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Database: PDB
Entry: 1XU2
LinkDB: 1XU2
Original site: 1XU2 
HEADER    CYTOKINE, HORMONE/GROWTH FACTOR RECEPTOR25-OCT-04   1XU2              
TITLE     THE CRYSTAL STRUCTURE OF APRIL BOUND TO BCMA                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUMOR NECROSIS FACTOR LIGAND SUPERFAMILY MEMBER 13;        
COMPND   3 CHAIN: A, B, D;                                                      
COMPND   4 FRAGMENT: TNF DOMAIN OF APRIL;                                       
COMPND   5 SYNONYM: A PROLIFERATION-INDUCING LIGAND, APRIL, TNFSF13B OR TALL-2; 
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 17;      
COMPND   9 CHAIN: R, S, T;                                                      
COMPND  10 FRAGMENT: BCMA ECD;                                                  
COMPND  11 SYNONYM: B-CELL MATURATION PROTEIN, TNFFSF17;                        
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: TNFSF13, APRIL;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ORIGAMI(DE3);                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET32A (MODIFIED);                        
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: TNFRSF17, BCM, BCMA;                                           
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PZCT                                      
KEYWDS    TNFSF, CYTOKINE, CRD, RECEPTOR, JELLY-ROLL, CYSTEINE-RICH, HORMONE-   
KEYWDS   2 GROWTH FACTOR RECEPTOR COMPLEX                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.G.HYMOWITZ,D.R.PATEL,H.J.A.WALLWEBER,S.RUNYON,M.YAN,J.YIN,          
AUTHOR   2 S.K.SHRIVER,N.C.GORDON,B.PAN,N.J.SKELTON,R.F.KELLEY,M.A.STAROVASNIK  
REVDAT   5   13-JUL-11 1XU2    1       VERSN                                    
REVDAT   4   24-FEB-09 1XU2    1       VERSN                                    
REVDAT   3   22-MAR-05 1XU2    1       JRNL                                     
REVDAT   2   23-NOV-04 1XU2    1       JRNL                                     
REVDAT   1   09-NOV-04 1XU2    0                                                
JRNL        AUTH   S.G.HYMOWITZ,D.R.PATEL,H.J.A.WALLWEBER,S.RUNYON,M.YAN,J.YIN, 
JRNL        AUTH 2 S.K.SHRIVER,N.C.GORDON,B.PAN,N.J.SKELTON,R.F.KELLEY,         
JRNL        AUTH 3 M.A.STAROVASNIK                                              
JRNL        TITL   STRUCTURES OF APRIL-RECEPTOR COMPLEXES: LIKE BCMA, TACI      
JRNL        TITL 2 EMPLOYS ONLY A SINGLE CYSTEINE-RICH DOMAIN FOR HIGH-AFFINITY 
JRNL        TITL 3 LIGAND BINDING                                               
JRNL        REF    J.BIOL.CHEM.                  V. 280  7218 2005              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   15542592                                                     
JRNL        DOI    10.1074/JBC.M411714200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 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) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 25409                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : THIN SHELLS                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.213                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 2856                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 25                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.40                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1680                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1950                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 0                            
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4082                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 36                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 52.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.89                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.11000                                             
REMARK   3    B22 (A**2) : -0.11000                                             
REMARK   3    B33 (A**2) : 0.16000                                              
REMARK   3    B12 (A**2) : -0.05000                                             
