GenomeNet

Database: PDB
Entry: 1OQD
LinkDB: 1OQD
Original site: 1OQD 
HEADER    IMMUNE RESPONSE                         07-MAR-03   1OQD              
TITLE     CRYSTAL STRUCTURE OF STALL-1 AND BCMA                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUMOR NECROSIS FACTOR LIGAND SUPERFAMILY MEMBER            
COMPND   3 13B, SOLUBLE FORM;                                                   
COMPND   4 CHAIN: A, B, C, D, E, F, G, H, I, J;                                 
COMPND   5 FRAGMENT: EXTRACELLULAR 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: TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY                 
COMPND  13 MEMBER 17;                                                           
COMPND  14 CHAIN: K, L, M, N, O, P, Q, R;                                       
COMPND  15 FRAGMENT: EXTRACELLULAR DOMAIN;                                      
COMPND  16 SYNONYM: B-CELL MATURATION PROTEIN;                                  
COMPND  17 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    LIGAND RECEPTOR COMPLEX, IMMUNE RESPONSE                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.ZHANG                                                               
REVDAT   2   24-FEB-09 1OQD    1       VERSN                                    
REVDAT   1   13-MAY-03 1OQD    0                                                
JRNL        AUTH   Y.LIU,X.HONG,J.KAPPLER,L.JIANG,R.ZHANG,L.XU,                 
JRNL        AUTH 2 C.H.PAN,W.E.MARTIN,R.C.MURPHY,H.B.SHU,S.DAI,G.ZHANG          
JRNL        TITL   LIGAND-RECEPTOR BINDING REVEALED BY THE TNF FAMILY           
JRNL        TITL 2 MEMBER TALL-1.                                               
JRNL        REF    NATURE                        V. 423    49 2003              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   12721620                                                     
JRNL        DOI    10.1038/NATURE01543                                          
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.87                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 75.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 78303                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.240                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1554                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.76                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 42.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 7062                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3560                       
REMARK   3   BIN FREE R VALUE                    : 0.3560                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 2.20                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 156                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.029                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13704                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 50.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.97000                                              
REMARK   3    B22 (A**2) : 2.97000                                              
REMARK   3    B33 (A**2) : -5.93000                                             
REMARK   3    B12 (A**2) : 8.35000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.38                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.59                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.41                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.62                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.91                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.32                                                 
REMARK   3   BSOL        : 31.15                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : CONSTR                                                  
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  3  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1OQD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAR-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB018561.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAR-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 1056776                            
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
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     (%) : 87.8                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.13600                            
REMARK 200  R SYM                      (I) : 0.11800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 46.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.60000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 58.000                             
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.78                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.21                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: DIOXANE, PH 9.0, VAPOR DIFFUSION,        
REMARK 280  HANGING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z                                              
REMARK 290      10555   -Y,-X,-Z+1/2                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/2                                            
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        0.00000            
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        0.00000            
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      106.23850            
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      106.23850            
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      106.23850            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      106.23850            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      106.23850            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      106.23850            
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 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: 108-MERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I,            
REMARK 350                    AND CHAINS: J, K, L, M, N, O, P, Q, R             
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   BIOMT1   2  0.500000  0.866025  0.000000     -116.42700            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000      201.65748            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000     -106.23850            
