALA F   110                                                      
REMARK 465     GLY F   111                                                      
REMARK 465     LEU F   112                                                      
REMARK 465     LYS F   113                                                      
REMARK 465     ILE F   114                                                      
REMARK 465     PHE F   115                                                      
REMARK 465     GLU F   116                                                      
REMARK 465     PRO F   117                                                      
REMARK 465     PRO F   118                                                      
REMARK 465     ALA F   119                                                      
REMARK 465     PRO F   120                                                      
REMARK 465     GLY F   121                                                      
REMARK 465     GLU F   122                                                      
REMARK 465     GLY F   123                                                      
REMARK 465     ASN F   124                                                      
REMARK 465     SER F   125                                                      
REMARK 465     SER F   126                                                      
REMARK 465     GLN F   127                                                      
REMARK 465     ASN F   128                                                      
REMARK 465     SER F   129                                                      
REMARK 465     ARG F   130                                                      
REMARK 465     ASN F   131                                                      
REMARK 465     LYS F   132                                                      
REMARK 465     ARG F   133                                                      
REMARK 465     ALA F   134                                                      
REMARK 465     VAL F   135                                                      
REMARK 465     GLN F   136                                                      
REMARK 465     GLY F   137                                                      
REMARK 465     PRO F   138                                                      
REMARK 465     GLU F   139                                                      
REMARK 465     GLU F   140                                                      
REMARK 465     THR F   141                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     HIS I  31    CG   ND1  CD2  CE1  NE2                             
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    ASP A 273   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP B 145   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP B 203   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP E 145   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP E 152   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP F 203   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP G  26   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP K  26   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 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    SER A 162      -33.39     80.75                                   
REMARK 500    ASN A 267       60.90     37.67                                   
REMARK 500    LYS B 160       62.08   -112.78                                   
REMARK 500    SER B 162      -33.39     91.24                                   
REMARK 500    GLU B 223      140.14    -38.58                                   
REMARK 500    LYS C 160       56.38   -143.75                                   
REMARK 500    SER C 162      -48.71    104.04                                   
REMARK 500    GLU C 255      105.01    -50.66                                   
REMARK 500    ASN C 267       72.79     38.82                                   
REMARK 500    LYS D 160       59.91    -98.49                                   
REMARK 500    SER D 162      -63.07     87.14                                   
REMARK 500    LYS D 188      -39.65   -132.78                                   
REMARK 500    GLU D 223      133.53    -38.41                                   
REMARK 500    ASN D 242       77.93   -178.99                                   
REMARK 500    PHE D 279      124.38   -172.46                                   
REMARK 500    THR E 157      171.11    -53.98                                   
REMARK 500    SER E 162       -8.02     76.09                                   
REMARK 500    TYR E 206      -31.78    -39.25                                   
REMARK 500    GLU E 255      110.21    -35.19                                   
REMARK 500    PRO E 264       48.30    -81.28                                   
REMARK 500    ASN E 267       79.65     27.22                                   
REMARK 500    SER F 162      -37.73     82.74                                   
REMARK 500    LYS F 181      108.72   -160.52                                   
REMARK 500    ASN F 242       78.40   -170.31                                   
REMARK 500    PRO F 264       49.30    -83.46                                   
REMARK 500    VAL F 276      -26.02   -140.90                                   
REMARK 500    PHE F 279      116.52   -164.52                                   
REMARK 500    LEU H  28      -60.89    -91.69                                   
REMARK 500    HIS I  31     -159.96   -130.66                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 701  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 234   OE1                                                    
REMARK 620 2 GLN B 234   OE1  77.2                                              
REMARK 620 3 GLN C 234   OE1  79.6  75.0                                        
REMARK 620 4  MG A 702  MG   117.8 140.1 141.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 802  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN E 234   OE1                                                    
REMARK 620 2 GLN F 234   OE1  74.6                                              
REMARK 620 3  MG E 801  MG   114.0 170.3                                        
REMARK 620 4 GLN D 234   OE1  64.7  69.1 109.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 701                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 702                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 801                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 802                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1MPV   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF BHPBR3, THE BAFF-BINDING LOOP OF BR3 EMBEDDED           
REMARK 900 IN A -HAIRPIN PEPTIDE                                                
REMARK 900 RELATED ID: 1KXG   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF BAFF                                            
REMARK 999                                                                      
REMARK 999 AN APPROPRIATE SEQUENCE DATABASE REFERENCE WAS NOT                   
REMARK 999 AVAILABLE FOR THE BR3 DERIVED PEPTIDE AT THE TIME OF PROCESSING.     