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): 0.294         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.209         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.143         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.871         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4187 ; 0.010 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  3760 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5686 ; 1.220 ; 1.946       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8723 ; 0.762 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   513 ; 7.064 ; 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):   635 ; 0.077 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4636 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   883 ; 0.003 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   589 ; 0.180 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4165 ; 0.229 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2776 ; 0.083 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    69 ; 0.133 ; 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 ; 0.142 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    47 ; 0.201 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     5 ; 0.232 ; 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):  2585 ; 2.575 ; 2.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4189 ; 4.084 ; 5.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1602 ; 3.077 ; 2.500       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1497 ; 4.711 ; 5.000       
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 : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   105        A   241                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.4510  84.0327   4.6368              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1011 T22:   0.1091                                     
REMARK   3      T33:   0.1583 T12:  -0.0141                                     
REMARK   3      T13:  -0.0341 T23:   0.1024                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1461 L22:   2.7331                                     
REMARK   3      L33:   2.5638 L12:  -0.1252                                     
REMARK   3      L13:   0.9115 L23:  -0.2272                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1006 S12:  -0.2092 S13:  -0.3960                       
REMARK   3      S21:   0.0627 S22:   0.0298 S23:   0.2027                       
REMARK   3      S31:   0.2755 S32:  -0.2148 S33:  -0.1305                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   105        B   241                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.1167 105.9483   9.1820              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0730 T22:   0.1615                                     
REMARK   3      T33:   0.1655 T12:   0.0442                                     
REMARK   3      T13:   0.0914 T23:   0.0533                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6695 L22:   2.6706                                     
REMARK   3      L33:   3.8296 L12:   0.4075                                     
REMARK   3      L13:   0.9553 L23:  -0.1667                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0179 S12:  -0.3133 S13:   0.2335                       
REMARK   3      S21:   0.3207 S22:  -0.0449 S23:   0.4227                       
REMARK   3      S31:  -0.2728 S32:  -0.2242 S33:   0.0270                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   105        D   241                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.0421 100.8884  -1.3595              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0501 T22:   0.1274                                     
REMARK   3      T33:   0.1136 T12:   0.0171                                     
REMARK   3      T13:   0.0550 T23:   0.0814                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9861 L22:   3.6954                                     
REMARK   3      L33:   2.9577 L12:   0.1324                                     
REMARK   3      L13:   0.9974 L23:  -0.8393                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0827 S12:   0.1931 S13:  -0.0274                       
REMARK   3      S21:  -0.0713 S22:  -0.0891 S23:  -0.4532                       
REMARK   3      S31:   0.1006 S32:   0.2988 S33:   0.0064                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   R     8        R    43                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.6636  83.1563  -9.5482              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2739 T22:   0.2909                                     
REMARK   3      T33:   0.3931 T12:  -0.1393                                     
REMARK   3      T13:  -0.1688 T23:   0.1414                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8149 L22:   9.5216                                     
REMARK   3      L33:  14.3511 L12:   1.5843                                     
REMARK   3      L13:   5.9660 L23:   4.6937                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2382 S12:  -0.0941 S13:  -0.6291                       
REMARK   3      S21:  -0.4535 S22:   0.1703 S23:   0.7924                       
