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Database: PDB
Entry: 4ACL
LinkDB: 4ACL
Original site: 4ACL 
HEADER    PROTEIN TRANSPORT                       16-DEC-11   4ACL              
TITLE     3D STRUCTURE OF DOTU FROM FRANCISELLA NOVICIDA                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TSSL;                                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CYTOPLASMIC DOMAIN, RESIDUES 1-185;                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: FRANCISELLA NOVICIDA;                           
SOURCE   3 ORGANISM_TAXID: 401614;                                              
SOURCE   4 STRAIN: U112;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET28                                      
KEYWDS    PROTEIN TRANSPORT, T6SS, MICROBIAL SURFACE STRUCTURES, MEMBRANE       
KEYWDS   2 PROTEIN, VIRULENCE FACTOR                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.S.ROBB,F.E.NANO,A.B.BORASTON                                        
REVDAT   4   13-SEP-17 4ACL    1       REMARK                                   
REVDAT   3   05-JUL-17 4ACL    1       REMARK                                   
REVDAT   2   06-JUN-12 4ACL    1       JRNL   REMARK                            
REVDAT   1   25-APR-12 4ACL    0                                                
JRNL        AUTH   C.S.ROBB,F.E.NANO,A.B.BORASTON                               
JRNL        TITL   THE STRUCTURE OF THE CONSERVED TYPE SIX SECRETION PROTEIN    
JRNL        TITL 2 TSSL (DOTU) FROM FRANCISELLA NOVICIDA                        
JRNL        REF    J.MOL.BIOL.                   V. 419   277 2012              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   22504227                                                     
JRNL        DOI    10.1016/J.JMB.2012.04.003                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.49 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0110                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.49                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 65.43                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 14199                          
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 + TEST SET) : 0.221                           
REMARK   3   R VALUE            (WORKING SET) : 0.218                           
REMARK   3   FREE R VALUE                     : 0.279                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 754                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.49                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.55                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 945                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.08                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2390                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 66                           
REMARK   3   BIN FREE R VALUE                    : 0.2630                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2565                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 21                                      
REMARK   3   SOLVENT ATOMS            : 40                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.05000                                             
REMARK   3    B22 (A**2) : 2.55000                                              
REMARK   3    B33 (A**2) : -0.43000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.17000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.473         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.306         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.250         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.962        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.891                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2635 ; 0.018 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3564 ; 1.649 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   310 ; 6.894 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   134 ;43.816 ;24.851       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   471 ;20.133 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;16.420 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   396 ; 0.127 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1977 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1549 ; 0.901 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2503 ; 1.682 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1086 ; 2.183 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1060 ; 3.509 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 4ACL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-DEC-11.                  
REMARK 100 THE DEPOSITION ID IS D_1290050730.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-APR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 113                                
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-002                
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : OSMIC BLUE                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU R-AXIS IV                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : D*TREK                             
REMARK 200  DATA SCALING SOFTWARE          : D*TREK                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15228                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.490                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 65.990                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 13.20                              
REMARK 200  R MERGE                    (I) : 0.12000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.60                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 12.20                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.50000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS                        
REMARK 200 SOFTWARE USED: AUTOSHARP                                             
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS, PH 8.8, 20% PEG 3350.        
