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Database: PDB
Entry: 4C2D
LinkDB: 4C2D
Original site: 4C2D 
HEADER    HYDROLASE/PEPTIDE                       17-AUG-13   4C2D              
TITLE     CRYSTAL STRUCTURE OF THE PROTEASE CTPB IN AN ACTIVE STATE             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CARBOXY-TERMINAL PROCESSING PROTEASE CTPB;                 
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: RESIDUES 44-480;                                           
COMPND   5 SYNONYM: C-TERMINAL PROCESSING PROTEASE, CTPB;                       
COMPND   6 EC: 3.4.21.102;                                                      
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: PEPTIDE1;                                                  
COMPND  10 CHAIN: E, F, G, H;                                                   
COMPND  11 OTHER_DETAILS: PEPTIDE CO-PURIFIED FROM E. COLI EXPRESSION;          
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: PEPTIDE2;                                                  
COMPND  14 CHAIN: M;                                                            
COMPND  15 OTHER_DETAILS: PEPTIDE CO-PURIFIED FROM E. COLI EXPRESSION;          
COMPND  16 MOL_ID: 4;                                                           
COMPND  17 MOLECULE: PEPTIDE2;                                                  
COMPND  18 CHAIN: N, O, P;                                                      
COMPND  19 OTHER_DETAILS: PEPTIDE CO-PURIFIED FROM E. COLI EXPRESSION           
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS SUBSP. SUBTILIS STR. 168;     
SOURCE   3 ORGANISM_TAXID: 224308;                                              
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET21;                                    
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  11 ORGANISM_TAXID: 511693;                                              
SOURCE  12 STRAIN: BL21;                                                        
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  15 ORGANISM_TAXID: 511693;                                              
SOURCE  16 STRAIN: BL21;                                                        
SOURCE  17 MOL_ID: 4;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  19 ORGANISM_TAXID: 511693;                                              
SOURCE  20 STRAIN: BL21                                                         
KEYWDS    HYDROLASE-PEPTIDE COMPLEX, PROTEOLYTIC TUNNEL                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.MASTNY,A.HEUCK,R.KURZBAUER,T.CLAUSEN                                
REVDAT   1   04-DEC-13 4C2D    0                                                
JRNL        AUTH   M.MASTNY,A.HEUCK,R.KURZBAUER,A.HEIDUK,P.BOISGUERIN,          
JRNL        AUTH 2 R.VOLKMER,M.EHRMANN,C.D.A.RODRIGUES,D.Z.RUDNER,T.CLAUSEN     
JRNL        TITL   CTPB ASSEMBLES A GATED PROTEASE TUNNEL REGULATING CELL-CELL  
JRNL        TITL 2 SIGNALING DURING SPORE FORMATION IN BACILLUS SUBTILIS.       
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 155   647 2013              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   24243021                                                     
JRNL        DOI    10.1016/J.CELL.2013.09.050                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.7                            
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.0                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000                          
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 70464                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.2271                          
REMARK   3   FREE R VALUE                     : 0.2413                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 3533                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13079                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 274                                     
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) : -1.358                                               
REMARK   3    B22 (A**2) : -14.798                                              
REMARK   3    B33 (A**2) : 16.156                                               
REMARK   3    B12 (A**2) : 0.000                                                
REMARK   3    B13 (A**2) : 1.597                                                
REMARK   3    B23 (A**2) : 0.000                                                
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.14                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : N/A                                       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) :  NULL ;  NULL                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) :  NULL ;  NULL                
REMARK   3   SIDE-CHAIN BOND              (A**2) :  NULL ;  NULL                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) :  NULL ;  NULL                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.33                                                 
REMARK   3   BSOL        : 60.6378                                              
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) :  NULL ;  NULL                
REMARK   3   GROUP  1  B-FACTOR           (A**2) :  NULL ;  NULL                
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4C2D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-AUG-13.                  
REMARK 100 THE PDBE ID CODE IS EBI-58060.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 79111                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.60                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -10.0                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.8                                
REMARK 200  R MERGE                    (I) : 0.14                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.60                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.6                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.81                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.10                               
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: PDB ENTRY 4C2C                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 13% PEG 3350, 0.1 M NA-MALONATE,         
REMARK 280   0.1 M HEPES PH 7.8                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       32.68750            
REMARK 290   SMTRY3   2  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: 8220 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 43770 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.7 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F, M, N                      
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: 7000 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 39540 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.6 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, G, H, O, P                      
