GenomeNet

Database: PDB
Entry: 3ALQ
LinkDB: 3ALQ
Original site: 3ALQ 
HEADER    CYTOKINE/CYTOKINE RECEPTOR              06-AUG-10   3ALQ              
TITLE     CRYSTAL STRUCTURE OF TNF-TNFR2 COMPLEX                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUMOR NECROSIS FACTOR;                                     
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 FRAGMENT: SOLUBLE FORM;                                              
COMPND   5 SYNONYM: TNF-ALPHA, TUMOR NECROSIS FACTOR LIGAND SUPERFAMILY MEMBER  
COMPND   6 2, TNF-A, CACHECTIN;                                                 
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 1B;      
COMPND  11 CHAIN: R, S, T, U, V, W;                                             
COMPND  12 FRAGMENT: RESIDUES IN UNP 33-205;                                    
COMPND  13 SYNONYM: TUMOR NECROSIS FACTOR RECEPTOR 2, TNF-R2, TUMOR NECROSIS    
COMPND  14 FACTOR-BINDING PROTEIN 2, TBPII, TBP-2;                              
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: TNF, TNFA, TNFSF2;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PYAS (MODIFIED FROM PUC18);               
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: TNFBR, TNFR2, TNFRSF1B;                                        
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PYAS (MODIFIED FROM PUC18)                
KEYWDS    LIGAND-RECEPTOR COMPLEX, CYTOKINE, CYTOKINE-CYTOKINE RECEPTOR COMPLEX 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.MUKAI,T.NAKAMURA,Y.YAMAGATA,Y.TSUTSUMI                              
REVDAT   2   01-DEC-10 3ALQ    1       JRNL                                     
REVDAT   1   17-NOV-10 3ALQ    0                                                
JRNL        AUTH   Y.MUKAI,T.NAKAMURA,M.YOSHIKAWA,Y.YOSHIOKA,S.I.TSUNODA,       
JRNL        AUTH 2 S.NAKAGAWA,Y.YAMAGATA,Y.TSUTSUMI                             
JRNL        TITL   SOLUTION OF THE STRUCTURE OF THE TNF-TNFR2 COMPLEX           
JRNL        REF    SCI.SIGNAL.                   V.   3  RA83 2010              
JRNL        REFN                   ESSN 1937-9145                               
JRNL        PMID   21081755                                                     
JRNL        DOI    10.1126/SCISIGNAL.2000954                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.5_2)                        
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.96                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.320                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 43981                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.220                           
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.281                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.090                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 4438                            
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 49.9668 -  9.3025    1.00     1470   151  0.2383 0.2933        
REMARK   3     2  9.3025 -  7.3914    1.00     1385   147  0.2169 0.2917        
REMARK   3     3  7.3914 -  6.4593    1.00     1395   143  0.2253 0.2912        
REMARK   3     4  6.4593 -  5.8697    1.00     1331   157  0.2271 0.2525        
REMARK   3     5  5.8697 -  5.4496    1.00     1325   175  0.2119 0.3237        
REMARK   3     6  5.4496 -  5.1286    1.00     1320   164  0.1981 0.2590        
REMARK   3     7  5.1286 -  4.8720    1.00     1340   149  0.1853 0.2588        
REMARK   3     8  4.8720 -  4.6601    1.00     1308   151  0.1593 0.2270        
REMARK   3     9  4.6601 -  4.4808    1.00     1317   171  0.1556 0.2362        
REMARK   3    10  4.4808 -  4.3263    1.00     1339   133  0.1655 0.2029        
REMARK   3    11  4.3263 -  4.1910    1.00     1323   153  0.1757 0.2323        
REMARK   3    12  4.1910 -  4.0713    1.00     1345   136  0.1761 0.2482        
REMARK   3    13  4.0713 -  3.9642    1.00     1286   154  0.1825 0.2646        
REMARK   3    14  3.9642 -  3.8675    1.00     1331   146  0.1885 0.2557        
REMARK   3    15  3.8675 -  3.7796    1.00     1327   146  0.1879 0.2423        
REMARK   3    16  3.7796 -  3.6992    1.00     1326   129  0.1958 0.2693        
REMARK   3    17  3.6992 -  3.6252    1.00     1344   138  0.2112 0.2569        
REMARK   3    18  3.6252 -  3.5568    1.00     1273   135  0.1988 0.2967        
REMARK   3    19  3.5568 -  3.4933    1.00     1339   153  0.2111 0.3033        
REMARK   3    20  3.4933 -  3.4341    1.00     1313   160  0.2240 0.2848        
REMARK   3    21  3.4341 -  3.3787    1.00     1283   126  0.2271 0.2919        
REMARK   3    22  3.3787 -  3.3268    1.00     1326   161  0.2304 0.3257        
REMARK   3    23  3.3268 -  3.2778    1.00     1282   146  0.2374 0.3297        
REMARK   3    24  3.2778 -  3.2317    1.00     1293   141  0.2341 0.3298        
REMARK   3    25  3.2317 -  3.1880    1.00     1341   143  0.2523 0.2998        
REMARK   3    26  3.1880 -  3.1466    1.00     1298   132  0.2606 0.3306        
REMARK   3    27  3.1466 -  3.1073    0.99     1260   154  0.2632 0.3675        
REMARK   3    28  3.1073 -  3.0699    0.98     1294   171  0.2648 0.3465        
REMARK   3    29  3.0699 -  3.0342    0.95     1237   146  0.2884 0.3550        
REMARK   3    30  3.0342 -  3.0001    0.92     1192   127  0.2752 0.3272        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.33                                          
REMARK   3   B_SOL              : 25.48                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.440            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.490           
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) : 23.58240                                             
REMARK   3    B22 (A**2) : -9.51320                                             
REMARK   3    B33 (A**2) : -14.06920                                            
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : -0.00000                                             
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      :  0.004          14288                                  
REMARK   3   ANGLE     :  0.759          19505                                  
REMARK   3   CHIRALITY :  0.050           2169                                  
REMARK   3   PLANARITY :  0.003           2562                                  
REMARK   3   DIHEDRAL  : 15.078           5135                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 3ALQ COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-AUG-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB029405.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-MAR-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45945                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.950                              
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     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.18300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.7500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.60300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.510                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 2E7A                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.68                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
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                                                                      
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       37.23500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      123.41750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       58.67800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      123.41750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.23500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       58.67800            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14240 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 41620 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, S, T, R                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14280 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 41460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, F, E, V, W, U                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     VAL A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     ARG A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     PRO A     8                                                      