DBREF  1OSG A   82   285  UNP    Q9Y275   TN13B_HUMAN     82    285             
DBREF  1OSG B   82   285  UNP    Q9Y275   TN13B_HUMAN     82    285             
DBREF  1OSG C   82   285  UNP    Q9Y275   TN13B_HUMAN     82    285             
DBREF  1OSG D   82   285  UNP    Q9Y275   TN13B_HUMAN     82    285             
DBREF  1OSG E   82   285  UNP    Q9Y275   TN13B_HUMAN     82    285             
DBREF  1OSG F   82   285  UNP    Q9Y275   TN13B_HUMAN     82    285             
DBREF  1OSG G   23    34  PDB    1OSG     1OSG            23     34             
DBREF  1OSG J   23    34  PDB    1OSG     1OSG            23     34             
DBREF  1OSG H   23    34  PDB    1OSG     1OSG            23     34             
DBREF  1OSG I   23    34  PDB    1OSG     1OSG            23     34             
DBREF  1OSG K   23    34  PDB    1OSG     1OSG            23     34             
DBREF  1OSG L   23    34  PDB    1OSG     1OSG            23     34             
SEQADV 1OSG GLY A   78  UNP  Q9Y275              CLONING ARTIFACT               
SEQADV 1OSG SER A   79  UNP  Q9Y275              CLONING ARTIFACT               
SEQADV 1OSG HIS A   80  UNP  Q9Y275              CLONING ARTIFACT               
SEQADV 1OSG MET A   81  UNP  Q9Y275              CLONING ARTIFACT               
SEQADV 1OSG GLY B   78  UNP  Q9Y275              CLONING ARTIFACT               
SEQADV 1OSG SER B   79  UNP  Q9Y275              CLONING ARTIFACT               
SEQADV 1OSG HIS B   80  UNP  Q9Y275              CLONING ARTIFACT               
SEQADV 1OSG MET B   81  UNP  Q9Y275              CLONING ARTIFACT               
SEQADV 1OSG GLY C   78  UNP  Q9Y275              CLONING ARTIFACT               
SEQADV 1OSG SER C   79  UNP  Q9Y275              CLONING ARTIFACT               
SEQADV 1OSG HIS C   80  UNP  Q9Y275              CLONING ARTIFACT               
SEQADV 1OSG MET C   81  UNP  Q9Y275              CLONING ARTIFACT               
SEQADV 1OSG GLY D   78  UNP  Q9Y275              CLONING ARTIFACT               
SEQADV 1OSG SER D   79  UNP  Q9Y275              CLONING ARTIFACT               
SEQADV 1OSG HIS D   80  UNP  Q9Y275              CLONING ARTIFACT               
SEQADV 1OSG MET D   81  UNP  Q9Y275              CLONING ARTIFACT               
SEQADV 1OSG GLY E   78  UNP  Q9Y275              CLONING ARTIFACT               
SEQADV 1OSG SER E   79  UNP  Q9Y275              CLONING ARTIFACT               
SEQADV 1OSG HIS E   80  UNP  Q9Y275              CLONING ARTIFACT               
SEQADV 1OSG MET E   81  UNP  Q9Y275              CLONING ARTIFACT               
SEQADV 1OSG GLY F   78  UNP  Q9Y275              CLONING ARTIFACT               
SEQADV 1OSG SER F   79  UNP  Q9Y275              CLONING ARTIFACT               
SEQADV 1OSG HIS F   80  UNP  Q9Y275              CLONING ARTIFACT               
SEQADV 1OSG MET F   81  UNP  Q9Y275              CLONING ARTIFACT               
SEQRES   1 A  208  GLY SER HIS MET GLU LEU GLN GLY HIS HIS ALA GLU LYS          
SEQRES   2 A  208  LEU PRO ALA GLY ALA GLY ALA PRO LYS ALA GLY LEU GLU          
