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Database: PDB
Entry: 1BNC
LinkDB: 1BNC
Original site: 1BNC 
HEADER    FATTY ACID BIOSYNTHESIS                 06-JUL-94   1BNC              
TITLE     THREE-DIMENSIONAL STRUCTURE OF THE BIOTIN CARBOXYLASE SUBUNIT OF      
TITLE    2 ACETYL-COA CARBOXYLASE                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BIOTIN CARBOXYLASE;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 6.3.4.14                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562                                                  
KEYWDS    FATTY ACID BIOSYNTHESIS                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.WALDROP,I.RAYMENT,H.M.HOLDEN                                        
REVDAT   3   29-NOV-17 1BNC    1       HELIX                                    
REVDAT   2   24-FEB-09 1BNC    1       VERSN                                    
REVDAT   1   30-AUG-95 1BNC    0                                                
JRNL        AUTH   G.L.WALDROP,I.RAYMENT,H.M.HOLDEN                             
JRNL        TITL   THREE-DIMENSIONAL STRUCTURE OF THE BIOTIN CARBOXYLASE        
JRNL        TITL 2 SUBUNIT OF ACETYL-COA CARBOXYLASE.                           
JRNL        REF    BIOCHEMISTRY                  V.  33 10249 1994              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   7915138                                                      
JRNL        DOI    10.1021/BI00200A004                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT                                                  
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.                                      
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.183                           
REMARK   3   R VALUE            (WORKING SET) : NULL                            
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.                                    
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6617                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 116                                     
REMARK   3                                                                      
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT           
REMARK   3   BOND LENGTHS                 (A) : 0.013 ; NULL  ; NULL            
REMARK   3   BOND ANGLES            (DEGREES) : 2.300 ; NULL  ; NULL            
REMARK   3   TORSION ANGLES         (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TRIGONAL CARBON PLANES       (A) : NULL  ; NULL  ; NULL            
REMARK   3   GENERAL PLANES               (A) : 0.010 ; NULL  ; NULL            
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL            
REMARK   3   NON-BONDED CONTACTS          (A) : NULL  ; NULL  ; NULL            
REMARK   3                                                                      
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL                             
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  RESTRAINT LIBRARIES.                                                
REMARK   3   STEREOCHEMISTRY : NULL                                             
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL                         
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1BNC 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_1000171935.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
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: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.75                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       30.95000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       90.30000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       48.05000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       90.30000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.95000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       48.05000            
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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     ALA A   160                                                      
REMARK 465     SER A   161                                                      
REMARK 465     GLY A   162                                                      
REMARK 465     GLY A   163                                                      
REMARK 465     GLY A   164                                                      
REMARK 465     GLY A   165                                                      
REMARK 465     GLY A   166                                                      
REMARK 465     ALA A   191                                                      
REMARK 465     ALA A   192                                                      
REMARK 465     PHE A   193                                                      
REMARK 465     SER A   194                                                      
REMARK 465     ASN A   195                                                      
REMARK 465     ASP A   196                                                      
REMARK 465     GLN A   447                                                      
REMARK 465     GLU A   448                                                      
REMARK 465     LYS A   449                                                      
REMARK 465     PRO B   137                                                      
REMARK 465     LEU B   138                                                      