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     MET A    43                                                      
REMARK 465     ALA A    44                                                      
REMARK 465     ASP A    45                                                      
REMARK 465     ASN A   480                                                      
REMARK 465     LEU A   481                                                      
REMARK 465     GLU A   482                                                      
REMARK 465     HIS A   483                                                      
REMARK 465     HIS A   484                                                      
REMARK 465     HIS A   485                                                      
REMARK 465     HIS A   486                                                      
REMARK 465     HIS A   487                                                      
REMARK 465     HIS A   488                                                      
REMARK 465     MET B    43                                                      
REMARK 465     ALA B    44                                                      
REMARK 465     ASP B    45                                                      
REMARK 465     ASN B   480                                                      
REMARK 465     LEU B   481                                                      
REMARK 465     GLU B   482                                                      
REMARK 465     HIS B   483                                                      
REMARK 465     HIS B   484                                                      
REMARK 465     HIS B   485                                                      
REMARK 465     HIS B   486                                                      
REMARK 465     HIS B   487                                                      
REMARK 465     HIS B   488                                                      
REMARK 465     MET C    43                                                      
REMARK 465     ALA C    44                                                      
REMARK 465     ASP C    45                                                      
REMARK 465     ASN C   480                                                      
REMARK 465     LEU C   481                                                      
REMARK 465     GLU C   482                                                      
REMARK 465     HIS C   483                                                      
REMARK 465     HIS C   484                                                      
REMARK 465     HIS C   485                                                      
REMARK 465     HIS C   486                                                      
REMARK 465     HIS C   487                                                      
REMARK 465     HIS C   488                                                      
REMARK 465     MET D    43                                                      
REMARK 465     ALA D    44                                                      
REMARK 465     ASP D    45                                                      
REMARK 465     SER D   109                                                      
REMARK 465     SER D   110                                                      
REMARK 465     PHE D   111                                                      
REMARK 465     GLU D   112                                                      
REMARK 465     GLY D   113                                                      
REMARK 465     ILE D   114                                                      
REMARK 465     GLY D   115                                                      
REMARK 465     ALA D   116                                                      
REMARK 465     GLU D   117                                                      
REMARK 465     VAL D   118                                                      
REMARK 465     GLY D   119                                                      
REMARK 465     MET D   120                                                      
REMARK 465     GLU D   121                                                      
REMARK 465     ASP D   122                                                      
REMARK 465     GLY D   123                                                      
REMARK 465     LYS D   124                                                      
REMARK 465     ILE D   125                                                      
REMARK 465     ILE D   126                                                      
REMARK 465     ILE D   127                                                      
REMARK 465     VAL D   128                                                      
REMARK 465     SER D   129                                                      
REMARK 465     PRO D   130                                                      
REMARK 465     PHE D   131                                                      
REMARK 465     LYS D   132                                                      
REMARK 465     LYS D   133                                                      
REMARK 465     SER D   134                                                      
REMARK 465     PRO D   135                                                      
REMARK 465     ALA D   136                                                      
REMARK 465     GLU D   137                                                      
REMARK 465     LYS D   138                                                      
REMARK 465     ALA D   139                                                      
REMARK 465     GLY D   140                                                      
REMARK 465     LEU D   141                                                      
REMARK 465     LYS D   142                                                      
REMARK 465     PRO D   143                                                      
REMARK 465     ASN D   144                                                      
REMARK 465     ASP D   145                                                      
REMARK 465     GLU D   146                                                      
REMARK 465     ILE D   147                                                      
REMARK 465     ILE D   148                                                      
REMARK 465     SER D   149                                                      
REMARK 465     ILE D   150                                                      
REMARK 465     ASN D   151                                                      
REMARK 465     GLY D   152                                                      
REMARK 465     GLU D   153                                                      
REMARK 465     SER D   154                                                      
REMARK 465     MET D   155                                                      
REMARK 465     ALA D   156                                                      
REMARK 465     GLY D   157                                                      
