GenomeNet

Database: PDB
Entry: 1JH5
LinkDB: 1JH5
Original site: 1JH5 
HEADER    IMMUNE SYSTEM, ANTITUMOR PROTEIN        27-JUN-01   1JH5              
TITLE     CRYSTAL STRUCTURE OF STALL-1 OF TNF FAMILY LIGAND                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUMOR NECROSIS FACTOR LIGAND SUPERFAMILY MEMBER 13B;       
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J;                                 
COMPND   4 FRAGMENT: STALL-1, SOLUBLE PART OF TALL-1;                           
COMPND   5 SYNONYM: TNF FAMILY LIGAND; TNF-AND APOL-RELATED LEUKOCYTE EXPRESSED 
COMPND   6 LIGAND 1; TALL-1; B LYMPHOCYTE STIMULATOR; BLYS; B CELL-ACTIVATING   
COMPND   7 FACTOR; TUMOR NECROSIS FACTOR (LIGAND) SUPERFAMILY, MEMBER 13B;      
COMPND   8 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                                         
KEYWDS    TALL-1, BLYS, THANK, BAFF, IMMUNE SYSTEM, ANTITUMOR PROTEIN           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.LIU,L.XU,N.OPALKA,H.-B.SHU,G.ZHANG                                  
REVDAT   6   04-MAR-20 1JH5    1       REMARK                                   
REVDAT   5   04-OCT-17 1JH5    1       REMARK                                   
REVDAT   4   13-JUL-11 1JH5    1       VERSN                                    
REVDAT   3   24-FEB-09 1JH5    1       VERSN                                    
REVDAT   2   01-APR-03 1JH5    1       JRNL                                     
REVDAT   1   08-FEB-02 1JH5    0                                                
JRNL        AUTH   Y.LIU,L.XU,N.OPALKA,J.KAPPLER,H.B.SHU,G.ZHANG                
JRNL        TITL   CRYSTAL STRUCTURE OF STALL-1 REVEALS A VIRUS-LIKE ASSEMBLY   
JRNL        TITL 2 OF TNF FAMILY LIGANDS.                                       
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 108   383 2002              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   11853672                                                     
JRNL        DOI    10.1016/S0092-8674(02)00631-1                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 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 : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.99                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 172269.280                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 79.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 54509                          
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) : 0.236                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2771                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.19                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 48.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5219                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3310                       
REMARK   3   BIN FREE R VALUE                    : 0.3440                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 275                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.021                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11430                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.50000                                              
REMARK   3    B22 (A**2) : 1.50000                                              
REMARK   3    B33 (A**2) : -3.00000                                             
REMARK   3    B12 (A**2) : 5.87000                                              
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) : 0.40                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.62                            
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) : 0.42                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.65                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.600                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.80                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.840                           
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        : 0.29                                                 
