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Database: PDB
Entry: 1KAW
LinkDB: 1KAW
Original site: 1KAW 
HEADER    DNA BINDING PROTEIN                     06-DEC-96   1KAW              
TITLE     STRUCTURE OF SINGLE STRANDED DNA BINDING PROTEIN (SSB)                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SINGLE-STRANDED DNA BINDING PROTEIN;                       
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: CHYMOTRYPTIC FRAGMENT, RESIDUES 1 - 135;                   
COMPND   5 SYNONYM: SSB                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562                                                  
KEYWDS    DNA-BINDING PROTEIN, SINGLE STRANDED DNA BINDING PROTEIN, SSB, DNA    
KEYWDS   2 BINDING PROTEIN                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.RAGHUNATHAN,G.WAKSMAN                                               
REVDAT   3   07-FEB-24 1KAW    1       KEYWDS                                   
REVDAT   2   24-FEB-09 1KAW    1       VERSN                                    
REVDAT   1   31-DEC-97 1KAW    0                                                
JRNL        AUTH   S.RAGHUNATHAN,C.S.RICARD,T.M.LOHMAN,G.WAKSMAN                
JRNL        TITL   CRYSTAL STRUCTURE OF THE HOMO-TETRAMERIC DNA BINDING DOMAIN  
JRNL        TITL 2 OF ESCHERICHIA COLI SINGLE-STRANDED DNA-BINDING PROTEIN      
JRNL        TITL 3 DETERMINED BY MULTIWAVELENGTH X-RAY DIFFRACTION ON THE       
JRNL        TITL 4 SELENOMETHIONYL PROTEIN AT 2.9-A RESOLUTION.                 
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V.  94  6652 1997              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   9192620                                                      
JRNL        DOI    10.1073/PNAS.94.13.6652                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.85                                          
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 10473                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.289                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
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            : 3032                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 35                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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) : 0.016                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.900                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  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: MOLECULAR DYNAMICS RESTRAINED             
REMARK   3  REFINEMENT FOLLOWED BY LEAST-SQUARES OPTIMIZATION                   
REMARK   4                                                                      
REMARK   4 1KAW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000174392.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-NOV-95                          
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               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0800                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14346                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.7                               
REMARK 200  DATA REDUNDANCY                : 2.600                              
REMARK 200  R MERGE                    (I) : 0.05300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR 3.85                                           
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       29.04000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.92500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       29.04000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       52.92500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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     ALA A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     PRO A    24                                                      
REMARK 465     ASN A    25                                                      
REMARK 465     GLY A    26                                                      
REMARK 465     GLY A    27                                                      
REMARK 465     TRP A    40                                                      
REMARK 465     ARG A    41                                                      
REMARK 465     ASP A    42                                                      
REMARK 465     LYS A    43                                                      
REMARK 465     ALA A    44                                                      
REMARK 465     THR A    45                                                      
REMARK 465     GLY A    46                                                      
REMARK 465     GLU A    47                                                      
REMARK 465     MET A    48                                                      
REMARK 465     LYS A    49                                                      
REMARK 465     GLY A   113                                                      
REMARK 465     GLY A   114                                                      
