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Database: PDB
Entry: 4C2C
LinkDB: 4C2C
Original site: 4C2C 
HEADER    HYDROLASE                               17-AUG-13   4C2C              
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;                                                            
COMPND   4 FRAGMENT: RESIDUES 44-480;                                           
COMPND   5 SYNONYM: CTPB, C-TERMINAL PROCESSING PROTEASE;                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PEPTIDE1;                                                  
COMPND   9 CHAIN: B;                                                            
COMPND  10 OTHER_DETAILS: PEPTIDE CO-PURIFIED FROM E. COLI EXPRESSION;          
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: PEPTIDE2;                                                  
COMPND  13 CHAIN: C;                                                            
COMPND  14 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_VECTOR: 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                                                         
KEYWDS    HYDROLASE, PDZ-PROTEASES, ALLOSTERIC REGULATION, CONFORMATIONAL       
KEYWDS   2 SWITCH, SPORULATION, PROTEOLYTIC TUNNEL                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.MASTNY,A.HEUCK,R.KURZBAUER,T.CLAUSEN                                
REVDAT   1   04-DEC-13 4C2C    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) : 1.9                            
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)   (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 46719                          
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) : 0.1953                          
REMARK   3   FREE R VALUE                     : 0.2158                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2332                            
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            : 3343                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 80                                      
REMARK   3   SOLVENT ATOMS            : 334                                     
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) : 3.962                                                
REMARK   3    B22 (A**2) : 3.962                                                
REMARK   3    B33 (A**2) : -7.923                                               
REMARK   3    B12 (A**2) : 0.000                                                
REMARK   3    B13 (A**2) : 0.000                                                
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) : 1.13                            
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        : 0.37                                                 
REMARK   3   BSOL        : 54.1172                                              
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 4C2C 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-58058.                                       
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               : SLS                                
REMARK 200  BEAMLINE                       : X06DA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9791                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46788                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.90                               
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                : 20.5                               
REMARK 200  R MERGE                    (I) : 0.06                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 36.50                              
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 20.9                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.67                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.60                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.17                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94                     
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       48.44000            
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       24.22000            
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       24.22000            
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       48.44000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1180 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.5 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B                               
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     MSE 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 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   OE2  GLU A    60     O    HOH A  2003              2.06            
REMARK 500   OD1  ASN A   161     O    HOH A  2090              1.97            
REMARK 500   OG1  THR A   269     OD1  ASP A   271              1.95            
REMARK 500   O    HOH A  2203     O    HOH A  2204              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 129      134.19   -174.94                                   
REMARK 500    ASN A 144       -3.38     78.97                                   
REMARK 500    SER A 309     -117.76     62.84                                   
REMARK 500    LYS A 367      -58.30   -130.32                                   
REMARK 500    ASP A 395       -5.29     86.84                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4C2D   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  4C2C A   44   480  UNP    O35002   CTPB_BACSU      44    480             
DBREF  4C2C B    3     5  PDB    4C2C     4C2C             3      5             
DBREF  4C2C C    2     5  PDB    4C2C     4C2C             2      5             
SEQADV 4C2C MSE A   43  UNP  O35002              INITIATING METHIONINE          