REMARK 465     LYS D   158                                                      
REMARK 465     ASP D   159                                                      
REMARK 465     LEU D   160                                                      
REMARK 465     ASN D   161                                                      
REMARK 465     HIS D   162                                                      
REMARK 465     ALA D   163                                                      
REMARK 465     VAL D   164                                                      
REMARK 465     LEU D   165                                                      
REMARK 465     LYS D   166                                                      
REMARK 465     ILE D   167                                                      
REMARK 465     ARG D   168                                                      
REMARK 465     GLY D   169                                                      
REMARK 465     LYS D   170                                                      
REMARK 465     LYS D   171                                                      
REMARK 465     GLY D   172                                                      
REMARK 465     SER D   173                                                      
REMARK 465     SER D   174                                                      
REMARK 465     VAL D   175                                                      
REMARK 465     SER D   176                                                      
REMARK 465     MET D   177                                                      
REMARK 465     LYS D   178                                                      
REMARK 465     ILE D   179                                                      
REMARK 465     GLN D   180                                                      
REMARK 465     ARG D   181                                                      
REMARK 465     PRO D   182                                                      
REMARK 465     GLY D   183                                                      
REMARK 465     THR D   184                                                      
REMARK 465     LYS D   185                                                      
REMARK 465     LYS D   186                                                      
REMARK 465     GLN D   187                                                      
REMARK 465     LEU D   188                                                      
REMARK 465     SER D   189                                                      
REMARK 465     PHE D   190                                                      
REMARK 465     ARG D   191                                                      
REMARK 465     ILE D   192                                                      
REMARK 465     LYS D   193                                                      
REMARK 465     ARG D   194                                                      
REMARK 465     ALA D   195                                                      
REMARK 465     GLU D   196                                                      
REMARK 465     ILE D   197                                                      
REMARK 465     PRO D   198                                                      
REMARK 465     ASN D   480                                                      
REMARK 465     LEU D   481                                                      
REMARK 465     GLU D   482                                                      
REMARK 465     HIS D   483                                                      
REMARK 465     HIS D   484                                                      
REMARK 465     HIS D   485                                                      
REMARK 465     HIS D   486                                                      
REMARK 465     HIS D   487                                                      
REMARK 465     HIS D   488                                                      
REMARK 465     ALA H     1                                                      
REMARK 465     ALA H     2                                                      
REMARK 465     PRO P     2                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     VAL A 479    CA   C    O    CB   CG1  CG2                        
REMARK 470     VAL B 479    CA   C    O    CB   CG1  CG2                        
REMARK 470     VAL C 479    CA   C    O    CB   CG1  CG2                        
REMARK 470     VAL D 479    CA   C    O    CB   CG1  CG2                        
REMARK 470     SER H   3    OG                                                  
REMARK 470     SER H   5    OG                                                  
REMARK 470     ALA H   6    CA   C    O    CB                                   
REMARK 470     THR O   4    OG1  CG2                                            
REMARK 470     GLN P   3    CG   CD   OE1  NE2                                  
REMARK 470     THR P   4    OG1  CG2                                            
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   OG   SER A    46     O    HOH A  2001              2.11            
REMARK 500   SD   MET A    95     O    HOH A  2017              2.07            
REMARK 500   OD2  ASP A   122     O    HOH A  2031              2.08            
REMARK 500   SD   MET A   177     O    HOH A  2044              2.11            
REMARK 500   OE2  GLU A   206     NZ   LYS A   208              2.15            
REMARK 500   O    VAL A   299     O    HOH A  2089              2.10            
REMARK 500   O    HIS A   323     O    HOH A  2094              2.15            
REMARK 500   NE2  HIS A   323     O    HOH A  2075              2.09            
REMARK 500   O    ASN A   360     O    HOH A  2105              2.12            
REMARK 500   OD1  ASP A   395     OH   TYR A   421              2.19            
REMARK 500   OD1  ASN A   397     ND2  ASN B   397              2.11            
REMARK 500   O    LEU A   439     O    HOH A  2112              2.00            
REMARK 500   O    ASP A   463     O    HOH A  2114              2.10            
REMARK 500   N    VAL A   479     O    HOH A  2117              2.04            
REMARK 500   OE2  GLU B    65     O    HOH B  2008              2.00            
REMARK 500   O    LEU B    84     O    HOH B  2013              2.18            
REMARK 500   NZ   LYS B    97     O    ASP B   345              2.17            
REMARK 500   O    PHE B   103     OG   SER B   106              2.02            
REMARK 500   O    ALA B   139     O    HOH B  2030              2.01            
REMARK 500   NZ   LYS B   166     O    HOH B  2034              2.17            
REMARK 500   N    LYS B   193     O    HOH B  2040              2.20            
REMARK 500   OE1  GLU B   206     NZ   LYS B   240              2.04            
REMARK 500   OE2  GLU B   206     NZ   LYS B   208              2.04            
REMARK 500   N    GLN B   276     O    HOH B  2062              2.14            