REMARK 465     ARG A   115                                                      
REMARK 465     GLN A   116                                                      
REMARK 465     GLY A   117                                                      
REMARK 465     GLY A   118                                                      
REMARK 465     GLY A   119                                                      
REMARK 465     ALA A   120                                                      
REMARK 465     PRO A   121                                                      
REMARK 465     ALA A   122                                                      
REMARK 465     GLY A   123                                                      
REMARK 465     GLY A   124                                                      
REMARK 465     ASN A   125                                                      
REMARK 465     ILE A   126                                                      
REMARK 465     GLY A   127                                                      
REMARK 465     GLY A   128                                                      
REMARK 465     GLY A   129                                                      
REMARK 465     GLN A   130                                                      
REMARK 465     PRO A   131                                                      
REMARK 465     GLN A   132                                                      
REMARK 465     GLY A   133                                                      
REMARK 465     GLY A   134                                                      
REMARK 465     TRP A   135                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     PRO B    24                                                      
REMARK 465     ASN B    25                                                      
REMARK 465     GLY B    26                                                      
REMARK 465     GLY B    27                                                      
REMARK 465     TRP B    40                                                      
REMARK 465     ARG B    41                                                      
REMARK 465     ASP B    42                                                      
REMARK 465     LYS B    43                                                      
REMARK 465     ALA B    44                                                      
REMARK 465     THR B    45                                                      
REMARK 465     GLY B    46                                                      
REMARK 465     GLU B    47                                                      
REMARK 465     MET B    48                                                      
REMARK 465     LYS B    49                                                      
REMARK 465     GLY B   113                                                      
REMARK 465     GLY B   114                                                      
REMARK 465     ARG B   115                                                      
REMARK 465     GLN B   116                                                      
REMARK 465     GLY B   117                                                      
REMARK 465     GLY B   118                                                      
REMARK 465     GLY B   119                                                      
REMARK 465     ALA B   120                                                      
REMARK 465     PRO B   121                                                      
REMARK 465     ALA B   122                                                      
REMARK 465     GLY B   123                                                      
REMARK 465     GLY B   124                                                      
REMARK 465     ASN B   125                                                      
REMARK 465     ILE B   126                                                      
REMARK 465     GLY B   127                                                      
REMARK 465     GLY B   128                                                      
REMARK 465     GLY B   129                                                      
REMARK 465     GLN B   130                                                      
REMARK 465     PRO B   131                                                      
REMARK 465     GLN B   132                                                      
REMARK 465     GLY B   133                                                      
REMARK 465     GLY B   134                                                      
REMARK 465     TRP B   135                                                      
REMARK 465     ALA C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     PRO C    24                                                      
REMARK 465     ASN C    25                                                      
REMARK 465     GLY C    26                                                      
REMARK 465     GLY C    27                                                      
REMARK 465     TRP C    40                                                      