REMARK   3   BSOL        : 10.00                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : 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 1JH5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUN-01.                  
REMARK 100 THE DEPOSITION ID IS D_1000013766.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 3                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : R-AXIS                             
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66001                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.7                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : 0.11700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 76.26                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 35% DIOXANE, PH 9.0, VAPOR DIFFUSION,    
REMARK 280  HANGING DROP AT 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      106.27500            
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      106.27500            
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      106.27500            
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      106.27500            
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      106.27500            
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      106.27500            
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: 60-MERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 60-MERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 171710 ANGSTROM**2                        
REMARK 350 SURFACE AREA OF THE COMPLEX: 291860 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -582.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J          
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      117.12100            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000      202.85952            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000     -117.12100            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000      202.85952            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.500000 -0.866025  0.000000      117.12100            
REMARK 350   BIOMT2   4 -0.866025 -0.500000  0.000000      202.85952            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000     -106.27500            
REMARK 350   BIOMT1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   5  0.000000  0.000000 -1.000000     -106.27500            
REMARK 350   BIOMT1   6  0.500000  0.866025  0.000000     -117.12100            
REMARK 350   BIOMT2   6  0.866025 -0.500000  0.000000      202.85952            
REMARK 350   BIOMT3   6  0.000000  0.000000 -1.000000     -106.27500            
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    GLY E 139   N   -  CA  -  C   ANGL. DEV. =  15.3 DEGREES          
REMARK 500    GLY F 139   N   -  CA  -  C   ANGL. DEV. =  15.4 DEGREES          
REMARK 500    GLY H 139   N   -  CA  -  C   ANGL. DEV. =  15.2 DEGREES          
REMARK 500    GLY J 139   N   -  CA  -  C   ANGL. DEV. =  15.3 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    SER A  12       22.47    -63.21                                   
REMARK 500    LYS A  19      131.29   -172.65                                   
REMARK 500    LYS A  40      103.36   -160.75                                   
REMARK 500    TYR A  65      -24.28     46.01                                   
REMARK 500    ALA A  66      117.51   -162.03                                   
REMARK 500    VAL A  78      -66.94   -122.76                                   
REMARK 500    PHE A  79      123.57     78.03                                   
REMARK 500    PHE A  89     -105.47     68.27                                   
REMARK 500    ARG A  90      128.94     67.53                                   
REMARK 500    PRO A  96     -168.97    -79.15                                   
REMARK 500    THR A  98      -71.95    -93.34                                   
REMARK 500    LEU A  99       72.02   -116.88                                   