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       42.65700            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     MET A   -20                                                      
REMARK 465     GLY A   -19                                                      
REMARK 465     SER A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     LEU A    -7                                                      
REMARK 465     VAL A    -6                                                      
REMARK 465     PRO A    -5                                                      
REMARK 465     ARG A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     MET A     0                                                      
REMARK 465     LYS A     1                                                      
REMARK 465     ASN A   157                                                      
REMARK 465     SER A   158                                                      
REMARK 465     THR A   159                                                      
REMARK 465     ILE A   160                                                      
REMARK 465     ASP A   161                                                      
REMARK 465     SER A   162                                                      
REMARK 465     VAL A   163                                                      
REMARK 465     ASN A   164                                                      
REMARK 465     PHE A   165                                                      
REMARK 465     ILE A   166                                                      
REMARK 465     ASP A   167                                                      
REMARK 465     ILE A   168                                                      
REMARK 465     PRO A   169                                                      
REMARK 465     VAL A   170                                                      
REMARK 465     ASN A   171                                                      
REMARK 465     SER A   172                                                      
REMARK 465     PRO A   173                                                      
REMARK 465     PRO A   174                                                      
REMARK 465     LEU A   175                                                      
REMARK 465     SER A   176                                                      
REMARK 465     ARG A   177                                                      
REMARK 465     LYS A   178                                                      
REMARK 465     TYR A   179                                                      
REMARK 465     SER A   180                                                      
REMARK 465     LYS A   181                                                      
REMARK 465     THR A   182                                                      
REMARK 465     LEU A   183                                                      
REMARK 465     LYS A   184                                                      
REMARK 465     MET B   -20                                                      
REMARK 465     GLY B   -19                                                      
REMARK 465     SER B   -18                                                      
REMARK 465     SER B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     SER B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     GLY B    -8                                                      
REMARK 465     LEU B    -7                                                      
REMARK 465     VAL B    -6                                                      
REMARK 465     PRO B    -5                                                      
REMARK 465     ARG B    -4                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     MET B     0                                                      
REMARK 465     LYS B     1                                                      
REMARK 465     ASN B   157                                                      
REMARK 465     SER B   158                                                      
REMARK 465     THR B   159                                                      
REMARK 465     ILE B   160                                                      
REMARK 465     ASP B   161                                                      
REMARK 465     SER B   162                                                      
REMARK 465     VAL B   163                                                      
REMARK 465     ASN B   164                                                      
REMARK 465     PHE B   165                                                      
REMARK 465     ILE B   166                                                      
REMARK 465     ASP B   167                                                      
REMARK 465     ILE B   168                                                      
REMARK 465     PRO B   169                                                      
REMARK 465     VAL B   170                                                      
REMARK 465     ASN B   171                                                      
REMARK 465     SER B   172                                                      
REMARK 465     PRO B   173                                                      
REMARK 465     PRO B   174                                                      
REMARK 465     LEU B   175                                                      
REMARK 465     SER B   176                                                      
REMARK 465     ARG B   177                                                      
REMARK 465     LYS B   178                                                      
REMARK 465     TYR B   179                                                      
REMARK 465     SER B   180                                                      
REMARK 465     LYS B   181                                                      
REMARK 465     THR B   182                                                      
REMARK 465     LEU B   183                                                      
REMARK 465     LYS B   184                                                      
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     ASP A   2    CG   OD1  OD2                                       
REMARK 470     LYS A   4    CG   CD   CE   NZ                                   
REMARK 470     ASP A  22    CG   OD1  OD2                                       
REMARK 470     ASN A  23    CG   OD1  ND2                                       
REMARK 470     CYS A  57    SG                                                  
REMARK 470     LYS A  78    CG   CD   CE   NZ                                   
REMARK 470     ASN A  82    CG   OD1  ND2                                       
REMARK 470     ASP A 107    CG   OD1  OD2                                       
