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Database: PDB
Entry: 5Y9J
LinkDB: 5Y9J
Original site: 5Y9J 
HEADER    PROTEIN BINDING                         25-AUG-17   5Y9J              
TITLE     BAFF IN COMPLEX WITH BELIMUMAB                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BELIBUMAB LIGHT CHAIN;                                     
COMPND   3 CHAIN: L;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: BELIMUMAB HEAVY CHAIN;                                     
COMPND   7 CHAIN: H;                                                            
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: TUMOR NECROSIS FACTOR LIGAND SUPERFAMILY MEMBER 13B;       
COMPND  11 CHAIN: A;                                                            
COMPND  12 SYNONYM: B LYMPHOCYTE STIMULATOR,BLYS,B-CELL-ACTIVATING FACTOR,BAFF, 
COMPND  13 DENDRITIC CELL-DERIVED TNF-LIKE MOLECULE,TNF- AND APOL-RELATED       
COMPND  14 LEUKOCYTE EXPRESSED LIGAND 1,TALL-1;                                 
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_TAXID: 9606;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   8 ORGANISM_TAXID: 9606;                                                
SOURCE   9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: TNFSF13B, BAFF, BLYS, TALL1, TNFSF20, ZTNF4, UNQ401/PRO738;    
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    BAFF, BELIMUMAB, ANTIBODY, LUPUS, PROTEIN BINDING                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.-S.HEO,W.SHIN                                                       
REVDAT   2   04-SEP-19 5Y9J    1       JRNL                                     
REVDAT   1   21-FEB-18 5Y9J    0                                                
JRNL        AUTH   W.SHIN,H.T.LEE,H.LIM,S.H.LEE,J.Y.SON,J.U.LEE,K.Y.YOO,        
JRNL        AUTH 2 S.E.RYU,J.RHIE,J.Y.LEE,Y.S.HEO                               
JRNL        TITL   BAFF-NEUTRALIZING INTERACTION OF BELIMUMAB RELATED TO ITS    
JRNL        TITL 2 THERAPEUTIC EFFICACY FOR TREATING SYSTEMIC LUPUS             
JRNL        TITL 3 ERYTHEMATOSUS.                                               
JRNL        REF    NAT COMMUN                    V.   9  1200 2018              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   29572471                                                     
JRNL        DOI    10.1038/S41467-018-03620-2                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.4_1496                                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.28                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 48698                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.217                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.050                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2457                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 26.2819 -  5.3586    0.97     2700   149  0.1661 0.1924        
REMARK   3     2  5.3586 -  4.2592    0.98     2650   153  0.1290 0.1681        
REMARK   3     3  4.2592 -  3.7225    0.99     2631   133  0.1488 0.1699        
REMARK   3     4  3.7225 -  3.3829    0.99     2680   131  0.1592 0.2054        
REMARK   3     5  3.3829 -  3.1409    0.99     2630   147  0.1732 0.2132        
REMARK   3     6  3.1409 -  2.9559    0.97     2557   153  0.1847 0.2184        
REMARK   3     7  2.9559 -  2.8081    0.96     2550   139  0.1915 0.2359        
REMARK   3     8  2.8081 -  2.6860    0.95     2487   133  0.2094 0.2247        
REMARK   3     9  2.6860 -  2.5827    0.95     2509   129  0.2102 0.2623        
REMARK   3    10  2.5827 -  2.4936    0.94     2487   121  0.2284 0.2314        
REMARK   3    11  2.4936 -  2.4157    0.95     2548   118  0.2344 0.2833        
REMARK   3    12  2.4157 -  2.3467    0.94     2436   148  0.2348 0.3483        
REMARK   3    13  2.3467 -  2.2849    0.94     2509   120  0.2317 0.2855        
REMARK   3    14  2.2849 -  2.2292    0.96     2524   130  0.2344 0.3124        
REMARK   3    15  2.2292 -  2.1786    0.97     2558   125  0.2290 0.2721        
REMARK   3    16  2.1786 -  2.1322    0.98     2590   131  0.2253 0.2616        
REMARK   3    17  2.1322 -  2.0896    0.99     2574   162  0.2264 0.2607        
REMARK   3    18  2.0896 -  2.0502    0.99     2621   135  0.2393 0.2724        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.200            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.970           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           4432                                  
REMARK   3   ANGLE     :  1.129           6025                                  
REMARK   3   CHIRALITY :  0.047            683                                  
REMARK   3   PLANARITY :  0.008            777                                  
REMARK   3   DIHEDRAL  : 13.453           1592                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'L' AND ((RESSEQ 111:211))                       
REMARK   3    ORIGIN FOR THE GROUP (A):  44.5347  50.1643  67.4291              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3037 T22:   0.2620                                     
REMARK   3      T33:   0.2853 T12:  -0.0097                                     
REMARK   3      T13:  -0.0020 T23:   0.0225                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6967 L22:   2.8080                                     
REMARK   3      L33:   5.2164 L12:  -0.6814                                     
REMARK   3      L13:  -1.6168 L23:   0.0041                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1395 S12:  -0.2220 S13:   0.2795                       
REMARK   3      S21:   0.1418 S22:   0.0043 S23:  -0.2301                       
REMARK   3      S31:  -0.2458 S32:   0.0856 S33:  -0.1149                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'L' AND ((RESSEQ 2:110))                         
REMARK   3    ORIGIN FOR THE GROUP (A):  41.6932  13.8948  52.9879              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2758 T22:   0.2730                                     
REMARK   3      T33:   0.2058 T12:  -0.0608                                     
REMARK   3      T13:   0.0312 T23:  -0.0465                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4556 L22:   5.1198                                     
REMARK   3      L33:   2.1518 L12:   1.0413                                     