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000     -106.23850            
REMARK 350   BIOMT1   4  0.500000 -0.866025  0.000000      116.42700            
REMARK 350   BIOMT2   4 -0.866025 -0.500000  0.000000      201.65748            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000     -106.23850            
REMARK 350   BIOMT1   5 -0.500000  0.866025  0.000000     -116.42700            
REMARK 350   BIOMT2   5 -0.866025 -0.500000  0.000000      201.65748            
REMARK 350   BIOMT3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   6 -0.500000 -0.866025  0.000000      116.42700            
REMARK 350   BIOMT2   6  0.866025 -0.500000  0.000000      201.65748            
REMARK 350   BIOMT3   6  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     SER N    22                                                      
REMARK 465     SER N    23                                                      
REMARK 465     ASN N    24                                                      
REMARK 465     THR N    25                                                      
REMARK 465     PRO N    26                                                      
REMARK 465     PRO N    27                                                      
REMARK 465     LEU N    28                                                      
REMARK 465     THR N    29                                                      
REMARK 465     CYS N    30                                                      
REMARK 465     GLN N    31                                                      
REMARK 465     ARG N    32                                                      
REMARK 465     TYR N    33                                                      
REMARK 465     CYS N    34                                                      
REMARK 465     ASN N    35                                                      
REMARK 465     ALA N    36                                                      
REMARK 465     SER N    37                                                      
REMARK 465     VAL N    38                                                      
REMARK 465     THR N    39                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS R  34   C     ASN R  35   N       0.159                       
REMARK 500    ASN R  35   C     ALA R  36   N      -0.386                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS A  91   CA  -  CB  -  SG  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    CYS B  91   CA  -  CB  -  SG  ANGL. DEV. =   9.9 DEGREES          
REMARK 500    CYS C  91   CA  -  CB  -  SG  ANGL. DEV. =   9.7 DEGREES          
REMARK 500    CYS D  91   CA  -  CB  -  SG  ANGL. DEV. =  10.4 DEGREES          
REMARK 500    CYS E  91   CA  -  CB  -  SG  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    CYS F  91   CA  -  CB  -  SG  ANGL. DEV. =   9.9 DEGREES          
REMARK 500    CYS G  91   CA  -  CB  -  SG  ANGL. DEV. =  10.3 DEGREES          
REMARK 500    CYS H  91   CA  -  CB  -  SG  ANGL. DEV. =  10.3 DEGREES          
REMARK 500    CYS I  91   CA  -  CB  -  SG  ANGL. DEV. =  10.3 DEGREES          
REMARK 500    CYS J  91   CA  -  CB  -  SG  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    ASN R  35   O   -  C   -  N   ANGL. DEV. = -10.3 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    LYS A  19      135.59   -175.28                                   
REMARK 500    THR A  64       47.52    -72.87                                   
REMARK 500    TYR A  65      -35.28     49.75                                   
REMARK 500    THR A  98      -97.49    -68.79                                   
REMARK 500    ASN A 101       77.20   -159.60                                   
REMARK 500    PRO A 123       47.41    -73.39                                   
REMARK 500    LYS B  19      135.26   -173.77                                   
REMARK 500    THR B  64       48.39    -73.54                                   
REMARK 500    TYR B  65      -34.10     49.09                                   
REMARK 500    THR B  98      -97.06    -69.17                                   
REMARK 500    ASN B 101       76.77   -160.19                                   
REMARK 500    PRO B 123       46.60    -73.93                                   
REMARK 500    LYS C  19      135.93   -173.94                                   
REMARK 500    GLU C  41       52.65     39.84                                   
REMARK 500    THR C  64       48.21    -73.64                                   
REMARK 500    TYR C  65      -34.71     49.38                                   
REMARK 500    THR C  98      -97.08    -69.25                                   
REMARK 500    ASN C 101       76.07   -159.97                                   
REMARK 500    PRO C 123       48.55    -73.97                                   
REMARK 500    LYS D  19      135.79   -173.48                                   
REMARK 500    THR D  64       47.86    -72.25                                   
REMARK 500    TYR D  65      -34.12     49.35                                   
REMARK 500    THR D  98      -97.11    -68.19                                   
REMARK 500    ASN D 101       76.50   -159.30                                   
REMARK 500    PRO D 123       48.35    -73.86                                   
REMARK 500    LYS E  19      135.19   -173.82                                   
REMARK 500    THR E  64       48.09    -73.51                                   
REMARK 500    TYR E  65      -34.60     49.36                                   
REMARK 500    THR E  98      -97.09    -68.56                                   
REMARK 500    ASN E 101       76.40   -160.73                                   
REMARK 500    LYS F  19      135.94   -174.00                                   
REMARK 500    THR F  64       47.21    -72.62                                   
REMARK 500    TYR F  65      -34.46     50.18                                   
REMARK 500    THR F  98      -96.72    -69.53                                   
REMARK 500    ASN F 101       76.96   -161.22                                   
REMARK 500    PRO F 123       46.15    -72.72                                   
REMARK 500    LYS G  19      135.02   -173.81                                   
REMARK 500    THR G  64       48.08    -72.27                                   
REMARK 500    TYR G  65      -34.19     49.17                                   