REMARK 470     SER A 111    OG                                                  
REMARK 470     GLU A 112    CG   CD   OE1  OE2                                  
REMARK 470     HIS A 128    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A 156    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  17    CZ   NH1  NH2                                       
REMARK 470     ASP B  22    CG   OD1  OD2                                       
REMARK 470     ASN B  23    CG   OD1  ND2                                       
REMARK 470     ASP B  24    CG   OD1  OD2                                       
REMARK 470     GLU B  46    CG   CD   OE1  OE2                                  
REMARK 470     CYS B  57    SG                                                  
REMARK 470     LYS B  78    CG   CD   CE   NZ                                   
REMARK 470     ASN B  82    CG   OD1  ND2                                       
REMARK 470     SER B 111    OG                                                  
REMARK 470     GLU B 112    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 114    CG1  CG2  CD1                                       
REMARK 470     HIS B 128    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS B 153    CG   CD   CE   NZ                                   
REMARK 470     GLU B 156    CG   CD   OE1  OE2                                  
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   3      117.08   -169.63                                   
REMARK 500    SER A  81      146.21    -39.97                                   
REMARK 500    ASP A  97       31.26    -99.87                                   
REMARK 500    ASN A 113      175.97    176.26                                   
REMARK 500    HIS A 128       -5.81    -59.68                                   
REMARK 500    ASP B  22      109.64    -56.25                                   
REMARK 500    ASP B  24       76.44   -105.88                                   
REMARK 500    ALA B  80      -87.82    -81.92                                   
REMARK 500    ASP B  97       41.87    -93.87                                   
REMARK 500    ASN B 113      174.63    178.64                                   
REMARK 500    GLN B 117      -31.69    -32.82                                   
REMARK 500    LYS B 153       21.33    -75.32                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1157                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1158                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AU A 1159                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AU A 1160                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AU A 1161                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AU A 1162                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AU B 1157                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AU B 1158                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AU B 1159                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AU B 1160                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AU B 1161                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AU B 1162                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AU A 1166                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4ACK   RELATED DB: PDB                                   
REMARK 900 3D STRUCTURE OF DOTU FROM FRANCISELLA NOVICIDA                       
DBREF  4ACL A    0   184  UNP    A0Q7H7   A0Q7H7_FRATN     1    185             
DBREF  4ACL B    0   184  UNP    A0Q7H7   A0Q7H7_FRATN     1    185             
SEQADV 4ACL MET A  -20  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL GLY A  -19  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL SER A  -18  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL SER A  -17  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL HIS A  -16  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL HIS A  -15  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL HIS A  -14  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL HIS A  -13  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL HIS A  -12  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL HIS A  -11  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL SER A  -10  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL SER A   -9  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL GLY A   -8  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL LEU A   -7  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL VAL A   -6  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL PRO A   -5  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL ARG A   -4  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL GLY A   -3  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL SER A   -2  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL HIS A   -1  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL MET B  -20  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL GLY B  -19  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL SER B  -18  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL SER B  -17  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL HIS B  -16  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL HIS B  -15  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL HIS B  -14  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL HIS B  -13  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL HIS B  -12  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL HIS B  -11  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL SER B  -10  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL SER B   -9  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL GLY B   -8  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL LEU B   -7  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL VAL B   -6  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL PRO B   -5  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL ARG B   -4  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL GLY B   -3  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL SER B   -2  UNP  A0Q7H7              EXPRESSION TAG                 
SEQADV 4ACL HIS B   -1  UNP  A0Q7H7              EXPRESSION TAG                 
SEQRES   1 A  205  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  205  LEU VAL PRO ARG GLY SER HIS MET LYS ASP PHE LYS GLU          
SEQRES   3 A  205  ILE GLU ILE ILE LEU ASP ILE ILE LYS THR THR ARG GLU          
SEQRES   4 A  205  ILE ILE GLU ASP ASN ASP ASN ASP ASN GLU LYS ILE SER          
SEQRES   5 A  205  TYR HIS ARG ASN ASN ILE ARG LYS SER ILE PHE PHE LEU          
SEQRES   6 A  205  GLN GLU GLU LEU LEU GLU LYS TYR SER GLU THR VAL CYS          
SEQRES   7 A  205  LYS TYR ILE VAL PHE PRO LEU LEU ALA TYR VAL ASP GLU          