REMARK 465     ARG C    41                                                      
REMARK 465     ASP C    42                                                      
REMARK 465     LYS C    43                                                      
REMARK 465     ALA C    44                                                      
REMARK 465     THR C    45                                                      
REMARK 465     GLY C    46                                                      
REMARK 465     GLU C    47                                                      
REMARK 465     MET C    48                                                      
REMARK 465     LYS C    49                                                      
REMARK 465     GLY C   113                                                      
REMARK 465     GLY C   114                                                      
REMARK 465     ARG C   115                                                      
REMARK 465     GLN C   116                                                      
REMARK 465     GLY C   117                                                      
REMARK 465     GLY C   118                                                      
REMARK 465     GLY C   119                                                      
REMARK 465     ALA C   120                                                      
REMARK 465     PRO C   121                                                      
REMARK 465     ALA C   122                                                      
REMARK 465     GLY C   123                                                      
REMARK 465     GLY C   124                                                      
REMARK 465     ASN C   125                                                      
REMARK 465     ILE C   126                                                      
REMARK 465     GLY C   127                                                      
REMARK 465     GLY C   128                                                      
REMARK 465     GLY C   129                                                      
REMARK 465     GLN C   130                                                      
REMARK 465     PRO C   131                                                      
REMARK 465     GLN C   132                                                      
REMARK 465     GLY C   133                                                      
REMARK 465     GLY C   134                                                      
REMARK 465     TRP C   135                                                      
REMARK 465     ALA D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     PRO D    24                                                      
REMARK 465     ASN D    25                                                      
REMARK 465     GLY D    26                                                      
REMARK 465     GLY D    27                                                      
REMARK 465     TRP D    40                                                      
REMARK 465     ARG D    41                                                      
REMARK 465     ASP D    42                                                      
REMARK 465     LYS D    43                                                      
REMARK 465     ALA D    44                                                      
REMARK 465     THR D    45                                                      
REMARK 465     GLY D    46                                                      
REMARK 465     GLU D    47                                                      
REMARK 465     MET D    48                                                      
REMARK 465     LYS D    49                                                      
REMARK 465     GLY D   113                                                      
REMARK 465     GLY D   114                                                      
REMARK 465     ARG D   115                                                      
REMARK 465     GLN D   116                                                      
REMARK 465     GLY D   117                                                      
REMARK 465     GLY D   118                                                      
REMARK 465     GLY D   119                                                      
REMARK 465     ALA D   120                                                      
REMARK 465     PRO D   121                                                      
REMARK 465     ALA D   122                                                      
REMARK 465     GLY D   123                                                      
REMARK 465     GLY D   124                                                      
REMARK 465     ASN D   125                                                      
REMARK 465     ILE D   126                                                      
REMARK 465     GLY D   127                                                      
REMARK 465     GLY D   128                                                      
REMARK 465     GLY D   129                                                      