REMARK 500   O    GLN B   276     O    HOH B  2062              1.98            
REMARK 500   O    LYS B   284     O    HOH B  2064              2.18            
REMARK 500   O    LEU B   357     O    HOH B  2062              1.95            
REMARK 500   NZ   LYS B   424     O    HOH B  2086              2.19            
REMARK 500   NZ   LYS C    54     OD2  ASP D   345              2.13            
REMARK 500   OH   TYR C    59     O    HOH C  2002              2.18            
REMARK 500   NZ   LYS C   207     OE2  GLU C   464              2.17            
REMARK 500   O    ILE C   219     ND2  ASN C   252              2.19            
REMARK 500   OE1  GLN C   276     NZ   LYS C   284              2.20            
REMARK 500   NH1  ARG C   280     O    ASN D    64              2.15            
REMARK 500   O    TYR C   297     O    HOH C  2028              2.06            
REMARK 500   NE   ARG C   417     OH   TYR C   421              1.98            
REMARK 500   O    GLU C   458     OG   SER C   462              2.01            
REMARK 500   O    THR C   472     OG   SER C   476              2.18            
REMARK 500   N    TYR D    94     O    HOH D  2008              2.20            
REMARK 500   N    GLY D   255     OXT  ALA P     5              1.83            
REMARK 500   OG   SER D   309     O    ALA P     5              2.09            
REMARK 500   NE2  GLN D   377     OD1  ASP D   467              2.16            
REMARK 500   N    LEU D   386     OD1  ASN D   454              2.06            
REMARK 500   O    SER D   423     NZ   LYS D   427              2.09            
REMARK 500   O    PHE D   478     O    HOH D  2022              2.19            
REMARK 500   O    HOH A  2033     O    HOH A  2066              2.19            
REMARK 500   O    HOH B  2003     O    HOH B  2004              2.08            
REMARK 500   O    HOH B  2065     O    HOH B  2067              2.15            
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   NZ   LYS A   438     O    ARG D   280     2656     2.16            
REMARK 500   OG   SER B   462     OE1  GLN D   210     2556     1.98            
REMARK 500   OE2  GLU C   112     NZ   LYS C   285     2646     2.15            
REMARK 500   OE2  GLU C   112     OH   TYR C   287     2646     2.14            
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    MET B  83   CG  -  SD  -  CE  ANGL. DEV. =   9.6 DEGREES          
REMARK 500    MET C 431   CA  -  CB  -  CG  ANGL. DEV. =  10.3 DEGREES          
REMARK 500    MET C 431   CB  -  CG  -  SD  ANGL. DEV. =  27.3 DEGREES          
REMARK 500    LYS C 441   CD  -  CE  -  NZ  ANGL. DEV. = -23.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A 131     -174.96    -69.64                                   
REMARK 500    LYS A 133       -0.06     69.30                                   
REMARK 500    SER A 309     -115.87     49.28                                   
REMARK 500    LYS A 366      -11.15     62.57                                   
REMARK 500    GLU A 390      151.70    179.99                                   
REMARK 500    SER A 476       -7.11    -56.70                                   
REMARK 500    LYS B 133       18.69     58.12                                   
REMARK 500    PHE B 267      -52.81   -123.75                                   
REMARK 500    SER B 309     -119.11     63.11                                   
REMARK 500    LYS B 366      -18.87     69.12                                   
REMARK 500    ARG B 417      165.30    175.65                                   
REMARK 500    ALA B 429      -68.34    -95.50                                   
REMARK 500    PHE B 433      -71.22    -56.91                                   
REMARK 500    ASN B 437      159.53    173.37                                   
REMARK 500    LEU B 439      176.36    168.46                                   
REMARK 500    ASN C 144       -9.49     73.49                                   
REMARK 500    PHE C 267      -60.71   -127.36                                   
REMARK 500    SER C 309     -121.75     58.58                                   
REMARK 500    ALA C 321      -61.18   -121.30                                   
REMARK 500    LYS C 367      -63.79   -132.51                                   
REMARK 500    ASN C 398     -177.26   -172.24                                   
REMARK 500    GLN C 405      -70.24    -57.85                                   
REMARK 500    ASP C 435      -73.53    -81.22                                   
REMARK 500    LYS C 438       -1.66     76.43                                   
REMARK 500    THR C 447      -73.83    -44.99                                   
REMARK 500    GLN D  98      -70.07    -55.34                                   
REMARK 500    PHE D 267      -65.15   -131.81                                   
REMARK 500    SER D 309     -115.99     57.27                                   
REMARK 500    LYS D 366       -4.53     64.73                                   
REMARK 500    LYS D 389      -64.18   -101.38                                   
REMARK 500    PRO D 391       83.29    -69.26                                   
REMARK 500    ASP D 395       73.99     44.94                                   
REMARK 500    THR D 442      -64.45   -133.96                                   
REMARK 500    GLN O   3       67.27     62.24                                   
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 ASP B  395     MET B  396                 -142.92                    
REMARK 500 ARG B  417     GLU B  418                  146.83                    
REMARK 500 GLY C  384     PRO C  385                  148.52                    
REMARK 500 GLN D  436     ASN D  437                  140.55                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4C2C   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE PROTEASE CTPB IN AN ACTIVE                 
REMARK 900  STATE                                                               
REMARK 900 RELATED ID: 4C2E   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE PROTEASE CTPB(S309A) PRESENT               
REMARK 900  IN A RESTING STATE                                                  
REMARK 900 RELATED ID: 4C2F   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE CTPB R168A MUTANT PRESENT IN               
REMARK 900   AN ACTIVE CONFORMATION                                             
REMARK 900 RELATED ID: 4C2G   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF CTPB(S309A) IN COMPLEX WITH A                  
REMARK 900  PEPTIDE HAVING A VAL-PRO-ALA C-TERMINUS                             
REMARK 900 RELATED ID: 4C2H   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE CTPB(V118Y) MUTANT                         
DBREF  4C2D A   44   480  UNP    O35002   CTPB_BACSU      44    480             
DBREF  4C2D B   44   480  UNP    O35002   CTPB_BACSU      44    480             
DBREF  4C2D C   44   480  UNP    O35002   CTPB_BACSU      44    480             
DBREF  4C2D D   44   480  UNP    O35002   CTPB_BACSU      44    480             