REMARK   3      S31:   0.8782 S32:  -0.5263 S33:  -0.4085                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   S     6        S    42                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.9554 117.8873 -10.0897              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2506 T22:   0.3033                                     
REMARK   3      T33:   0.4320 T12:   0.0712                                     
REMARK   3      T13:  -0.1136 T23:   0.1626                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.2180 L22:  10.6111                                     
REMARK   3      L33:  11.1624 L12:  -3.9994                                     
REMARK   3      L13:   1.4052 L23:  -0.4374                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0251 S12:   0.3173 S13:   0.2861                       
REMARK   3      S21:  -0.6638 S22:   0.0771 S23:   1.4078                       
REMARK   3      S31:  -0.5072 S32:  -1.1028 S33:  -0.0520                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   T     8        T    42                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.3902  94.1774 -23.5163              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5681 T22:   0.5537                                     
REMARK   3      T33:   0.1712 T12:  -0.0691                                     
REMARK   3      T13:   0.1130 T23:  -0.0916                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.8575 L22:   6.2674                                     
REMARK   3      L33:  21.7778 L12:   4.1672                                     
REMARK   3      L13:  -1.6925 L23:  -4.1417                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4791 S12:   1.7580 S13:  -0.3046                       
REMARK   3      S21:  -1.6534 S22:   0.6037 S23:  -0.6857                       
REMARK   3      S31:   0.4978 S32:   0.0757 S33:  -0.1245                       
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 1XU2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-NOV-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB030770.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-JUN-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98040                            
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : SBC-3                              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28292                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 9.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.43                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.42500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
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: APRIL ALONE (1U5Z)                                   
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: WELL SOLUTION: 0.1M MES, 5% PEG 8000,    
REMARK 280  10% PEG 1000, PH 5.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE    
REMARK 280  292K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
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       30.39333            
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       60.78667            
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       45.59000            
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       75.98333            
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       15.19667            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE ASSYMMETRIC UNIT CONTAINS THE BIOLOGICALLY RELEVANT      
REMARK 300 ASSEMBLY OF A TRIMER OF APRIL BOUND TO 3 COPIES OF BCMA              
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10580 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 20560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, R, S, T                      
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     LYS A   104                                                      
REMARK 465     LYS B   104                                                      
REMARK 465     LYS D   104                                                      
REMARK 465     ALA R     5                                                      
REMARK 465     GLY R     6                                                      
REMARK 465     GLN R     7                                                      
REMARK 465     SER R    44                                                      
REMARK 465     VAL R    45                                                      
REMARK 465     THR R    46                                                      
REMARK 465     ASN R    47                                                      
REMARK 465     SER R    48                                                      
REMARK 465     VAL R    49                                                      
REMARK 465     LYS R    50                                                      
REMARK 465     GLY R    51                                                      