REMARK 500    THR G  98      -97.36    -68.66                                   
REMARK 500    ASN G 101       76.25   -160.53                                   
REMARK 500    PRO G 123       48.65    -72.79                                   
REMARK 500    LYS H  19      134.51   -173.65                                   
REMARK 500    THR H  64       48.68    -72.95                                   
REMARK 500    TYR H  65      -33.67     48.81                                   
REMARK 500    THR H  98      -96.79    -68.89                                   
REMARK 500    ASN H 101       76.87   -160.05                                   
REMARK 500    LYS I  19      136.05   -173.61                                   
REMARK 500    GLU I  41       52.09     39.98                                   
REMARK 500    THR I  64       48.19    -72.61                                   
REMARK 500    TYR I  65      -35.22     49.67                                   
REMARK 500    THR I  98      -96.64    -69.68                                   
REMARK 500    ASN I 101       76.84   -159.77                                   
REMARK 500    PRO I 123       48.02    -73.76                                   
REMARK 500    GLU I 125      -71.12    -37.74                                   
REMARK 500    LYS J  19      135.78   -174.57                                   
REMARK 500    THR J  64       47.94    -72.79                                   
REMARK 500    TYR J  65      -33.84     49.48                                   
REMARK 500    THR J  98      -96.83    -68.39                                   
REMARK 500    ASN J 101       76.07   -159.78                                   
REMARK 500    PRO J 123       47.64    -73.70                                   
REMARK 500    SER K   2     -120.77   -158.55                                   
REMARK 500    GLU K   5     -153.65   -109.98                                   
REMARK 500    SER K  22       -9.07    -41.32                                   
REMARK 500    SER K  23      -30.35    159.91                                   
REMARK 500    ASN K  24       49.65    -83.82                                   
REMARK 500    THR K  25       83.78     19.80                                   
REMARK 500    PRO K  26      177.78    -49.16                                   
REMARK 500    LEU K  28      -75.62    -49.67                                   
REMARK 500    THR K  29       19.78    -59.31                                   
REMARK 500    CYS K  30      -44.22   -136.03                                   
REMARK 500    GLN K  31      -46.68    -28.10                                   
REMARK 500    ASN K  35      -24.99    161.43                                   
REMARK 500    SER L   2     -121.29   -158.48                                   
REMARK 500    GLU L   5     -153.61   -110.46                                   
REMARK 500    CYS L  17      -37.00    -39.59                                   
REMARK 500    SER L  22      -39.60    -30.73                                   
REMARK 500    SER L  23       10.78    163.73                                   
REMARK 500    ASN L  24       58.09   -113.23                                   
REMARK 500    THR L  25       70.42     13.98                                   
REMARK 500    PRO L  26      150.88    -40.16                                   
REMARK 500    PRO L  27     -133.58    -57.47                                   
REMARK 500    THR L  29       22.27     48.71                                   
REMARK 500    CYS L  30      -49.88   -143.70                                   
REMARK 500    ALA L  36      -48.73   -146.05                                   
REMARK 500    SER L  37       32.69    -81.71                                   
REMARK 500    VAL L  38      -40.87   -146.31                                   
REMARK 500    SER M   2     -121.83   -157.73                                   
REMARK 500    GLU M   5     -153.92   -110.32                                   
REMARK 500    CYS M  17      -36.70    -39.99                                   
REMARK 500    ASN M  24      -21.21    -38.91                                   
REMARK 500    THR M  25       56.72   -115.65                                   
REMARK 500    LEU M  28     -163.92    -48.75                                   
REMARK 500    THR M  29       76.15    -17.92                                   
REMARK 500    CYS M  30      -24.65    178.00                                   
REMARK 500    CYS M  34       -9.46    -54.70                                   
REMARK 500    GLN N   3       97.41     58.95                                   
REMARK 500    ASN N   4      -12.95     45.98                                   
REMARK 500    GLU N   5     -167.11    -50.06                                   
REMARK 500    ALA N  13     -166.45   -118.38                                   
REMARK 500    CYS N  17      -21.29    -16.83                                   
REMARK 500    ARG N  20       -6.44    -47.72                                   
REMARK 500    SER O   2     -121.42   -157.84                                   
REMARK 500    GLU O   5     -154.17   -110.40                                   
REMARK 500    CYS O  17      -37.15    -39.10                                   
REMARK 500    SER O  22       76.22    -69.76                                   
REMARK 500    SER O  23       60.63     66.12                                   
REMARK 500    ASN O  24       99.28    178.47                                   
REMARK 500    THR O  25       71.69      0.35                                   
REMARK 500    LEU O  28     -174.55    -58.95                                   
REMARK 500    THR O  29       24.78     35.50                                   
REMARK 500    CYS O  30      -29.71   -152.66                                   
REMARK 500    SER P   2     -121.54   -158.32                                   
REMARK 500    GLU P   5     -154.02   -111.03                                   
REMARK 500    SER P  23      -14.04     54.35                                   
REMARK 500    THR P  25       92.35    -44.55                                   
REMARK 500    PRO P  27     -161.75    -73.80                                   
REMARK 500    LEU P  28     -144.81    -78.76                                   
REMARK 500    THR P  29       36.00     17.33                                   
REMARK 500    CYS P  30      -16.29   -155.62                                   