REMARK 465     GLY B   139                                                      
REMARK 465     ALA B   160                                                      
REMARK 465     SER B   161                                                      
REMARK 465     GLY B   162                                                      
REMARK 465     GLY B   163                                                      
REMARK 465     GLY B   164                                                      
REMARK 465     GLY B   165                                                      
REMARK 465     GLY B   166                                                      
REMARK 465     ARG B   167                                                      
REMARK 465     GLY B   168                                                      
REMARK 465     MET B   169                                                      
REMARK 465     GLU B   188                                                      
REMARK 465     ALA B   189                                                      
REMARK 465     LYS B   190                                                      
REMARK 465     ALA B   191                                                      
REMARK 465     ALA B   192                                                      
REMARK 465     PHE B   193                                                      
REMARK 465     SER B   194                                                      
REMARK 465     ASN B   195                                                      
REMARK 465     ASP B   196                                                      
REMARK 465     MET B   197                                                      
REMARK 465     VAL B   198                                                      
REMARK 465     LYS B   449                                                      
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     MET A 197    CG   SD   CE                                        
REMARK 470     ARG B 170    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 177    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 180    CG   CD   OE1  NE2                                  
REMARK 470     ILE B 182    CG1  CG2  CD1                                       
REMARK 470     SER B 183    OG                                                  
REMARK 470     MET B 184    CG   SD   CE                                        
REMARK 470     THR B 185    OG1  CG2                                            
REMARK 470     ARG B 186    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR B 199    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE2  GLU A   296     O3   PO4 A   953              1.92            
REMARK 500   OE1  GLU B   296     O3   PO4 B   954              2.09            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A  12   CD    GLU A  12   OE1     0.073                       
REMARK 500    GLU A  47   CD    GLU A  47   OE1     0.091                       
REMARK 500    GLU A  71   CD    GLU A  71   OE1     0.068                       
REMARK 500    GLU A 108   CD    GLU A 108   OE2     0.072                       
REMARK 500    GLU A 188   CD    GLU A 188   OE2     0.085                       
REMARK 500    GLU A 201   CD    GLU A 201   OE1     0.072                       
REMARK 500    GLU A 205   CD    GLU A 205   OE1     0.088                       
REMARK 500    GLU A 227   CD    GLU A 227   OE2    -0.073                       
REMARK 500    GLU A 241   CD    GLU A 241   OE1     0.074                       
REMARK 500    GLU A 242   CD    GLU A 242   OE1     0.069                       
REMARK 500    GLU A 258   CD    GLU A 258   OE1     0.069                       
REMARK 500    GLU A 280   CD    GLU A 280   OE2     0.078                       
REMARK 500    GLU A 283   CD    GLU A 283   OE2     0.069                       
REMARK 500    GLU A 288   CD    GLU A 288   OE2     0.074                       
REMARK 500    GLU A 296   CD    GLU A 296   OE2    -0.096                       
REMARK 500    GLU A 301   CD    GLU A 301   OE1     0.070                       
REMARK 500    GLU A 311   CD    GLU A 311   OE1     0.084                       
REMARK 500    GLU A 428   CD    GLU A 428   OE1     0.072                       
REMARK 500    GLU A 441   CD    GLU A 441   OE1     0.070                       
REMARK 500    GLU B  71   CD    GLU B  71   OE2     0.067                       
REMARK 500    GLU B  87   CD    GLU B  87   OE1     0.074                       
REMARK 500    GLU B  93   CD    GLU B  93   OE1     0.070                       
REMARK 500    GLU B 108   CD    GLU B 108   OE1     0.072                       
REMARK 500    GLU B 205   CD    GLU B 205   OE1     0.074                       
REMARK 500    GLU B 283   CD    GLU B 283   OE2     0.069                       
REMARK 500    GLU B 296   CD    GLU B 296   OE2     0.078                       
REMARK 500    GLU B 326   CD    GLU B 326   OE2     0.075                       
REMARK 500    GLU B 327   CD    GLU B 327   OE1     0.070                       
REMARK 500    GLU B 368   CD    GLU B 368   OE1     0.069                       
REMARK 500    GLU B 448   CD    GLU B 448   OE1     0.076                       