REMARK   3      L13:  -0.4886 L23:  -0.9186                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0611 S12:   0.0271 S13:  -0.0946                       
REMARK   3      S21:  -0.2580 S22:   0.0513 S23:  -0.2137                       
REMARK   3      S31:  -0.0227 S32:   0.2131 S33:   0.0056                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'H' AND ((RESSEQ 2:123))                         
REMARK   3    ORIGIN FOR THE GROUP (A):  29.9103  13.0969  71.2499              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2473 T22:   0.3091                                     
REMARK   3      T33:   0.2344 T12:  -0.0428                                     
REMARK   3      T13:  -0.0017 T23:  -0.0173                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7636 L22:   3.8127                                     
REMARK   3      L33:   3.8753 L12:   1.3781                                     
REMARK   3      L13:   1.4889 L23:   2.7376                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0347 S12:  -0.0500 S13:   0.0373                       
REMARK   3      S21:   0.0683 S22:  -0.0299 S23:   0.1299                       
REMARK   3      S31:  -0.0815 S32:   0.0573 S33:   0.0486                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'H' AND ((RESSEQ 124:224))                       
REMARK   3    ORIGIN FOR THE GROUP (A):  28.9844  44.9991  69.9380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2796 T22:   0.4250                                     
REMARK   3      T33:   0.2890 T12:  -0.0019                                     
REMARK   3      T13:  -0.0134 T23:   0.0753                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4468 L22:   4.2871                                     
REMARK   3      L33:   4.3129 L12:  -0.9259                                     
REMARK   3      L13:   1.1863 L23:  -1.6445                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0387 S12:  -0.3573 S13:  -0.1259                       
REMARK   3      S21:  -0.0397 S22:   0.3439 S23:   0.4661                       
REMARK   3      S31:  -0.1489 S32:  -0.6970 S33:  -0.3073                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A'                                              
REMARK   3    ORIGIN FOR THE GROUP (A):  29.8279 -17.1739  55.9756              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1918 T22:   0.2223                                     
REMARK   3      T33:   0.1868 T12:  -0.0230                                     
REMARK   3      T13:  -0.0371 T23:   0.0074                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5445 L22:   1.6936                                     
REMARK   3      L33:   1.6944 L12:  -0.8829                                     
REMARK   3      L13:  -1.0456 L23:   0.7951                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0233 S12:  -0.1069 S13:   0.0232                       
REMARK   3      S21:   0.1079 S22:   0.0360 S23:  -0.1945                       
REMARK   3      S31:  -0.0225 S32:   0.2245 S33:  -0.0428                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5Y9J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-AUG-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300004893.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-SEP-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 5C (4A)                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48698                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY                : 14.60                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 52.3000                            
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS(HYDROXYMETHYL)AMINOMETHANE    
REMARK 280  PH 8.5, 20% (W/V)POLYETHYLENE GLYCOL 1,000, VAPOR DIFFUSION,        
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 3                           
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z+1/2,-X+1/2,-Y                                         
REMARK 290       7555   -Z+1/2,-X,Y+1/2                                         
REMARK 290       8555   -Z,X+1/2,-Y+1/2                                         
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z+1/2,-X+1/2                                         
REMARK 290      11555   Y+1/2,-Z+1/2,-X                                         
REMARK 290      12555   -Y+1/2,-Z,X+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 -1.000000  0.000000  0.000000       67.00050            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       67.00050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       67.00050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       67.00050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       67.00050            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       67.00050            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000       67.00050            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000       67.00050            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000       67.00050            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000       67.00050            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000       67.00050            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000       67.00050            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000       67.00050            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000       67.00050            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000       67.00050            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000       67.00050            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000       67.00050            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000       67.00050            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4960 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25920 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, A                               
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 306  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 343  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 367  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 424  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 431  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 436  LIES ON A SPECIAL POSITION.                          