REMARK 500    ARG P  32      -18.93    -43.72                                   
REMARK 500    TYR P  33      -69.15   -104.48                                   
REMARK 500    SER P  37      -18.83    -44.72                                   
REMARK 500    VAL P  38     -111.84    -81.88                                   
REMARK 500    SER Q   2     -122.03   -157.87                                   
REMARK 500    GLU Q   5     -154.19   -110.06                                   
REMARK 500    CYS Q  17      -37.33    -39.15                                   
REMARK 500    CYS Q  21      -20.40    -36.55                                   
REMARK 500    SER Q  22      -92.24    -45.60                                   
REMARK 500    ASN Q  24      163.88     82.50                                   
REMARK 500    THR Q  25      109.46    -14.89                                   
REMARK 500    PRO Q  26       93.05    -58.12                                   
REMARK 500    CYS Q  30      -32.18   -140.31                                   
REMARK 500    GLN Q  31      -77.49    -33.19                                   
REMARK 500    VAL Q  38       54.02   -155.44                                   
REMARK 500    SER R   2     -122.00   -158.29                                   
REMARK 500    GLU R   5     -154.40   -110.07                                   
REMARK 500    CYS R  17      -37.20    -38.59                                   
REMARK 500    SER R  22       50.51    -35.96                                   
REMARK 500    PRO R  27     -156.42   -113.50                                   
REMARK 500    THR R  29       44.74     23.14                                   
REMARK 500    CYS R  30      -23.43   -146.87                                   
REMARK 500    ASN R  35      -81.34    -69.95                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1JH5   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH BCMA                                 
REMARK 900 RELATED ID: 1OQE   RELATED DB: PDB                                   
DBREF  1OQD A    1   144  UNP    Q9Y275   TN13B_HUMAN    142    285             
DBREF  1OQD B    1   144  UNP    Q9Y275   TN13B_HUMAN    142    285             
DBREF  1OQD C    1   144  UNP    Q9Y275   TN13B_HUMAN    142    285             
DBREF  1OQD D    1   144  UNP    Q9Y275   TN13B_HUMAN    142    285             
DBREF  1OQD E    1   144  UNP    Q9Y275   TN13B_HUMAN    142    285             
DBREF  1OQD F    1   144  UNP    Q9Y275   TN13B_HUMAN    142    285             
DBREF  1OQD G    1   144  UNP    Q9Y275   TN13B_HUMAN    142    285             
DBREF  1OQD H    1   144  UNP    Q9Y275   TN13B_HUMAN    142    285             
DBREF  1OQD I    1   144  UNP    Q9Y275   TN13B_HUMAN    142    285             
DBREF  1OQD J    1   144  UNP    Q9Y275   TN13B_HUMAN    142    285             
DBREF  1OQD K    1    39  UNP    Q02223   TNR17_HUMAN      8     46             
DBREF  1OQD L    1    39  UNP    Q02223   TNR17_HUMAN      8     46             
DBREF  1OQD M    1    39  UNP    Q02223   TNR17_HUMAN      8     46             
DBREF  1OQD N    1    39  UNP    Q02223   TNR17_HUMAN      8     46             
DBREF  1OQD O    1    39  UNP    Q02223   TNR17_HUMAN      8     46             
DBREF  1OQD P    1    39  UNP    Q02223   TNR17_HUMAN      8     46             
DBREF  1OQD Q    1    39  UNP    Q02223   TNR17_HUMAN      8     46             
DBREF  1OQD R    1    39  UNP    Q02223   TNR17_HUMAN      8     46             
SEQRES   1 A  144  VAL THR GLN ASP CYS LEU GLN LEU ILE ALA ASP SER GLU          
SEQRES   2 A  144  THR PRO THR ILE GLN LYS GLY SER TYR THR PHE VAL PRO          
SEQRES   3 A  144  TRP LEU LEU SER PHE LYS ARG GLY SER ALA LEU GLU GLU          
SEQRES   4 A  144  LYS GLU ASN LYS ILE LEU VAL LYS GLU THR GLY TYR PHE          
SEQRES   5 A  144  PHE ILE TYR GLY GLN VAL LEU TYR THR ASP LYS THR TYR          
SEQRES   6 A  144  ALA MET GLY HIS LEU ILE GLN ARG LYS LYS VAL HIS VAL          
SEQRES   7 A  144  PHE GLY ASP GLU LEU SER LEU VAL THR LEU PHE ARG CYS          
SEQRES   8 A  144  ILE GLN ASN MET PRO GLU THR LEU PRO ASN ASN SER CYS          
SEQRES   9 A  144  TYR SER ALA GLY ILE ALA LYS LEU GLU GLU GLY ASP GLU          
SEQRES  10 A  144  LEU GLN LEU ALA ILE PRO ARG GLU ASN ALA GLN ILE SER          
SEQRES  11 A  144  LEU ASP GLY ASP VAL THR PHE PHE GLY ALA LEU LYS LEU          
SEQRES  12 A  144  LEU                                                          
SEQRES   1 B  144  VAL THR GLN ASP CYS LEU GLN LEU ILE ALA ASP SER GLU          
SEQRES   2 B  144  THR PRO THR ILE GLN LYS GLY SER TYR THR PHE VAL PRO          
SEQRES   3 B  144  TRP LEU LEU SER PHE LYS ARG GLY SER ALA LEU GLU GLU          
SEQRES   4 B  144  LYS GLU ASN LYS ILE LEU VAL LYS GLU THR GLY TYR PHE          
SEQRES   5 B  144  PHE ILE TYR GLY GLN VAL LEU TYR THR ASP LYS THR TYR          
SEQRES   6 B  144  ALA MET GLY HIS LEU ILE GLN ARG LYS LYS VAL HIS VAL          
SEQRES   7 B  144  PHE GLY ASP GLU LEU SER LEU VAL THR LEU PHE ARG CYS          
SEQRES   8 B  144  ILE GLN ASN MET PRO GLU THR LEU PRO ASN ASN SER CYS          
SEQRES   9 B  144  TYR SER ALA GLY ILE ALA LYS LEU GLU GLU GLY ASP GLU          
SEQRES  10 B  144  LEU GLN LEU ALA ILE PRO ARG GLU ASN ALA GLN ILE SER          
SEQRES  11 B  144  LEU ASP GLY ASP VAL THR PHE PHE GLY ALA LEU LYS LEU          
SEQRES  12 B  144  LEU                                                          
SEQRES   1 C  144  VAL THR GLN ASP CYS LEU GLN LEU ILE ALA ASP SER GLU          
SEQRES   2 C  144  THR PRO THR ILE GLN LYS GLY SER TYR THR PHE VAL PRO          
SEQRES   3 C  144  TRP LEU LEU SER PHE LYS ARG GLY SER ALA LEU GLU GLU          
SEQRES   4 C  144  LYS GLU ASN LYS ILE LEU VAL LYS GLU THR GLY TYR PHE          
SEQRES   5 C  144  PHE ILE TYR GLY GLN VAL LEU TYR THR ASP LYS THR TYR          
SEQRES   6 C  144  ALA MET GLY HIS LEU ILE GLN ARG LYS LYS VAL HIS VAL          
SEQRES   7 C  144  PHE GLY ASP GLU LEU SER LEU VAL THR LEU PHE ARG CYS          
SEQRES   8 C  144  ILE GLN ASN MET PRO GLU THR LEU PRO ASN ASN SER CYS          
SEQRES   9 C  144  TYR SER ALA GLY ILE ALA LYS LEU GLU GLU GLY ASP GLU          
SEQRES  10 C  144  LEU GLN LEU ALA ILE PRO ARG GLU ASN ALA GLN ILE SER          
SEQRES  11 C  144  LEU ASP GLY ASP VAL THR PHE PHE GLY ALA LEU LYS LEU          
SEQRES  12 C  144  LEU                                                          
SEQRES   1 D  144  VAL THR GLN ASP CYS LEU GLN LEU ILE ALA ASP SER GLU          