REMARK 465     ARG A   103                                                      
REMARK 465     GLU A   104                                                      
REMARK 465     THR A   105                                                      
REMARK 465     PRO A   106                                                      
REMARK 465     GLU A   107                                                      
REMARK 465     GLY A   108                                                      
REMARK 465     ALA A   109                                                      
REMARK 465     GLU A   110                                                      
REMARK 465     VAL B     1                                                      
REMARK 465     ARG B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     ARG B     6                                                      
REMARK 465     THR B     7                                                      
REMARK 465     PRO B     8                                                      
REMARK 465     ARG B   103                                                      
REMARK 465     GLU B   104                                                      
REMARK 465     THR B   105                                                      
REMARK 465     PRO B   106                                                      
REMARK 465     GLU B   107                                                      
REMARK 465     GLY B   108                                                      
REMARK 465     ALA B   109                                                      
REMARK 465     GLU B   110                                                      
REMARK 465     VAL C     1                                                      
REMARK 465     ARG C     2                                                      
REMARK 465     SER C     3                                                      
REMARK 465     SER C     4                                                      
REMARK 465     SER C     5                                                      
REMARK 465     ARG C     6                                                      
REMARK 465     THR C     7                                                      
REMARK 465     PRO C     8                                                      
REMARK 465     ARG C   103                                                      
REMARK 465     GLU C   104                                                      
REMARK 465     THR C   105                                                      
REMARK 465     PRO C   106                                                      
REMARK 465     GLU C   107                                                      
REMARK 465     GLY C   108                                                      
REMARK 465     ALA C   109                                                      
REMARK 465     GLU C   110                                                      
REMARK 465     VAL D     1                                                      
REMARK 465     ARG D     2                                                      
REMARK 465     SER D     3                                                      
REMARK 465     SER D     4                                                      
REMARK 465     SER D     5                                                      
REMARK 465     ARG D     6                                                      
REMARK 465     THR D     7                                                      
REMARK 465     PRO D     8                                                      
REMARK 465     ARG D   103                                                      
REMARK 465     GLU D   104                                                      
REMARK 465     THR D   105                                                      
REMARK 465     PRO D   106                                                      
REMARK 465     GLU D   107                                                      
REMARK 465     GLY D   108                                                      
REMARK 465     ALA D   109                                                      
REMARK 465     GLU D   110                                                      
REMARK 465     VAL E     1                                                      
REMARK 465     ARG E     2                                                      
REMARK 465     SER E     3                                                      
REMARK 465     SER E     4                                                      
REMARK 465     SER E     5                                                      
REMARK 465     ARG E     6                                                      
REMARK 465     THR E     7                                                      
REMARK 465     PRO E     8                                                      
REMARK 465     ARG E   103                                                      
REMARK 465     GLU E   104                                                      
REMARK 465     THR E   105                                                      
REMARK 465     PRO E   106                                                      
REMARK 465     GLU E   107                                                      
REMARK 465     GLY E   108                                                      
REMARK 465     ALA E   109                                                      
REMARK 465     GLU E   110                                                      
REMARK 465     VAL F     1                                                      
REMARK 465     ARG F     2                                                      
REMARK 465     SER F     3                                                      
REMARK 465     SER F     4                                                      
REMARK 465     SER F     5                                                      
REMARK 465     ARG F     6                                                      
REMARK 465     THR F     7                                                      
REMARK 465     PRO F     8                                                      
REMARK 465     ARG F   103                                                      
REMARK 465     GLU F   104                                                      
REMARK 465     THR F   105                                                      
REMARK 465     PRO F   106                                                      
REMARK 465     GLU F   107                                                      
REMARK 465     GLY F   108                                                      
REMARK 465     ALA F   109                                                      
REMARK 465     GLU F   110                                                      
REMARK 465     ALA R    11                                                      
REMARK 465     PRO R    12                                                      
REMARK 465     GLU R    13                                                      
REMARK 465     PRO R    14                                                      
REMARK 465     GLY R    15                                                      
REMARK 465     SER R    16                                                      
REMARK 465     THR R   179                                                      
REMARK 465     SER R   180                                                      
REMARK 465     THR R   181                                                      
REMARK 465     SER R   182                                                      
REMARK 465     PRO R   183                                                      
REMARK 465     ALA S    11                                                      
REMARK 465     PRO S    12                                                      