SEQRES   3 A  208  GLU ALA PRO ALA VAL THR ALA GLY LEU LYS ILE PHE GLU          
SEQRES   4 A  208  PRO PRO ALA PRO GLY GLU GLY ASN SER SER GLN ASN SER          
SEQRES   5 A  208  ARG ASN LYS ARG ALA VAL GLN GLY PRO GLU GLU THR VAL          
SEQRES   6 A  208  THR GLN ASP CYS LEU GLN LEU ILE ALA ASP SER GLU THR          
SEQRES   7 A  208  PRO THR ILE GLN LYS GLY SER TYR THR PHE VAL PRO TRP          
SEQRES   8 A  208  LEU LEU SER PHE LYS ARG GLY SER ALA LEU GLU GLU LYS          
SEQRES   9 A  208  GLU ASN LYS ILE LEU VAL LYS GLU THR GLY TYR PHE PHE          
SEQRES  10 A  208  ILE TYR GLY GLN VAL LEU TYR THR ASP LYS THR TYR ALA          
SEQRES  11 A  208  MET GLY HIS LEU ILE GLN ARG LYS LYS VAL HIS VAL PHE          
SEQRES  12 A  208  GLY ASP GLU LEU SER LEU VAL THR LEU PHE ARG CYS ILE          
SEQRES  13 A  208  GLN ASN MET PRO GLU THR LEU PRO ASN ASN SER CYS TYR          
SEQRES  14 A  208  SER ALA GLY ILE ALA LYS LEU GLU GLU GLY ASP GLU LEU          
SEQRES  15 A  208  GLN LEU ALA ILE PRO ARG GLU ASN ALA GLN ILE SER LEU          
SEQRES  16 A  208  ASP GLY ASP VAL THR PHE PHE GLY ALA LEU LYS LEU LEU          
SEQRES   1 B  208  GLY SER HIS MET GLU LEU GLN GLY HIS HIS ALA GLU LYS          
SEQRES   2 B  208  LEU PRO ALA GLY ALA GLY ALA PRO LYS ALA GLY LEU GLU          
SEQRES   3 B  208  GLU ALA PRO ALA VAL THR ALA GLY LEU LYS ILE PHE GLU          
SEQRES   4 B  208  PRO PRO ALA PRO GLY GLU GLY ASN SER SER GLN ASN SER          
SEQRES   5 B  208  ARG ASN LYS ARG ALA VAL GLN GLY PRO GLU GLU THR VAL          
SEQRES   6 B  208  THR GLN ASP CYS LEU GLN LEU ILE ALA ASP SER GLU THR          
SEQRES   7 B  208  PRO THR ILE GLN LYS GLY SER TYR THR PHE VAL PRO TRP          
SEQRES   8 B  208  LEU LEU SER PHE LYS ARG GLY SER ALA LEU GLU GLU LYS          
SEQRES   9 B  208  GLU ASN LYS ILE LEU VAL LYS GLU THR GLY TYR PHE PHE          
SEQRES  10 B  208  ILE TYR GLY GLN VAL LEU TYR THR ASP LYS THR TYR ALA          
SEQRES  11 B  208  MET GLY HIS LEU ILE GLN ARG LYS LYS VAL HIS VAL PHE          
SEQRES  12 B  208  GLY ASP GLU LEU SER LEU VAL THR LEU PHE ARG CYS ILE          
SEQRES  13 B  208  GLN ASN MET PRO GLU THR LEU PRO ASN ASN SER CYS TYR          
SEQRES  14 B  208  SER ALA GLY ILE ALA LYS LEU GLU GLU GLY ASP GLU LEU          
SEQRES  15 B  208  GLN LEU ALA ILE PRO ARG GLU ASN ALA GLN ILE SER LEU          
SEQRES  16 B  208  ASP GLY ASP VAL THR PHE PHE GLY ALA LEU LYS LEU LEU          
SEQRES   1 C  208  GLY SER HIS MET GLU LEU GLN GLY HIS HIS ALA GLU LYS          
SEQRES   2 C  208  LEU PRO ALA GLY ALA GLY ALA PRO LYS ALA GLY LEU GLU          
SEQRES   3 C  208  GLU ALA PRO ALA VAL THR ALA GLY LEU LYS ILE PHE GLU          
SEQRES   4 C  208  PRO PRO ALA PRO GLY GLU GLY ASN SER SER GLN ASN SER          
SEQRES   5 C  208  ARG ASN LYS ARG ALA VAL GLN GLY PRO GLU GLU THR VAL          
SEQRES   6 C  208  THR GLN ASP CYS LEU GLN LEU ILE ALA ASP SER GLU THR          
SEQRES   7 C  208  PRO THR ILE GLN LYS GLY SER TYR THR PHE VAL PRO TRP          
SEQRES   8 C  208  LEU LEU SER PHE LYS ARG GLY SER ALA LEU GLU GLU LYS          