SEQRES   2 D  144  THR PRO THR ILE GLN LYS GLY SER TYR THR PHE VAL PRO          
SEQRES   3 D  144  TRP LEU LEU SER PHE LYS ARG GLY SER ALA LEU GLU GLU          
SEQRES   4 D  144  LYS GLU ASN LYS ILE LEU VAL LYS GLU THR GLY TYR PHE          
SEQRES   5 D  144  PHE ILE TYR GLY GLN VAL LEU TYR THR ASP LYS THR TYR          
SEQRES   6 D  144  ALA MET GLY HIS LEU ILE GLN ARG LYS LYS VAL HIS VAL          
SEQRES   7 D  144  PHE GLY ASP GLU LEU SER LEU VAL THR LEU PHE ARG CYS          
SEQRES   8 D  144  ILE GLN ASN MET PRO GLU THR LEU PRO ASN ASN SER CYS          
SEQRES   9 D  144  TYR SER ALA GLY ILE ALA LYS LEU GLU GLU GLY ASP GLU          
SEQRES  10 D  144  LEU GLN LEU ALA ILE PRO ARG GLU ASN ALA GLN ILE SER          
SEQRES  11 D  144  LEU ASP GLY ASP VAL THR PHE PHE GLY ALA LEU LYS LEU          
SEQRES  12 D  144  LEU                                                          
SEQRES   1 E  144  VAL THR GLN ASP CYS LEU GLN LEU ILE ALA ASP SER GLU          
SEQRES   2 E  144  THR PRO THR ILE GLN LYS GLY SER TYR THR PHE VAL PRO          
SEQRES   3 E  144  TRP LEU LEU SER PHE LYS ARG GLY SER ALA LEU GLU GLU          
SEQRES   4 E  144  LYS GLU ASN LYS ILE LEU VAL LYS GLU THR GLY TYR PHE          
SEQRES   5 E  144  PHE ILE TYR GLY GLN VAL LEU TYR THR ASP LYS THR TYR          
SEQRES   6 E  144  ALA MET GLY HIS LEU ILE GLN ARG LYS LYS VAL HIS VAL          
SEQRES   7 E  144  PHE GLY ASP GLU LEU SER LEU VAL THR LEU PHE ARG CYS          
SEQRES   8 E  144  ILE GLN ASN MET PRO GLU THR LEU PRO ASN ASN SER CYS          
SEQRES   9 E  144  TYR SER ALA GLY ILE ALA LYS LEU GLU GLU GLY ASP GLU          
SEQRES  10 E  144  LEU GLN LEU ALA ILE PRO ARG GLU ASN ALA GLN ILE SER          
SEQRES  11 E  144  LEU ASP GLY ASP VAL THR PHE PHE GLY ALA LEU LYS LEU          
SEQRES  12 E  144  LEU                                                          
SEQRES   1 F  144  VAL THR GLN ASP CYS LEU GLN LEU ILE ALA ASP SER GLU          
SEQRES   2 F  144  THR PRO THR ILE GLN LYS GLY SER TYR THR PHE VAL PRO          
SEQRES   3 F  144  TRP LEU LEU SER PHE LYS ARG GLY SER ALA LEU GLU GLU          
SEQRES   4 F  144  LYS GLU ASN LYS ILE LEU VAL LYS GLU THR GLY TYR PHE          
SEQRES   5 F  144  PHE ILE TYR GLY GLN VAL LEU TYR THR ASP LYS THR TYR          
SEQRES   6 F  144  ALA MET GLY HIS LEU ILE GLN ARG LYS LYS VAL HIS VAL          
SEQRES   7 F  144  PHE GLY ASP GLU LEU SER LEU VAL THR LEU PHE ARG CYS          
SEQRES   8 F  144  ILE GLN ASN MET PRO GLU THR LEU PRO ASN ASN SER CYS          
SEQRES   9 F  144  TYR SER ALA GLY ILE ALA LYS LEU GLU GLU GLY ASP GLU          
SEQRES  10 F  144  LEU GLN LEU ALA ILE PRO ARG GLU ASN ALA GLN ILE SER          
SEQRES  11 F  144  LEU ASP GLY ASP VAL THR PHE PHE GLY ALA LEU LYS LEU          
SEQRES  12 F  144  LEU                                                          
SEQRES   1 G  144  VAL THR GLN ASP CYS LEU GLN LEU ILE ALA ASP SER GLU          
SEQRES   2 G  144  THR PRO THR ILE GLN LYS GLY SER TYR THR PHE VAL PRO          
SEQRES   3 G  144  TRP LEU LEU SER PHE LYS ARG GLY SER ALA LEU GLU GLU          
SEQRES   4 G  144  LYS GLU ASN LYS ILE LEU VAL LYS GLU THR GLY TYR PHE          
SEQRES   5 G  144  PHE ILE TYR GLY GLN VAL LEU TYR THR ASP LYS THR TYR          
SEQRES   6 G  144  ALA MET GLY HIS LEU ILE GLN ARG LYS LYS VAL HIS VAL          
SEQRES   7 G  144  PHE GLY ASP GLU LEU SER LEU VAL THR LEU PHE ARG CYS          
SEQRES   8 G  144  ILE GLN ASN MET PRO GLU THR LEU PRO ASN ASN SER CYS          
SEQRES   9 G  144  TYR SER ALA GLY ILE ALA LYS LEU GLU GLU GLY ASP GLU          
SEQRES  10 G  144  LEU GLN LEU ALA ILE PRO ARG GLU ASN ALA GLN ILE SER          
SEQRES  11 G  144  LEU ASP GLY ASP VAL THR PHE PHE GLY ALA LEU LYS LEU          
SEQRES  12 G  144  LEU                                                          
SEQRES   1 H  144  VAL THR GLN ASP CYS LEU GLN LEU ILE ALA ASP SER GLU          
SEQRES   2 H  144  THR PRO THR ILE GLN LYS GLY SER TYR THR PHE VAL PRO          
SEQRES   3 H  144  TRP LEU LEU SER PHE LYS ARG GLY SER ALA LEU GLU GLU          
SEQRES   4 H  144  LYS GLU ASN LYS ILE LEU VAL LYS GLU THR GLY TYR PHE          
SEQRES   5 H  144  PHE ILE TYR GLY GLN VAL LEU TYR THR ASP LYS THR TYR          
SEQRES   6 H  144  ALA MET GLY HIS LEU ILE GLN ARG LYS LYS VAL HIS VAL          
SEQRES   7 H  144  PHE GLY ASP GLU LEU SER LEU VAL THR LEU PHE ARG CYS          
SEQRES   8 H  144  ILE GLN ASN MET PRO GLU THR LEU PRO ASN ASN SER CYS          
SEQRES   9 H  144  TYR SER ALA GLY ILE ALA LYS LEU GLU GLU GLY ASP GLU          
SEQRES  10 H  144  LEU GLN LEU ALA ILE PRO ARG GLU ASN ALA GLN ILE SER          
SEQRES  11 H  144  LEU ASP GLY ASP VAL THR PHE PHE GLY ALA LEU LYS LEU          
SEQRES  12 H  144  LEU                                                          
SEQRES   1 I  144  VAL THR GLN ASP CYS LEU GLN LEU ILE ALA ASP SER GLU          
SEQRES   2 I  144  THR PRO THR ILE GLN LYS GLY SER TYR THR PHE VAL PRO          
SEQRES   3 I  144  TRP LEU LEU SER PHE LYS ARG GLY SER ALA LEU GLU GLU          
SEQRES   4 I  144  LYS GLU ASN LYS ILE LEU VAL LYS GLU THR GLY TYR PHE          
SEQRES   5 I  144  PHE ILE TYR GLY GLN VAL LEU TYR THR ASP LYS THR TYR          
SEQRES   6 I  144  ALA MET GLY HIS LEU ILE GLN ARG LYS LYS VAL HIS VAL          
SEQRES   7 I  144  PHE GLY ASP GLU LEU SER LEU VAL THR LEU PHE ARG CYS          
SEQRES   8 I  144  ILE GLN ASN MET PRO GLU THR LEU PRO ASN ASN SER CYS          
SEQRES   9 I  144  TYR SER ALA GLY ILE ALA LYS LEU GLU GLU GLY ASP GLU          
SEQRES  10 I  144  LEU GLN LEU ALA ILE PRO ARG GLU ASN ALA GLN ILE SER          
SEQRES  11 I  144  LEU ASP GLY ASP VAL THR PHE PHE GLY ALA LEU LYS LEU          
SEQRES  12 I  144  LEU                                                          
SEQRES   1 J  144  VAL THR GLN ASP CYS LEU GLN LEU ILE ALA ASP SER GLU          
SEQRES   2 J  144  THR PRO THR ILE GLN LYS GLY SER TYR THR PHE VAL PRO          
SEQRES   3 J  144  TRP LEU LEU SER PHE LYS ARG GLY SER ALA LEU GLU GLU          
SEQRES   4 J  144  LYS GLU ASN LYS ILE LEU VAL LYS GLU THR GLY TYR PHE          
SEQRES   5 J  144  PHE ILE TYR GLY GLN VAL LEU TYR THR ASP LYS THR TYR          
SEQRES   6 J  144  ALA MET GLY HIS LEU ILE GLN ARG LYS LYS VAL HIS VAL          
SEQRES   7 J  144  PHE GLY ASP GLU LEU SER LEU VAL THR LEU PHE ARG CYS          
SEQRES   8 J  144  ILE GLN ASN MET PRO GLU THR LEU PRO ASN ASN SER CYS          
SEQRES   9 J  144  TYR SER ALA GLY ILE ALA LYS LEU GLU GLU GLY ASP GLU          