REMARK 465     GLU S    13                                                      
REMARK 465     PRO S    14                                                      
REMARK 465     THR S   179                                                      
REMARK 465     SER S   180                                                      
REMARK 465     THR S   181                                                      
REMARK 465     SER S   182                                                      
REMARK 465     PRO S   183                                                      
REMARK 465     ALA T    11                                                      
REMARK 465     PRO T    12                                                      
REMARK 465     GLU T    13                                                      
REMARK 465     PRO T    14                                                      
REMARK 465     GLY T    15                                                      
REMARK 465     SER T    16                                                      
REMARK 465     THR T   179                                                      
REMARK 465     SER T   180                                                      
REMARK 465     THR T   181                                                      
REMARK 465     SER T   182                                                      
REMARK 465     PRO T   183                                                      
REMARK 465     ALA U    11                                                      
REMARK 465     PRO U    12                                                      
REMARK 465     GLU U    13                                                      
REMARK 465     PRO U    14                                                      
REMARK 465     GLY U    15                                                      
REMARK 465     SER U    16                                                      
REMARK 465     THR U    17                                                      
REMARK 465     THR U   179                                                      
REMARK 465     SER U   180                                                      
REMARK 465     THR U   181                                                      
REMARK 465     SER U   182                                                      
REMARK 465     PRO U   183                                                      
REMARK 465     ALA V    11                                                      
REMARK 465     PRO V    12                                                      
REMARK 465     GLU V    13                                                      
REMARK 465     PRO V    14                                                      
REMARK 465     GLY V    15                                                      
REMARK 465     SER V    16                                                      
REMARK 465     THR V    17                                                      
REMARK 465     THR V   179                                                      
REMARK 465     SER V   180                                                      
REMARK 465     THR V   181                                                      
REMARK 465     SER V   182                                                      
REMARK 465     PRO V   183                                                      
REMARK 465     ALA W    11                                                      
REMARK 465     PRO W    12                                                      
REMARK 465     GLU W    13                                                      
REMARK 465     PRO W    14                                                      
REMARK 465     GLY W    15                                                      
REMARK 465     SER W    16                                                      
REMARK 465     THR W   179                                                      
REMARK 465     SER W   180                                                      
REMARK 465     THR W   181                                                      
REMARK 465     SER W   182                                                      
REMARK 465     PRO W   183                                                      
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    TYR A  87       80.67   -168.33                                   
REMARK 500    ALA B  22       49.46   -106.13                                   
REMARK 500    TYR B  87       82.07   -165.55                                   
REMARK 500    ALA C  22       59.72    -64.92                                   
REMARK 500    ARG C  31       47.97    -72.69                                   
REMARK 500    ASP C  45       48.19     39.91                                   
REMARK 500    SER C  60      136.96   -173.20                                   
REMARK 500    PRO C  70      -99.91    -68.01                                   
REMARK 500    HIS C  73       77.44   -158.60                                   
REMARK 500    TYR C  87       85.36   -174.06                                   
REMARK 500    LEU D  37       88.53   -170.24                                   
REMARK 500    PRO D  51      -70.53    -70.91                                   
REMARK 500    PRO D  70      169.75    -46.87                                   
REMARK 500    SER D  71       -6.18    -59.21                                   
REMARK 500    ALA D 145      -73.60    -35.62                                   
REMARK 500    LEU E  37       98.91   -173.01                                   
REMARK 500    SER E  60      145.71   -172.06                                   
REMARK 500    TYR E  87       93.78   -166.51                                   
REMARK 500    ASN F  30      -25.64   -142.73                                   
REMARK 500    ARG F  31       49.70    -75.58                                   
REMARK 500    LEU F  37       96.99   -174.97                                   
REMARK 500    PRO F  70      -80.07    -59.68                                   
REMARK 500    ARG F 138       77.24   -117.33                                   
REMARK 500    GLN R  29       60.01     62.55                                   
REMARK 500    MET R  30      168.24    179.71                                   
REMARK 500    GLU R  57     -155.70    -91.45                                   
REMARK 500    TRP R  67       48.00   -147.58                                   
REMARK 500    THR R  89     -164.66   -119.38                                   
REMARK 500    ARG R 122     -178.54    -66.01                                   
REMARK 500    VAL R 127       98.46    -68.59                                   
REMARK 500    ALA R 128      -73.70    -57.52                                   
REMARK 500    PRO R 130     -153.46    -82.84                                   
REMARK 500    THR R 132       20.41    -68.09                                   
REMARK 500    GLU R 133      -86.00    -94.97                                   
REMARK 500    THR R 134       33.15   -140.59                                   
REMARK 500    SER R 148      106.85   -167.28                                   
REMARK 500    ASN R 149       36.52    -88.67                                   
REMARK 500    THR R 154      -54.52   -123.75                                   
REMARK 500    CYS R 157       92.61    -65.30                                   
REMARK 500    ALA R 167      -85.02    -87.71                                   
REMARK 500    PRO R 169     -175.52    -55.46                                   
REMARK 500    ARG S  19      161.22    -46.61                                   
REMARK 500    THR S  48      -62.67    -97.82                                   
REMARK 500    GLU S  57     -131.02    -99.68                                   
REMARK 500    TRP S  67       48.69   -143.81                                   
REMARK 500    GLN S  86      117.69   -165.35                                   
REMARK 500    THR S  89     -167.34   -117.76                                   
REMARK 500    ARG S 122     -179.39    -62.93                                   
REMARK 500    PRO S 130      176.37    -55.72                                   