REMARK 500    ASN A 101       82.51   -164.87                                   
REMARK 500    SER A 103      129.85     59.89                                   
REMARK 500    LEU A 131       33.28    -97.59                                   
REMARK 500    ALA A 140      105.48     90.88                                   
REMARK 500    SER B  12       22.54    -63.58                                   
REMARK 500    LYS B  19      130.63   -172.58                                   
REMARK 500    LYS B  40      103.77   -160.30                                   
REMARK 500    TYR B  65      -24.12     46.42                                   
REMARK 500    ALA B  66      118.12   -162.05                                   
REMARK 500    VAL B  78      -66.14   -123.03                                   
REMARK 500    PHE B  79      122.96     77.26                                   
REMARK 500    ASP B  81       30.12    -97.42                                   
REMARK 500    PHE B  89     -105.93     68.72                                   
REMARK 500    ARG B  90      128.63     68.10                                   
REMARK 500    PRO B  96     -169.28    -78.67                                   
REMARK 500    THR B  98      -72.93    -93.25                                   
REMARK 500    LEU B  99       71.93   -115.79                                   
REMARK 500    ASN B 101       82.34   -165.56                                   
REMARK 500    SER B 103      130.57     60.18                                   
REMARK 500    LEU B 131       33.71    -97.71                                   
REMARK 500    ALA B 140      105.49     90.89                                   
REMARK 500    SER C  12       22.28    -63.86                                   
REMARK 500    LYS C  19      131.31   -171.83                                   
REMARK 500    LYS C  40      104.21   -160.98                                   
REMARK 500    TYR C  65      -24.43     46.15                                   
REMARK 500    ALA C  66      117.69   -162.10                                   
REMARK 500    VAL C  78      -66.94   -122.39                                   
REMARK 500    PHE C  79      123.92     77.39                                   
REMARK 500    PHE C  89     -105.20     67.59                                   
REMARK 500    ARG C  90      128.72     68.04                                   
REMARK 500    PRO C  96     -169.75    -79.10                                   
REMARK 500    THR C  98      -72.38    -93.10                                   
REMARK 500    LEU C  99       72.14   -116.38                                   
REMARK 500    ASN C 101       82.26   -165.43                                   
REMARK 500    SER C 103      130.06     60.97                                   
REMARK 500    LEU C 131       32.84    -96.80                                   
REMARK 500    ALA C 140      104.93     90.84                                   
REMARK 500    SER D  12       22.21    -63.49                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     160 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1JH5 A    1   144  UNP    Q9Y275   TN13B_HUMAN    142    285             
DBREF  1JH5 B    1   144  UNP    Q9Y275   TN13B_HUMAN    142    285             
DBREF  1JH5 C    1   144  UNP    Q9Y275   TN13B_HUMAN    142    285             
DBREF  1JH5 D    1   144  UNP    Q9Y275   TN13B_HUMAN    142    285             
DBREF  1JH5 E    1   144  UNP    Q9Y275   TN13B_HUMAN    142    285             
DBREF  1JH5 F    1   144  UNP    Q9Y275   TN13B_HUMAN    142    285             
DBREF  1JH5 G    1   144  UNP    Q9Y275   TN13B_HUMAN    142    285             
DBREF  1JH5 H    1   144  UNP    Q9Y275   TN13B_HUMAN    142    285             
DBREF  1JH5 I    1   144  UNP    Q9Y275   TN13B_HUMAN    142    285             
DBREF  1JH5 J    1   144  UNP    Q9Y275   TN13B_HUMAN    142    285             
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                                                          
SHEET    1   A 5 TRP A  27  ARG A  33  0                                        