SEQRES  10 J  144  LEU GLN LEU ALA ILE PRO ARG GLU ASN ALA GLN ILE SER          
SEQRES  11 J  144  LEU ASP GLY ASP VAL THR PHE PHE GLY ALA LEU LYS LEU          
SEQRES  12 J  144  LEU                                                          
SEQRES   1 K   39  CYS SER GLN ASN GLU TYR PHE ASP SER LEU LEU HIS ALA          
SEQRES   2 K   39  CYS ILE PRO CYS GLN LEU ARG CYS SER SER ASN THR PRO          
SEQRES   3 K   39  PRO LEU THR CYS GLN ARG TYR CYS ASN ALA SER VAL THR          
SEQRES   1 L   39  CYS SER GLN ASN GLU TYR PHE ASP SER LEU LEU HIS ALA          
SEQRES   2 L   39  CYS ILE PRO CYS GLN LEU ARG CYS SER SER ASN THR PRO          
SEQRES   3 L   39  PRO LEU THR CYS GLN ARG TYR CYS ASN ALA SER VAL THR          
SEQRES   1 M   39  CYS SER GLN ASN GLU TYR PHE ASP SER LEU LEU HIS ALA          
SEQRES   2 M   39  CYS ILE PRO CYS GLN LEU ARG CYS SER SER ASN THR PRO          
SEQRES   3 M   39  PRO LEU THR CYS GLN ARG TYR CYS ASN ALA SER VAL THR          
SEQRES   1 N   39  CYS SER GLN ASN GLU TYR PHE ASP SER LEU LEU HIS ALA          
SEQRES   2 N   39  CYS ILE PRO CYS GLN LEU ARG CYS SER SER ASN THR PRO          
SEQRES   3 N   39  PRO LEU THR CYS GLN ARG TYR CYS ASN ALA SER VAL THR          
SEQRES   1 O   39  CYS SER GLN ASN GLU TYR PHE ASP SER LEU LEU HIS ALA          
SEQRES   2 O   39  CYS ILE PRO CYS GLN LEU ARG CYS SER SER ASN THR PRO          
SEQRES   3 O   39  PRO LEU THR CYS GLN ARG TYR CYS ASN ALA SER VAL THR          
SEQRES   1 P   39  CYS SER GLN ASN GLU TYR PHE ASP SER LEU LEU HIS ALA          
SEQRES   2 P   39  CYS ILE PRO CYS GLN LEU ARG CYS SER SER ASN THR PRO          
SEQRES   3 P   39  PRO LEU THR CYS GLN ARG TYR CYS ASN ALA SER VAL THR          
SEQRES   1 Q   39  CYS SER GLN ASN GLU TYR PHE ASP SER LEU LEU HIS ALA          
SEQRES   2 Q   39  CYS ILE PRO CYS GLN LEU ARG CYS SER SER ASN THR PRO          
SEQRES   3 Q   39  PRO LEU THR CYS GLN ARG TYR CYS ASN ALA SER VAL THR          
SEQRES   1 R   39  CYS SER GLN ASN GLU TYR PHE ASP SER LEU LEU HIS ALA          
SEQRES   2 R   39  CYS ILE PRO CYS GLN LEU ARG CYS SER SER ASN THR PRO          
SEQRES   3 R   39  PRO LEU THR CYS GLN ARG TYR CYS ASN ALA SER VAL THR          
HELIX    1   1 CYS K   17  SER K   22  1                                   6    
HELIX    2   2 PRO K   27  ARG K   32  1                                   6    
HELIX    3   3 ARG K   32  SER K   37  1                                   6    
HELIX    4   4 CYS L   17  SER L   22  1                                   6    
HELIX    5   5 CYS M   17  SER M   23  1                                   7    
HELIX    6   6 ARG M   32  SER M   37  1                                   6    
HELIX    7   7 PRO N   16  CYS N   21  5                                   6    
HELIX    8   8 CYS O   17  SER O   22  1                                   6    
HELIX    9   9 CYS O   30  THR O   39  1                                  10    
HELIX   10  10 CYS P   17  SER P   22  1                                   6    
HELIX   11  11 CYS P   30  ASN P   35  1                                   6    
HELIX   12  12 ALA P   36  VAL P   38  5                                   3    
HELIX   13  13 CYS Q   17  SER Q   22  1                                   6    
HELIX   14  14 CYS Q   30  ALA Q   36  1                                   7    
HELIX   15  15 CYS R   17  SER R   22  1                                   6    
HELIX   16  16 CYS R   30  THR R   39  1                                  10    
SHEET    1   A 5 TRP A  27  ARG A  33  0                                        
SHEET    2   A 5 CYS A   5  ALA A  10 -1  N  ILE A   9   O  LEU A  28           
SHEET    3   A 5 PHE A 137  LYS A 142 -1  O  PHE A 138   N  LEU A   8           
SHEET    4   A 5 GLY A  50  TYR A  60 -1  N  PHE A  53   O  LEU A 141           
SHEET    5   A 5 ASN A 102  LEU A 112 -1  O  ASN A 102   N  TYR A  60           
SHEET    1   B 5 LEU A  85  ASN A  94  0                                        
SHEET    2   B 5 ALA A  66  LYS A  74 -1  N  ARG A  73   O  VAL A  86           
SHEET    3   B 5 GLU A 117  ILE A 122 -1  O  GLN A 119   N  GLN A  72           
SHEET    4   B 5 TYR A  22  PHE A  24 -1  N  THR A  23   O  ILE A 122           
SHEET    5   B 5 ILE A  17  LYS A  19 -1  N  ILE A  17   O  PHE A  24           
SHEET    1   C 5 LEU A  85  ASN A  94  0                                        
SHEET    2   C 5 ALA A  66  LYS A  74 -1  N  ARG A  73   O  VAL A  86           
SHEET    3   C 5 GLU A 117  ILE A 122 -1  O  GLN A 119   N  GLN A  72           
SHEET    4   C 5 LYS A  43  VAL A  46 -1  N  ILE A  44   O  LEU A 118           
SHEET    5   C 5 LEU A  37  LYS A  40 -1  N  GLU A  38   O  LEU A  45           
SHEET    1   D 5 TRP B  27  ARG B  33  0                                        
SHEET    2   D 5 CYS B   5  ALA B  10 -1  N  ILE B   9   O  LEU B  28           
SHEET    3   D 5 PHE B 137  LYS B 142 -1  O  PHE B 138   N  LEU B   8           
SHEET    4   D 5 GLY B  50  TYR B  60 -1  N  PHE B  53   O  LEU B 141           
SHEET    5   D 5 ASN B 102  LEU B 112 -1  O  ASN B 102   N  TYR B  60           
SHEET    1   E 5 LEU B  85  ASN B  94  0                                        
SHEET    2   E 5 ALA B  66  LYS B  74 -1  N  ARG B  73   O  VAL B  86           
SHEET    3   E 5 GLU B 117  ILE B 122 -1  O  ALA B 121   N  LEU B  70           
SHEET    4   E 5 TYR B  22  PHE B  24 -1  N  THR B  23   O  ILE B 122           
SHEET    5   E 5 ILE B  17  LYS B  19 -1  N  ILE B  17   O  PHE B  24           
SHEET    1   F 5 LEU B  85  ASN B  94  0                                        
SHEET    2   F 5 ALA B  66  LYS B  74 -1  N  ARG B  73   O  VAL B  86           
SHEET    3   F 5 GLU B 117  ILE B 122 -1  O  ALA B 121   N  LEU B  70           
SHEET    4   F 5 LYS B  43  VAL B  46 -1  N  ILE B  44   O  LEU B 118           
SHEET    5   F 5 LEU B  37  LYS B  40 -1  N  GLU B  38   O  LEU B  45           
SHEET    1   G 5 TRP C  27  ARG C  33  0                                        
SHEET    2   G 5 CYS C   5  ALA C  10 -1  N  ILE C   9   O  LEU C  28           
SHEET    3   G 5 PHE C 137  LYS C 142 -1  O  PHE C 138   N  LEU C   8           
SHEET    4   G 5 GLY C  50  TYR C  60 -1  N  PHE C  53   O  LEU C 141           
SHEET    5   G 5 ASN C 102  LEU C 112 -1  O  ASN C 102   N  TYR C  60           
SHEET    1   H 5 LEU C  85  ASN C  94  0                                        
SHEET    2   H 5 ALA C  66  LYS C  74 -1  N  ARG C  73   O  VAL C  86           
SHEET    3   H 5 GLU C 117  ILE C 122 -1  O  ALA C 121   N  LEU C  70           