REMARK 500    ASP S 136     -175.47    -66.24                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      89 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CO R   2  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP R  54   OD1                                                    
REMARK 620 2 HIS R  40   NE2  78.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CO S   1  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS S  40   NE2                                                    
REMARK 620 2 ASP S  54   OD1 105.0                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CO U   4  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS U  40   NE2                                                    
REMARK 620 2 ASP U  54   OD1 108.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CO T   3  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP T  54   OD1                                                    
REMARK 620 2 HIS T  40   NE2  92.3                                              
REMARK 620 3 GLU T  57   OE2  61.6 131.2                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CO V   5  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS V  40   NE2                                                    
REMARK 620 2 ASP V  54   OD1 109.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CO W   6  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP W  54   OD1                                                    
REMARK 620 2 HIS W  40   NE2  86.7                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO R 2                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO S 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO T 3                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO U 4                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO V 5                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO W 6                    
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1TNR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1TNF   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2E7A   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2ZJC   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2ZPX   RELATED DB: PDB                                   
DBREF  3ALQ A    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  3ALQ B    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  3ALQ C    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  3ALQ D    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  3ALQ E    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  3ALQ F    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  3ALQ R   11   183  UNP    P20333   TNR1B_HUMAN     33    205             
DBREF  3ALQ S   11   183  UNP    P20333   TNR1B_HUMAN     33    205             
DBREF  3ALQ T   11   183  UNP    P20333   TNR1B_HUMAN     33    205             
DBREF  3ALQ U   11   183  UNP    P20333   TNR1B_HUMAN     33    205             
DBREF  3ALQ V   11   183  UNP    P20333   TNR1B_HUMAN     33    205             
DBREF  3ALQ W   11   183  UNP    P20333   TNR1B_HUMAN     33    205             
SEQADV 3ALQ MET A   11  UNP  P01375    LYS    87 ENGINEERED MUTATION            
SEQADV 3ALQ SER A   65  UNP  P01375    LYS   141 ENGINEERED MUTATION            
SEQADV 3ALQ PRO A   90  UNP  P01375    LYS   166 ENGINEERED MUTATION            
SEQADV 3ALQ ARG A   98  UNP  P01375    LYS   174 ENGINEERED MUTATION            
SEQADV 3ALQ ASN A  112  UNP  P01375    LYS   188 ENGINEERED MUTATION            
SEQADV 3ALQ PRO A  128  UNP  P01375    LYS   204 ENGINEERED MUTATION            
SEQADV 3ALQ MET B   11  UNP  P01375    LYS    87 ENGINEERED MUTATION            
SEQADV 3ALQ SER B   65  UNP  P01375    LYS   141 ENGINEERED MUTATION            
SEQADV 3ALQ PRO B   90  UNP  P01375    LYS   166 ENGINEERED MUTATION            
SEQADV 3ALQ ARG B   98  UNP  P01375    LYS   174 ENGINEERED MUTATION            
SEQADV 3ALQ ASN B  112  UNP  P01375    LYS   188 ENGINEERED MUTATION            
SEQADV 3ALQ PRO B  128  UNP  P01375    LYS   204 ENGINEERED MUTATION            
SEQADV 3ALQ MET C   11  UNP  P01375    LYS    87 ENGINEERED MUTATION            
SEQADV 3ALQ SER C   65  UNP  P01375    LYS   141 ENGINEERED MUTATION            
SEQADV 3ALQ PRO C   90  UNP  P01375    LYS   166 ENGINEERED MUTATION            
SEQADV 3ALQ ARG C   98  UNP  P01375    LYS   174 ENGINEERED MUTATION            
SEQADV 3ALQ ASN C  112  UNP  P01375    LYS   188 ENGINEERED MUTATION            
SEQADV 3ALQ PRO C  128  UNP  P01375    LYS   204 ENGINEERED MUTATION            
SEQADV 3ALQ MET D   11  UNP  P01375    LYS    87 ENGINEERED MUTATION            
SEQADV 3ALQ SER D   65  UNP  P01375    LYS   141 ENGINEERED MUTATION            
SEQADV 3ALQ PRO D   90  UNP  P01375    LYS   166 ENGINEERED MUTATION            
SEQADV 3ALQ ARG D   98  UNP  P01375    LYS   174 ENGINEERED MUTATION            
SEQADV 3ALQ ASN D  112  UNP  P01375    LYS   188 ENGINEERED MUTATION            
SEQADV 3ALQ PRO D  128  UNP  P01375    LYS   204 ENGINEERED MUTATION            
SEQADV 3ALQ MET E   11  UNP  P01375    LYS    87 ENGINEERED MUTATION            
SEQADV 3ALQ SER E   65  UNP  P01375    LYS   141 ENGINEERED MUTATION            
SEQADV 3ALQ PRO E   90  UNP  P01375    LYS   166 ENGINEERED MUTATION            
SEQADV 3ALQ ARG E   98  UNP  P01375    LYS   174 ENGINEERED MUTATION            
SEQADV 3ALQ ASN E  112  UNP  P01375    LYS   188 ENGINEERED MUTATION            
SEQADV 3ALQ PRO E  128  UNP  P01375    LYS   204 ENGINEERED MUTATION            
SEQADV 3ALQ MET F   11  UNP  P01375    LYS    87 ENGINEERED MUTATION            
SEQADV 3ALQ SER F   65  UNP  P01375    LYS   141 ENGINEERED MUTATION            
SEQADV 3ALQ PRO F   90  UNP  P01375    LYS   166 ENGINEERED MUTATION            
SEQADV 3ALQ ARG F   98  UNP  P01375    LYS   174 ENGINEERED MUTATION            
SEQADV 3ALQ ASN F  112  UNP  P01375    LYS   188 ENGINEERED MUTATION            
SEQADV 3ALQ PRO F  128  UNP  P01375    LYS   204 ENGINEERED MUTATION            
SEQRES   1 A  157  VAL ARG SER SER SER ARG THR PRO SER ASP MET PRO VAL          
SEQRES   2 A  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU          
SEQRES   3 A  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN          
SEQRES   4 A  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER          
SEQRES   5 A  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE SER          
SEQRES   6 A  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS          
SEQRES   7 A  157  THR ILE SER ARG ILE ALA VAL SER TYR GLN THR PRO VAL          
SEQRES   8 A  157  ASN LEU LEU SER ALA ILE ARG SER PRO CYS GLN ARG GLU          
SEQRES   9 A  157  THR PRO GLU GLY ALA GLU ALA ASN PRO TRP TYR GLU PRO          
SEQRES  10 A  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU PRO GLY ASP          
SEQRES  11 A  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU ASP          
SEQRES  12 A  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA          
SEQRES  13 A  157  LEU                                                          
SEQRES   1 B  157  VAL ARG SER SER SER ARG THR PRO SER ASP MET PRO VAL          
SEQRES   2 B  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU          
SEQRES   3 B  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN          
SEQRES   4 B  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER          
SEQRES   5 B  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE SER          
SEQRES   6 B  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS          
SEQRES   7 B  157  THR ILE SER ARG ILE ALA VAL SER TYR GLN THR PRO VAL          
SEQRES   8 B  157  ASN LEU LEU SER ALA ILE ARG SER PRO CYS GLN ARG GLU          
SEQRES   9 B  157  THR PRO GLU GLY ALA GLU ALA ASN PRO TRP TYR GLU PRO          
SEQRES  10 B  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU PRO GLY ASP          
SEQRES  11 B  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU ASP          
SEQRES  12 B  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA          
SEQRES  13 B  157  LEU                                                          