DBREF  4C2D E    1     6  PDB    4C2D     4C2D             1      6             
DBREF  4C2D F    1     6  PDB    4C2D     4C2D             1      6             
DBREF  4C2D G    1     6  PDB    4C2D     4C2D             1      6             
DBREF  4C2D H    1     6  PDB    4C2D     4C2D             1      6             
DBREF  4C2D M    1     5  PDB    4C2D     4C2D             1      5             
DBREF  4C2D N    2     5  PDB    4C2D     4C2D             2      5             
DBREF  4C2D O    2     5  PDB    4C2D     4C2D             2      5             
DBREF  4C2D P    2     5  PDB    4C2D     4C2D             2      5             
SEQADV 4C2D MET A   43  UNP  O35002              INITIATING METHIONINE          
SEQADV 4C2D LEU A  481  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2D GLU A  482  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2D HIS A  483  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2D HIS A  484  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2D HIS A  485  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2D HIS A  486  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2D HIS A  487  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2D HIS A  488  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2D MET B   43  UNP  O35002              INITIATING METHIONINE          
SEQADV 4C2D LEU B  481  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2D GLU B  482  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2D HIS B  483  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2D HIS B  484  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2D HIS B  485  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2D HIS B  486  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2D HIS B  487  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2D HIS B  488  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2D MET C   43  UNP  O35002              INITIATING METHIONINE          
SEQADV 4C2D LEU C  481  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2D GLU C  482  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2D HIS C  483  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2D HIS C  484  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2D HIS C  485  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2D HIS C  486  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2D HIS C  487  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2D HIS C  488  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2D MET D   43  UNP  O35002              INITIATING METHIONINE          
SEQADV 4C2D LEU D  481  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2D GLU D  482  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2D HIS D  483  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2D HIS D  484  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2D HIS D  485  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2D HIS D  486  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2D HIS D  487  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2D HIS D  488  UNP  O35002              EXPRESSION TAG                 
SEQRES   1 A  446  MET ALA ASP SER GLU ARG ASP LYS ALA MET ASP LYS ILE          
SEQRES   2 A  446  GLU LYS ALA TYR GLU LEU ILE SER ASN GLU TYR VAL GLU          
SEQRES   3 A  446  LYS VAL ASP ARG GLU LYS LEU LEU GLU GLY ALA ILE GLN          
SEQRES   4 A  446  GLY MET LEU SER THR LEU ASN ASP PRO TYR SER VAL TYR          
SEQRES   5 A  446  MET ASP LYS GLN THR ALA LYS GLN PHE SER ASP SER LEU          
SEQRES   6 A  446  ASP SER SER PHE GLU GLY ILE GLY ALA GLU VAL GLY MET          
SEQRES   7 A  446  GLU ASP GLY LYS ILE ILE ILE VAL SER PRO PHE LYS LYS          
SEQRES   8 A  446  SER PRO ALA GLU LYS ALA GLY LEU LYS PRO ASN ASP GLU          
SEQRES   9 A  446  ILE ILE SER ILE ASN GLY GLU SER MET ALA GLY LYS ASP          
SEQRES  10 A  446  LEU ASN HIS ALA VAL LEU LYS ILE ARG GLY LYS LYS GLY          
SEQRES  11 A  446  SER SER VAL SER MET LYS ILE GLN ARG PRO GLY THR LYS          
SEQRES  12 A  446  LYS GLN LEU SER PHE ARG ILE LYS ARG ALA GLU ILE PRO          
SEQRES  13 A  446  LEU GLU THR VAL PHE ALA SER GLU LYS LYS VAL GLN GLY          
SEQRES  14 A  446  HIS SER VAL GLY TYR ILE ALA ILE SER THR PHE SER GLU          
SEQRES  15 A  446  HIS THR ALA GLU ASP PHE ALA LYS ALA LEU ARG GLU LEU          
SEQRES  16 A  446  GLU LYS LYS GLU ILE GLU GLY LEU VAL ILE ASP VAL ARG          
SEQRES  17 A  446  GLY ASN PRO GLY GLY TYR LEU GLN SER VAL GLU GLU ILE          
SEQRES  18 A  446  LEU LYS HIS PHE VAL THR LYS ASP GLN PRO TYR ILE GLN          
SEQRES  19 A  446  ILE ALA GLU ARG ASN GLY ASP LYS LYS ARG TYR PHE SER          
SEQRES  20 A  446  THR LEU THR HIS LYS LYS ALA TYR PRO VAL ASN VAL ILE          
SEQRES  21 A  446  THR ASP LYS GLY SER ALA SER ALA SER GLU ILE LEU ALA          
SEQRES  22 A  446  GLY ALA LEU LYS GLU ALA GLY HIS TYR ASP VAL VAL GLY          
SEQRES  23 A  446  ASP THR SER PHE GLY LYS GLY THR VAL GLN GLN ALA VAL          
SEQRES  24 A  446  PRO MET GLY ASP GLY SER ASN ILE LYS LEU THR LEU TYR          
SEQRES  25 A  446  LYS TRP LEU THR PRO ASN GLY ASN TRP ILE HIS LYS LYS          
SEQRES  26 A  446  GLY ILE GLU PRO THR ILE ALA ILE LYS GLN PRO ASP TYR          
SEQRES  27 A  446  PHE SER ALA GLY PRO LEU GLN LEU LYS GLU PRO LEU LYS          
SEQRES  28 A  446  VAL ASP MET ASN ASN GLU ASP VAL LYS HIS ALA GLN VAL          
SEQRES  29 A  446  LEU LEU LYS GLY LEU SER PHE ASP PRO GLY ARG GLU ASP          
SEQRES  30 A  446  GLY TYR PHE SER LYS ASP MET LYS LYS ALA VAL MET ALA          
SEQRES  31 A  446  PHE GLN ASP GLN ASN LYS LEU ASN LYS THR GLY VAL ILE          
SEQRES  32 A  446  ASP THR ARG THR ALA GLU THR LEU ASN GLN GLN ILE GLU          
SEQRES  33 A  446  LYS LYS LYS SER ASP GLU LYS ASN ASP LEU GLN LEU GLN          
SEQRES  34 A  446  THR ALA LEU LYS SER LEU PHE VAL ASN LEU GLU HIS HIS          
SEQRES  35 A  446  HIS HIS HIS HIS                                              
SEQRES   1 B  446  MET ALA ASP SER GLU ARG ASP LYS ALA MET ASP LYS ILE          
SEQRES   2 B  446  GLU LYS ALA TYR GLU LEU ILE SER ASN GLU TYR VAL GLU          
SEQRES   3 B  446  LYS VAL ASP ARG GLU LYS LEU LEU GLU GLY ALA ILE GLN          
SEQRES   4 B  446  GLY MET LEU SER THR LEU ASN ASP PRO TYR SER VAL TYR          
SEQRES   5 B  446  MET ASP LYS GLN THR ALA LYS GLN PHE SER ASP SER LEU          
SEQRES   6 B  446  ASP SER SER PHE GLU GLY ILE GLY ALA GLU VAL GLY MET          
SEQRES   7 B  446  GLU ASP GLY LYS ILE ILE ILE VAL SER PRO PHE LYS LYS          
SEQRES   8 B  446  SER PRO ALA GLU LYS ALA GLY LEU LYS PRO ASN ASP GLU          
SEQRES   9 B  446  ILE ILE SER ILE ASN GLY GLU SER MET ALA GLY LYS ASP          
SEQRES  10 B  446  LEU ASN HIS ALA VAL LEU LYS ILE ARG GLY LYS LYS GLY          
SEQRES  11 B  446  SER SER VAL SER MET LYS ILE GLN ARG PRO GLY THR LYS          
SEQRES  12 B  446  LYS GLN LEU SER PHE ARG ILE LYS ARG ALA GLU ILE PRO          
SEQRES  13 B  446  LEU GLU THR VAL PHE ALA SER GLU LYS LYS VAL GLN GLY          
SEQRES  14 B  446  HIS SER VAL GLY TYR ILE ALA ILE SER THR PHE SER GLU          