REMARK 465     GLN D   130                                                      
REMARK 465     PRO D   131                                                      
REMARK 465     GLN D   132                                                      
REMARK 465     GLY D   133                                                      
REMARK 465     GLY D   134                                                      
REMARK 465     TRP D   135                                                      
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   NH2  ARG C    96     CD   ARG D    96              0.96            
REMARK 500   NH2  ARG A    96     CD   ARG B    96              0.96            
REMARK 500   NE   ARG A    96     CZ   ARG B    96              0.97            
REMARK 500   NE   ARG C    96     CZ   ARG D    96              0.97            
REMARK 500   CZ   ARG A    96     NE   ARG B    96              1.04            
REMARK 500   CZ   ARG C    96     NE   ARG D    96              1.04            
REMARK 500   NH2  ARG A    96     NE   ARG B    96              1.07            
REMARK 500   NH2  ARG C    96     NE   ARG D    96              1.07            
REMARK 500   NH2  ARG C     3     O    HOH C   148              1.20            
REMARK 500   NE   ARG A    96     NH2  ARG B    96              1.32            
REMARK 500   NE   ARG C    96     NH2  ARG D    96              1.32            
REMARK 500   NE   ARG A    96     NE   ARG B    96              1.35            
REMARK 500   NE   ARG C    96     NE   ARG D    96              1.35            
REMARK 500   CD   ARG A    96     NH2  ARG B    96              1.49            
REMARK 500   CD   ARG C    96     NH2  ARG D    96              1.49            
REMARK 500   OE2  GLU C    50     O    HOH C   142              1.60            
REMARK 500   OG1  THR D    98     O    HOH D   138              1.69            
REMARK 500   O    SER D    92     O    HOH D   140              1.86            
REMARK 500   CZ   ARG A    96     CZ   ARG B    96              1.94            
REMARK 500   CZ   ARG C    96     CZ   ARG D    96              1.94            
REMARK 500   CZ   ARG C    96     CD   ARG D    96              2.00            
REMARK 500   CZ   ARG A    96     CD   ARG B    96              2.00            
REMARK 500   NH2  ARG A    84     O    GLN C    91              2.01            
REMARK 500   NE2  GLN C    94     NE2  GLN D    94              2.03            
REMARK 500   NE2  GLN A    94     NE2  GLN B    94              2.03            
REMARK 500   CD   ARG A    96     CZ   ARG B    96              2.14            
REMARK 500   CD   ARG C    96     CZ   ARG D    96              2.14            
REMARK 500   NH1  ARG C    84     OE2  GLU C   100              2.15            
REMARK 500   NH1  ARG B    84     OE2  GLU B   100              2.15            
REMARK 500   NH1  ARG A    84     OE2  GLU A   100              2.15            
REMARK 500   NH1  ARG D    84     OE2  GLU D   100              2.15            
REMARK 500   NE   ARG A    96     NH1  ARG B    96              2.15            
REMARK 500   NE   ARG C    96     NH1  ARG D    96              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CE   LYS B     7     OE2  GLU B    80     2556     1.78            
REMARK 500   CG2  VAL B     5     OE1  GLN B   110     2556     1.95            
REMARK 500   OE1  GLU B    65     O    LYS D    87     3445     2.05            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A  10   CA  -  CB  -  CG  ANGL. DEV. =  22.7 DEGREES          
REMARK 500    ARG A  72   NE  -  CZ  -  NH2 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    LEU B  10   CA  -  CB  -  CG  ANGL. DEV. =  22.8 DEGREES          
REMARK 500    ARG B  72   NE  -  CZ  -  NH2 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    LEU C  10   CA  -  CB  -  CG  ANGL. DEV. =  22.8 DEGREES          
REMARK 500    ARG C  72   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    LEU D  10   CA  -  CB  -  CG  ANGL. DEV. =  22.8 DEGREES          
REMARK 500    ARG D  72   NE  -  CZ  -  NH2 ANGL. DEV. =   3.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  17      153.10    -41.62                                   
REMARK 500    GLU A  19       70.91   -105.20                                   
REMARK 500    GLN A  51       46.52     20.01                                   
REMARK 500    PHE A  60     -142.96    -66.40                                   
REMARK 500    LEU A  63      -17.60    -44.68                                   
REMARK 500    TYR A  70       11.82   -141.86                                   
REMARK 500    LEU A  71      -91.18    -70.92                                   
REMARK 500    ARG A  72      112.30     73.25                                   
REMARK 500    LYS A  73      131.39      2.51                                   
REMARK 500    SER A  92        9.45    -65.90                                   
REMARK 500    VAL A 103       73.33   -118.43                                   
REMARK 500    ASN A 104     -101.77    -86.85                                   
REMARK 500    ASP B  17      153.11    -41.60                                   