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 L     1                                                      
REMARK 465     GLU L   212                                                      
REMARK 465     CYS L   213                                                      
REMARK 465     SER L   214                                                      
REMARK 465     GLN H     1                                                      
REMARK 465     SER H   138                                                      
REMARK 465     LYS H   139                                                      
REMARK 465     SER H   140                                                      
REMARK 465     THR H   141                                                      
REMARK 465     SER H   142                                                      
REMARK 465     SER H   225                                                      
REMARK 465     CYS H   226                                                      
REMARK 465     ASP H   227                                                      
REMARK 465     LYS H   228                                                      
REMARK 465     THR H   229                                                      
REMARK 465     HIS H   230                                                      
REMARK 465     HIS H   231                                                      
REMARK 465     HIS H   232                                                      
REMARK 465     HIS H   233                                                      
REMARK 465     HIS H   234                                                      
REMARK 465     HIS H   235                                                      
REMARK 465     ALA A   134                                                      
REMARK 465     VAL A   135                                                      
REMARK 465     GLN A   136                                                      
REMARK 465     GLY A   137                                                      
REMARK 465     PRO A   138                                                      
REMARK 465     GLU A   139                                                      
REMARK 465     GLU A   140                                                      
REMARK 465     THR A   141                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH H   393     O    HOH H   462              1.86            
REMARK 500   OE1  GLN A   260     O    HOH A   301              1.86            
REMARK 500   O    HOH A   328     O    HOH A   358              1.90            
REMARK 500   O    HOH A   330     O    HOH A   411              1.91            
REMARK 500   O    HOH H   426     O    HOH H   431              1.93            
REMARK 500   O    HOH L   329     O    HOH L   462              2.02            
REMARK 500   O    HOH L   448     O    HOH L   461              2.06            
REMARK 500   O    HOH H   411     O    HOH H   460              2.06            
REMARK 500   O    HOH A   433     O    HOH A   434              2.12            
REMARK 500   O    HOH L   433     O    HOH L   471              2.12            
REMARK 500   OG   SER L   167     O    HOH L   301              2.14            
REMARK 500   OG   SER H   171     O    HOH H   301              2.15            
REMARK 500   O    HOH L   392     O    HOH L   465              2.18            
REMARK 500   O    HOH H   359     O    HOH H   463              2.19            
REMARK 500   O    HOH L   445     O    HOH H   403              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   382     O    HOH A   414    10545     1.86            
REMARK 500   O    HOH A   401     O    HOH A   401    10545     1.87            
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    PRO H 112   C   -  N   -  CD  ANGL. DEV. = -16.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA L  83      175.15    177.94                                   