SEQRES   8 A  205  LYS LEU MET LEU LEU ARG GLU LYS SER ALA SER ASN ILE          
SEQRES   9 A  205  SER TRP SER LEU LEU GLN LEU GLU TYR TYR ASP ARG LYS          
SEQRES  10 A  205  ASP GLY GLY GLU TYR VAL PHE GLU ILE THR ASP ASN ILE          
SEQRES  11 A  205  LEU SER GLU ASN ILE TYR PRO GLN ILE CYS TYR GLN THR          
SEQRES  12 A  205  ILE SER LEU ILE LEU HIS ASN ASP PHE TYR GLY LYS TYR          
SEQRES  13 A  205  TYR ASP ASN ILE TYR ASN HIS SER PHE LEU ALA TYR LYS          
SEQRES  14 A  205  LYS GLU ILE ASP LYS HIS ILE GLU ASN SER THR ILE ASP          
SEQRES  15 A  205  SER VAL ASN PHE ILE ASP ILE PRO VAL ASN SER PRO PRO          
SEQRES  16 A  205  LEU SER ARG LYS TYR SER LYS THR LEU LYS                      
SEQRES   1 B  205  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  205  LEU VAL PRO ARG GLY SER HIS MET LYS ASP PHE LYS GLU          
SEQRES   3 B  205  ILE GLU ILE ILE LEU ASP ILE ILE LYS THR THR ARG GLU          
SEQRES   4 B  205  ILE ILE GLU ASP ASN ASP ASN ASP ASN GLU LYS ILE SER          
SEQRES   5 B  205  TYR HIS ARG ASN ASN ILE ARG LYS SER ILE PHE PHE LEU          
SEQRES   6 B  205  GLN GLU GLU LEU LEU GLU LYS TYR SER GLU THR VAL CYS          
SEQRES   7 B  205  LYS TYR ILE VAL PHE PRO LEU LEU ALA TYR VAL ASP GLU          
SEQRES   8 B  205  LYS LEU MET LEU LEU ARG GLU LYS SER ALA SER ASN ILE          
SEQRES   9 B  205  SER TRP SER LEU LEU GLN LEU GLU TYR TYR ASP ARG LYS          
SEQRES  10 B  205  ASP GLY GLY GLU TYR VAL PHE GLU ILE THR ASP ASN ILE          
SEQRES  11 B  205  LEU SER GLU ASN ILE TYR PRO GLN ILE CYS TYR GLN THR          
SEQRES  12 B  205  ILE SER LEU ILE LEU HIS ASN ASP PHE TYR GLY LYS TYR          
SEQRES  13 B  205  TYR ASP ASN ILE TYR ASN HIS SER PHE LEU ALA TYR LYS          
SEQRES  14 B  205  LYS GLU ILE ASP LYS HIS ILE GLU ASN SER THR ILE ASP          
SEQRES  15 B  205  SER VAL ASN PHE ILE ASP ILE PRO VAL ASN SER PRO PRO          
SEQRES  16 B  205  LEU SER ARG LYS TYR SER LYS THR LEU LYS                      
HET     NA  A1156       1                                                       
HET    EDO  A1157       4                                                       
HET    EDO  A1158       4                                                       
HET     AU  A1159       1                                                       
HET     AU  A1160       1                                                       
HET     AU  A1161       1                                                       
HET     AU  A1162       1                                                       
HET     AU  A1164       1                                                       
HET     AU  A1166       1                                                       
HET     AU  B1157       1                                                       
HET     AU  B1158       1                                                       
HET     AU  B1159       1                                                       
HET     AU  B1160       1                                                       
HET     AU  B1161       1                                                       
HET     AU  B1162       1                                                       
HETNAM      NA SODIUM ION                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM      AU GOLD ION                                                         
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3   NA    NA 1+                                                        
FORMUL   4  EDO    2(C2 H6 O2)                                                  
FORMUL   6   AU    12(AU 1+)                                                    
FORMUL  18  HOH   *40(H2 O)                                                     
HELIX    1   1 PHE A    3  ASP A   22  1                                  20    
HELIX    2   2 ASP A   26  TYR A   52  1                                  27    
HELIX    3   3 SER A   53  SER A   79  1                                  27    
HELIX    4   4 LEU A   87  ASP A   94  1                                   8    
HELIX    5   5 ASP A   97  GLU A  112  1                                  16    
HELIX    6   6 PRO A  116  HIS A  128  1                                  13    
HELIX    7   7 TYR A  132  TYR A  136  5                                   5    
HELIX    8   8 ASN A  141  LYS A  153  1                                  13    
HELIX    9   9 LYS B    4  ASP B   22  1                                  19    
HELIX   10  10 ASP B   26  TYR B   52  1                                  27    
HELIX   11  11 SER B   53  LYS B   78  1                                  26    
HELIX   12  12 LEU B   87  ASP B   94  1                                   8    
HELIX   13  13 ASP B   97  GLU B  112  1                                  16    
HELIX   14  14 PRO B  116  ASN B  129  1                                  14    
HELIX   15  15 TYR B  132  TYR B  136  5                                   5    
HELIX   16  16 ASN B  141  LYS B  153  1                                  13    
LINK        AU    AU A1160                 ND1 HIS A 154     1555   1555  2.56  
LINK        AU    AU B1157                 ND1 HIS B 154     1555   1555  2.78  
LINK        AU    AU B1158                 OD2 ASP B 152     1555   1555  2.74  
LINK        AU    AU B1159                 ND1 HIS B 142     1555   1555  2.19  
SITE     1 AC1  4 LYS A  96  GLY A  98  GLY A  99  HOH A2018                    
SITE     1 AC2  5 ARG A  38  ASP A 137  ASN A 138  ILE A 139                    
SITE     2 AC2  5 TYR A 140                                                     
SITE     1 AC3  2 LEU A  49  CYS A  57                                          
SITE     1 AC4  3 TYR A 120  HIS A 154  HOH A2022                               
SITE     1 AC5  2 LEU A 110  HIS A 154                                          
SITE     1 AC6  2 HIS A 128  SER B  81                                          
SITE     1 AC7  2 TYR B 120  HIS B 154                                          
SITE     1 AC8  1 ASP B 152                                                     
SITE     1 AC9  1 HIS B 142                                                     
SITE     1 BC1  3 GLN B  45  LEU B  49  CYS B  57                               
SITE     1 BC2  2 HIS B 128  HOH B2011                                          
SITE     1 BC3  1 HIS B 154                                                     
SITE     1 BC4  1 ASP A 152                                                     
CRYST1   39.309   85.314   66.989  90.00 102.38  90.00 P 1 21 1      4          
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      0.025439  0.000000  0.005584        0.00000                         
SCALE2      0.000000  0.011721  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015283        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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