REMARK 500    GLU B  19       70.93   -105.23                                   
REMARK 500    GLN B  51       46.49     20.04                                   
REMARK 500    PHE B  60     -142.93    -66.40                                   
REMARK 500    LEU B  63      -17.64    -44.62                                   
REMARK 500    TYR B  70       11.77   -141.81                                   
REMARK 500    LEU B  71      -91.14    -70.93                                   
REMARK 500    ARG B  72      112.30     73.22                                   
REMARK 500    LYS B  73      131.35      2.55                                   
REMARK 500    SER B  92        9.39    -65.85                                   
REMARK 500    VAL B 103       73.31   -118.43                                   
REMARK 500    ASN B 104     -101.79    -86.80                                   
REMARK 500    ASP C  17      153.10    -41.61                                   
REMARK 500    GLU C  19       70.91   -105.25                                   
REMARK 500    GLN C  51       46.57     19.98                                   
REMARK 500    PHE C  60     -142.96    -66.41                                   
REMARK 500    LEU C  63      -17.55    -44.74                                   
REMARK 500    TYR C  70       11.80   -141.79                                   
REMARK 500    LEU C  71      -91.17    -70.96                                   
REMARK 500    ARG C  72      112.28     73.28                                   
REMARK 500    LYS C  73      131.41      2.50                                   
REMARK 500    SER C  92        9.50    -65.93                                   
REMARK 500    VAL C 103       73.39   -118.43                                   
REMARK 500    ASN C 104     -101.81    -86.89                                   
REMARK 500    ASP D  17      153.14    -41.68                                   
REMARK 500    GLU D  19       70.98   -105.23                                   
REMARK 500    GLN D  51       46.46     20.06                                   
REMARK 500    PHE D  60     -142.92    -66.40                                   
REMARK 500    LEU D  63      -17.66    -44.64                                   
REMARK 500    TYR D  70       11.81   -141.79                                   
REMARK 500    LEU D  71      -91.08    -70.98                                   
REMARK 500    ARG D  72      112.31     73.15                                   
REMARK 500    LYS D  73      131.39      2.56                                   
REMARK 500    SER D  92        9.42    -65.85                                   
REMARK 500    VAL D 103       73.28   -118.41                                   
REMARK 500    ASN D 104     -101.73    -86.80                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1KAW A    1   135  UNP    P02339   SSB_ECOLI        1    135             
DBREF  1KAW B    1   135  UNP    P02339   SSB_ECOLI        1    135             
DBREF  1KAW C    1   135  UNP    P02339   SSB_ECOLI        1    135             
DBREF  1KAW D    1   135  UNP    P02339   SSB_ECOLI        1    135             
SEQRES   1 A  135  ALA SER ARG GLY VAL ASN LYS VAL ILE LEU VAL GLY ASN          
SEQRES   2 A  135  LEU GLY GLN ASP PRO GLU VAL ARG TYR MET PRO ASN GLY          
SEQRES   3 A  135  GLY ALA VAL ALA ASN ILE THR LEU ALA THR SER GLU SER          
SEQRES   4 A  135  TRP ARG ASP LYS ALA THR GLY GLU MET LYS GLU GLN THR          
SEQRES   5 A  135  GLU TRP HIS ARG VAL VAL LEU PHE GLY LYS LEU ALA GLU          
SEQRES   6 A  135  VAL ALA SER GLU TYR LEU ARG LYS GLY SER GLN VAL TYR          
SEQRES   7 A  135  ILE GLU GLY GLN LEU ARG THR ARG LYS TRP THR ASP GLN          
SEQRES   8 A  135  SER GLY GLN ASP ARG TYR THR THR GLU VAL VAL VAL ASN          
SEQRES   9 A  135  VAL GLY GLY THR MET GLN MET LEU GLY GLY ARG GLN GLY          
SEQRES  10 A  135  GLY GLY ALA PRO ALA GLY GLY ASN ILE GLY GLY GLY GLN          
SEQRES  11 A  135  PRO GLN GLY GLY TRP                                          
SEQRES   1 B  135  ALA SER ARG GLY VAL ASN LYS VAL ILE LEU VAL GLY ASN          
SEQRES   2 B  135  LEU GLY GLN ASP PRO GLU VAL ARG TYR MET PRO ASN GLY          
SEQRES   3 B  135  GLY ALA VAL ALA ASN ILE THR LEU ALA THR SER GLU SER          
SEQRES   4 B  135  TRP ARG ASP LYS ALA THR GLY GLU MET LYS GLU GLN THR          
SEQRES   5 B  135  GLU TRP HIS ARG VAL VAL LEU PHE GLY LYS LEU ALA GLU          
SEQRES   6 B  135  VAL ALA SER GLU TYR LEU ARG LYS GLY SER GLN VAL TYR          
SEQRES   7 B  135  ILE GLU GLY GLN LEU ARG THR ARG LYS TRP THR ASP GLN          
SEQRES   8 B  135  SER GLY GLN ASP ARG TYR THR THR GLU VAL VAL VAL ASN          
SEQRES   9 B  135  VAL GLY GLY THR MET GLN MET LEU GLY GLY ARG GLN GLY          
SEQRES  10 B  135  GLY GLY ALA PRO ALA GLY GLY ASN ILE GLY GLY GLY GLN          
SEQRES  11 B  135  PRO GLN GLY GLY TRP                                          
SEQRES   1 C  135  ALA SER ARG GLY VAL ASN LYS VAL ILE LEU VAL GLY ASN          
SEQRES   2 C  135  LEU GLY GLN ASP PRO GLU VAL ARG TYR MET PRO ASN GLY          
