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Database: PDB
Entry: 4C2G
LinkDB: 4C2G
Original site: 4C2G 
HEADER    HYDROLASE/PEPTIDE                       17-AUG-13   4C2G              
TITLE     CRYSTAL STRUCTURE OF CTPB(S309A) IN COMPLEX WITH A PEPTIDE HAVING A   
TITLE    2 VAL-PRO-ALA C-TERMINUS                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CARBOXY-TERMINAL PROCESSING PROTEASE CTPB;                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 46-478;                                           
COMPND   5 SYNONYM: CTPB, C-TERMINAL PROCESSING PROTEASE;                       
COMPND   6 EC: 3.4.21.102;                                                      
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: PEPTIDE1;                                                  
COMPND  11 CHAIN: B;                                                            
COMPND  12 OTHER_DETAILS: PEPTIDE CO-PURIFIED FROM E. COLI EXPRESSION;          
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: CARBOXY-TERMINAL PROCESSING PROTEASE CTPB;                 
COMPND  15 CHAIN: C;                                                            
COMPND  16 FRAGMENT: RESIDUES 29-40;                                            
COMPND  17 SYNONYM: PEPTIDE VPA, CTPB, C-TERMINAL PROCESSING PROTEASE;          
COMPND  18 EC: 3.4.21.102;                                                      
COMPND  19 ENGINEERED: YES;                                                     
COMPND  20 OTHER_DETAILS: PEPTIDE NH2-EMDKPQTAAVPA-COOH                         
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 SYNTHETIC: YES;                                                      
SOURCE  15 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS SUBSP. SUBTILIS STR. 168;     
SOURCE  16 ORGANISM_TAXID: 224308                                               
KEYWDS    HYDROLASE-PEPTIDE COMPLEX, PDZ-PROTEASES, ALLOSTERIC REGULATION,      
KEYWDS   2 CONFORMATIONAL SWITCH, SPORULATION, PROTEOLYTIC TUNNEL               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.MASTNY,A.HEUCK,R.KURZBAUER,T.CLAUSEN                                
REVDAT   4   13-SEP-17 4C2G    1       REMARK                                   
REVDAT   3   15-JUL-15 4C2G    1       REMARK                                   
REVDAT   2   08-JAN-14 4C2G    1       SOURCE                                   
REVDAT   1   04-DEC-13 4C2G    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.    1.90 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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000.000                      
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 45467                          
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) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2269                            
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            : 3427                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 359                                     
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) : 4.57800                                              
REMARK   3    B22 (A**2) : 4.57800                                              
REMARK   3    B33 (A**2) : -9.15600                                             
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  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) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.310                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
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        : 0.36                                                 
REMARK   3   BSOL        : 54.39                                                
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 4C2G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-AUG-13.                  
REMARK 100 THE DEPOSITION ID IS D_1290058065.                                   
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               : PETRA III, EMBL C/O DESY           
REMARK 200  BEAMLINE                       : P14 (MX2)                          
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                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45714                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 102.810                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -10.000                            
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.03000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.70000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
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   (%): 57.14                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.1 M NA-MALONATE PH 7.8                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       48.24267            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       24.12133            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       24.12133            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       48.24267            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7730 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 41830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2 -0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -24.12133            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A2139  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     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     GLU C    -6                                                      
REMARK 465     MET C    -5                                                      
REMARK 465     ASP C    -4                                                      
REMARK 465     LYS C    -3                                                      
REMARK 465     PRO C    -2                                                      
REMARK 465     GLN C    -1                                                      
REMARK 465     THR C     0                                                      
REMARK 465     ALA C     1                                                      