SEQRES   9 C  208  GLU ASN LYS ILE LEU VAL LYS GLU THR GLY TYR PHE PHE          
SEQRES  10 C  208  ILE TYR GLY GLN VAL LEU TYR THR ASP LYS THR TYR ALA          
SEQRES  11 C  208  MET GLY HIS LEU ILE GLN ARG LYS LYS VAL HIS VAL PHE          
SEQRES  12 C  208  GLY ASP GLU LEU SER LEU VAL THR LEU PHE ARG CYS ILE          
SEQRES  13 C  208  GLN ASN MET PRO GLU THR LEU PRO ASN ASN SER CYS TYR          
SEQRES  14 C  208  SER ALA GLY ILE ALA LYS LEU GLU GLU GLY ASP GLU LEU          
SEQRES  15 C  208  GLN LEU ALA ILE PRO ARG GLU ASN ALA GLN ILE SER LEU          
SEQRES  16 C  208  ASP GLY ASP VAL THR PHE PHE GLY ALA LEU LYS LEU LEU          
SEQRES   1 D  208  GLY SER HIS MET GLU LEU GLN GLY HIS HIS ALA GLU LYS          
SEQRES   2 D  208  LEU PRO ALA GLY ALA GLY ALA PRO LYS ALA GLY LEU GLU          
SEQRES   3 D  208  GLU ALA PRO ALA VAL THR ALA GLY LEU LYS ILE PHE GLU          
SEQRES   4 D  208  PRO PRO ALA PRO GLY GLU GLY ASN SER SER GLN ASN SER          
SEQRES   5 D  208  ARG ASN LYS ARG ALA VAL GLN GLY PRO GLU GLU THR VAL          
SEQRES   6 D  208  THR GLN ASP CYS LEU GLN LEU ILE ALA ASP SER GLU THR          
SEQRES   7 D  208  PRO THR ILE GLN LYS GLY SER TYR THR PHE VAL PRO TRP          
SEQRES   8 D  208  LEU LEU SER PHE LYS ARG GLY SER ALA LEU GLU GLU LYS          
SEQRES   9 D  208  GLU ASN LYS ILE LEU VAL LYS GLU THR GLY TYR PHE PHE          
SEQRES  10 D  208  ILE TYR GLY GLN VAL LEU TYR THR ASP LYS THR TYR ALA          
SEQRES  11 D  208  MET GLY HIS LEU ILE GLN ARG LYS LYS VAL HIS VAL PHE          
SEQRES  12 D  208  GLY ASP GLU LEU SER LEU VAL THR LEU PHE ARG CYS ILE          
SEQRES  13 D  208  GLN ASN MET PRO GLU THR LEU PRO ASN ASN SER CYS TYR          
SEQRES  14 D  208  SER ALA GLY ILE ALA LYS LEU GLU GLU GLY ASP GLU LEU          
SEQRES  15 D  208  GLN LEU ALA ILE PRO ARG GLU ASN ALA GLN ILE SER LEU          
SEQRES  16 D  208  ASP GLY ASP VAL THR PHE PHE GLY ALA LEU LYS LEU LEU          
SEQRES   1 E  208  GLY SER HIS MET GLU LEU GLN GLY HIS HIS ALA GLU LYS          
SEQRES   2 E  208  LEU PRO ALA GLY ALA GLY ALA PRO LYS ALA GLY LEU GLU          
SEQRES   3 E  208  GLU ALA PRO ALA VAL THR ALA GLY LEU LYS ILE PHE GLU          
SEQRES   4 E  208  PRO PRO ALA PRO GLY GLU GLY ASN SER SER GLN ASN SER          
SEQRES   5 E  208  ARG ASN LYS ARG ALA VAL GLN GLY PRO GLU GLU THR VAL          
SEQRES   6 E  208  THR GLN ASP CYS LEU GLN LEU ILE ALA ASP SER GLU THR          
SEQRES   7 E  208  PRO THR ILE GLN LYS GLY SER TYR THR PHE VAL PRO TRP          
SEQRES   8 E  208  LEU LEU SER PHE LYS ARG GLY SER ALA LEU GLU GLU LYS          
SEQRES   9 E  208  GLU ASN LYS ILE LEU VAL LYS GLU THR GLY TYR PHE PHE          
SEQRES  10 E  208  ILE TYR GLY GLN VAL LEU TYR THR ASP LYS THR TYR ALA          
SEQRES  11 E  208  MET GLY HIS LEU ILE GLN ARG LYS LYS VAL HIS VAL PHE          
SEQRES  12 E  208  GLY ASP GLU LEU SER LEU VAL THR LEU PHE ARG CYS ILE          
SEQRES  13 E  208  GLN ASN MET PRO GLU THR LEU PRO ASN ASN SER CYS TYR          
SEQRES  14 E  208  SER ALA GLY ILE ALA LYS LEU GLU GLU GLY ASP GLU LEU          