SHEET    4   H 5 TYR C  22  PHE C  24 -1  N  THR C  23   O  ILE C 122           
SHEET    5   H 5 ILE C  17  LYS C  19 -1  N  ILE C  17   O  PHE C  24           
SHEET    1   I 5 LEU C  85  ASN C  94  0                                        
SHEET    2   I 5 ALA C  66  LYS C  74 -1  N  ARG C  73   O  VAL C  86           
SHEET    3   I 5 GLU C 117  ILE C 122 -1  O  ALA C 121   N  LEU C  70           
SHEET    4   I 5 LYS C  43  VAL C  46 -1  N  ILE C  44   O  LEU C 118           
SHEET    5   I 5 LEU C  37  LYS C  40 -1  N  GLU C  38   O  LEU C  45           
SHEET    1   J 5 TRP D  27  ARG D  33  0                                        
SHEET    2   J 5 CYS D   5  ALA D  10 -1  N  ILE D   9   O  LEU D  28           
SHEET    3   J 5 PHE D 137  LYS D 142 -1  O  PHE D 138   N  LEU D   8           
SHEET    4   J 5 GLY D  50  TYR D  60 -1  N  PHE D  53   O  LEU D 141           
SHEET    5   J 5 ASN D 102  LEU D 112 -1  O  ASN D 102   N  TYR D  60           
SHEET    1   K 2 ILE D  17  LYS D  19  0                                        
SHEET    2   K 2 TYR D  22  PHE D  24 -1  O  PHE D  24   N  ILE D  17           
SHEET    1   L 5 LEU D  37  LYS D  40  0                                        
SHEET    2   L 5 LYS D  43  VAL D  46 -1  O  LEU D  45   N  GLU D  38           
SHEET    3   L 5 GLU D 117  ALA D 121 -1  O  LEU D 118   N  ILE D  44           
SHEET    4   L 5 ALA D  66  LYS D  74 -1  N  LEU D  70   O  ALA D 121           
SHEET    5   L 5 LEU D  85  ASN D  94 -1  O  VAL D  86   N  ARG D  73           
SHEET    1   M 5 TRP E  27  ARG E  33  0                                        
SHEET    2   M 5 CYS E   5  ALA E  10 -1  N  ILE E   9   O  LEU E  28           
SHEET    3   M 5 PHE E 137  LYS E 142 -1  O  PHE E 138   N  LEU E   8           
SHEET    4   M 5 GLY E  50  TYR E  60 -1  N  PHE E  53   O  LEU E 141           
SHEET    5   M 5 ASN E 102  LEU E 112 -1  O  ASN E 102   N  TYR E  60           
SHEET    1   N 5 LEU E  85  ASN E  94  0                                        
SHEET    2   N 5 ALA E  66  LYS E  74 -1  N  ARG E  73   O  VAL E  86           
SHEET    3   N 5 GLU E 117  ILE E 122 -1  O  ALA E 121   N  LEU E  70           
SHEET    4   N 5 TYR E  22  PHE E  24 -1  N  THR E  23   O  ILE E 122           
SHEET    5   N 5 ILE E  17  LYS E  19 -1  N  ILE E  17   O  PHE E  24           
SHEET    1   O 5 LEU E  85  ASN E  94  0                                        
SHEET    2   O 5 ALA E  66  LYS E  74 -1  N  ARG E  73   O  VAL E  86           
SHEET    3   O 5 GLU E 117  ILE E 122 -1  O  ALA E 121   N  LEU E  70           
SHEET    4   O 5 LYS E  43  VAL E  46 -1  N  ILE E  44   O  LEU E 118           
SHEET    5   O 5 LEU E  37  LYS E  40 -1  N  GLU E  38   O  LEU E  45           
SHEET    1   P 5 TRP F  27  ARG F  33  0                                        
SHEET    2   P 5 CYS F   5  ALA F  10 -1  N  ILE F   9   O  LEU F  28           
SHEET    3   P 5 PHE F 137  LYS F 142 -1  O  PHE F 138   N  LEU F   8           
SHEET    4   P 5 GLY F  50  TYR F  60 -1  N  PHE F  53   O  LEU F 141           
SHEET    5   P 5 ASN F 102  LEU F 112 -1  O  ASN F 102   N  TYR F  60           
SHEET    1   Q 5 LEU F  85  ASN F  94  0                                        
SHEET    2   Q 5 ALA F  66  LYS F  74 -1  N  ARG F  73   O  VAL F  86           
SHEET    3   Q 5 GLU F 117  ILE F 122 -1  O  GLN F 119   N  GLN F  72           
SHEET    4   Q 5 TYR F  22  PHE F  24 -1  N  THR F  23   O  ILE F 122           
SHEET    5   Q 5 ILE F  17  LYS F  19 -1  N  ILE F  17   O  PHE F  24           
SHEET    1   R 5 LEU F  85  ASN F  94  0                                        
SHEET    2   R 5 ALA F  66  LYS F  74 -1  N  ARG F  73   O  VAL F  86           
SHEET    3   R 5 GLU F 117  ILE F 122 -1  O  GLN F 119   N  GLN F  72           
SHEET    4   R 5 LYS F  43  VAL F  46 -1  N  ILE F  44   O  LEU F 118           
SHEET    5   R 5 LEU F  37  LYS F  40 -1  N  GLU F  38   O  LEU F  45           
SHEET    1   S 5 TRP G  27  ARG G  33  0                                        
SHEET    2   S 5 CYS G   5  ALA G  10 -1  N  ILE G   9   O  LEU G  28           
SHEET    3   S 5 PHE G 137  LYS G 142 -1  O  PHE G 138   N  LEU G   8           
SHEET    4   S 5 GLY G  50  TYR G  60 -1  N  PHE G  53   O  LEU G 141           
SHEET    5   S 5 ASN G 102  LEU G 112 -1  O  ASN G 102   N  TYR G  60           
SHEET    1   T 5 LEU G  85  ASN G  94  0                                        
SHEET    2   T 5 ALA G  66  LYS G  74 -1  N  ARG G  73   O  VAL G  86           
SHEET    3   T 5 GLU G 117  ILE G 122 -1  O  ALA G 121   N  LEU G  70           
SHEET    4   T 5 TYR G  22  PHE G  24 -1  N  THR G  23   O  ILE G 122           
SHEET    5   T 5 ILE G  17  LYS G  19 -1  N  ILE G  17   O  PHE G  24           
SHEET    1   U 5 LEU G  85  ASN G  94  0                                        
SHEET    2   U 5 ALA G  66  LYS G  74 -1  N  ARG G  73   O  VAL G  86           
SHEET    3   U 5 GLU G 117  ILE G 122 -1  O  ALA G 121   N  LEU G  70           
SHEET    4   U 5 LYS G  43  VAL G  46 -1  N  ILE G  44   O  LEU G 118           
SHEET    5   U 5 LEU G  37  LYS G  40 -1  N  GLU G  38   O  LEU G  45           
SHEET    1   V 5 TRP H  27  ARG H  33  0                                        
SHEET    2   V 5 CYS H   5  ALA H  10 -1  N  ILE H   9   O  LEU H  28           
SHEET    3   V 5 PHE H 137  LYS H 142 -1  O  PHE H 138   N  LEU H   8           
SHEET    4   V 5 GLY H  50  TYR H  60 -1  N  PHE H  53   O  LEU H 141           
SHEET    5   V 5 ASN H 102  LEU H 112 -1  O  ASN H 102   N  TYR H  60           
SHEET    1   W 5 LEU H  85  ASN H  94  0                                        
SHEET    2   W 5 ALA H  66  LYS H  74 -1  N  ARG H  73   O  VAL H  86           
SHEET    3   W 5 GLU H 117  ILE H 122 -1  O  ALA H 121   N  LEU H  70           
SHEET    4   W 5 TYR H  22  PHE H  24 -1  N  THR H  23   O  ILE H 122           
SHEET    5   W 5 ILE H  17  LYS H  19 -1  N  ILE H  17   O  PHE H  24           
SHEET    1   X 5 LEU H  85  ASN H  94  0                                        
SHEET    2   X 5 ALA H  66  LYS H  74 -1  N  ARG H  73   O  VAL H  86           
SHEET    3   X 5 GLU H 117  ILE H 122 -1  O  ALA H 121   N  LEU H  70           
SHEET    4   X 5 LYS H  43  VAL H  46 -1  N  ILE H  44   O  LEU H 118           
SHEET    5   X 5 LEU H  37  LYS H  40 -1  N  GLU H  38   O  LEU H  45           
SHEET    1   Y 5 TRP I  27  ARG I  33  0                                        
SHEET    2   Y 5 CYS I   5  ALA I  10 -1  N  ILE I   9   O  LEU I  28           