REMARK 500    HIS L  96     -169.63     60.28                                   
REMARK 500    ASP L 153     -114.79     55.39                                   
REMARK 500    SER H  16     -158.57    -88.27                                   
REMARK 500    ASN H  30     -130.56     44.08                                   
REMARK 500    ALA H 109     -159.81   -125.14                                   
REMARK 500    SER H 111      113.10   -178.06                                   
REMARK 500    ASP H 154       61.43     63.81                                   
REMARK 500    ASN A 242       87.31   -158.10                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 SER H  111     PRO H  112                   57.41                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    SER H 111         11.08                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH L 477        DISTANCE =  6.90 ANGSTROMS                       
REMARK 525    HOH H 487        DISTANCE =  6.52 ANGSTROMS                       
REMARK 525    HOH A 436        DISTANCE =  6.79 ANGSTROMS                       
DBREF  5Y9J L    1   214  PDB    5Y9J     5Y9J             1    214             
DBREF  5Y9J H    1   235  PDB    5Y9J     5Y9J             1    235             
DBREF  5Y9J A  134   285  UNP    Q9Y275   TN13B_HUMAN    134    285             
SEQRES   1 L  214  SER SER GLU LEU THR GLN ASP PRO ALA VAL SER VAL ALA          
SEQRES   2 L  214  LEU GLY GLN THR VAL ARG VAL THR CYS GLN GLY ASP SER          
SEQRES   3 L  214  LEU ARG SER TYR TYR ALA SER TRP TYR GLN GLN LYS PRO          
SEQRES   4 L  214  GLY GLN ALA PRO VAL LEU VAL ILE TYR GLY LYS ASN ASN          
SEQRES   5 L  214  ARG PRO SER GLY ILE PRO ASP ARG PHE SER GLY SER SER          
SEQRES   6 L  214  SER GLY ASN THR ALA SER LEU THR ILE THR GLY ALA GLN          
SEQRES   7 L  214  ALA GLU ASP GLU ALA ASP TYR TYR CYS SER SER ARG ASP          
SEQRES   8 L  214  SER SER GLY ASN HIS TRP VAL PHE GLY GLY GLY THR GLU          
SEQRES   9 L  214  LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL          
SEQRES  10 L  214  THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN          
SEQRES  11 L  214  LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO          
SEQRES  12 L  214  GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO          
SEQRES  13 L  214  VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN          
SEQRES  14 L  214  SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU          
SEQRES  15 L  214  THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS          
SEQRES  16 L  214  GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL          
SEQRES  17 L  214  ALA PRO THR GLU CYS SER                                      
SEQRES   1 H  235  GLN VAL GLN LEU GLN GLN SER GLY ALA GLU VAL LYS LYS          
SEQRES   2 H  235  PRO GLY SER SER VAL ARG VAL SER CYS LYS ALA SER GLY          
SEQRES   3 H  235  GLY THR PHE ASN ASN ASN ALA ILE ASN TRP VAL ARG GLN          
SEQRES   4 H  235  ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE ILE          
SEQRES   5 H  235  PRO MET PHE GLY THR ALA LYS TYR SER GLN ASN PHE GLN          
SEQRES   6 H  235  GLY ARG VAL ALA ILE THR ALA ASP GLU SER THR GLY THR          
SEQRES   7 H  235  ALA SER MET GLU LEU SER SER LEU ARG SER GLU ASP THR          
SEQRES   8 H  235  ALA VAL TYR TYR CYS ALA ARG SER ARG ASP LEU LEU LEU          
SEQRES   9 H  235  PHE PRO HIS HIS ALA LEU SER PRO TRP GLY ARG GLY THR          
SEQRES  10 H  235  MET VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER          
SEQRES  11 H  235  VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY          
SEQRES  12 H  235  GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE          
SEQRES  13 H  235  PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU          