SEQADV 4C2C LEU A  481  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2C GLU A  482  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2C HIS A  483  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2C HIS A  484  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2C HIS A  485  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2C HIS A  486  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2C HIS A  487  UNP  O35002              EXPRESSION TAG                 
SEQADV 4C2C HIS A  488  UNP  O35002              EXPRESSION TAG                 
SEQRES   1 A  446  MSE ALA ASP SER GLU ARG ASP LYS ALA MSE 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 MSE LEU SER THR LEU ASN ASP PRO TYR SER VAL TYR          
SEQRES   5 A  446  MSE 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 MSE          
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 MSE 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 MSE 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 MSE 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 MSE 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 MSE LYS LYS ALA VAL MSE 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    3  ALA ALA ALA                                                  
SEQRES   1 C    4  ALA VAL PRO ALA                                              
MODRES 4C2C MSE A   52  MET  SELENOMETHIONINE                                   
MODRES 4C2C MSE A   83  MET  SELENOMETHIONINE                                   
MODRES 4C2C MSE A   95  MET  SELENOMETHIONINE                                   
MODRES 4C2C MSE A  120  MET  SELENOMETHIONINE                                   
MODRES 4C2C MSE A  155  MET  SELENOMETHIONINE                                   
MODRES 4C2C MSE A  177  MET  SELENOMETHIONINE                                   
MODRES 4C2C MSE A  343  MET  SELENOMETHIONINE                                   
MODRES 4C2C MSE A  396  MET  SELENOMETHIONINE                                   
MODRES 4C2C MSE A  426  MET  SELENOMETHIONINE                                   
MODRES 4C2C MSE A  431  MET  SELENOMETHIONINE                                   
HET    MSE  A  52       8                                                       
HET    MSE  A  83       8                                                       
HET    MSE  A  95       8                                                       
HET    MSE  A 120       8                                                       
HET    MSE  A 155       8                                                       
HET    MSE  A 177       8                                                       
HET    MSE  A 343       8                                                       
HET    MSE  A 396       8                                                       
HET    MSE  A 426       8                                                       
HET    MSE  A 431       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   4  MSE    10(C5 H11 N O2 SE)                                           
FORMUL   5  HOH   *334(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 TYR A  256  LYS A  265  1                                  10    
HELIX    8   8 SER 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  MSE A  95  0                                        
SHEET    2  AA 2 ASN A 348  LEU A 357 -1  O  ASN A 348   N  MSE A  95           
SHEET    1  AB 5 LYS A 284  TYR A 287  0                                        
SHEET    2  AB 5 ILE A 275  ALA A 278 -1  O  ILE A 275   N  TYR A 287           
SHEET    3  AB 5 ASN A 348  LEU A 357 -1  O  LYS A 355   N  ALA A 278           
SHEET    4  AB 5 THR A 336  PRO A 342 -1  O  VAL A 337   N  LEU A 353           
SHEET    5  AB 5 ALA B   4  ALA B   5 -1  O  ALA B   5   N  GLN A 338           
SHEET    1  AC 4 LYS A 284  TYR A 287  0                                        
SHEET    2  AC 4 ILE A 275  ALA A 278 -1  O  ILE A 275   N  TYR A 287           
SHEET    3  AC 4 ASN A 348  LEU A 357 -1  O  LYS A 355   N  ALA A 278           
SHEET    4  AC 4 VAL A  93  MSE 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           
LINK         C   ALA A  51                 N   MSE A  52     1555   1555  1.33  
LINK         C   MSE A  52                 N   ASP A  53     1555   1555  1.33  
LINK         C   GLY A  82                 N   MSE A  83     1555   1555  1.34  
LINK         C   MSE A  83                 N   LEU A  84     1555   1555  1.33  
LINK         C   TYR A  94                 N   MSE A  95     1555   1555  1.33  
LINK         C   MSE A  95                 N   ASP A  96     1555   1555  1.33  
LINK         C   GLY A 119                 N   MSE A 120     1555   1555  1.33  
LINK         C   MSE A 120                 N   GLU A 121     1555   1555  1.33  
LINK         C   SER A 154                 N   MSE A 155     1555   1555  1.33  
LINK         C   MSE A 155                 N   ALA A 156     1555   1555  1.33  
LINK         C   SER A 176                 N   MSE A 177     1555   1555  1.32  
LINK         C   MSE A 177                 N   LYS A 178     1555   1555  1.33  
LINK         C   PRO A 342                 N   MSE A 343     1555   1555  1.32  
LINK         C   MSE A 343                 N   GLY A 344     1555   1555  1.33  
LINK         C   ASP A 395                 N   MSE A 396     1555   1555  1.33  
LINK         C   MSE A 396                 N   ASN A 397     1555   1555  1.32  
LINK         C   ASP A 425                 N   MSE A 426     1555   1555  1.32  
LINK         C   MSE A 426                 N   LYS A 427     1555   1555  1.33  
LINK         C   VAL A 430                 N   MSE A 431     1555   1555  1.33  
LINK         C   MSE A 431                 N   ALA A 432     1555   1555  1.33  
CRYST1  118.785  118.785   72.660  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      0.008419  0.004860  0.000000        0.00000                         
SCALE2      0.000000  0.009721  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013763        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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