SHEET    3   Y 5 PHE I 137  LYS I 142 -1  O  PHE I 138   N  LEU I   8           
SHEET    4   Y 5 GLY I  50  TYR I  60 -1  N  PHE I  53   O  LEU I 141           
SHEET    5   Y 5 ASN I 102  LEU I 112 -1  O  ASN I 102   N  TYR I  60           
SHEET    1   Z 5 LEU I  85  ASN I  94  0                                        
SHEET    2   Z 5 ALA I  66  LYS I  74 -1  N  ARG I  73   O  VAL I  86           
SHEET    3   Z 5 GLU I 117  ILE I 122 -1  O  ALA I 121   N  LEU I  70           
SHEET    4   Z 5 TYR I  22  PHE I  24 -1  N  THR I  23   O  ILE I 122           
SHEET    5   Z 5 ILE I  17  LYS I  19 -1  N  ILE I  17   O  PHE I  24           
SHEET    1  AA 5 LEU I  85  ASN I  94  0                                        
SHEET    2  AA 5 ALA I  66  LYS I  74 -1  N  ARG I  73   O  VAL I  86           
SHEET    3  AA 5 GLU I 117  ILE I 122 -1  O  ALA I 121   N  LEU I  70           
SHEET    4  AA 5 LYS I  43  VAL I  46 -1  N  ILE I  44   O  LEU I 118           
SHEET    5  AA 5 LEU I  37  LYS I  40 -1  N  GLU I  38   O  LEU I  45           
SHEET    1  AB 5 TRP J  27  ARG J  33  0                                        
SHEET    2  AB 5 CYS J   5  ALA J  10 -1  N  ILE J   9   O  LEU J  28           
SHEET    3  AB 5 PHE J 137  LYS J 142 -1  O  PHE J 138   N  LEU J   8           
SHEET    4  AB 5 GLY J  50  TYR J  60 -1  N  PHE J  53   O  LEU J 141           
SHEET    5  AB 5 ASN J 102  LEU J 112 -1  O  ASN J 102   N  TYR J  60           
SHEET    1  AC 5 LEU J  85  ASN J  94  0                                        
SHEET    2  AC 5 ALA J  66  LYS J  74 -1  N  ARG J  73   O  VAL J  86           
SHEET    3  AC 5 GLU J 117  ILE J 122 -1  O  ALA J 121   N  LEU J  70           
SHEET    4  AC 5 TYR J  22  PHE J  24 -1  N  THR J  23   O  ILE J 122           
SHEET    5  AC 5 ILE J  17  LYS J  19 -1  N  ILE J  17   O  PHE J  24           
SHEET    1  AD 5 LEU J  85  ASN J  94  0                                        
SHEET    2  AD 5 ALA J  66  LYS J  74 -1  N  ARG J  73   O  VAL J  86           
SHEET    3  AD 5 GLU J 117  ILE J 122 -1  O  ALA J 121   N  LEU J  70           
SHEET    4  AD 5 LYS J  43  VAL J  46 -1  N  ILE J  44   O  LEU J 118           
SHEET    5  AD 5 LEU J  37  LYS J  40 -1  N  GLU J  38   O  LEU J  45           
SHEET    1  AE 2 GLU K   5  ASP K   8  0                                        
SHEET    2  AE 2 ALA K  13  PRO K  16 -1  O  ILE K  15   N  TYR K   6           
SHEET    1  AF 2 GLU L   5  ASP L   8  0                                        
SHEET    2  AF 2 ALA L  13  PRO L  16 -1  O  ILE L  15   N  TYR L   6           
SHEET    1  AG 2 GLU M   5  ASP M   8  0                                        
SHEET    2  AG 2 ALA M  13  PRO M  16 -1  O  ILE M  15   N  TYR M   6           
SHEET    1  AH 2 TYR N   6  ASP N   8  0                                        
SHEET    2  AH 2 ALA N  13  ILE N  15 -1  O  ILE N  15   N  TYR N   6           
SHEET    1  AI 2 GLU O   5  ASP O   8  0                                        
SHEET    2  AI 2 ALA O  13  PRO O  16 -1  O  ILE O  15   N  TYR O   6           
SHEET    1  AJ 2 GLU P   5  ASP P   8  0                                        
SHEET    2  AJ 2 ALA P  13  PRO P  16 -1  O  ILE P  15   N  TYR P   6           
SHEET    1  AK 2 GLU Q   5  ASP Q   8  0                                        
SHEET    2  AK 2 ALA Q  13  PRO Q  16 -1  O  ILE Q  15   N  TYR Q   6           
SHEET    1  AL 2 GLU R   5  ASP R   8  0                                        
SHEET    2  AL 2 ALA R  13  PRO R  16 -1  O  ILE R  15   N  TYR R   6           
SSBOND   1 CYS A   91    CYS A  104                          1555   1555  2.08  
SSBOND   2 CYS B   91    CYS B  104                          1555   1555  2.08  
SSBOND   3 CYS C   91    CYS C  104                          1555   1555  2.08  
SSBOND   4 CYS D   91    CYS D  104                          1555   1555  2.08  
SSBOND   5 CYS E   91    CYS E  104                          1555   1555  2.10  
SSBOND   6 CYS F   91    CYS F  104                          1555   1555  2.09  
SSBOND   7 CYS G   91    CYS G  104                          1555   1555  2.09  
SSBOND   8 CYS H   91    CYS H  104                          1555   1555  2.09  
SSBOND   9 CYS I   91    CYS I  104                          1555   1555  2.09  
SSBOND  10 CYS J   91    CYS J  104                          1555   1555  2.08  
SSBOND  11 CYS K    1    CYS K   14                          1555   1555  2.05  
SSBOND  12 CYS K   17    CYS K   30                          1555   1555  2.05  
SSBOND  13 CYS K   21    CYS K   34                          1555   1555  2.05  
SSBOND  14 CYS L    1    CYS L   14                          1555   1555  2.04  
SSBOND  15 CYS L   17    CYS L   30                          1555   1555  2.05  
SSBOND  16 CYS L   21    CYS L   34                          1555   1555  2.05  
SSBOND  17 CYS M    1    CYS M   14                          1555   1555  2.05  
SSBOND  18 CYS M   17    CYS M   30                          1555   1555  2.04  
SSBOND  19 CYS M   21    CYS M   34                          1555   1555  2.05  
SSBOND  20 CYS N    1    CYS N   14                          1555   1555  2.06  
SSBOND  21 CYS O    1    CYS O   14                          1555   1555  2.04  
SSBOND  22 CYS O   17    CYS O   30                          1555   1555  2.05  
SSBOND  23 CYS O   21    CYS O   34                          1555   1555  2.05  
SSBOND  24 CYS P    1    CYS P   14                          1555   1555  2.04  
SSBOND  25 CYS P   17    CYS P   30                          1555   1555  2.06  
SSBOND  26 CYS P   21    CYS P   34                          1555   1555  2.05  
SSBOND  27 CYS Q    1    CYS Q   14                          1555   1555  2.04  
SSBOND  28 CYS Q   17    CYS Q   30                          1555   1555  2.05  
SSBOND  29 CYS Q   21    CYS Q   34                          1555   1555  2.06  
SSBOND  30 CYS R    1    CYS R   14                          1555   1555  2.04  
SSBOND  31 CYS R   17    CYS R   30                          1555   1555  2.05  
SSBOND  32 CYS R   21    CYS R   34                          1555   1555  2.05  
CRYST1  232.854  232.854  212.477  90.00  90.00 120.00 P 63 2 2    120          
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      0.004295  0.002479  0.000000        0.00000                         
SCALE2      0.000000  0.004959  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004706        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system