SEQRES  15 E  208  GLN LEU ALA ILE PRO ARG GLU ASN ALA GLN ILE SER LEU          
SEQRES  16 E  208  ASP GLY ASP VAL THR PHE PHE GLY ALA LEU LYS LEU LEU          
SEQRES   1 F  208  GLY SER HIS MET GLU LEU GLN GLY HIS HIS ALA GLU LYS          
SEQRES   2 F  208  LEU PRO ALA GLY ALA GLY ALA PRO LYS ALA GLY LEU GLU          
SEQRES   3 F  208  GLU ALA PRO ALA VAL THR ALA GLY LEU LYS ILE PHE GLU          
SEQRES   4 F  208  PRO PRO ALA PRO GLY GLU GLY ASN SER SER GLN ASN SER          
SEQRES   5 F  208  ARG ASN LYS ARG ALA VAL GLN GLY PRO GLU GLU THR VAL          
SEQRES   6 F  208  THR GLN ASP CYS LEU GLN LEU ILE ALA ASP SER GLU THR          
SEQRES   7 F  208  PRO THR ILE GLN LYS GLY SER TYR THR PHE VAL PRO TRP          
SEQRES   8 F  208  LEU LEU SER PHE LYS ARG GLY SER ALA LEU GLU GLU LYS          
SEQRES   9 F  208  GLU ASN LYS ILE LEU VAL LYS GLU THR GLY TYR PHE PHE          
SEQRES  10 F  208  ILE TYR GLY GLN VAL LEU TYR THR ASP LYS THR TYR ALA          
SEQRES  11 F  208  MET GLY HIS LEU ILE GLN ARG LYS LYS VAL HIS VAL PHE          
SEQRES  12 F  208  GLY ASP GLU LEU SER LEU VAL THR LEU PHE ARG CYS ILE          
SEQRES  13 F  208  GLN ASN MET PRO GLU THR LEU PRO ASN ASN SER CYS TYR          
SEQRES  14 F  208  SER ALA GLY ILE ALA LYS LEU GLU GLU GLY ASP GLU LEU          
SEQRES  15 F  208  GLN LEU ALA ILE PRO ARG GLU ASN ALA GLN ILE SER LEU          
SEQRES  16 F  208  ASP GLY ASP VAL THR PHE PHE GLY ALA LEU LYS LEU LEU          
SEQRES   1 G   12  CYS HIS TRP ASP LEU LEU VAL ARG HIS TRP VAL CYS              
SEQRES   1 J   12  CYS HIS TRP ASP LEU LEU VAL ARG HIS TRP VAL CYS              
SEQRES   1 H   12  CYS HIS TRP ASP LEU LEU VAL ARG HIS TRP VAL CYS              
SEQRES   1 I   12  CYS HIS TRP ASP LEU LEU VAL ARG HIS TRP VAL CYS              
SEQRES   1 K   12  CYS HIS TRP ASP LEU LEU VAL ARG HIS TRP VAL CYS              
SEQRES   1 L   12  CYS HIS TRP ASP LEU LEU VAL ARG HIS TRP VAL CYS              
HET     MG  A 701       1                                                       
HET     MG  A 702       1                                                       
HET     MG  E 801       1                                                       
HET     MG  D 802       1                                                       
HETNAM      MG MAGNESIUM ION                                                    
FORMUL  13   MG    4(MG 2+)                                                     
FORMUL  17  HOH   *20(H2 O)                                                     
SHEET    1   A 5 TRP A 168  ARG A 174  0                                        
SHEET    2   A 5 CYS A 146  ALA A 151 -1  N  GLN A 148   O  SER A 171           
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 LEU A 178  LYS A 181  0                                        
SHEET    2   C 5 LYS A 184  VAL A 187 -1  O  LYS A 184   N  LYS A 181           
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 3 ASN B 243  LEU B 253  0                                        
SHEET    2   D 3 GLY B 191  TYR B 201 -1  N  TYR B 201   O  ASN B 243           
