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Database: PDB
Entry: 4ACK
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Original site: 4ACK 
HEADER    PROTEIN TRANSPORT                       15-DEC-11   4ACK              
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, VIRULENCE      
KEYWDS   2 FACTOR                                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.S.ROBB,F.E.NANO,A.B.BORASTON                                        
REVDAT   2   06-JUN-12 4ACK    1       JRNL   REMARK                            
REVDAT   1   25-APR-12 4ACK    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.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.0                                           
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) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 65.99                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.83                          
REMARK   3   NUMBER OF REFLECTIONS             : 22858                          
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) : 0.19691                         
REMARK   3   R VALUE            (WORKING SET) : 0.19391                         
REMARK   3   FREE R VALUE                     : 0.25118                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1227                            
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) : 2.150                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.206                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1726                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.89                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.239                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 90                           
REMARK   3   BIN FREE R VALUE                    : 0.345                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2603                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 139                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.180                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.46                                                
REMARK   3    B22 (A**2) : 2.42                                                 
REMARK   3    B33 (A**2) : -1.21                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : -0.55                                                
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.206         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.191         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.127         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.774         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.921                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2679 ; 0.023 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3606 ; 1.778 ; 1.964       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   308 ; 6.140 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   139 ;42.064 ;24.892       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   498 ;17.211 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;18.775 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   393 ; 0.125 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1993 ; 0.010 ; 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):  1539 ; 1.317 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2502 ; 2.401 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1140 ; 3.363 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1103 ; 5.242 ; 4.500       
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          
REMARK   3   RIDING POSITIONS. RESIDUES A23-25 B24 B113-114 ARE DISORDERED      
REMARK   4                                                                      
REMARK   4 4ACK 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 PDBE ID CODE IS EBI-50729.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-APR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.920                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (MX-325)                       
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24116                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.15                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 65.99                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.6                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.90                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.27                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.6                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.41                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.00                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIRAS                        
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   (%): 51.85                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.115 M KBR, 0.1 M TRIS, PH 8.5,         
REMARK 280   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       42.92000            
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     ASP A    23                                                      
REMARK 465     ASN A    24                                                      
REMARK 465     ASP A    25                                                      
REMARK 465     ILE A   156                                                      
REMARK 465     GLU A   157                                                      
REMARK 465     ASN A   158                                                      
REMARK 465     SER A   159                                                      
REMARK 465     THR A   160                                                      
REMARK 465     ILE A   161                                                      
REMARK 465     ASP A   162                                                      
REMARK 465     SER A   163                                                      
REMARK 465     VAL A   164                                                      
REMARK 465     ASN A   165                                                      
REMARK 465     PHE A   166                                                      