REMARK 465     ALA S     5                                                      
REMARK 465     ALA S    43                                                      
REMARK 465     SER S    44                                                      
REMARK 465     VAL S    45                                                      
REMARK 465     THR S    46                                                      
REMARK 465     ASN S    47                                                      
REMARK 465     SER S    48                                                      
REMARK 465     VAL S    49                                                      
REMARK 465     LYS S    50                                                      
REMARK 465     GLY S    51                                                      
REMARK 465     ALA T     5                                                      
REMARK 465     GLY T     6                                                      
REMARK 465     GLN T     7                                                      
REMARK 465     ALA T    43                                                      
REMARK 465     SER T    44                                                      
REMARK 465     VAL T    45                                                      
REMARK 465     THR T    46                                                      
REMARK 465     ASN T    47                                                      
REMARK 465     SER T    48                                                      
REMARK 465     VAL T    49                                                      
REMARK 465     LYS T    50                                                      
REMARK 465     GLY T    51                                                      
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     ARG S  39    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN T  38    CG   CD   OE1  NE2                                  
REMARK 470     ARG T  39    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN T  42    CG   OD1                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A     2     O    HOH A    38              2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ASN T  42   C     ASN T  42   O       0.240                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A 221       46.87    -72.17                                   
REMARK 500    ASP B 123       55.66   -114.89                                   
REMARK 500    ARG B 180      106.71   -170.12                                   
REMARK 500    PRO B 221       42.82    -74.03                                   
REMARK 500    ALA D 120      -83.92    -54.12                                   
REMARK 500    ASP D 123       60.86   -117.90                                   
REMARK 500    ARG D 137     -149.05   -119.47                                   
REMARK 500    PRO D 221       42.72    -72.56                                   
REMARK 500    ASN R  31     -121.45     48.75                                   
REMARK 500    ASN R  42      -68.23    -92.13                                   
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                              NI B 301  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 106   NE2                                                    
REMARK 620 2 HIS B 106   NE2  83.5                                              
REMARK 620 3 HIS D 106   NE2  75.7 108.1                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 301                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1XU1   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF APRIL BOUND TO TACI                             
REMARK 900 RELATED ID: 1U5X   RELATED DB: PDB                                   
REMARK 900 APRIL                                                                
REMARK 900 RELATED ID: 1U5Y   RELATED DB: PDB                                   
REMARK 900 APRIL                                                                
REMARK 900 RELATED ID: 1U5Z   RELATED DB: PDB                                   
REMARK 900 APRIL                                                                
REMARK 900 RELATED ID: 1XUT   RELATED DB: PDB                                   
DBREF  1XU2 A  104   241  UNP    Q9D777   TNF13_MOUSE    104    241             
DBREF  1XU2 B  104   241  UNP    Q9D777   TNF13_MOUSE    104    241             
DBREF  1XU2 D  104   241  UNP    Q9D777   TNF13_MOUSE    104    241             
DBREF  1XU2 R    5    51  UNP    Q02223   TNR17_HUMAN      5     51             
DBREF  1XU2 S    5    51  UNP    Q02223   TNR17_HUMAN      5     51             
DBREF  1XU2 T    5    51  UNP    Q02223   TNR17_HUMAN      5     51             
SEQRES   1 A  138  LYS LYS HIS SER VAL LEU HIS LEU VAL PRO VAL ASN ILE          