SHEET    2   A 5 CYS A   5  ALA A  10 -1  N  CYS A   5   O  ARG A  33           
SHEET    3   A 5 PHE A 137  PHE A 138 -1  O  PHE A 138   N  LEU A   8           
SHEET    4   A 5 GLY A  50  TYR A  60 -1  N  GLN A  57   O  PHE A 137           
SHEET    5   A 5 ILE A 129  SER A 130 -1  O  SER A 130   N  LEU A  59           
SHEET    1   B 3 CYS A 104  LEU A 112  0                                        
SHEET    2   B 3 GLY A  50  TYR A  60 -1  N  ILE A  54   O  GLY A 108           
SHEET    3   B 3 LEU A 141  LYS A 142 -1  O  LEU A 141   N  PHE A  53           
SHEET    1   C 2 ILE A  17  LYS A  19  0                                        
SHEET    2   C 2 TYR A  22  PHE A  24 -1  O  PHE A  24   N  ILE A  17           
SHEET    1   D 5 LEU A  37  LYS A  40  0                                        
SHEET    2   D 5 LYS A  43  VAL A  46 -1  O  LEU A  45   N  GLU A  38           
SHEET    3   D 5 GLU A 117  ALA A 121 -1  O  LEU A 118   N  ILE A  44           
SHEET    4   D 5 ALA A  66  LYS A  74 -1  N  GLN A  72   O  GLN A 119           
SHEET    5   D 5 LEU A  85  ASN A  94 -1  O  VAL A  86   N  ARG A  73           
SHEET    1   E 5 TRP B  27  ARG B  33  0                                        
SHEET    2   E 5 CYS B   5  ALA B  10 -1  N  CYS B   5   O  ARG B  33           
SHEET    3   E 5 PHE B 137  PHE B 138 -1  O  PHE B 138   N  LEU B   8           
SHEET    4   E 5 GLY B  50  TYR B  60 -1  N  GLN B  57   O  PHE B 137           
SHEET    5   E 5 ILE B 129  SER B 130 -1  O  SER B 130   N  LEU B  59           
SHEET    1   F 3 CYS B 104  LEU B 112  0                                        
SHEET    2   F 3 GLY B  50  TYR B  60 -1  N  ILE B  54   O  GLY B 108           
SHEET    3   F 3 LEU B 141  LYS B 142 -1  O  LEU B 141   N  PHE B  53           
SHEET    1   G 2 ILE B  17  LYS B  19  0                                        
SHEET    2   G 2 TYR B  22  PHE B  24 -1  O  PHE B  24   N  ILE B  17           
SHEET    1   H 5 LEU B  37  LYS B  40  0                                        
SHEET    2   H 5 LYS B  43  VAL B  46 -1  O  LEU B  45   N  GLU B  38           
SHEET    3   H 5 GLU B 117  ALA B 121 -1  O  LEU B 118   N  ILE B  44           
SHEET    4   H 5 ALA B  66  LYS B  74 -1  N  GLN B  72   O  GLN B 119           
SHEET    5   H 5 LEU B  85  ASN B  94 -1  O  VAL B  86   N  ARG B  73           
SHEET    1   I 5 TRP C  27  ARG C  33  0                                        
SHEET    2   I 5 CYS C   5  ALA C  10 -1  N  CYS C   5   O  ARG C  33           
SHEET    3   I 5 PHE C 137  PHE C 138 -1  O  PHE C 138   N  LEU C   8           
SHEET    4   I 5 GLY C  50  TYR C  60 -1  N  GLN C  57   O  PHE C 137           
SHEET    5   I 5 ILE C 129  SER C 130 -1  O  SER C 130   N  LEU C  59           
SHEET    1   J 3 CYS C 104  LEU C 112  0                                        
SHEET    2   J 3 GLY C  50  TYR C  60 -1  N  ILE C  54   O  GLY C 108           
SHEET    3   J 3 LEU C 141  LYS C 142 -1  O  LEU C 141   N  PHE C  53           
SHEET    1   K 2 ILE C  17  LYS C  19  0                                        
SHEET    2   K 2 TYR C  22  PHE C  24 -1  O  PHE C  24   N  ILE C  17           
SHEET    1   L 5 LEU C  37  LYS C  40  0                                        
SHEET    2   L 5 LYS C  43  VAL C  46 -1  O  LEU C  45   N  GLU C  38           
SHEET    3   L 5 GLU C 117  ALA C 121 -1  O  LEU C 118   N  ILE C  44           
SHEET    4   L 5 ALA C  66  LYS C  74 -1  N  GLN C  72   O  GLN C 119           
SHEET    5   L 5 LEU C  85  ASN C  94 -1  O  VAL C  86   N  ARG C  73           
SHEET    1   M 5 TRP D  27  ARG D  33  0                                        
SHEET    2   M 5 CYS D   5  ALA D  10 -1  N  CYS D   5   O  ARG D  33           
SHEET    3   M 5 PHE D 137  PHE D 138 -1  O  PHE D 138   N  LEU D   8           
SHEET    4   M 5 GLY D  50  TYR D  60 -1  N  GLN D  57   O  PHE D 137           
SHEET    5   M 5 ILE D 129  SER D 130 -1  O  SER D 130   N  LEU D  59           
SHEET    1   N 3 CYS D 104  LEU D 112  0                                        
SHEET    2   N 3 GLY D  50  TYR D  60 -1  N  ILE D  54   O  GLY D 108           