SEQRES  14 H  235  THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER          
SEQRES  15 H  235  SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO          
SEQRES  16 H  235  SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL          
SEQRES  17 H  235  ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL          
SEQRES  18 H  235  GLU PRO LYS SER CYS ASP LYS THR HIS HIS HIS HIS HIS          
SEQRES  19 H  235  HIS                                                          
SEQRES   1 A  152  ALA VAL GLN GLY PRO GLU GLU THR VAL THR GLN ASP CYS          
SEQRES   2 A  152  LEU GLN LEU ILE ALA ASP SER GLU THR PRO THR ILE GLN          
SEQRES   3 A  152  LYS GLY SER TYR THR PHE VAL PRO TRP LEU LEU SER PHE          
SEQRES   4 A  152  LYS ARG GLY SER ALA LEU GLU GLU LYS GLU ASN LYS ILE          
SEQRES   5 A  152  LEU VAL LYS GLU THR GLY TYR PHE PHE ILE TYR GLY GLN          
SEQRES   6 A  152  VAL LEU TYR THR ASP LYS THR TYR ALA MET GLY HIS LEU          
SEQRES   7 A  152  ILE GLN ARG LYS LYS VAL HIS VAL PHE GLY ASP GLU LEU          
SEQRES   8 A  152  SER LEU VAL THR LEU PHE ARG CYS ILE GLN ASN MET PRO          
SEQRES   9 A  152  GLU THR LEU PRO ASN ASN SER CYS TYR SER ALA GLY ILE          
SEQRES  10 A  152  ALA LYS LEU GLU GLU GLY ASP GLU LEU GLN LEU ALA ILE          
SEQRES  11 A  152  PRO ARG GLU ASN ALA GLN ILE SER LEU ASP GLY ASP VAL          
SEQRES  12 A  152  THR PHE PHE GLY ALA LEU LYS LEU LEU                          
FORMUL   4  HOH   *500(H2 O)                                                    
HELIX    1 AA1 ASP L   25  SER L   29  5                                   5    
HELIX    2 AA2 GLN L   78  GLU L   82  5                                   5    
HELIX    3 AA3 SER L  123  ALA L  129  1                                   7    
HELIX    4 AA4 THR L  183  HIS L  190  1                                   8    
HELIX    5 AA5 GLU H   74  THR H   76  5                                   3    
HELIX    6 AA6 ARG H   87  THR H   91  5                                   5    
HELIX    7 AA7 SER H  166  ALA H  168  5                                   3    
HELIX    8 AA8 SER H  197  LEU H  199  5                                   3    
HELIX    9 AA9 LYS H  211  ASN H  214  5                                   4    
SHEET    1 AA1 4 THR L   5  GLN L   6  0                                        
SHEET    2 AA1 4 VAL L  18  GLN L  23 -1  O  GLN L  23   N  THR L   5           
SHEET    3 AA1 4 THR L  69  ILE L  74 -1  O  ALA L  70   N  CYS L  22           
SHEET    4 AA1 4 PHE L  61  SER L  66 -1  N  SER L  62   O  THR L  73           
SHEET    1 AA2 5 ALA L   9  ALA L  13  0                                        
SHEET    2 AA2 5 THR L 103  LEU L 108  1  O  LEU L 108   N  VAL L  12           
SHEET    3 AA2 5 ALA L  83  SER L  89 -1  N  ALA L  83   O  LEU L 105           
SHEET    4 AA2 5 SER L  33  GLN L  37 -1  N  TYR L  35   O  TYR L  86           
SHEET    5 AA2 5 VAL L  44  ILE L  47 -1  O  ILE L  47   N  TRP L  34           
SHEET    1 AA3 4 ALA L   9  ALA L  13  0                                        
SHEET    2 AA3 4 THR L 103  LEU L 108  1  O  LEU L 108   N  VAL L  12           
SHEET    3 AA3 4 ALA L  83  SER L  89 -1  N  ALA L  83   O  LEU L 105           
SHEET    4 AA3 4 VAL L  98  PHE L  99 -1  O  VAL L  98   N  SER L  89           
SHEET    1 AA4 4 SER L 116  PHE L 120  0                                        
SHEET    2 AA4 4 ALA L 132  PHE L 141 -1  O  LEU L 137   N  THR L 118           
SHEET    3 AA4 4 TYR L 174  LEU L 182 -1  O  SER L 178   N  CYS L 136           
SHEET    4 AA4 4 VAL L 161  THR L 163 -1  N  GLU L 162   O  TYR L 179           
SHEET    1 AA5 4 SER L 116  PHE L 120  0                                        
SHEET    2 AA5 4 ALA L 132  PHE L 141 -1  O  LEU L 137   N  THR L 118           
SHEET    3 AA5 4 TYR L 174  LEU L 182 -1  O  SER L 178   N  CYS L 136           
SHEET    4 AA5 4 SER L 167  LYS L 168 -1  N  SER L 167   O  ALA L 175           