SEQRES   3 C  135  GLY ALA VAL ALA ASN ILE THR LEU ALA THR SER GLU SER          
SEQRES   4 C  135  TRP ARG ASP LYS ALA THR GLY GLU MET LYS GLU GLN THR          
SEQRES   5 C  135  GLU TRP HIS ARG VAL VAL LEU PHE GLY LYS LEU ALA GLU          
SEQRES   6 C  135  VAL ALA SER GLU TYR LEU ARG LYS GLY SER GLN VAL TYR          
SEQRES   7 C  135  ILE GLU GLY GLN LEU ARG THR ARG LYS TRP THR ASP GLN          
SEQRES   8 C  135  SER GLY GLN ASP ARG TYR THR THR GLU VAL VAL VAL ASN          
SEQRES   9 C  135  VAL GLY GLY THR MET GLN MET LEU GLY GLY ARG GLN GLY          
SEQRES  10 C  135  GLY GLY ALA PRO ALA GLY GLY ASN ILE GLY GLY GLY GLN          
SEQRES  11 C  135  PRO GLN GLY GLY TRP                                          
SEQRES   1 D  135  ALA SER ARG GLY VAL ASN LYS VAL ILE LEU VAL GLY ASN          
SEQRES   2 D  135  LEU GLY GLN ASP PRO GLU VAL ARG TYR MET PRO ASN GLY          
SEQRES   3 D  135  GLY ALA VAL ALA ASN ILE THR LEU ALA THR SER GLU SER          
SEQRES   4 D  135  TRP ARG ASP LYS ALA THR GLY GLU MET LYS GLU GLN THR          
SEQRES   5 D  135  GLU TRP HIS ARG VAL VAL LEU PHE GLY LYS LEU ALA GLU          
SEQRES   6 D  135  VAL ALA SER GLU TYR LEU ARG LYS GLY SER GLN VAL TYR          
SEQRES   7 D  135  ILE GLU GLY GLN LEU ARG THR ARG LYS TRP THR ASP GLN          
SEQRES   8 D  135  SER GLY GLN ASP ARG TYR THR THR GLU VAL VAL VAL ASN          
SEQRES   9 D  135  VAL GLY GLY THR MET GLN MET LEU GLY GLY ARG GLN GLY          
SEQRES  10 D  135  GLY GLY ALA PRO ALA GLY GLY ASN ILE GLY GLY GLY GLN          
SEQRES  11 D  135  PRO GLN GLY GLY TRP                                          
FORMUL   5  HOH   *35(H2 O)                                                     
HELIX    1   1 GLY A   61  TYR A   70  1                                  10    
HELIX    2   2 GLY B   61  TYR B   70  1                                  10    
HELIX    3   3 GLY C   61  TYR C   70  1                                  10    
HELIX    4   4 GLY D   61  TYR D   70  1                                  10    
SHEET    1   A 6 THR A 108  MET A 111  0                                        
SHEET    2   A 6 GLN A  76  GLY A  81 -1  N  GLU A  80   O  THR A 108           
SHEET    3   A 6 VAL A   5  ASN A  13 -1  N  GLY A  12   O  VAL A  77           
SHEET    4   A 6 VAL B   5  ASN B  13 -1  N  VAL B  11   O  VAL A   5           
SHEET    5   A 6 GLN B  76  GLY B  81 -1  N  GLY B  81   O  VAL B   8           
SHEET    6   A 6 THR B 108  MET B 111 -1  N  GLN B 110   O  TYR B  78           
SHEET    1   B 4 ALA A  30  THR A  36  0                                        
SHEET    2   B 4 GLU A  53  LEU A  59 -1  N  LEU A  59   O  ALA A  30           
SHEET    3   B 4 TYR A  97  VAL A 103  1  N  VAL A 101   O  VAL A  58           
SHEET    4   B 4 GLN A  82  LYS A  87 -1  N  ARG A  86   O  THR A  98           
SHEET    1   C 4 ALA B  30  THR B  36  0                                        
SHEET    2   C 4 GLU B  53  LEU B  59 -1  N  LEU B  59   O  ALA B  30           
SHEET    3   C 4 TYR B  97  VAL B 103  1  N  VAL B 101   O  VAL B  58           
SHEET    4   C 4 GLN B  82  LYS B  87 -1  N  ARG B  86   O  THR B  98           
SHEET    1   D 6 THR C 108  MET C 111  0                                        
SHEET    2   D 6 GLN C  76  GLY C  81 -1  N  GLU C  80   O  THR C 108           
SHEET    3   D 6 VAL C   5  ASN C  13 -1  N  GLY C  12   O  VAL C  77           
SHEET    4   D 6 VAL D   5  ASN D  13 -1  N  VAL D  11   O  VAL C   5           
SHEET    5   D 6 GLN D  76  GLY D  81 -1  N  GLY D  81   O  VAL D   8           
SHEET    6   D 6 THR D 108  MET D 111 -1  N  GLN D 110   O  TYR D  78           
SHEET    1   E 4 ALA C  30  THR C  36  0                                        
SHEET    2   E 4 GLU C  53  LEU C  59 -1  N  LEU C  59   O  ALA C  30           
SHEET    3   E 4 TYR C  97  VAL C 103  1  N  VAL C 101   O  VAL C  58           
SHEET    4   E 4 GLN C  82  LYS C  87 -1  N  ARG C  86   O  THR C  98           
SHEET    1   F 4 ALA D  30  THR D  36  0                                        
SHEET    2   F 4 GLU D  53  LEU D  59 -1  N  LEU D  59   O  ALA D  30           
SHEET    3   F 4 TYR D  97  VAL D 103  1  N  VAL D 101   O  VAL D  58           
SHEET    4   F 4 GLN D  82  LYS D  87 -1  N  ARG D  86   O  THR D  98           
CRYST1   58.080  105.850   90.240  90.00  99.00  90.00 C 1 2 1      16          
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      0.017218  0.000000  0.002727        0.00000                         
SCALE2      0.000000  0.009447  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011220        0.00000                         
MTRIX1   1  0.030100 -0.036800 -0.998900       40.56470    1                    
MTRIX2   1 -0.029800 -0.998900  0.035900       79.58260    1                    
MTRIX3   1 -0.999100  0.028700 -0.031200       38.55650    1                    
MTRIX1   2  0.231800 -0.004400  0.972700      -13.00480    1                    
MTRIX2   2 -0.025700 -0.999700  0.001600      101.95840    1                    
MTRIX3   2  0.972400 -0.025300 -0.231900       18.32200    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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