SEQRES   1 C  157  VAL ARG SER SER SER ARG THR PRO SER ASP MET PRO VAL          
SEQRES   2 C  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU          
SEQRES   3 C  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN          
SEQRES   4 C  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER          
SEQRES   5 C  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE SER          
SEQRES   6 C  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS          
SEQRES   7 C  157  THR ILE SER ARG ILE ALA VAL SER TYR GLN THR PRO VAL          
SEQRES   8 C  157  ASN LEU LEU SER ALA ILE ARG SER PRO CYS GLN ARG GLU          
SEQRES   9 C  157  THR PRO GLU GLY ALA GLU ALA ASN PRO TRP TYR GLU PRO          
SEQRES  10 C  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU PRO GLY ASP          
SEQRES  11 C  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU ASP          
SEQRES  12 C  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA          
SEQRES  13 C  157  LEU                                                          
SEQRES   1 D  157  VAL ARG SER SER SER ARG THR PRO SER ASP MET PRO VAL          
SEQRES   2 D  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU          
SEQRES   3 D  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN          
SEQRES   4 D  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER          
SEQRES   5 D  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE SER          
SEQRES   6 D  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS          
SEQRES   7 D  157  THR ILE SER ARG ILE ALA VAL SER TYR GLN THR PRO VAL          
SEQRES   8 D  157  ASN LEU LEU SER ALA ILE ARG SER PRO CYS GLN ARG GLU          
SEQRES   9 D  157  THR PRO GLU GLY ALA GLU ALA ASN PRO TRP TYR GLU PRO          
SEQRES  10 D  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU PRO GLY ASP          
SEQRES  11 D  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU ASP          
SEQRES  12 D  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA          
SEQRES  13 D  157  LEU                                                          
SEQRES   1 E  157  VAL ARG SER SER SER ARG THR PRO SER ASP MET PRO VAL          
SEQRES   2 E  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU          
SEQRES   3 E  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN          
SEQRES   4 E  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER          
SEQRES   5 E  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE SER          
SEQRES   6 E  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS          
SEQRES   7 E  157  THR ILE SER ARG ILE ALA VAL SER TYR GLN THR PRO VAL          
SEQRES   8 E  157  ASN LEU LEU SER ALA ILE ARG SER PRO CYS GLN ARG GLU          
SEQRES   9 E  157  THR PRO GLU GLY ALA GLU ALA ASN PRO TRP TYR GLU PRO          
SEQRES  10 E  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU PRO GLY ASP          
SEQRES  11 E  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU ASP          
SEQRES  12 E  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA          
SEQRES  13 E  157  LEU                                                          
SEQRES   1 F  157  VAL ARG SER SER SER ARG THR PRO SER ASP MET PRO VAL          
SEQRES   2 F  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU          
SEQRES   3 F  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN          
SEQRES   4 F  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER          
SEQRES   5 F  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE SER          
SEQRES   6 F  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS          
SEQRES   7 F  157  THR ILE SER ARG ILE ALA VAL SER TYR GLN THR PRO VAL          
SEQRES   8 F  157  ASN LEU LEU SER ALA ILE ARG SER PRO CYS GLN ARG GLU          
SEQRES   9 F  157  THR PRO GLU GLY ALA GLU ALA ASN PRO TRP TYR GLU PRO          
SEQRES  10 F  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU PRO GLY ASP          
SEQRES  11 F  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU ASP          
SEQRES  12 F  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA          
SEQRES  13 F  157  LEU                                                          
SEQRES   1 R  173  ALA PRO GLU PRO GLY SER THR CYS ARG LEU ARG GLU TYR          
SEQRES   2 R  173  TYR ASP GLN THR ALA GLN MET CYS CYS SER LYS CYS SER          
SEQRES   3 R  173  PRO GLY GLN HIS ALA LYS VAL PHE CYS THR LYS THR SER          
SEQRES   4 R  173  ASP THR VAL CYS ASP SER CYS GLU ASP SER THR TYR THR          
SEQRES   5 R  173  GLN LEU TRP ASN TRP VAL PRO GLU CYS LEU SER CYS GLY          
SEQRES   6 R  173  SER ARG CYS SER SER ASP GLN VAL GLU THR GLN ALA CYS          
SEQRES   7 R  173  THR ARG GLU GLN ASN ARG ILE CYS THR CYS ARG PRO GLY          
SEQRES   8 R  173  TRP TYR CYS ALA LEU SER LYS GLN GLU GLY CYS ARG LEU          
SEQRES   9 R  173  CYS ALA PRO LEU ARG LYS CYS ARG PRO GLY PHE GLY VAL          
SEQRES  10 R  173  ALA ARG PRO GLY THR GLU THR SER ASP VAL VAL CYS LYS          
SEQRES  11 R  173  PRO CYS ALA PRO GLY THR PHE SER ASN THR THR SER SER          
SEQRES  12 R  173  THR ASP ILE CYS ARG PRO HIS GLN ILE CYS ASN VAL VAL          
SEQRES  13 R  173  ALA ILE PRO GLY ASN ALA SER MET ASP ALA VAL CYS THR          
SEQRES  14 R  173  SER THR SER PRO                                              
SEQRES   1 S  173  ALA PRO GLU PRO GLY SER THR CYS ARG LEU ARG GLU TYR          
SEQRES   2 S  173  TYR ASP GLN THR ALA GLN MET CYS CYS SER LYS CYS SER          
SEQRES   3 S  173  PRO GLY GLN HIS ALA LYS VAL PHE CYS THR LYS THR SER          
SEQRES   4 S  173  ASP THR VAL CYS ASP SER CYS GLU ASP SER THR TYR THR          
SEQRES   5 S  173  GLN LEU TRP ASN TRP VAL PRO GLU CYS LEU SER CYS GLY          
SEQRES   6 S  173  SER ARG CYS SER SER ASP GLN VAL GLU THR GLN ALA CYS          
SEQRES   7 S  173  THR ARG GLU GLN ASN ARG ILE CYS THR CYS ARG PRO GLY          
SEQRES   8 S  173  TRP TYR CYS ALA LEU SER LYS GLN GLU GLY CYS ARG LEU          
SEQRES   9 S  173  CYS ALA PRO LEU ARG LYS CYS ARG PRO GLY PHE GLY VAL          
SEQRES  10 S  173  ALA ARG PRO GLY THR GLU THR SER ASP VAL VAL CYS LYS          
SEQRES  11 S  173  PRO CYS ALA PRO GLY THR PHE SER ASN THR THR SER SER          
SEQRES  12 S  173  THR ASP ILE CYS ARG PRO HIS GLN ILE CYS ASN VAL VAL          
SEQRES  13 S  173  ALA ILE PRO GLY ASN ALA SER MET ASP ALA VAL CYS THR          
SEQRES  14 S  173  SER THR SER PRO                                              
SEQRES   1 T  173  ALA PRO GLU PRO GLY SER THR CYS ARG LEU ARG GLU TYR          
SEQRES   2 T  173  TYR ASP GLN THR ALA GLN MET CYS CYS SER LYS CYS SER          
SEQRES   3 T  173  PRO GLY GLN HIS ALA LYS VAL PHE CYS THR LYS THR SER          
SEQRES   4 T  173  ASP THR VAL CYS ASP SER CYS GLU ASP SER THR TYR THR          
SEQRES   5 T  173  GLN LEU TRP ASN TRP VAL PRO GLU CYS LEU SER CYS GLY          
SEQRES   6 T  173  SER ARG CYS SER SER ASP GLN VAL GLU THR GLN ALA CYS          
SEQRES   7 T  173  THR ARG GLU GLN ASN ARG ILE CYS THR CYS ARG PRO GLY          
SEQRES   8 T  173  TRP TYR CYS ALA LEU SER LYS GLN GLU GLY CYS ARG LEU          
SEQRES   9 T  173  CYS ALA PRO LEU ARG LYS CYS ARG PRO GLY PHE GLY VAL          
SEQRES  10 T  173  ALA ARG PRO GLY THR GLU THR SER ASP VAL VAL CYS LYS          
SEQRES  11 T  173  PRO CYS ALA PRO GLY THR PHE SER ASN THR THR SER SER          
SEQRES  12 T  173  THR ASP ILE CYS ARG PRO HIS GLN ILE CYS ASN VAL VAL          
SEQRES  13 T  173  ALA ILE PRO GLY ASN ALA SER MET ASP ALA VAL CYS THR          
SEQRES  14 T  173  SER THR SER PRO                                              
SEQRES   1 U  173  ALA PRO GLU PRO GLY SER THR CYS ARG LEU ARG GLU TYR          
SEQRES   2 U  173  TYR ASP GLN THR ALA GLN MET CYS CYS SER LYS CYS SER          
SEQRES   3 U  173  PRO GLY GLN HIS ALA LYS VAL PHE CYS THR LYS THR SER          
SEQRES   4 U  173  ASP THR VAL CYS ASP SER CYS GLU ASP SER THR TYR THR          
SEQRES   5 U  173  GLN LEU TRP ASN TRP VAL PRO GLU CYS LEU SER CYS GLY          
SEQRES   6 U  173  SER ARG CYS SER SER ASP GLN VAL GLU THR GLN ALA CYS          
SEQRES   7 U  173  THR ARG GLU GLN ASN ARG ILE CYS THR CYS ARG PRO GLY          