SEQRES  15 B  446  HIS THR ALA GLU ASP PHE ALA LYS ALA LEU ARG GLU LEU          
SEQRES  16 B  446  GLU LYS LYS GLU ILE GLU GLY LEU VAL ILE ASP VAL ARG          
SEQRES  17 B  446  GLY ASN PRO GLY GLY TYR LEU GLN SER VAL GLU GLU ILE          
SEQRES  18 B  446  LEU LYS HIS PHE VAL THR LYS ASP GLN PRO TYR ILE GLN          
SEQRES  19 B  446  ILE ALA GLU ARG ASN GLY ASP LYS LYS ARG TYR PHE SER          
SEQRES  20 B  446  THR LEU THR HIS LYS LYS ALA TYR PRO VAL ASN VAL ILE          
SEQRES  21 B  446  THR ASP LYS GLY SER ALA SER ALA SER GLU ILE LEU ALA          
SEQRES  22 B  446  GLY ALA LEU LYS GLU ALA GLY HIS TYR ASP VAL VAL GLY          
SEQRES  23 B  446  ASP THR SER PHE GLY LYS GLY THR VAL GLN GLN ALA VAL          
SEQRES  24 B  446  PRO MET GLY ASP GLY SER ASN ILE LYS LEU THR LEU TYR          
SEQRES  25 B  446  LYS TRP LEU THR PRO ASN GLY ASN TRP ILE HIS LYS LYS          
SEQRES  26 B  446  GLY ILE GLU PRO THR ILE ALA ILE LYS GLN PRO ASP TYR          
SEQRES  27 B  446  PHE SER ALA GLY PRO LEU GLN LEU LYS GLU PRO LEU LYS          
SEQRES  28 B  446  VAL ASP MET ASN ASN GLU ASP VAL LYS HIS ALA GLN VAL          
SEQRES  29 B  446  LEU LEU LYS GLY LEU SER PHE ASP PRO GLY ARG GLU ASP          
SEQRES  30 B  446  GLY TYR PHE SER LYS ASP MET LYS LYS ALA VAL MET ALA          
SEQRES  31 B  446  PHE GLN ASP GLN ASN LYS LEU ASN LYS THR GLY VAL ILE          
SEQRES  32 B  446  ASP THR ARG THR ALA GLU THR LEU ASN GLN GLN ILE GLU          
SEQRES  33 B  446  LYS LYS LYS SER ASP GLU LYS ASN ASP LEU GLN LEU GLN          
SEQRES  34 B  446  THR ALA LEU LYS SER LEU PHE VAL ASN LEU GLU HIS HIS          
SEQRES  35 B  446  HIS HIS HIS HIS                                              
SEQRES   1 C  446  MET ALA ASP SER GLU ARG ASP LYS ALA MET ASP LYS ILE          
SEQRES   2 C  446  GLU LYS ALA TYR GLU LEU ILE SER ASN GLU TYR VAL GLU          
SEQRES   3 C  446  LYS VAL ASP ARG GLU LYS LEU LEU GLU GLY ALA ILE GLN          
SEQRES   4 C  446  GLY MET LEU SER THR LEU ASN ASP PRO TYR SER VAL TYR          
SEQRES   5 C  446  MET ASP LYS GLN THR ALA LYS GLN PHE SER ASP SER LEU          
SEQRES   6 C  446  ASP SER SER PHE GLU GLY ILE GLY ALA GLU VAL GLY MET          
SEQRES   7 C  446  GLU ASP GLY LYS ILE ILE ILE VAL SER PRO PHE LYS LYS          
SEQRES   8 C  446  SER PRO ALA GLU LYS ALA GLY LEU LYS PRO ASN ASP GLU          
SEQRES   9 C  446  ILE ILE SER ILE ASN GLY GLU SER MET ALA GLY LYS ASP          
SEQRES  10 C  446  LEU ASN HIS ALA VAL LEU LYS ILE ARG GLY LYS LYS GLY          
SEQRES  11 C  446  SER SER VAL SER MET LYS ILE GLN ARG PRO GLY THR LYS          
SEQRES  12 C  446  LYS GLN LEU SER PHE ARG ILE LYS ARG ALA GLU ILE PRO          
SEQRES  13 C  446  LEU GLU THR VAL PHE ALA SER GLU LYS LYS VAL GLN GLY          
SEQRES  14 C  446  HIS SER VAL GLY TYR ILE ALA ILE SER THR PHE SER GLU          
SEQRES  15 C  446  HIS THR ALA GLU ASP PHE ALA LYS ALA LEU ARG GLU LEU          
SEQRES  16 C  446  GLU LYS LYS GLU ILE GLU GLY LEU VAL ILE ASP VAL ARG          
SEQRES  17 C  446  GLY ASN PRO GLY GLY TYR LEU GLN SER VAL GLU GLU ILE          
SEQRES  18 C  446  LEU LYS HIS PHE VAL THR LYS ASP GLN PRO TYR ILE GLN          
SEQRES  19 C  446  ILE ALA GLU ARG ASN GLY ASP LYS LYS ARG TYR PHE SER          
SEQRES  20 C  446  THR LEU THR HIS LYS LYS ALA TYR PRO VAL ASN VAL ILE          
SEQRES  21 C  446  THR ASP LYS GLY SER ALA SER ALA SER GLU ILE LEU ALA          
SEQRES  22 C  446  GLY ALA LEU LYS GLU ALA GLY HIS TYR ASP VAL VAL GLY          
SEQRES  23 C  446  ASP THR SER PHE GLY LYS GLY THR VAL GLN GLN ALA VAL          
SEQRES  24 C  446  PRO MET GLY ASP GLY SER ASN ILE LYS LEU THR LEU TYR          
SEQRES  25 C  446  LYS TRP LEU THR PRO ASN GLY ASN TRP ILE HIS LYS LYS          
SEQRES  26 C  446  GLY ILE GLU PRO THR ILE ALA ILE LYS GLN PRO ASP TYR          
SEQRES  27 C  446  PHE SER ALA GLY PRO LEU GLN LEU LYS GLU PRO LEU LYS          
SEQRES  28 C  446  VAL ASP MET ASN ASN GLU ASP VAL LYS HIS ALA GLN VAL          
SEQRES  29 C  446  LEU LEU LYS GLY LEU SER PHE ASP PRO GLY ARG GLU ASP          
SEQRES  30 C  446  GLY TYR PHE SER LYS ASP MET LYS LYS ALA VAL MET ALA          
SEQRES  31 C  446  PHE GLN ASP GLN ASN LYS LEU ASN LYS THR GLY VAL ILE          
SEQRES  32 C  446  ASP THR ARG THR ALA GLU THR LEU ASN GLN GLN ILE GLU          
SEQRES  33 C  446  LYS LYS LYS SER ASP GLU LYS ASN ASP LEU GLN LEU GLN          
SEQRES  34 C  446  THR ALA LEU LYS SER LEU PHE VAL ASN LEU GLU HIS HIS          
SEQRES  35 C  446  HIS HIS HIS HIS                                              
SEQRES   1 D  446  MET ALA ASP SER GLU ARG ASP LYS ALA MET ASP LYS ILE          
SEQRES   2 D  446  GLU LYS ALA TYR GLU LEU ILE SER ASN GLU TYR VAL GLU          
SEQRES   3 D  446  LYS VAL ASP ARG GLU LYS LEU LEU GLU GLY ALA ILE GLN          
SEQRES   4 D  446  GLY MET LEU SER THR LEU ASN ASP PRO TYR SER VAL TYR          
SEQRES   5 D  446  MET ASP LYS GLN THR ALA LYS GLN PHE SER ASP SER LEU          
SEQRES   6 D  446  ASP SER SER PHE GLU GLY ILE GLY ALA GLU VAL GLY MET          
SEQRES   7 D  446  GLU ASP GLY LYS ILE ILE ILE VAL SER PRO PHE LYS LYS          
SEQRES   8 D  446  SER PRO ALA GLU LYS ALA GLY LEU LYS PRO ASN ASP GLU          
SEQRES   9 D  446  ILE ILE SER ILE ASN GLY GLU SER MET ALA GLY LYS ASP          
SEQRES  10 D  446  LEU ASN HIS ALA VAL LEU LYS ILE ARG GLY LYS LYS GLY          
SEQRES  11 D  446  SER SER VAL SER MET LYS ILE GLN ARG PRO GLY THR LYS          
SEQRES  12 D  446  LYS GLN LEU SER PHE ARG ILE LYS ARG ALA GLU ILE PRO          
SEQRES  13 D  446  LEU GLU THR VAL PHE ALA SER GLU LYS LYS VAL GLN GLY          
SEQRES  14 D  446  HIS SER VAL GLY TYR ILE ALA ILE SER THR PHE SER GLU          
SEQRES  15 D  446  HIS THR ALA GLU ASP PHE ALA LYS ALA LEU ARG GLU LEU          
SEQRES  16 D  446  GLU LYS LYS GLU ILE GLU GLY LEU VAL ILE ASP VAL ARG          
SEQRES  17 D  446  GLY ASN PRO GLY GLY TYR LEU GLN SER VAL GLU GLU ILE          
SEQRES  18 D  446  LEU LYS HIS PHE VAL THR LYS ASP GLN PRO TYR ILE GLN          
SEQRES  19 D  446  ILE ALA GLU ARG ASN GLY ASP LYS LYS ARG TYR PHE SER          
SEQRES  20 D  446  THR LEU THR HIS LYS LYS ALA TYR PRO VAL ASN VAL ILE          
SEQRES  21 D  446  THR ASP LYS GLY SER ALA SER ALA SER GLU ILE LEU ALA          
SEQRES  22 D  446  GLY ALA LEU LYS GLU ALA GLY HIS TYR ASP VAL VAL GLY          
SEQRES  23 D  446  ASP THR SER PHE GLY LYS GLY THR VAL GLN GLN ALA VAL          
SEQRES  24 D  446  PRO MET GLY ASP GLY SER ASN ILE LYS LEU THR LEU TYR          
SEQRES  25 D  446  LYS TRP LEU THR PRO ASN GLY ASN TRP ILE HIS LYS LYS          
SEQRES  26 D  446  GLY ILE GLU PRO THR ILE ALA ILE LYS GLN PRO ASP TYR          
SEQRES  27 D  446  PHE SER ALA GLY PRO LEU GLN LEU LYS GLU PRO LEU LYS          
SEQRES  28 D  446  VAL ASP MET ASN ASN GLU ASP VAL LYS HIS ALA GLN VAL          
SEQRES  29 D  446  LEU LEU LYS GLY LEU SER PHE ASP PRO GLY ARG GLU ASP          
SEQRES  30 D  446  GLY TYR PHE SER LYS ASP MET LYS LYS ALA VAL MET ALA          
SEQRES  31 D  446  PHE GLN ASP GLN ASN LYS LEU ASN LYS THR GLY VAL ILE          
SEQRES  32 D  446  ASP THR ARG THR ALA GLU THR LEU ASN GLN GLN ILE GLU          