SHEET    3   N 3 LEU D 141  LYS D 142 -1  O  LEU D 141   N  PHE D  53           
SHEET    1   O 2 ILE D  17  LYS D  19  0                                        
SHEET    2   O 2 TYR D  22  PHE D  24 -1  O  PHE D  24   N  ILE D  17           
SHEET    1   P 5 LEU D  37  LYS D  40  0                                        
SHEET    2   P 5 LYS D  43  VAL D  46 -1  O  LEU D  45   N  GLU D  38           
SHEET    3   P 5 GLU D 117  ALA D 121 -1  O  LEU D 118   N  ILE D  44           
SHEET    4   P 5 ALA D  66  LYS D  74 -1  N  GLN D  72   O  GLN D 119           
SHEET    5   P 5 LEU D  85  ASN D  94 -1  O  VAL D  86   N  ARG D  73           
SHEET    1   Q 5 TRP E  27  ARG E  33  0                                        
SHEET    2   Q 5 CYS E   5  ALA E  10 -1  N  CYS E   5   O  ARG E  33           
SHEET    3   Q 5 PHE E 137  PHE E 138 -1  O  PHE E 138   N  LEU E   8           
SHEET    4   Q 5 GLY E  50  TYR E  60 -1  N  GLN E  57   O  PHE E 137           
SHEET    5   Q 5 ILE E 129  SER E 130 -1  O  SER E 130   N  LEU E  59           
SHEET    1   R 3 CYS E 104  LEU E 112  0                                        
SHEET    2   R 3 GLY E  50  TYR E  60 -1  N  ILE E  54   O  GLY E 108           
SHEET    3   R 3 LEU E 141  LYS E 142 -1  O  LEU E 141   N  PHE E  53           
SHEET    1   S 2 ILE E  17  LYS E  19  0                                        
SHEET    2   S 2 TYR E  22  PHE E  24 -1  O  PHE E  24   N  ILE E  17           
SHEET    1   T 5 LEU E  37  LYS E  40  0                                        
SHEET    2   T 5 LYS E  43  VAL E  46 -1  O  LEU E  45   N  GLU E  38           
SHEET    3   T 5 GLU E 117  ALA E 121 -1  O  LEU E 118   N  ILE E  44           
SHEET    4   T 5 ALA E  66  LYS E  74 -1  N  GLN E  72   O  GLN E 119           
SHEET    5   T 5 LEU E  85  ASN E  94 -1  O  VAL E  86   N  ARG E  73           
SHEET    1   U 5 TRP F  27  ARG F  33  0                                        
SHEET    2   U 5 CYS F   5  ALA F  10 -1  N  CYS F   5   O  ARG F  33           
SHEET    3   U 5 PHE F 137  PHE F 138 -1  O  PHE F 138   N  LEU F   8           
SHEET    4   U 5 GLY F  50  TYR F  60 -1  N  GLN F  57   O  PHE F 137           
SHEET    5   U 5 ILE F 129  SER F 130 -1  O  SER F 130   N  LEU F  59           
SHEET    1   V 3 CYS F 104  LEU F 112  0                                        
SHEET    2   V 3 GLY F  50  TYR F  60 -1  N  ILE F  54   O  GLY F 108           
SHEET    3   V 3 LEU F 141  LYS F 142 -1  O  LEU F 141   N  PHE F  53           
SHEET    1   W 2 ILE F  17  LYS F  19  0                                        
SHEET    2   W 2 TYR F  22  PHE F  24 -1  O  PHE F  24   N  ILE F  17           
SHEET    1   X 5 LEU F  37  LYS F  40  0                                        
SHEET    2   X 5 LYS F  43  VAL F  46 -1  O  LEU F  45   N  GLU F  38           
SHEET    3   X 5 GLU F 117  ALA F 121 -1  O  LEU F 118   N  ILE F  44           
SHEET    4   X 5 ALA F  66  LYS F  74 -1  N  GLN F  72   O  GLN F 119           
SHEET    5   X 5 LEU F  85  ASN F  94 -1  O  VAL F  86   N  ARG F  73           
SHEET    1   Y 5 TRP G  27  ARG G  33  0                                        
SHEET    2   Y 5 CYS G   5  ALA G  10 -1  N  CYS G   5   O  ARG G  33           
SHEET    3   Y 5 PHE G 137  PHE G 138 -1  O  PHE G 138   N  LEU G   8           
SHEET    4   Y 5 GLY G  50  TYR G  60 -1  N  GLN G  57   O  PHE G 137           
SHEET    5   Y 5 ILE G 129  SER G 130 -1  O  SER G 130   N  LEU G  59           
SHEET    1   Z 3 CYS G 104  LEU G 112  0                                        
SHEET    2   Z 3 GLY G  50  TYR G  60 -1  N  ILE G  54   O  GLY G 108           
SHEET    3   Z 3 LEU G 141  LYS G 142 -1  O  LEU G 141   N  PHE G  53           
SHEET    1  AA 2 ILE G  17  LYS G  19  0                                        
SHEET    2  AA 2 TYR G  22  PHE G  24 -1  O  PHE G  24   N  ILE G  17           
SHEET    1  AB 5 LEU G  37  LYS G  40  0                                        
SHEET    2  AB 5 LYS G  43  VAL G  46 -1  O  LEU G  45   N  GLU G  38           
SHEET    3  AB 5 GLU G 117  ALA G 121 -1  O  LEU G 118   N  ILE G  44           