SEQRES   2 A  138  THR SER LYS ALA ASP SER ASP VAL THR GLU VAL MET TRP          
SEQRES   3 A  138  GLN PRO VAL LEU ARG ARG GLY ARG GLY LEU GLU ALA GLN          
SEQRES   4 A  138  GLY ASP ILE VAL ARG VAL TRP ASP THR GLY ILE TYR LEU          
SEQRES   5 A  138  LEU TYR SER GLN VAL LEU PHE HIS ASP VAL THR PHE THR          
SEQRES   6 A  138  MET GLY GLN VAL VAL SER ARG GLU GLY GLN GLY ARG ARG          
SEQRES   7 A  138  GLU THR LEU PHE ARG CYS ILE ARG SER MET PRO SER ASP          
SEQRES   8 A  138  PRO ASP ARG ALA TYR ASN SER CYS TYR SER ALA GLY VAL          
SEQRES   9 A  138  PHE HIS LEU HIS GLN GLY ASP ILE ILE THR VAL LYS ILE          
SEQRES  10 A  138  PRO ARG ALA ASN ALA LYS LEU SER LEU SER PRO HIS GLY          
SEQRES  11 A  138  THR PHE LEU GLY PHE VAL LYS LEU                              
SEQRES   1 B  138  LYS LYS HIS SER VAL LEU HIS LEU VAL PRO VAL ASN ILE          
SEQRES   2 B  138  THR SER LYS ALA ASP SER ASP VAL THR GLU VAL MET TRP          
SEQRES   3 B  138  GLN PRO VAL LEU ARG ARG GLY ARG GLY LEU GLU ALA GLN          
SEQRES   4 B  138  GLY ASP ILE VAL ARG VAL TRP ASP THR GLY ILE TYR LEU          
SEQRES   5 B  138  LEU TYR SER GLN VAL LEU PHE HIS ASP VAL THR PHE THR          
SEQRES   6 B  138  MET GLY GLN VAL VAL SER ARG GLU GLY GLN GLY ARG ARG          
SEQRES   7 B  138  GLU THR LEU PHE ARG CYS ILE ARG SER MET PRO SER ASP          
SEQRES   8 B  138  PRO ASP ARG ALA TYR ASN SER CYS TYR SER ALA GLY VAL          
SEQRES   9 B  138  PHE HIS LEU HIS GLN GLY ASP ILE ILE THR VAL LYS ILE          
SEQRES  10 B  138  PRO ARG ALA ASN ALA LYS LEU SER LEU SER PRO HIS GLY          
SEQRES  11 B  138  THR PHE LEU GLY PHE VAL LYS LEU                              
SEQRES   1 D  138  LYS LYS HIS SER VAL LEU HIS LEU VAL PRO VAL ASN ILE          
SEQRES   2 D  138  THR SER LYS ALA ASP SER ASP VAL THR GLU VAL MET TRP          
SEQRES   3 D  138  GLN PRO VAL LEU ARG ARG GLY ARG GLY LEU GLU ALA GLN          
SEQRES   4 D  138  GLY ASP ILE VAL ARG VAL TRP ASP THR GLY ILE TYR LEU          
SEQRES   5 D  138  LEU TYR SER GLN VAL LEU PHE HIS ASP VAL THR PHE THR          
SEQRES   6 D  138  MET GLY GLN VAL VAL SER ARG GLU GLY GLN GLY ARG ARG          
SEQRES   7 D  138  GLU THR LEU PHE ARG CYS ILE ARG SER MET PRO SER ASP          
SEQRES   8 D  138  PRO ASP ARG ALA TYR ASN SER CYS TYR SER ALA GLY VAL          
SEQRES   9 D  138  PHE HIS LEU HIS GLN GLY ASP ILE ILE THR VAL LYS ILE          
SEQRES  10 D  138  PRO ARG ALA ASN ALA LYS LEU SER LEU SER PRO HIS GLY          
SEQRES  11 D  138  THR PHE LEU GLY PHE VAL LYS LEU                              
SEQRES   1 R   47  ALA GLY GLN CYS SER GLN ASN GLU TYR PHE ASP SER LEU          
SEQRES   2 R   47  LEU HIS ALA CYS ILE PRO CYS GLN LEU ARG CYS SER SER          
SEQRES   3 R   47  ASN THR PRO PRO LEU THR CYS GLN ARG TYR CYS ASN ALA          
SEQRES   4 R   47  SER VAL THR ASN SER VAL LYS GLY                              
SEQRES   1 S   47  ALA GLY GLN CYS SER GLN ASN GLU TYR PHE ASP SER LEU          
SEQRES   2 S   47  LEU HIS ALA CYS ILE PRO CYS GLN LEU ARG CYS SER SER          
SEQRES   3 S   47  ASN THR PRO PRO LEU THR CYS GLN ARG TYR CYS ASN ALA          
SEQRES   4 S   47  SER VAL THR ASN SER VAL LYS GLY                              
SEQRES   1 T   47  ALA GLY GLN CYS SER GLN ASN GLU TYR PHE ASP SER LEU          
SEQRES   2 T   47  LEU HIS ALA CYS ILE PRO CYS GLN LEU ARG CYS SER SER          
SEQRES   3 T   47  ASN THR PRO PRO LEU THR CYS GLN ARG TYR CYS ASN ALA          
SEQRES   4 T   47  SER VAL THR ASN SER VAL LYS GLY                              
HET     NI  B 301       1                                                       
HETNAM      NI NICKEL (II) ION                                                  
FORMUL   7   NI    NI 2+                                                        
FORMUL   8  HOH   *36(H2 O)                                                     
HELIX    1   1 ASP A  194  ARG A  197  5                                   4    
HELIX    2   2 GLN R   25  ARG R   27  5                                   3    
HELIX    3   3 PRO R   34  THR R   36  5                                   3    
HELIX    4   4 CYS R   37  ALA R   43  1                                   7    
HELIX    5   5 GLN S   25  CYS S   28  5                                   4    
HELIX    6   6 CYS S   37  ASN S   42  1                                   6    
HELIX    7   7 GLN T   25  CYS T   28  5                                   4    
SHEET    1   A 5 LEU A 139  GLN A 142  0                                        
SHEET    2   A 5 ILE A 145  VAL A 148 -1  O  ARG A 147   N  GLU A 140           
SHEET    3   A 5 ILE A 215  ILE A 220 -1  O  ILE A 216   N  VAL A 146           
SHEET    4   A 5 THR A 168  GLU A 176 -1  N  GLU A 176   O  ILE A 215           
SHEET    5   A 5 ARG A 181  SER A 190 -1  O  PHE A 185   N  VAL A 173           