REMARK 465     ILE A   167                                                      
REMARK 465     ASP A   168                                                      
REMARK 465     ILE A   169                                                      
REMARK 465     PRO A   170                                                      
REMARK 465     VAL A   171                                                      
REMARK 465     ASN A   172                                                      
REMARK 465     SER A   173                                                      
REMARK 465     PRO A   174                                                      
REMARK 465     PRO A   175                                                      
REMARK 465     LEU A   176                                                      
REMARK 465     SER A   177                                                      
REMARK 465     ARG A   178                                                      
REMARK 465     LYS A   179                                                      
REMARK 465     TYR A   180                                                      
REMARK 465     SER A   181                                                      
REMARK 465     LYS A   182                                                      
REMARK 465     THR A   183                                                      
REMARK 465     LEU A   184                                                      
REMARK 465     LYS A   185                                                      
REMARK 465     ASN B    24                                                      
REMARK 465     GLU B   113                                                      
REMARK 465     ASN B   114                                                      
REMARK 465     GLU B   157                                                      
REMARK 465     ASN B   158                                                      
REMARK 465     SER B   159                                                      
REMARK 465     THR B   160                                                      
REMARK 465     ILE B   161                                                      
REMARK 465     ASP B   162                                                      
REMARK 465     SER B   163                                                      
REMARK 465     VAL B   164                                                      
REMARK 465     ASN B   165                                                      
REMARK 465     PHE B   166                                                      
REMARK 465     ILE B   167                                                      
REMARK 465     ASP B   168                                                      
REMARK 465     ILE B   169                                                      
REMARK 465     PRO B   170                                                      
REMARK 465     VAL B   171                                                      
REMARK 465     ASN B   172                                                      
REMARK 465     SER B   173                                                      
REMARK 465     PRO B   174                                                      
REMARK 465     PRO B   175                                                      
REMARK 465     LEU B   176                                                      
REMARK 465     SER B   177                                                      
REMARK 465     ARG B   178                                                      
REMARK 465     LYS B   179                                                      
REMARK 465     TYR B   180                                                      
REMARK 465     SER B   181                                                      
REMARK 465     LYS B   182                                                      
REMARK 465     THR B   183                                                      
REMARK 465     LEU B   184                                                      
REMARK 465     LYS B   185                                                      
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     ARG A  18    NE   CZ   NH1  NH2                                  
REMARK 470     GLU A  22    CG   CD   OE1  OE2                                  
REMARK 470     ASN A  26    CG   OD1  ND2                                       
REMARK 470     LYS A  79    CG   CD   CE   NZ                                   
REMARK 470     MET B   1    CG   SD   CE                                        
REMARK 470     ASP B  23    CG   OD1  OD2                                       
REMARK 470     ASP B  25    CG   OD1  OD2                                       
REMARK 470     LYS B  79    CG   CD   CE   NZ                                   
REMARK 470     ILE B 115    CG1  CG2  CD1                                       
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    TRP A  86       99.47   -160.89                                   
REMARK 500    ASN A 114       49.03    -84.96                                   
REMARK 500    ASN A 139       98.72   -162.38                                   
REMARK 500    LYS A 154        0.55    -67.28                                   
REMARK 500    LYS B  79       60.66   -113.29                                   
REMARK 500    ASN B 139       75.36   -161.03                                   
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  BR A1156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1157                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  BR B1157                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  BR B1158                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1159                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1160                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1161                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1162                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1163                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4ACL   RELATED DB: PDB                                   
REMARK 900  3D STRUCTURE OF DOTU FROM FRANCISELLA NOVICIDA                      
DBREF  4ACK A    1   185  UNP    A0Q7H7   A0Q7H7_FRATN     1    185             