SEQRES   8 U  173  TRP TYR CYS ALA LEU SER LYS GLN GLU GLY CYS ARG LEU          
SEQRES   9 U  173  CYS ALA PRO LEU ARG LYS CYS ARG PRO GLY PHE GLY VAL          
SEQRES  10 U  173  ALA ARG PRO GLY THR GLU THR SER ASP VAL VAL CYS LYS          
SEQRES  11 U  173  PRO CYS ALA PRO GLY THR PHE SER ASN THR THR SER SER          
SEQRES  12 U  173  THR ASP ILE CYS ARG PRO HIS GLN ILE CYS ASN VAL VAL          
SEQRES  13 U  173  ALA ILE PRO GLY ASN ALA SER MET ASP ALA VAL CYS THR          
SEQRES  14 U  173  SER THR SER PRO                                              
SEQRES   1 V  173  ALA PRO GLU PRO GLY SER THR CYS ARG LEU ARG GLU TYR          
SEQRES   2 V  173  TYR ASP GLN THR ALA GLN MET CYS CYS SER LYS CYS SER          
SEQRES   3 V  173  PRO GLY GLN HIS ALA LYS VAL PHE CYS THR LYS THR SER          
SEQRES   4 V  173  ASP THR VAL CYS ASP SER CYS GLU ASP SER THR TYR THR          
SEQRES   5 V  173  GLN LEU TRP ASN TRP VAL PRO GLU CYS LEU SER CYS GLY          
SEQRES   6 V  173  SER ARG CYS SER SER ASP GLN VAL GLU THR GLN ALA CYS          
SEQRES   7 V  173  THR ARG GLU GLN ASN ARG ILE CYS THR CYS ARG PRO GLY          
SEQRES   8 V  173  TRP TYR CYS ALA LEU SER LYS GLN GLU GLY CYS ARG LEU          
SEQRES   9 V  173  CYS ALA PRO LEU ARG LYS CYS ARG PRO GLY PHE GLY VAL          
SEQRES  10 V  173  ALA ARG PRO GLY THR GLU THR SER ASP VAL VAL CYS LYS          
SEQRES  11 V  173  PRO CYS ALA PRO GLY THR PHE SER ASN THR THR SER SER          
SEQRES  12 V  173  THR ASP ILE CYS ARG PRO HIS GLN ILE CYS ASN VAL VAL          
SEQRES  13 V  173  ALA ILE PRO GLY ASN ALA SER MET ASP ALA VAL CYS THR          
SEQRES  14 V  173  SER THR SER PRO                                              
SEQRES   1 W  173  ALA PRO GLU PRO GLY SER THR CYS ARG LEU ARG GLU TYR          
SEQRES   2 W  173  TYR ASP GLN THR ALA GLN MET CYS CYS SER LYS CYS SER          
SEQRES   3 W  173  PRO GLY GLN HIS ALA LYS VAL PHE CYS THR LYS THR SER          
SEQRES   4 W  173  ASP THR VAL CYS ASP SER CYS GLU ASP SER THR TYR THR          
SEQRES   5 W  173  GLN LEU TRP ASN TRP VAL PRO GLU CYS LEU SER CYS GLY          
SEQRES   6 W  173  SER ARG CYS SER SER ASP GLN VAL GLU THR GLN ALA CYS          
SEQRES   7 W  173  THR ARG GLU GLN ASN ARG ILE CYS THR CYS ARG PRO GLY          
SEQRES   8 W  173  TRP TYR CYS ALA LEU SER LYS GLN GLU GLY CYS ARG LEU          
SEQRES   9 W  173  CYS ALA PRO LEU ARG LYS CYS ARG PRO GLY PHE GLY VAL          
SEQRES  10 W  173  ALA ARG PRO GLY THR GLU THR SER ASP VAL VAL CYS LYS          
SEQRES  11 W  173  PRO CYS ALA PRO GLY THR PHE SER ASN THR THR SER SER          
SEQRES  12 W  173  THR ASP ILE CYS ARG PRO HIS GLN ILE CYS ASN VAL VAL          
SEQRES  13 W  173  ALA ILE PRO GLY ASN ALA SER MET ASP ALA VAL CYS THR          
SEQRES  14 W  173  SER THR SER PRO                                              
HET     CO  R   2       1                                                       
HET     CO  S   1       1                                                       
HET     CO  T   3       1                                                       
HET     CO  U   4       1                                                       
HET     CO  V   5       1                                                       
HET     CO  W   6       1                                                       
HETNAM      CO COBALT (II) ION                                                  
FORMUL  13   CO    6(CO 2+)                                                     
FORMUL  19  HOH   *11(H2 O)                                                     
HELIX    1   1 ARG A  138  LEU A  142  5                                   5    
HELIX    2   2 ARG B  138  LEU B  142  5                                   5    
HELIX    3   3 ARG C  138  LEU C  142  5                                   5    
HELIX    4   4 ARG D  138  LEU D  142  5                                   5    
HELIX    5   5 ARG E  138  LEU E  142  5                                   5    
SHEET    1   A 3 TRP A  28  LEU A  29  0                                        
SHEET    2   A 3 VAL A  13  ALA A  18 -1  N  VAL A  17   O  LEU A  29           
SHEET    3   A 3 LEU A  36  ALA A  38 -1  O  LEU A  36   N  HIS A  15           
SHEET    1   B 5 TRP A  28  LEU A  29  0                                        
SHEET    2   B 5 VAL A  13  ALA A  18 -1  N  VAL A  17   O  LEU A  29           
SHEET    3   B 5 TYR A 151  ALA A 156 -1  O  ILE A 154   N  ALA A  14           
SHEET    4   B 5 GLY A  54  GLY A  66 -1  N  TYR A  59   O  GLY A 153           
SHEET    5   B 5 TRP A 114  LEU A 126 -1  O  PHE A 124   N  TYR A  56           
SHEET    1   C 5 GLU A  42  ARG A  44  0                                        
SHEET    2   C 5 GLN A  47  VAL A  49 -1  O  VAL A  49   N  GLU A  42           
SHEET    3   C 5 ARG A 131  ILE A 136 -1  O  LEU A 132   N  LEU A  48           
SHEET    4   C 5 LEU A  76  ALA A  84 -1  N  THR A  79   O  GLU A 135           
SHEET    5   C 5 TYR A  87  ARG A  98 -1  O  ARG A  98   N  LEU A  76           
SHEET    1   D 3 TRP B  28  LEU B  29  0                                        
SHEET    2   D 3 VAL B  13  ALA B  18 -1  N  VAL B  17   O  LEU B  29           
SHEET    3   D 3 LEU B  36  ALA B  38 -1  O  LEU B  36   N  HIS B  15           
SHEET    1   E 5 TRP B  28  LEU B  29  0                                        
SHEET    2   E 5 VAL B  13  ALA B  18 -1  N  VAL B  17   O  LEU B  29           
SHEET    3   E 5 TYR B 151  ALA B 156 -1  O  PHE B 152   N  VAL B  16           
SHEET    4   E 5 GLY B  54  GLY B  66 -1  N  TYR B  59   O  GLY B 153           
SHEET    5   E 5 TRP B 114  LEU B 126 -1  O  PHE B 124   N  TYR B  56           
SHEET    1   F 5 GLU B  42  ARG B  44  0                                        
SHEET    2   F 5 GLN B  47  VAL B  49 -1  O  VAL B  49   N  GLU B  42           
SHEET    3   F 5 ARG B 131  ILE B 136 -1  O  LEU B 132   N  LEU B  48           
SHEET    4   F 5 LEU B  76  ALA B  84 -1  N  SER B  81   O  SER B 133           
SHEET    5   F 5 TYR B  87  ARG B  98 -1  O  ARG B  98   N  LEU B  76           
SHEET    1   G 3 TRP C  28  LEU C  29  0                                        
SHEET    2   G 3 VAL C  13  ALA C  18 -1  N  VAL C  17   O  LEU C  29           
SHEET    3   G 3 LEU C  36  ALA C  38 -1  O  LEU C  36   N  HIS C  15           
SHEET    1   H 5 TRP C  28  LEU C  29  0                                        
SHEET    2   H 5 VAL C  13  ALA C  18 -1  N  VAL C  17   O  LEU C  29           
SHEET    3   H 5 TYR C 151  ALA C 156 -1  O  PHE C 152   N  VAL C  16           
SHEET    4   H 5 GLY C  54  GLY C  66 -1  N  TYR C  59   O  GLY C 153           
SHEET    5   H 5 TRP C 114  LEU C 126 -1  O  GLY C 122   N  ILE C  58           
SHEET    1   I 5 GLU C  42  ARG C  44  0                                        
SHEET    2   I 5 GLN C  47  VAL C  49 -1  O  VAL C  49   N  GLU C  42           
SHEET    3   I 5 ARG C 131  ILE C 136 -1  O  LEU C 132   N  LEU C  48           
SHEET    4   I 5 LEU C  76  ALA C  84 -1  N  ILE C  83   O  ARG C 131           
SHEET    5   I 5 TYR C  87  ARG C  98 -1  O  VAL C  91   N  ARG C  82           
SHEET    1   J 3 TRP D  28  LEU D  29  0                                        
SHEET    2   J 3 VAL D  13  ALA D  18 -1  N  VAL D  17   O  LEU D  29           
SHEET    3   J 3 LEU D  36  ALA D  38 -1  O  LEU D  36   N  HIS D  15           
SHEET    1   K 5 TRP D  28  LEU D  29  0                                        
SHEET    2   K 5 VAL D  13  ALA D  18 -1  N  VAL D  17   O  LEU D  29           
SHEET    3   K 5 TYR D 151  ALA D 156 -1  O  PHE D 152   N  VAL D  16           
SHEET    4   K 5 GLY D  54  GLY D  66 -1  N  LEU D  57   O  ILE D 155           
SHEET    5   K 5 TRP D 114  LEU D 126 -1  O  GLU D 116   N  PHE D  64           
SHEET    1   L 5 GLU D  42  ARG D  44  0                                        
SHEET    2   L 5 GLN D  47  VAL D  49 -1  O  GLN D  47   N  ARG D  44           
SHEET    3   L 5 ARG D 131  ILE D 136 -1  O  LEU D 132   N  LEU D  48           
SHEET    4   L 5 LEU D  76  ILE D  83 -1  N  THR D  79   O  GLU D 135           
SHEET    5   L 5 VAL D  91  ARG D  98 -1  O  ARG D  98   N  LEU D  76           
SHEET    1   M 3 TRP E  28  LEU E  29  0                                        