SEQRES  33 D  446  LYS LYS LYS SER ASP GLU LYS ASN ASP LEU GLN LEU GLN          
SEQRES  34 D  446  THR ALA LEU LYS SER LEU PHE VAL ASN LEU GLU HIS HIS          
SEQRES  35 D  446  HIS HIS HIS HIS                                              
SEQRES   1 E    6  ALA ALA SER LEU SER ALA                                      
SEQRES   1 F    6  ALA ALA SER LEU SER ALA                                      
SEQRES   1 G    6  ALA ALA SER LEU SER ALA                                      
SEQRES   1 H    6  ALA ALA SER LEU SER ALA                                      
SEQRES   1 M    5  ALA ALA PRO GLN ALA                                          
SEQRES   1 N    4  PRO GLN THR ALA                                              
SEQRES   1 O    4  PRO GLN THR ALA                                              
SEQRES   1 P    4  PRO GLN THR ALA                                              
FORMUL  13  HOH   *274(H2 O)                                                    
HELIX    1   1 GLU A   47  TYR A   66  1                                  20    
HELIX    2   2 ASP A   71  THR A   86  1                                  16    
HELIX    3   3 ASP A   96  ASP A  108  1                                  13    
HELIX    4   4 SER A  134  ALA A  139  1                                   6    
HELIX    5   5 ASP A  159  ARG A  168  1                                  10    
HELIX    6   6 HIS A  225  LYS A  239  1                                  15    
HELIX    7   7 LEU A  257  LYS A  265  1                                   9    
HELIX    8   8 SER A  309  GLY A  322  1                                  14    
HELIX    9   9 PRO A  378  SER A  382  5                                   5    
HELIX   10  10 ASN A  398  LEU A  411  1                                  14    
HELIX   11  11 SER A  423  ASN A  437  1                                  15    
HELIX   12  12 ASP A  446  ASP A  463  1                                  18    
HELIX   13  13 GLU A  464  ASN A  466  5                                   3    
HELIX   14  14 ASP A  467  LEU A  477  1                                  11    
HELIX   15  15 SER B   46  TYR B   66  1                                  21    
HELIX   16  16 ASP B   71  THR B   86  1                                  16    
HELIX   17  17 ASP B   96  LEU B  107  1                                  12    
HELIX   18  18 SER B  134  ALA B  139  1                                   6    
HELIX   19  19 ASP B  159  ARG B  168  1                                  10    
HELIX   20  20 HIS B  225  LYS B  240  1                                  16    
HELIX   21  21 LEU B  257  LYS B  265  1                                   9    
HELIX   22  22 SER B  309  GLY B  322  1                                  14    
HELIX   23  23 PRO B  378  ALA B  383  1                                   6    
HELIX   24  24 ASN B  398  LEU B  411  1                                  14    
HELIX   25  25 SER B  423  GLN B  436  1                                  14    
HELIX   26  26 ASP B  446  ASP B  463  1                                  18    
HELIX   27  27 GLU B  464  ASN B  466  5                                   3    
HELIX   28  28 ASP B  467  SER B  476  1                                  10    
HELIX   29  29 ARG C   48  TYR C   66  1                                  19    
HELIX   30  30 ASP C   71  THR C   86  1                                  16    
HELIX   31  31 ASP C   96  LEU C  107  1                                  12    
HELIX   32  32 ASP C  159  ARG C  168  1                                  10    
HELIX   33  33 HIS C  225  LYS C  239  1                                  15    
HELIX   34  34 LEU C  257  HIS C  266  1                                  10    
HELIX   35  35 SER C  309  ALA C  321  1                                  13    
HELIX   36  36 PRO C  378  SER C  382  5                                   5    
HELIX   37  37 ASN C  398  LEU C  411  1                                  14    
HELIX   38  38 MET C  426  ASN C  437  1                                  12    
HELIX   39  39 ASP C  446  ILE C  457  1                                  12    
HELIX   40  40 ILE C  457  SER C  462  1                                   6    
HELIX   41  41 ASP C  467  SER C  476  1                                  10    
HELIX   42  42 GLU D   47  TYR D   66  1                                  20    
HELIX   43  43 ASP D   71  THR D   86  1                                  16    
HELIX   44  44 ASP D   96  ASP D  105  1                                  10    
HELIX   45  45 HIS D  225  LYS D  240  1                                  16    
HELIX   46  46 TYR D  256  LYS D  265  1                                  10    
HELIX   47  47 SER D  309  ALA D  321  1                                  13    
HELIX   48  48 PRO D  378  SER D  382  5                                   5    
HELIX   49  49 GLU D  399  LYS D  409  1                                  11    
HELIX   50  50 SER D  423  ASN D  437  1                                  15    
HELIX   51  51 ASP D  446  LYS D  461  1                                  16    
HELIX   52  52 ASP D  463  ASN D  466  5                                   4    
HELIX   53  53 ASP D  467  LEU D  477  1                                  11    
SHEET    1  AA 2 VAL A  93  MET A  95  0                                        
SHEET    2  AA 2 ASN A 348  LEU A 357  1  O  ASN A 348   N  MET A  95           
SHEET    1  AB 6 GLY A 255  TYR A 256  0                                        
SHEET    2  AB 6 LEU E   4  ALA E   6 -1  O  ALA E   6   N  GLY A 255           
SHEET    3  AB 6 THR A 336  PRO A 342 -1  O  GLN A 338   N  SER E   5           
SHEET    4  AB 6 ASN A 348  LEU A 357 -1  O  ILE A 349   N  VAL A 341           
SHEET    5  AB 6 PRO A 273  ALA A 278 -1  O  GLN A 276   N  LEU A 357           
SHEET    6  AB 6 LYS A 284  PHE A 288 -1  O  LYS A 285   N  ILE A 277           
SHEET    1  AC 5 GLY A 255  TYR A 256  0                                        
SHEET    2  AC 5 LEU E   4  ALA E   6 -1  O  ALA E   6   N  GLY A 255           
SHEET    3  AC 5 THR A 336  PRO A 342 -1  O  GLN A 338   N  SER E   5           
SHEET    4  AC 5 ASN A 348  LEU A 357 -1  O  ILE A 349   N  VAL A 341           
SHEET    5  AC 5 VAL A  93  MET A  95  1  O  VAL A  93   N  LYS A 350           
SHEET    1  AD 2 SER A 110  GLY A 113  0                                        
SHEET    2  AD 2 ALA A 195  PRO A 198 -1  O  ALA A 195   N  GLY A 113           
SHEET    1  AE 4 ALA A 116  GLU A 121  0                                        
SHEET    2  AE 4 LYS A 124  PRO A 130 -1  O  LYS A 124   N  GLU A 121           
SHEET    3  AE 4 ASP A 145  ILE A 150 -1  O  ASP A 145   N  ILE A 127           
SHEET    4  AE 4 GLU A 153  SER A 154  1  O  GLU A 153   N  ILE A 150           
SHEET    1  AF 5 ALA A 116  GLU A 121  0                                        
SHEET    2  AF 5 LYS A 124  PRO A 130 -1  O  LYS A 124   N  GLU A 121           
SHEET    3  AF 5 ASP A 145  ILE A 150 -1  O  ASP A 145   N  ILE A 127           
SHEET    4  AF 5 SER A 174  GLN A 180 -1  O  LYS A 178   N  ILE A 148           