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 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   NE2  GLN A   339     O    HOH A  2256              2.11            
REMARK 500   O    HOH A  2124     O    HOH A  2289              2.13            
REMARK 500   N    VAL A   479     O    HOH A  2356              2.13            
REMARK 500   O    HOH A  2335     O    HOH A  2336              2.13            
REMARK 500   OE2  GLU A   464     O    HOH A  2351              2.16            
REMARK 500   O    SER A    85     O    HOH A  2015              2.17            
REMARK 500   O    HOH A  2021     O    HOH A  2063              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A 285      102.44   -171.61                                   
REMARK 500    ALA A 309     -106.40     52.85                                   
REMARK 500    LYS A 366       17.61     56.74                                   
REMARK 500    LYS A 367      -33.34   -138.15                                   
REMARK 500    ASP A 395       -3.47     83.43                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2034        DISTANCE =  6.32 ANGSTROMS                       
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 STATE            
REMARK 900 RELATED ID: 4C2D   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE PROTEASE CTPB IN AN ACTIVE STATE            
REMARK 900 RELATED ID: 4C2E   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE PROTEASE CTPB(S309A) PRESENT IN A RESTING   
REMARK 900 STATE                                                                
REMARK 900 RELATED ID: 4C2F   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CTPB R168A MUTANT PRESENT IN AN ACTIVE      
REMARK 900 CONFORMATION                                                         
REMARK 900 RELATED ID: 4C2H   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CTPB(V118Y) MUTANT                          
DBREF  4C2G A   44   480  UNP    O35002   CTPB_BACSU      44    480             
DBREF  4C2G B    3     6  PDB    4C2G     4C2G             3      6             
DBREF  4C2G C   -6     5  UNP    O35002   CTPB_BACSU      29     40             
SEQADV 4C2G MET A   43  UNP  O35002              INITIATING METHIONINE          
SEQADV 4C2G LEU A  481  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2G GLU A  482  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2G HIS A  483  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2G HIS A  484  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2G HIS A  485  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2G HIS A  486  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2G HIS A  487  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2G HIS A  488  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2G ALA A  309  UNP  O35002    SER   309 ENGINEERED MUTATION            
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 ALA 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    4  ALA ALA ALA ALA                                              
SEQRES   1 C   12  GLU MET ASP LYS PRO GLN THR ALA ALA VAL PRO ALA              
FORMUL   4  HOH   *359(H2 O)                                                    
HELIX    1   1 SER A   46  TYR A   66  1                                  21    
HELIX    2   2 ASP A   71  THR A   86  1                                  16    
HELIX    3   3 ASP A   96  LEU A  107  1                                  12    
HELIX    4   4 SER A  134  GLY A  140  1                                   7    
HELIX    5   5 ASP A  159  ARG A  168  1                                  10    
HELIX    6   6 HIS A  225  LYS A  240  1                                  16    
HELIX    7   7 LEU A  257  LYS A  265  1                                   9    
HELIX    8   8 ALA A  309  ALA A  321  1                                  13    
HELIX    9   9 PRO A  378  ALA A  383  5                                   6    
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    
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 ALA B   4  ALA B   6 -1  N  ALA B   6   O  GLY A 255           
SHEET    3  AB 6 THR A 336  PRO A 342 -1  O  GLN A 338   N  ALA B   5           
SHEET    4  AB 6 ASN A 348  LEU A 357 -1  O  ILE A 349   N  VAL A 341           
SHEET    5  AB 6 ILE A 275  ALA A 278 -1  O  GLN A 276   N  LEU A 357           
SHEET    6  AB 6 ARG A 286  TYR A 287 -1  N  TYR A 287   O  ILE A 275           
SHEET    1  AC 5 GLY A 255  TYR A 256  0                                        
SHEET    2  AC 5 ALA B   4  ALA B   6 -1  N  ALA B   6   O  GLY A 255           
SHEET    3  AC 5 THR A 336  PRO A 342 -1  O  GLN A 338   N  ALA B   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 3 LYS A 124  PRO A 130  0                                        
SHEET    2  AE 3 ALA A 116  GLU A 121 -1  O  GLU A 117   N  VAL A 128           
SHEET    3  AE 3 VAL C   3  PRO C   4 -1  O  VAL C   3   N  VAL A 118           
SHEET    1  AF 4 GLU A 153  SER A 154  0                                        
SHEET    2  AF 4 GLU A 146  ILE A 150 -1  O  ILE A 150   N  GLU A 153           
SHEET    3  AF 4 SER A 174  GLN A 180 -1  O  LYS A 178   N  ILE A 148           
SHEET    4  AF 4 LEU A 188  LYS A 193 -1  O  LEU A 188   N  ILE A 179           
SHEET    1  AG 6 VAL A 202  VAL A 209  0                                        
SHEET    2  AG 6 HIS A 212  ILE A 219 -1  O  HIS A 212   N  VAL A 209           
SHEET    3  AG 6 LEU A 245  ASP A 248  1  O  VAL A 246   N  ILE A 217           
SHEET    4  AG 6 VAL A 299  THR A 303  1  O  ASN A 300   N  ILE A 247           
SHEET    5  AG 6 ASP A 325  GLY A 328  1  O  ASP A 325   N  VAL A 301           
SHEET    6  AG 6 ILE A 373  ALA A 374  1  O  ILE A 373   N  GLY A 328           
CRYST1  118.712  118.712   72.364  90.00  90.00 120.00 P 32 2 1      6          
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      0.008424  0.004863  0.000000        0.00000                         
SCALE2      0.000000  0.009727  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013819        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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