DBREF  4ACK B    1   185  UNP    A0Q7H7   A0Q7H7_FRATN     1    185             
SEQRES   1 A  185  MET LYS ASP PHE LYS GLU ILE GLU ILE ILE LEU ASP ILE          
SEQRES   2 A  185  ILE LYS THR THR ARG GLU ILE ILE GLU ASP ASN ASP ASN          
SEQRES   3 A  185  ASP ASN GLU LYS ILE SER TYR HIS ARG ASN ASN ILE ARG          
SEQRES   4 A  185  LYS SER ILE PHE PHE LEU GLN GLU GLU LEU LEU GLU LYS          
SEQRES   5 A  185  TYR SER GLU THR VAL CYS LYS TYR ILE VAL PHE PRO LEU          
SEQRES   6 A  185  LEU ALA TYR VAL ASP GLU LYS LEU MET LEU LEU ARG GLU          
SEQRES   7 A  185  LYS SER ALA SER ASN ILE SER TRP SER LEU LEU GLN LEU          
SEQRES   8 A  185  GLU TYR TYR ASP ARG LYS ASP GLY GLY GLU TYR VAL PHE          
SEQRES   9 A  185  GLU ILE THR ASP ASN ILE LEU SER GLU ASN ILE TYR PRO          
SEQRES  10 A  185  GLN ILE CYS TYR GLN THR ILE SER LEU ILE LEU HIS ASN          
SEQRES  11 A  185  ASP PHE TYR GLY LYS TYR TYR ASP ASN ILE TYR ASN HIS          
SEQRES  12 A  185  SER PHE LEU ALA TYR LYS LYS GLU ILE ASP LYS HIS ILE          
SEQRES  13 A  185  GLU ASN SER THR ILE ASP SER VAL ASN PHE ILE ASP ILE          
SEQRES  14 A  185  PRO VAL ASN SER PRO PRO LEU SER ARG LYS TYR SER LYS          
SEQRES  15 A  185  THR LEU LYS                                                  
SEQRES   1 B  185  MET LYS ASP PHE LYS GLU ILE GLU ILE ILE LEU ASP ILE          
SEQRES   2 B  185  ILE LYS THR THR ARG GLU ILE ILE GLU ASP ASN ASP ASN          
SEQRES   3 B  185  ASP ASN GLU LYS ILE SER TYR HIS ARG ASN ASN ILE ARG          
SEQRES   4 B  185  LYS SER ILE PHE PHE LEU GLN GLU GLU LEU LEU GLU LYS          
SEQRES   5 B  185  TYR SER GLU THR VAL CYS LYS TYR ILE VAL PHE PRO LEU          
SEQRES   6 B  185  LEU ALA TYR VAL ASP GLU LYS LEU MET LEU LEU ARG GLU          
SEQRES   7 B  185  LYS SER ALA SER ASN ILE SER TRP SER LEU LEU GLN LEU          
SEQRES   8 B  185  GLU TYR TYR ASP ARG LYS ASP GLY GLY GLU TYR VAL PHE          
SEQRES   9 B  185  GLU ILE THR ASP ASN ILE LEU SER GLU ASN ILE TYR PRO          
SEQRES  10 B  185  GLN ILE CYS TYR GLN THR ILE SER LEU ILE LEU HIS ASN          
SEQRES  11 B  185  ASP PHE TYR GLY LYS TYR TYR ASP ASN ILE TYR ASN HIS          
SEQRES  12 B  185  SER PHE LEU ALA TYR LYS LYS GLU ILE ASP LYS HIS ILE          
SEQRES  13 B  185  GLU ASN SER THR ILE ASP SER VAL ASN PHE ILE ASP ILE          
SEQRES  14 B  185  PRO VAL ASN SER PRO PRO LEU SER ARG LYS TYR SER LYS          
SEQRES  15 B  185  THR LEU LYS                                                  
HET     BR  A1156       1                                                       
HET    EDO  A1157       4                                                       
HET     BR  A1158       1                                                       
HET     BR  B1157       1                                                       
HET     BR  B1158       1                                                       
HET    EDO  B1159       4                                                       
HET    EDO  B1160       4                                                       
HET    EDO  B1161       4                                                       
HET    EDO  B1162       4                                                       
HET    EDO  B1163       4                                                       
HETNAM      BR BROMIDE ION                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3   BR    4(BR 1-)                                                     
FORMUL   4  EDO    6(C2 H6 O2)                                                  
FORMUL   5  HOH   *139(H2 O)                                                    
HELIX    1   1 ASP A    3  ILE A   21  1                                  19    
HELIX    2   2 GLU A   29  TYR A   53  1                                  25    
HELIX    3   3 SER A   54  SER A   80  1                                  27    
HELIX    4   4 LEU A   88  ASP A   95  1                                   8    
HELIX    5   5 ASP A   98  GLU A  113  1                                  16    
HELIX    6   6 PRO A  117  ASN A  130  1                                  14    
HELIX    7   7 TYR A  133  TYR A  137  5                                   5    
HELIX    8   8 ASN A  142  LYS A  154  1                                  13    
HELIX    9   9 ASP B    3  ASP B   23  1                                  21    
HELIX   10  10 ASP B   27  TYR B   53  1                                  27    
HELIX   11  11 SER B   54  LYS B   79  1                                  26    
HELIX   12  12 LEU B   88  ASP B   95  1                                   8    
HELIX   13  13 ASP B   98  SER B  112  1                                  15    
HELIX   14  14 PRO B  117  ASN B  130  1                                  14    
HELIX   15  15 TYR B  133  TYR B  137  5                                   5    
HELIX   16  16 ASN B  142  ILE B  156  1                                  15    
SITE     1 AC1  2 THR A  16  SER A  41                                          
SITE     1 AC2  2 LYS A 135  HOH A2023                                          
SITE     1 AC3  2 LYS B   2  HOH B2061                                          
SITE     1 AC4  3 ARG B  77  SER B  80  SER B  82                               
SITE     1 AC5  7 ASP A 138  ASN A 139  SER B  87  LEU B  88                    
SITE     2 AC5  7 LEU B  91  HOH B2046  HOH B2083                               
SITE     1 AC6  3 LEU B 128  HIS B 129  LYS B 149                               
SITE     1 AC7  5 TYR A 141  ARG B  39  ASN B 139  ILE B 140                    
SITE     2 AC7  5 TYR B 141                                                     
SITE     1 AC8  5 ARG B  39  PHE B  43  GLN B  46  TYR B  93                    
SITE     2 AC8  5 HIS B 143                                                     
SITE     1 AC9  5 ARG B  96  ASP B  98  GLU B 101  TYR B 102                    
SITE     2 AC9  5 GLU B 105                                                     
CRYST1   39.660   85.840   67.710  90.00 102.93  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      0.025214  0.000000  0.005789        0.00000                         
SCALE2      0.000000  0.011650  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015153        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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