SHEET    4  AB 5 ALA G  66  LYS G  74 -1  N  GLN G  72   O  GLN G 119           
SHEET    5  AB 5 LEU G  85  ASN G  94 -1  O  VAL G  86   N  ARG G  73           
SHEET    1  AC 5 TRP H  27  ARG H  33  0                                        
SHEET    2  AC 5 CYS H   5  ALA H  10 -1  N  CYS H   5   O  ARG H  33           
SHEET    3  AC 5 PHE H 137  PHE H 138 -1  O  PHE H 138   N  LEU H   8           
SHEET    4  AC 5 GLY H  50  TYR H  60 -1  N  GLN H  57   O  PHE H 137           
SHEET    5  AC 5 ILE H 129  SER H 130 -1  O  SER H 130   N  LEU H  59           
SHEET    1  AD 3 CYS H 104  LEU H 112  0                                        
SHEET    2  AD 3 GLY H  50  TYR H  60 -1  N  ILE H  54   O  GLY H 108           
SHEET    3  AD 3 LEU H 141  LYS H 142 -1  O  LEU H 141   N  PHE H  53           
SHEET    1  AE 2 ILE H  17  LYS H  19  0                                        
SHEET    2  AE 2 TYR H  22  PHE H  24 -1  O  PHE H  24   N  ILE H  17           
SHEET    1  AF 5 LEU H  37  LYS H  40  0                                        
SHEET    2  AF 5 LYS H  43  VAL H  46 -1  O  LEU H  45   N  GLU H  38           
SHEET    3  AF 5 GLU H 117  ALA H 121 -1  O  LEU H 118   N  ILE H  44           
SHEET    4  AF 5 ALA H  66  LYS H  74 -1  N  GLN H  72   O  GLN H 119           
SHEET    5  AF 5 LEU H  85  ASN H  94 -1  O  VAL H  86   N  ARG H  73           
SHEET    1  AG 5 TRP I  27  ARG I  33  0                                        
SHEET    2  AG 5 CYS I   5  ALA I  10 -1  N  CYS I   5   O  ARG I  33           
SHEET    3  AG 5 PHE I 137  PHE I 138 -1  O  PHE I 138   N  LEU I   8           
SHEET    4  AG 5 GLY I  50  TYR I  60 -1  N  GLN I  57   O  PHE I 137           
SHEET    5  AG 5 ILE I 129  SER I 130 -1  O  SER I 130   N  LEU I  59           
SHEET    1  AH 3 CYS I 104  LEU I 112  0                                        
SHEET    2  AH 3 GLY I  50  TYR I  60 -1  N  ILE I  54   O  GLY I 108           
SHEET    3  AH 3 LEU I 141  LYS I 142 -1  O  LEU I 141   N  PHE I  53           
SHEET    1  AI 2 ILE I  17  LYS I  19  0                                        
SHEET    2  AI 2 TYR I  22  PHE I  24 -1  O  PHE I  24   N  ILE I  17           
SHEET    1  AJ 5 LEU I  37  LYS I  40  0                                        
SHEET    2  AJ 5 LYS I  43  VAL I  46 -1  O  LEU I  45   N  GLU I  38           
SHEET    3  AJ 5 GLU I 117  ALA I 121 -1  O  LEU I 118   N  ILE I  44           
SHEET    4  AJ 5 ALA I  66  LYS I  74 -1  N  GLN I  72   O  GLN I 119           
SHEET    5  AJ 5 LEU I  85  ASN I  94 -1  O  VAL I  86   N  ARG I  73           
SHEET    1  AK 5 TRP J  27  ARG J  33  0                                        
SHEET    2  AK 5 CYS J   5  ALA J  10 -1  N  CYS J   5   O  ARG J  33           
SHEET    3  AK 5 PHE J 137  PHE J 138 -1  O  PHE J 138   N  LEU J   8           
SHEET    4  AK 5 GLY J  50  TYR J  60 -1  N  GLN J  57   O  PHE J 137           
SHEET    5  AK 5 ILE J 129  SER J 130 -1  O  SER J 130   N  LEU J  59           
SHEET    1  AL 3 CYS J 104  LEU J 112  0                                        
SHEET    2  AL 3 GLY J  50  TYR J  60 -1  N  ILE J  54   O  GLY J 108           
SHEET    3  AL 3 LEU J 141  LYS J 142 -1  O  LEU J 141   N  PHE J  53           
SHEET    1  AM 2 ILE J  17  LYS J  19  0                                        
SHEET    2  AM 2 TYR J  22  PHE J  24 -1  O  PHE J  24   N  ILE J  17           
SHEET    1  AN 5 LEU J  37  LYS J  40  0                                        
SHEET    2  AN 5 LYS J  43  VAL J  46 -1  O  LEU J  45   N  GLU J  38           
SHEET    3  AN 5 GLU J 117  ALA J 121 -1  O  LEU J 118   N  ILE J  44           
SHEET    4  AN 5 ALA J  66  LYS J  74 -1  N  GLN J  72   O  GLN J 119           
SHEET    5  AN 5 LEU J  85  ASN J  94 -1  O  VAL J  86   N  ARG J  73           
CRYST1  234.242  234.242  212.550  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      0.004269  0.002465  0.000000        0.00000                         
SCALE2      0.000000  0.004930  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004705        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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