SHEET    1   B 8 LEU A 139  GLN A 142  0                                        
SHEET    2   B 8 ILE A 145  VAL A 148 -1  O  ARG A 147   N  GLU A 140           
SHEET    3   B 8 ILE A 215  ILE A 220 -1  O  ILE A 216   N  VAL A 146           
SHEET    4   B 8 THR A 125  ARG A 135 -1  N  THR A 125   O  ILE A 220           
SHEET    5   B 8 VAL A 108  THR A 117 -1  N  THR A 117   O  GLU A 126           
SHEET    6   B 8 PHE A 235  LYS A 240 -1  O  LEU A 236   N  LEU A 111           
SHEET    7   B 8 GLY A 152  HIS A 163 -1  N  LEU A 155   O  VAL A 239           
SHEET    8   B 8 TYR A 199  LEU A 210 -1  O  GLY A 206   N  LEU A 156           
SHEET    1   C 5 LEU B 139  GLN B 142  0                                        
SHEET    2   C 5 ILE B 145  VAL B 148 -1  O  ARG B 147   N  GLU B 140           
SHEET    3   C 5 ILE B 215  ILE B 220 -1  O  ILE B 216   N  VAL B 146           
SHEET    4   C 5 THR B 168  GLU B 176 -1  N  GLU B 176   O  ILE B 215           
SHEET    5   C 5 ARG B 181  SER B 190 -1  O  ARG B 189   N  MET B 169           
SHEET    1   D 8 LEU B 139  GLN B 142  0                                        
SHEET    2   D 8 ILE B 145  VAL B 148 -1  O  ARG B 147   N  GLU B 140           
SHEET    3   D 8 ILE B 215  ILE B 220 -1  O  ILE B 216   N  VAL B 146           
SHEET    4   D 8 THR B 125  ARG B 135 -1  N  THR B 125   O  ILE B 220           
SHEET    5   D 8 VAL B 108  THR B 117 -1  N  ASN B 115   O  MET B 128           
SHEET    6   D 8 PHE B 235  LYS B 240 -1  O  LEU B 236   N  LEU B 111           
SHEET    7   D 8 GLY B 152  PHE B 162 -1  N  LEU B 155   O  VAL B 239           
SHEET    8   D 8 ASN B 200  LEU B 210 -1  O  GLY B 206   N  LEU B 156           
SHEET    1   E 5 LEU D 139  GLN D 142  0                                        
SHEET    2   E 5 ILE D 145  VAL D 148 -1  O  ARG D 147   N  GLU D 140           
SHEET    3   E 5 ILE D 215  ILE D 220 -1  O  ILE D 216   N  VAL D 146           
SHEET    4   E 5 THR D 168  GLU D 176 -1  N  VAL D 172   O  LYS D 219           
SHEET    5   E 5 ARG D 181  SER D 190 -1  O  LEU D 184   N  VAL D 173           
SHEET    1   F 8 LEU D 139  GLN D 142  0                                        
SHEET    2   F 8 ILE D 145  VAL D 148 -1  O  ARG D 147   N  GLU D 140           
SHEET    3   F 8 ILE D 215  ILE D 220 -1  O  ILE D 216   N  VAL D 146           
SHEET    4   F 8 THR D 125  ARG D 135 -1  N  THR D 125   O  ILE D 220           
SHEET    5   F 8 VAL D 108  THR D 117 -1  N  HIS D 110   O  VAL D 132           
SHEET    6   F 8 PHE D 235  LYS D 240 -1  O  LEU D 236   N  LEU D 111           
SHEET    7   F 8 GLY D 152  HIS D 163 -1  N  LEU D 155   O  VAL D 239           
SHEET    8   F 8 TYR D 199  LEU D 210 -1  O  GLY D 206   N  LEU D 156           
SHEET    1   G 2 GLU R  12  ASP R  15  0                                        
SHEET    2   G 2 ALA R  20  PRO R  23 -1  O  ALA R  20   N  ASP R  15           
SHEET    1   H 2 GLU S  12  ASP S  15  0                                        
SHEET    2   H 2 ALA S  20  PRO S  23 -1  O  ALA S  20   N  ASP S  15           
SHEET    1   I 2 GLU T  12  ASP T  15  0                                        
SHEET    2   I 2 ALA T  20  PRO T  23 -1  O  ILE T  22   N  TYR T  13           
SSBOND   1 CYS A  187    CYS A  202                          1555   1555  2.03  
SSBOND   2 CYS B  187    CYS B  202                          1555   1555  2.04  
SSBOND   3 CYS D  187    CYS D  202                          1555   1555  2.05  
SSBOND   4 CYS R    8    CYS R   21                          1555   1555  2.05  
SSBOND   5 CYS R   24    CYS R   37                          1555   1555  2.10  
SSBOND   6 CYS R   28    CYS R   41                          1555   1555  2.06  
SSBOND   7 CYS S    8    CYS S   21                          1555   1555  2.08  
SSBOND   8 CYS S   24    CYS S   37                          1555   1555  2.07  
SSBOND   9 CYS S   28    CYS S   41                          1555   1555  2.05  
SSBOND  10 CYS T    8    CYS T   21                          1555   1555  2.05  
SSBOND  11 CYS T   24    CYS T   37                          1555   1555  2.07  
SSBOND  12 CYS T   28    CYS T   41                          1555   1555  2.06  
LINK        NI    NI B 301                 NE2 HIS A 106     1555   1555  2.56  
LINK        NI    NI B 301                 NE2 HIS B 106     1555   1555  2.18  
LINK        NI    NI B 301                 NE2 HIS D 106     1555   1555  2.34  
SITE     1 AC1  3 HIS A 106  HIS B 106  HIS D 106                               
CRYST1  114.294  114.294   91.180  90.00  90.00 120.00 P 61         18          
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      0.008749  0.005051  0.000000        0.00000                         
SCALE2      0.000000  0.010103  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010967        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system