SHEET    3   D 3 ILE B 270  SER B 271 -1  O  SER B 271   N  LEU B 200           
SHEET    1   E 5 ASN B 243  LEU B 253  0                                        
SHEET    2   E 5 GLY B 191  TYR B 201 -1  N  TYR B 201   O  ASN B 243           
SHEET    3   E 5 PHE B 278  LYS B 283 -1  O  PHE B 278   N  GLN B 198           
SHEET    4   E 5 CYS B 146  ALA B 151 -1  N  LEU B 149   O  PHE B 279           
SHEET    5   E 5 TRP B 168  ARG B 174 -1  O  LEU B 169   N  ILE B 150           
SHEET    1   F 2 ILE B 158  LYS B 160  0                                        
SHEET    2   F 2 TYR B 163  PHE B 165 -1  O  PHE B 165   N  ILE B 158           
SHEET    1   G 5 LEU B 178  LYS B 181  0                                        
SHEET    2   G 5 LYS B 184  VAL B 187 -1  O  LEU B 186   N  GLU B 179           
SHEET    3   G 5 GLU B 258  ALA B 262 -1  O  LEU B 259   N  ILE B 185           
SHEET    4   G 5 LEU B 211  LYS B 215 -1  N  LEU B 211   O  ALA B 262           
SHEET    5   G 5 LEU B 226  ARG B 231 -1  O  PHE B 230   N  ILE B 212           
SHEET    1   H 2 ALA B 207  MET B 208  0                                        
SHEET    2   H 2 GLN B 234  ASN B 235 -1  O  GLN B 234   N  MET B 208           
SHEET    1   I 5 TRP C 168  ARG C 174  0                                        
SHEET    2   I 5 CYS C 146  ALA C 151 -1  N  GLN C 148   O  PHE C 172           
SHEET    3   I 5 PHE C 278  LYS C 283 -1  O  PHE C 279   N  LEU C 149           
SHEET    4   I 5 GLY C 191  TYR C 201 -1  N  PHE C 194   O  LEU C 282           
SHEET    5   I 5 ASN C 243  LEU C 253 -1  O  LEU C 253   N  GLY C 191           
SHEET    1   J 5 LEU C 226  ASN C 235  0                                        
SHEET    2   J 5 ALA C 207  LYS C 215 -1  N  ARG C 214   O  VAL C 227           
SHEET    3   J 5 GLU C 258  ILE C 263 -1  O  GLN C 260   N  GLN C 213           
SHEET    4   J 5 TYR C 163  PHE C 165 -1  N  THR C 164   O  ILE C 263           
SHEET    5   J 5 ILE C 158  LYS C 160 -1  N  LYS C 160   O  TYR C 163           
SHEET    1   K 5 LEU C 226  ASN C 235  0                                        
SHEET    2   K 5 ALA C 207  LYS C 215 -1  N  ARG C 214   O  VAL C 227           
SHEET    3   K 5 GLU C 258  ILE C 263 -1  O  GLN C 260   N  GLN C 213           
SHEET    4   K 5 LYS C 184  VAL C 187 -1  N  ILE C 185   O  LEU C 259           
SHEET    5   K 5 LEU C 178  LYS C 181 -1  N  GLU C 179   O  LEU C 186           
SHEET    1   L 3 ASN D 243  LEU D 253  0                                        
SHEET    2   L 3 GLY D 191  TYR D 201 -1  N  TYR D 201   O  ASN D 243           
SHEET    3   L 3 ILE D 270  SER D 271 -1  O  SER D 271   N  LEU D 200           
SHEET    1   M 5 ASN D 243  LEU D 253  0                                        
SHEET    2   M 5 GLY D 191  TYR D 201 -1  N  TYR D 201   O  ASN D 243           
SHEET    3   M 5 PHE D 278  LYS D 283 -1  O  LEU D 282   N  PHE D 194           
SHEET    4   M 5 CYS D 146  ALA D 151 -1  N  LEU D 149   O  PHE D 279           
SHEET    5   M 5 TRP D 168  ARG D 174 -1  O  LEU D 169   N  ILE D 150           