SHEET    2   M 3 VAL E  13  ALA E  18 -1  N  VAL E  17   O  LEU E  29           
SHEET    3   M 3 LEU E  36  ALA E  38 -1  O  LEU E  36   N  HIS E  15           
SHEET    1   N 5 TRP E  28  LEU E  29  0                                        
SHEET    2   N 5 VAL E  13  ALA E  18 -1  N  VAL E  17   O  LEU E  29           
SHEET    3   N 5 TYR E 151  ALA E 156 -1  O  ILE E 154   N  ALA E  14           
SHEET    4   N 5 GLY E  54  GLY E  66 -1  N  TYR E  59   O  GLY E 153           
SHEET    5   N 5 TRP E 114  LEU E 126 -1  O  GLU E 116   N  PHE E  64           
SHEET    1   O 5 GLU E  42  ARG E  44  0                                        
SHEET    2   O 5 GLN E  47  VAL E  49 -1  O  GLN E  47   N  ARG E  44           
SHEET    3   O 5 ARG E 131  ILE E 136 -1  O  LEU E 132   N  LEU E  48           
SHEET    4   O 5 LEU E  76  ILE E  83 -1  N  ILE E  83   O  ARG E 131           
SHEET    5   O 5 VAL E  91  ARG E  98 -1  O  LEU E  93   N  ILE E  80           
SHEET    1   P 3 TRP F  28  LEU F  29  0                                        
SHEET    2   P 3 VAL F  13  ALA F  18 -1  N  VAL F  17   O  LEU F  29           
SHEET    3   P 3 LEU F  36  ALA F  38 -1  O  LEU F  36   N  HIS F  15           
SHEET    1   Q 5 TRP F  28  LEU F  29  0                                        
SHEET    2   Q 5 VAL F  13  ALA F  18 -1  N  VAL F  17   O  LEU F  29           
SHEET    3   Q 5 TYR F 151  ALA F 156 -1  O  PHE F 152   N  VAL F  16           
SHEET    4   Q 5 GLY F  54  GLY F  66 -1  N  LEU F  57   O  ILE F 155           
SHEET    5   Q 5 TRP F 114  LEU F 126 -1  O  GLY F 122   N  ILE F  58           
SHEET    1   R 5 GLU F  42  ARG F  44  0                                        
SHEET    2   R 5 GLN F  47  VAL F  49 -1  O  VAL F  49   N  GLU F  42           
SHEET    3   R 5 ARG F 131  ILE F 136 -1  O  LEU F 132   N  LEU F  48           
SHEET    4   R 5 LEU F  76  ILE F  83 -1  N  ILE F  83   O  ARG F 131           
SHEET    5   R 5 VAL F  91  ARG F  98 -1  O  ARG F  98   N  LEU F  76           
SHEET    1   S 2 GLU R  22  ASP R  25  0                                        
SHEET    2   S 2 MET R  30  SER R  33 -1  O  CYS R  32   N  TYR R  23           
SHEET    1   T 2 GLN R  39  VAL R  43  0                                        
SHEET    2   T 2 VAL R  52  SER R  55 -1  O  VAL R  52   N  VAL R  43           
SHEET    1   U 2 THR R  60  TYR R  61  0                                        
SHEET    2   U 2 LEU R  72  SER R  73 -1  O  LEU R  72   N  TYR R  61           
SHEET    1   V 2 GLN R  82  GLN R  86  0                                        
SHEET    2   V 2 ILE R  95  CYS R  98 -1  O  THR R  97   N  VAL R  83           
SHEET    1   W 2 TRP R 102  SER R 107  0                                        
SHEET    2   W 2 CYS R 112  PRO R 117 -1  O  ARG R 113   N  LEU R 106           
SHEET    1   X 2 PHE R 125  ARG R 129  0                                        
SHEET    2   X 2 VAL R 138  PRO R 141 -1  O  LYS R 140   N  GLY R 126           
SHEET    1   Y 2 THR R 146  PHE R 147  0                                        
SHEET    2   Y 2 ARG R 158  PRO R 159 -1  O  ARG R 158   N  PHE R 147           
SHEET    1   Z 2 GLU S  22  ASP S  25  0                                        
SHEET    2   Z 2 MET S  30  SER S  33 -1  O  CYS S  32   N  TYR S  23           
SHEET    1  AA 2 GLN S  39  VAL S  43  0                                        
SHEET    2  AA 2 VAL S  52  SER S  55 -1  O  VAL S  52   N  LYS S  42           
SHEET    1  AB 2 THR S  60  TYR S  61  0                                        
SHEET    2  AB 2 LEU S  72  SER S  73 -1  O  LEU S  72   N  TYR S  61           
SHEET    1  AC 2 GLN S  82  GLN S  86  0                                        
SHEET    2  AC 2 ILE S  95  CYS S  98 -1  O  THR S  97   N  VAL S  83           
SHEET    1  AD 2 TRP S 102  SER S 107  0                                        
SHEET    2  AD 2 CYS S 112  PRO S 117 -1  O  ALA S 116   N  TYR S 103           
SHEET    1  AE 2 PHE S 125  ARG S 129  0                                        
SHEET    2  AE 2 VAL S 138  PRO S 141 -1  O  VAL S 138   N  ALA S 128           
SHEET    1  AF 2 THR S 146  PHE S 147  0                                        
SHEET    2  AF 2 ARG S 158  PRO S 159 -1  O  ARG S 158   N  PHE S 147           
SHEET    1  AG 2 GLU T  22  ASP T  25  0                                        
SHEET    2  AG 2 MET T  30  SER T  33 -1  O  CYS T  32   N  TYR T  23           
SHEET    1  AH 2 GLN T  39  VAL T  43  0                                        
SHEET    2  AH 2 VAL T  52  SER T  55 -1  O  VAL T  52   N  VAL T  43           
SHEET    1  AI 2 THR T  60  TYR T  61  0                                        
SHEET    2  AI 2 LEU T  72  SER T  73 -1  O  LEU T  72   N  TYR T  61           
SHEET    1  AJ 2 GLN T  82  GLN T  86  0                                        
SHEET    2  AJ 2 ILE T  95  CYS T  98 -1  O  THR T  97   N  VAL T  83           
SHEET    1  AK 2 TRP T 102  LYS T 108  0                                        
SHEET    2  AK 2 GLY T 111  PRO T 117 -1  O  ALA T 116   N  TYR T 103           
SHEET    1  AL 2 PHE T 125  ARG T 129  0                                        
SHEET    2  AL 2 VAL T 138  PRO T 141 -1  O  LYS T 140   N  GLY T 126           
SHEET    1  AM 2 THR T 146  PHE T 147  0                                        
SHEET    2  AM 2 ARG T 158  PRO T 159 -1  O  ARG T 158   N  PHE T 147           
SHEET    1  AN 2 GLU U  22  ASP U  25  0                                        
SHEET    2  AN 2 MET U  30  SER U  33 -1  O  CYS U  32   N  TYR U  23           
SHEET    1  AO 2 GLN U  39  VAL U  43  0                                        
SHEET    2  AO 2 VAL U  52  SER U  55 -1  O  VAL U  52   N  VAL U  43           
SHEET    1  AP 2 THR U  60  TYR U  61  0                                        
SHEET    2  AP 2 LEU U  72  SER U  73 -1  O  LEU U  72   N  TYR U  61           
SHEET    1  AQ 2 GLN U  82  GLN U  86  0                                        
SHEET    2  AQ 2 ILE U  95  CYS U  98 -1  O  THR U  97   N  VAL U  83           
SHEET    1  AR 2 TRP U 102  SER U 107  0                                        
SHEET    2  AR 2 CYS U 112  PRO U 117 -1  O  ARG U 113   N  LEU U 106           
SHEET    1  AS 2 PHE U 125  ARG U 129  0                                        
SHEET    2  AS 2 VAL U 138  PRO U 141 -1  O  VAL U 138   N  ALA U 128           
SHEET    1  AT 2 THR U 146  PHE U 147  0                                        
SHEET    2  AT 2 ARG U 158  PRO U 159 -1  O  ARG U 158   N  PHE U 147           
SHEET    1  AU 2 GLU V  22  ASP V  25  0                                        
SHEET    2  AU 2 MET V  30  SER V  33 -1  O  CYS V  32   N  TYR V  23           
SHEET    1  AV 2 GLN V  39  VAL V  43  0                                        
SHEET    2  AV 2 VAL V  52  SER V  55 -1  O  VAL V  52   N  VAL V  43           
SHEET    1  AW 2 THR V  60  TYR V  61  0                                        
SHEET    2  AW 2 LEU V  72  SER V  73 -1  O  LEU V  72   N  TYR V  61           
SHEET    1  AX 2 GLN V  82  GLN V  86  0                                        
SHEET    2  AX 2 ILE V  95  CYS V  98 -1  O  THR V  97   N  VAL V  83           
SHEET    1  AY 2 TRP V 102  SER V 107  0                                        
SHEET    2  AY 2 CYS V 112  PRO V 117 -1  O  ARG V 113   N  LEU V 106           
SHEET    1  AZ 2 PHE V 125  ARG V 129  0                                        
SHEET    2  AZ 2 VAL V 138  PRO V 141 -1  O  LYS V 140   N  GLY V 126           
SHEET    1  BA 2 THR V 146  PHE V 147  0                                        
SHEET    2  BA 2 ARG V 158  PRO V 159 -1  O  ARG V 158   N  PHE V 147           
SHEET    1  BB 2 GLU W  22  ASP W  25  0                                        
SHEET    2  BB 2 MET W  30  SER W  33 -1  O  MET W  30   N  ASP W  25           
SHEET    1  BC 2 GLN W  39  VAL W  43  0                                        
SHEET    2  BC 2 VAL W  52  SER W  55 -1  O  ASP W  54   N  HIS W  40           
SHEET    1  BD 2 THR W  60  TYR W  61  0                                        
SHEET    2  BD 2 LEU W  72  SER W  73 -1  O  LEU W  72   N  TYR W  61           
SHEET    1  BE 2 GLN W  82  GLN W  86  0                                        