SHEET    1 AA6 4 SER L 155  VAL L 157  0                                        
SHEET    2 AA6 4 THR L 147  ALA L 152 -1  N  ALA L 152   O  SER L 155           
SHEET    3 AA6 4 TYR L 193  HIS L 199 -1  O  GLN L 196   N  ALA L 149           
SHEET    4 AA6 4 SER L 202  VAL L 208 -1  O  VAL L 204   N  VAL L 197           
SHEET    1 AA7 4 LEU H   4  GLN H   6  0                                        
SHEET    2 AA7 4 VAL H  18  ALA H  24 -1  O  LYS H  23   N  GLN H   5           
SHEET    3 AA7 4 THR H  78  LEU H  83 -1  O  ALA H  79   N  CYS H  22           
SHEET    4 AA7 4 VAL H  68  ASP H  73 -1  N  ALA H  69   O  GLU H  82           
SHEET    1 AA8 6 GLU H  10  LYS H  12  0                                        
SHEET    2 AA8 6 THR H 117  VAL H 121  1  O  THR H 120   N  GLU H  10           
SHEET    3 AA8 6 ALA H  92  SER H  99 -1  N  ALA H  92   O  VAL H 119           
SHEET    4 AA8 6 ALA H  33  GLN H  39 -1  N  ALA H  33   O  SER H  99           
SHEET    5 AA8 6 LEU H  45  ILE H  51 -1  O  MET H  48   N  TRP H  36           
SHEET    6 AA8 6 LYS H  59  TYR H  60 -1  O  LYS H  59   N  GLY H  50           
SHEET    1 AA9 4 SER H 130  LEU H 134  0                                        
SHEET    2 AA9 4 THR H 145  TYR H 155 -1  O  GLY H 149   N  LEU H 134           
SHEET    3 AA9 4 TYR H 186  PRO H 195 -1  O  LEU H 188   N  VAL H 152           
SHEET    4 AA9 4 VAL H 173  THR H 175 -1  N  HIS H 174   O  VAL H 191           
SHEET    1 AB1 4 SER H 130  LEU H 134  0                                        
SHEET    2 AB1 4 THR H 145  TYR H 155 -1  O  GLY H 149   N  LEU H 134           
SHEET    3 AB1 4 TYR H 186  PRO H 195 -1  O  LEU H 188   N  VAL H 152           
SHEET    4 AB1 4 VAL H 179  LEU H 180 -1  N  VAL H 179   O  SER H 187           
SHEET    1 AB2 3 THR H 161  TRP H 164  0                                        
SHEET    2 AB2 3 ILE H 205  HIS H 210 -1  O  ASN H 207   N  SER H 163           
SHEET    3 AB2 3 THR H 215  LYS H 220 -1  O  VAL H 217   N  VAL H 208           
SHEET    1 AB3 5 TRP A 168  ARG A 174  0                                        
SHEET    2 AB3 5 CYS A 146  ALA A 151 -1  N  CYS A 146   O  ARG A 174           
SHEET    3 AB3 5 PHE A 278  LYS A 283 -1  O  PHE A 279   N  LEU A 149           
SHEET    4 AB3 5 GLY A 191  TYR A 201 -1  N  PHE A 194   O  LEU A 282           
SHEET    5 AB3 5 ASN A 243  LEU A 253 -1  O  GLY A 249   N  ILE A 195           
SHEET    1 AB4 2 ILE A 158  LYS A 160  0                                        
SHEET    2 AB4 2 TYR A 163  PHE A 165 -1  O  PHE A 165   N  ILE A 158           
SHEET    1 AB5 5 LEU A 178  LYS A 181  0                                        
SHEET    2 AB5 5 LYS A 184  VAL A 187 -1  O  LEU A 186   N  GLU A 179           
SHEET    3 AB5 5 GLU A 258  ALA A 262 -1  O  LEU A 259   N  ILE A 185           
SHEET    4 AB5 5 ALA A 207  LYS A 215 -1  N  LYS A 215   O  GLU A 258           
SHEET    5 AB5 5 LEU A 226  ASN A 235 -1  O  VAL A 227   N  ARG A 214           
SSBOND   1 CYS L   22    CYS L   87                          1555   1555  2.05  
SSBOND   2 CYS L  136    CYS L  195                          1555   1555  2.05  
SSBOND   3 CYS H   22    CYS H   96                          1555   1555  2.06  
SSBOND   4 CYS H  150    CYS H  206                          1555   1555  2.04  
CISPEP   1 TYR L  142    PRO L  143          0         1.08                     
CISPEP   2 PHE H  156    PRO H  157          0        -6.19                     
CISPEP   3 GLU H  158    PRO H  159          0         1.80                     
CRYST1  134.001  134.001  134.001  90.00  90.00  90.00 P 21 3       12          
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      0.007463  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007463  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007463        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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