SHEET    1   N 5 LEU D 178  GLU D 180  0                                        
SHEET    2   N 5 ILE D 185  VAL D 187 -1  O  LEU D 186   N  GLU D 179           
SHEET    3   N 5 GLU D 258  ALA D 262 -1  O  LEU D 259   N  ILE D 185           
SHEET    4   N 5 LEU D 211  LYS D 215 -1  N  LEU D 211   O  ALA D 262           
SHEET    5   N 5 LEU D 226  ARG D 231 -1  O  VAL D 227   N  ARG D 214           
SHEET    1   O 2 ALA D 207  MET D 208  0                                        
SHEET    2   O 2 GLN D 234  ASN D 235 -1  O  GLN D 234   N  MET D 208           
SHEET    1   P 5 TRP E 168  ARG E 174  0                                        
SHEET    2   P 5 CYS E 146  ALA E 151 -1  N  GLN E 148   O  PHE E 172           
SHEET    3   P 5 PHE E 278  LYS E 283 -1  O  PHE E 279   N  LEU E 149           
SHEET    4   P 5 GLY E 191  TYR E 201 -1  N  PHE E 194   O  LEU E 282           
SHEET    5   P 5 ASN E 243  LEU E 253 -1  O  ALA E 251   N  PHE E 193           
SHEET    1   Q 2 ILE E 158  GLN E 159  0                                        
SHEET    2   Q 2 THR E 164  PHE E 165 -1  O  PHE E 165   N  ILE E 158           
SHEET    1   R 5 LEU E 178  GLU E 180  0                                        
SHEET    2   R 5 ILE E 185  VAL E 187 -1  O  LEU E 186   N  GLU E 179           
SHEET    3   R 5 GLU E 258  ALA E 262 -1  O  LEU E 259   N  ILE E 185           
SHEET    4   R 5 ALA E 207  LYS E 215 -1  N  LYS E 215   O  GLU E 258           
SHEET    5   R 5 LEU E 226  ASN E 235 -1  O  VAL E 227   N  ARG E 214           
SHEET    1   S 5 TRP F 168  ARG F 174  0                                        
SHEET    2   S 5 CYS F 146  ALA F 151 -1  N  ILE F 150   O  LEU F 169           
SHEET    3   S 5 PHE F 278  LYS F 283 -1  O  PHE F 279   N  LEU F 149           
SHEET    4   S 5 GLY F 191  TYR F 201 -1  N  PHE F 194   O  LEU F 282           
SHEET    5   S 5 ASN F 243  LEU F 253 -1  O  ASN F 243   N  TYR F 201           
SHEET    1   T 5 LEU F 226  ARG F 231  0                                        
SHEET    2   T 5 LEU F 211  LYS F 215 -1  N  ILE F 212   O  PHE F 230           
SHEET    3   T 5 GLU F 258  ILE F 263 -1  O  ALA F 262   N  LEU F 211           
SHEET    4   T 5 TYR F 163  PHE F 165 -1  N  THR F 164   O  ILE F 263           
SHEET    5   T 5 ILE F 158  LYS F 160 -1  N  ILE F 158   O  PHE F 165           
SHEET    1   U 5 LEU F 226  ARG F 231  0                                        
SHEET    2   U 5 LEU F 211  LYS F 215 -1  N  ILE F 212   O  PHE F 230           
SHEET    3   U 5 GLU F 258  ILE F 263 -1  O  ALA F 262   N  LEU F 211           
SHEET    4   U 5 LYS F 184  VAL F 187 -1  N  ILE F 185   O  LEU F 259           
SHEET    5   U 5 LEU F 178  LYS F 181 -1  N  GLU F 179   O  LEU F 186           
SHEET    1   V 2 ALA F 207  MET F 208  0                                        
SHEET    2   V 2 GLN F 234  ASN F 235 -1  O  GLN F 234   N  MET F 208           
SHEET    1   W 2 HIS G  24  ASP G  26  0                                        
SHEET    2   W 2 HIS G  31  VAL G  33 -1  O  VAL G  33   N  HIS G  24           