SHEET    5  AF 5 LEU A 188  LYS A 193 -1  O  LEU A 188   N  ILE A 179           
SHEET    1  AG 2 GLU A 153  SER A 154  0                                        
SHEET    2  AG 2 ASP A 145  ILE A 150  1  O  ILE A 150   N  GLU A 153           
SHEET    1  AH 6 VAL A 202  VAL A 209  0                                        
SHEET    2  AH 6 HIS A 212  ILE A 219 -1  O  HIS A 212   N  VAL A 209           
SHEET    3  AH 6 LEU A 245  ASP A 248  1  O  VAL A 246   N  ILE A 217           
SHEET    4  AH 6 VAL A 299  THR A 303  1  O  ASN A 300   N  ILE A 247           
SHEET    5  AH 6 ASP A 325  GLY A 328  1  O  ASP A 325   N  VAL A 301           
SHEET    6  AH 6 ILE A 373  ALA A 374  1  O  ILE A 373   N  GLY A 328           
SHEET    1  BA 2 VAL B  93  MET B  95  0                                        
SHEET    2  BA 2 ASN B 348  LEU B 357 -1  O  ASN B 348   N  MET B  95           
SHEET    1  BB 6 GLY B 255  TYR B 256  0                                        
SHEET    2  BB 6 LEU F   4  ALA F   6 -1  N  ALA F   6   O  GLY B 255           
SHEET    3  BB 6 THR B 336  PRO B 342 -1  O  GLN B 338   N  SER F   5           
SHEET    4  BB 6 ASN B 348  LEU B 357 -1  O  ILE B 349   N  VAL B 341           
SHEET    5  BB 6 ILE B 275  ALA B 278 -1  O  GLN B 276   N  LEU B 357           
SHEET    6  BB 6 ARG B 286  TYR B 287 -1  N  TYR B 287   O  ILE B 275           
SHEET    1  BC 5 GLY B 255  TYR B 256  0                                        
SHEET    2  BC 5 LEU F   4  ALA F   6 -1  N  ALA F   6   O  GLY B 255           
SHEET    3  BC 5 THR B 336  PRO B 342 -1  O  GLN B 338   N  SER F   5           
SHEET    4  BC 5 ASN B 348  LEU B 357 -1  O  ILE B 349   N  VAL B 341           
SHEET    5  BC 5 VAL B  93  MET B  95 -1  O  VAL B  93   N  LYS B 350           
SHEET    1  BD 2 SER B 110  GLY B 113  0                                        
SHEET    2  BD 2 ALA B 195  PRO B 198 -1  O  ALA B 195   N  GLY B 113           
SHEET    1  BE 4 ALA B 116  GLU B 121  0                                        
SHEET    2  BE 4 LYS B 124  PRO B 130 -1  O  LYS B 124   N  GLU B 121           
SHEET    3  BE 4 ASP B 145  ILE B 150 -1  O  ASP B 145   N  ILE B 127           
SHEET    4  BE 4 GLU B 153  SER B 154  1  O  GLU B 153   N  ILE B 150           
SHEET    1  BF 5 ALA B 116  GLU B 121  0                                        
SHEET    2  BF 5 LYS B 124  PRO B 130 -1  O  LYS B 124   N  GLU B 121           
SHEET    3  BF 5 ASP B 145  ILE B 150 -1  O  ASP B 145   N  ILE B 127           
SHEET    4  BF 5 SER B 174  GLN B 180 -1  O  LYS B 178   N  SER B 149           
SHEET    5  BF 5 LEU B 188  LYS B 193 -1  O  LEU B 188   N  ILE B 179           
SHEET    1  BG 2 GLU B 153  SER B 154  0                                        
SHEET    2  BG 2 ASP B 145  ILE B 150  1  O  ILE B 150   N  GLU B 153           
SHEET    1  BH 6 VAL B 202  VAL B 209  0                                        
SHEET    2  BH 6 HIS B 212  ILE B 219 -1  O  HIS B 212   N  VAL B 209           
SHEET    3  BH 6 LEU B 245  ASP B 248  1  O  VAL B 246   N  ILE B 217           
SHEET    4  BH 6 VAL B 299  THR B 303  1  O  ASN B 300   N  ILE B 247           
SHEET    5  BH 6 VAL B 326  GLY B 328  1  O  VAL B 327   N  THR B 303           
SHEET    6  BH 6 ILE B 373  ALA B 374  1  O  ILE B 373   N  GLY B 328           
SHEET    1  CA 2 VAL C  93  MET C  95  0                                        
SHEET    2  CA 2 ASN C 348  LEU C 357  1  O  ASN C 348   N  MET C  95           
SHEET    1  CB 6 GLY C 255  TYR C 256  0                                        
SHEET    2  CB 6 LEU G   4  ALA G   6 -1  O  ALA G   6   N  GLY C 255           
SHEET    3  CB 6 THR C 336  PRO C 342 -1  O  GLN C 338   N  SER G   5           
SHEET    4  CB 6 ASN C 348  LEU C 357 -1  O  ILE C 349   N  VAL C 341           
SHEET    5  CB 6 ILE C 275  ALA C 278 -1  O  GLN C 276   N  LEU C 357           
SHEET    6  CB 6 LYS C 284  TYR C 287 -1  O  LYS C 285   N  ILE C 277           
SHEET    1  CC 5 GLY C 255  TYR C 256  0                                        
SHEET    2  CC 5 LEU G   4  ALA G   6 -1  O  ALA G   6   N  GLY C 255           
SHEET    3  CC 5 THR C 336  PRO C 342 -1  O  GLN C 338   N  SER G   5           
SHEET    4  CC 5 ASN C 348  LEU C 357 -1  O  ILE C 349   N  VAL C 341           
SHEET    5  CC 5 VAL C  93  MET C  95  1  O  VAL C  93   N  LYS C 350           
SHEET    1  CD 2 SER C 110  GLY C 113  0                                        
SHEET    2  CD 2 ALA C 195  PRO C 198 -1  O  ALA C 195   N  GLY C 113           
SHEET    1  CE 2 ALA C 116  MET C 120  0                                        
SHEET    2  CE 2 ILE C 125  PRO C 130 -1  O  ILE C 126   N  GLY C 119           
SHEET    1  CF 4 GLU C 153  SER C 154  0                                        
SHEET    2  CF 4 GLU C 146  ILE C 150 -1  O  ILE C 150   N  GLU C 153           
SHEET    3  CF 4 SER C 174  GLN C 180 -1  O  LYS C 178   N  ILE C 148           
SHEET    4  CF 4 LEU C 188  LYS C 193 -1  O  LEU C 188   N  ILE C 179           
SHEET    1  CG 5 VAL C 202  VAL C 209  0                                        
SHEET    2  CG 5 HIS C 212  ILE C 219 -1  O  HIS C 212   N  VAL C 209           
SHEET    3  CG 5 GLY C 244  ASP C 248  1  O  GLY C 244   N  GLY C 215           
SHEET    4  CG 5 VAL C 299  THR C 303  1  O  ASN C 300   N  ILE C 247           
SHEET    5  CG 5 ASP C 325  GLY C 328  1  O  ASP C 325   N  VAL C 301           
SHEET    1  DA 2 VAL D  93  MET D  95  0                                        
SHEET    2  DA 2 ASN D 348  LEU D 357 -1  O  ASN D 348   N  MET D  95           
SHEET    1  DB 5 LYS D 284  TYR D 287  0                                        
SHEET    2  DB 5 ILE D 275  ALA D 278 -1  O  ILE D 275   N  TYR D 287           
SHEET    3  DB 5 ASN D 348  LEU D 357 -1  O  LYS D 355   N  ALA D 278           
SHEET    4  DB 5 THR D 336  PRO D 342 -1  O  VAL D 337   N  LEU D 353           
SHEET    5  DB 5 LEU H   4  SER H   5 -1  O  SER H   5   N  GLN D 338           
SHEET    1  DC 4 LYS D 284  TYR D 287  0                                        
SHEET    2  DC 4 ILE D 275  ALA D 278 -1  O  ILE D 275   N  TYR D 287           
SHEET    3  DC 4 ASN D 348  LEU D 357 -1  O  LYS D 355   N  ALA D 278           
SHEET    4  DC 4 VAL D  93  MET D  95 -1  O  VAL D  93   N  LYS D 350           
SHEET    1  DD 5 VAL D 202  VAL D 209  0                                        
SHEET    2  DD 5 HIS D 212  ILE D 219 -1  O  HIS D 212   N  VAL D 209           
SHEET    3  DD 5 LEU D 245  ASP D 248  1  O  VAL D 246   N  ILE D 217           
SHEET    4  DD 5 VAL D 299  THR D 303  1  O  ASN D 300   N  ILE D 247           
SHEET    5  DD 5 ASP D 325  GLY D 328  1  O  ASP D 325   N  VAL D 301           
CRYST1  117.050   65.375  169.065  90.00  95.03  90.00 P 1 21 1      8          
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      0.008543  0.000000  0.000752        0.00000                         
SCALE2      0.000000  0.015296  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005938        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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