SHEET    2  BE 2 ILE W  95  CYS W  98 -1  O  THR W  97   N  VAL W  83           
SHEET    1  BF 2 TRP W 102  SER W 107  0                                        
SHEET    2  BF 2 CYS W 112  PRO W 117 -1  O  ALA W 116   N  TYR W 103           
SHEET    1  BG 2 PHE W 125  ARG W 129  0                                        
SHEET    2  BG 2 VAL W 138  PRO W 141 -1  O  VAL W 138   N  ARG W 129           
SHEET    1  BH 2 THR W 146  PHE W 147  0                                        
SHEET    2  BH 2 ARG W 158  PRO W 159 -1  O  ARG W 158   N  PHE W 147           
SSBOND   1 CYS A   69    CYS A  101                          1555   1555  2.03  
SSBOND   2 CYS B   69    CYS B  101                          1555   1555  2.04  
SSBOND   3 CYS C   69    CYS C  101                          1555   1555  2.03  
SSBOND   4 CYS D   69    CYS D  101                          1555   1555  2.03  
SSBOND   5 CYS E   69    CYS E  101                          1555   1555  2.03  
SSBOND   6 CYS F   69    CYS F  101                          1555   1555  2.03  
SSBOND   7 CYS R   18    CYS R   31                          1555   1555  2.04  
SSBOND   8 CYS R   32    CYS R   45                          1555   1555  2.03  
SSBOND   9 CYS R   35    CYS R   53                          1555   1555  2.05  
SSBOND  10 CYS R   56    CYS R   71                          1555   1555  2.04  
SSBOND  11 CYS R   74    CYS R   88                          1555   1555  2.03  
SSBOND  12 CYS R   78    CYS R   96                          1555   1555  2.04  
SSBOND  13 CYS R   98    CYS R  115                          1555   1555  2.03  
SSBOND  14 CYS R  104    CYS R  112                          1555   1555  2.04  
SSBOND  15 CYS R  121    CYS R  139                          1555   1555  2.03  
SSBOND  16 CYS R  142    CYS R  157                          1555   1555  2.03  
SSBOND  17 CYS R  163    CYS R  178                          1555   1555  2.04  
SSBOND  18 CYS S   18    CYS S   31                          1555   1555  2.03  
SSBOND  19 CYS S   32    CYS S   45                          1555   1555  2.03  
SSBOND  20 CYS S   35    CYS S   53                          1555   1555  2.03  
SSBOND  21 CYS S   56    CYS S   71                          1555   1555  2.04  
SSBOND  22 CYS S   74    CYS S   88                          1555   1555  2.04  
SSBOND  23 CYS S   78    CYS S   96                          1555   1555  2.03  
SSBOND  24 CYS S   98    CYS S  115                          1555   1555  2.04  
SSBOND  25 CYS S  104    CYS S  112                          1555   1555  2.03  
SSBOND  26 CYS S  121    CYS S  139                          1555   1555  2.04  
SSBOND  27 CYS S  142    CYS S  157                          1555   1555  2.03  
SSBOND  28 CYS S  163    CYS S  178                          1555   1555  2.02  
SSBOND  29 CYS T   18    CYS T   31                          1555   1555  2.04  
SSBOND  30 CYS T   32    CYS T   45                          1555   1555  2.03  
SSBOND  31 CYS T   35    CYS T   53                          1555   1555  2.04  
SSBOND  32 CYS T   56    CYS T   71                          1555   1555  2.03  
SSBOND  33 CYS T   74    CYS T   88                          1555   1555  2.04  
SSBOND  34 CYS T   78    CYS T   96                          1555   1555  2.04  
SSBOND  35 CYS T   98    CYS T  115                          1555   1555  2.03  
SSBOND  36 CYS T  104    CYS T  112                          1555   1555  2.03  
SSBOND  37 CYS T  121    CYS T  139                          1555   1555  2.03  
SSBOND  38 CYS T  142    CYS T  157                          1555   1555  2.03  
SSBOND  39 CYS T  163    CYS T  178                          1555   1555  2.02  
SSBOND  40 CYS U   18    CYS U   31                          1555   1555  2.03  
SSBOND  41 CYS U   32    CYS U   45                          1555   1555  2.03  
SSBOND  42 CYS U   35    CYS U   53                          1555   1555  2.05  
SSBOND  43 CYS U   56    CYS U   71                          1555   1555  2.04  
SSBOND  44 CYS U   74    CYS U   88                          1555   1555  2.02  
SSBOND  45 CYS U   78    CYS U   96                          1555   1555  2.03  
SSBOND  46 CYS U   98    CYS U  115                          1555   1555  2.03  
SSBOND  47 CYS U  104    CYS U  112                          1555   1555  2.04  
SSBOND  48 CYS U  121    CYS U  139                          1555   1555  2.04  
SSBOND  49 CYS U  142    CYS U  157                          1555   1555  2.05  
SSBOND  50 CYS U  163    CYS U  178                          1555   1555  2.04  
SSBOND  51 CYS V   18    CYS V   31                          1555   1555  2.03  
SSBOND  52 CYS V   32    CYS V   45                          1555   1555  2.03  
SSBOND  53 CYS V   35    CYS V   53                          1555   1555  2.04  
SSBOND  54 CYS V   56    CYS V   71                          1555   1555  2.04  
SSBOND  55 CYS V   74    CYS V   88                          1555   1555  2.04  
SSBOND  56 CYS V   78    CYS V   96                          1555   1555  2.04  
SSBOND  57 CYS V   98    CYS V  115                          1555   1555  2.04  
SSBOND  58 CYS V  104    CYS V  112                          1555   1555  2.03  
SSBOND  59 CYS V  121    CYS V  139                          1555   1555  2.03  
SSBOND  60 CYS V  142    CYS V  157                          1555   1555  2.04  
SSBOND  61 CYS V  163    CYS V  178                          1555   1555  2.04  
SSBOND  62 CYS W   18    CYS W   31                          1555   1555  2.04  
SSBOND  63 CYS W   32    CYS W   45                          1555   1555  2.04  
SSBOND  64 CYS W   35    CYS W   53                          1555   1555  2.04  
SSBOND  65 CYS W   56    CYS W   71                          1555   1555  2.04  
SSBOND  66 CYS W   74    CYS W   88                          1555   1555  2.02  
SSBOND  67 CYS W   78    CYS W   96                          1555   1555  2.04  
SSBOND  68 CYS W   98    CYS W  115                          1555   1555  2.03  
SSBOND  69 CYS W  104    CYS W  112                          1555   1555  2.04  
SSBOND  70 CYS W  121    CYS W  139                          1555   1555  2.03  
SSBOND  71 CYS W  142    CYS W  157                          1555   1555  2.04  
SSBOND  72 CYS W  163    CYS W  178                          1555   1555  2.02  
LINK         OD1 ASP R  54                CO    CO R   2     1555   1555  2.14  
LINK         NE2 HIS S  40                CO    CO S   1     1555   1555  2.17  
LINK         NE2 HIS U  40                CO    CO U   4     1555   1555  2.19  
LINK         OD1 ASP S  54                CO    CO S   1     1555   1555  2.25  
LINK         OD1 ASP T  54                CO    CO T   3     1555   1555  2.28  
LINK         NE2 HIS R  40                CO    CO R   2     1555   1555  2.31  
LINK         NE2 HIS V  40                CO    CO V   5     1555   1555  2.31  
LINK         OD1 ASP W  54                CO    CO W   6     1555   1555  2.36  
LINK         NE2 HIS T  40                CO    CO T   3     1555   1555  2.37  
LINK         NE2 HIS W  40                CO    CO W   6     1555   1555  2.44  
LINK         OD1 ASP U  54                CO    CO U   4     1555   1555  2.47  
LINK         OE2 GLU T  57                CO    CO T   3     1555   1555  2.75  
LINK         OD1 ASP V  54                CO    CO V   5     1555   1555  2.77  
SITE     1 AC1  3 HIS R  40  ASP R  54  GLU R  57                               
SITE     1 AC2  3 HIS S  40  ASP S  54  GLU S  57                               
SITE     1 AC3  3 HIS T  40  ASP T  54  GLU T  57                               
SITE     1 AC4  2 HIS U  40  ASP U  54                                          
SITE     1 AC5  2 HIS V  40  ASP V  54                                          
SITE     1 AC6  3 HIS W  40  ASP W  54  GLU W  57                               
CRYST1   74.470  117.356  246.835  90.00  90.00  90.00 P 21 21 21   24          
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      0.013428  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008521  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004051        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system