SHEET    1   X 2 HIS H  24  ASP H  26  0                                        
SHEET    2   X 2 HIS H  31  VAL H  33 -1  O  VAL H  33   N  HIS H  24           
SHEET    1   Y 2 HIS I  24  ASP I  26  0                                        
SHEET    2   Y 2 HIS I  31  VAL I  33 -1  O  VAL I  33   N  HIS I  24           
SHEET    1   Z 2 HIS K  24  ASP K  26  0                                        
SHEET    2   Z 2 HIS K  31  VAL K  33 -1  O  VAL K  33   N  HIS K  24           
SHEET    1  AA 2 HIS L  24  ASP L  26  0                                        
SHEET    2  AA 2 HIS L  31  VAL L  33 -1  O  VAL L  33   N  HIS L  24           
SSBOND   1 CYS A  232    CYS A  245                          1555   1555  2.08  
SSBOND   2 CYS B  232    CYS B  245                          1555   1555  2.09  
SSBOND   3 CYS C  232    CYS C  245                          1555   1555  2.09  
SSBOND   4 CYS D  232    CYS D  245                          1555   1555  2.09  
SSBOND   5 CYS E  232    CYS E  245                          1555   1555  2.11  
SSBOND   6 CYS F  232    CYS F  245                          1555   1555  2.10  
SSBOND   7 CYS G   23    CYS G   34                          1555   1555  2.03  
SSBOND   8 CYS J   23    CYS J   34                          1555   1555  2.05  
SSBOND   9 CYS H   23    CYS H   34                          1555   1555  2.03  
SSBOND  10 CYS I   23    CYS I   34                          1555   1555  2.03  
SSBOND  11 CYS K   23    CYS K   34                          1555   1555  2.04  
SSBOND  12 CYS L   23    CYS L   34                          1555   1555  2.04  
LINK        MG    MG A 701                 OE1 GLN A 234     1555   1555  2.42  
LINK        MG    MG A 701                 OE1 GLN B 234     1555   1555  2.54  
LINK        MG    MG A 701                 OE1 GLN C 234     1555   1555  2.85  
LINK        MG    MG A 701                MG    MG A 702     1555   1555  2.44  
LINK        MG    MG D 802                 OE1 GLN E 234     1555   1555  2.85  
LINK        MG    MG D 802                 OE1 GLN F 234     1555   1555  2.72  
LINK        MG    MG D 802                MG    MG E 801     1555   1555  1.93  
LINK        MG    MG D 802                 OE1 GLN D 234     1555   1555  2.58  
SITE     1 AC1  5 GLN A 234   MG A 702  GLN B 234  ASN B 243                    
SITE     2 AC1  5 GLN C 234                                                     
SITE     1 AC2  3 ASN A 235   MG A 701  ASN B 243                               
SITE     1 AC3  3 ASN D 235   MG D 802  ASN E 243                               
SITE     1 AC4  4 GLN D 234  GLN E 234   MG E 801  GLN F 234                    
CRYST1  121.633  121.633  157.214  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      0.008221  0.004747  0.000000        0.00000                         
SCALE2      0.000000  0.009493  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006361        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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