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    ASP A   3   CB  -  CG  -  OD1 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    ASP A  36   CB  -  CG  -  OD1 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ASP A  38   CB  -  CG  -  OD1 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ASP A  38   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG A 111   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ASP A 135   CB  -  CG  -  OD1 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ASP A 135   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A 140   CB  -  CG  -  OD1 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500    ASP A 175   CB  -  CG  -  OD1 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    ASP A 175   CB  -  CG  -  OD2 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ARG A 228   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG A 259   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG A 366   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ASN A 417   N   -  CA  -  CB  ANGL. DEV. = -16.8 DEGREES          
REMARK 500    ASP A 419   CB  -  CG  -  OD1 ANGL. DEV. =  -7.0 DEGREES          
REMARK 500    ARG A 423   N   -  CA  -  CB  ANGL. DEV. = -12.2 DEGREES          
REMARK 500    ASP B   3   CB  -  CG  -  OD1 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ASP B  36   CB  -  CG  -  OD1 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ASP B  38   CB  -  CG  -  OD1 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ASP B  46   CB  -  CG  -  OD1 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    ASP B 115   CB  -  CG  -  OD1 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    MET B 123   CA  -  CB  -  CG  ANGL. DEV. = -10.3 DEGREES          
REMARK 500    MET B 123   CG  -  SD  -  CE  ANGL. DEV. =  10.4 DEGREES          
REMARK 500    ASP B 143   CB  -  CG  -  OD1 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    ASP B 175   CB  -  CG  -  OD1 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ARG B 208   N   -  CA  -  CB  ANGL. DEV. =  12.0 DEGREES          
REMARK 500    ARG B 228   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    ARG B 253   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ASP B 266   CB  -  CG  -  OD1 ANGL. DEV. =  -6.7 DEGREES          
REMARK 500    ASP B 266   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ARG B 270   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ILE B 287   CB  -  CA  -  C   ANGL. DEV. = -12.8 DEGREES          
REMARK 500    PRO B 320   C   -  N   -  CD  ANGL. DEV. = -17.4 DEGREES          
REMARK 500    ASP B 382   CB  -  CG  -  OD1 ANGL. DEV. =  -7.0 DEGREES          
REMARK 500    ASN B 394   CB  -  CA  -  C   ANGL. DEV. = -14.1 DEGREES          
REMARK 500    ASN B 417   CB  -  CA  -  C   ANGL. DEV. = -12.3 DEGREES          
REMARK 500    ASN B 417   N   -  CA  -  CB  ANGL. DEV. = -13.5 DEGREES          
REMARK 500    ASP B 419   CB  -  CG  -  OD1 ANGL. DEV. =  -6.7 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    SER A  59      -86.54   -124.61                                   
REMARK 500    PHE A  84      -83.90   -122.48                                   
REMARK 500    ALA A 226     -157.78     52.38                                   
REMARK 500    MET A 232       91.54    -68.22                                   
REMARK 500    ARG A 235       47.84     74.87                                   
REMARK 500    THR A 291       57.29    -93.63                                   
REMARK 500    TYR A 381     -153.18   -115.61                                   
REMARK 500    ASN B   9     -161.73   -169.40                                   
REMARK 500    SER B  59      -79.27   -112.26                                   
REMARK 500    PHE B  84      -96.42   -132.30                                   
REMARK 500    ASN B 145      -30.36    -39.09                                   
REMARK 500    ALA B 176      -71.58    -46.26                                   
REMARK 500    GLU B 177        2.72    -62.06                                   
REMARK 500    LEU B 225       54.74   -111.45                                   
REMARK 500    ALA B 226     -163.09     63.47                                   
REMARK 500    PRO B 244     -166.09    -76.57                                   
REMARK 500    GLU B 296        0.12    -61.79                                   
REMARK 500    PRO B 349      152.75    -46.30                                   
REMARK 500    SER B 369      148.25   -171.02                                   
REMARK 500    ILE B 437       -7.66    -58.40                                   
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 PO4 A 953                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 954                 
DBREF  1BNC A    1   449  UNP    P24182   ACCC_ECOLI       1    449             
DBREF  1BNC B    1   449  UNP    P24182   ACCC_ECOLI       1    449             
SEQRES   1 A  449  MET LEU ASP LYS ILE VAL ILE ALA ASN ARG GLY GLU ILE          
SEQRES   2 A  449  ALA LEU ARG ILE LEU ARG ALA CYS LYS GLU LEU GLY ILE          
SEQRES   3 A  449  LYS THR VAL ALA VAL HIS SER SER ALA ASP ARG ASP LEU          
SEQRES   4 A  449  LYS HIS VAL LEU LEU ALA ASP GLU THR VAL CYS ILE GLY          
SEQRES   5 A  449  PRO ALA PRO SER VAL LYS SER TYR LEU ASN ILE PRO ALA          
SEQRES   6 A  449  ILE ILE SER ALA ALA GLU ILE THR GLY ALA VAL ALA ILE          
SEQRES   7 A  449  HIS PRO GLY TYR GLY PHE LEU SER GLU ASN ALA ASN PHE          
SEQRES   8 A  449  ALA GLU GLN VAL GLU ARG SER GLY PHE ILE PHE ILE GLY          
SEQRES   9 A  449  PRO LYS ALA GLU THR ILE ARG LEU MET GLY ASP LYS VAL          
SEQRES  10 A  449  SER ALA ILE ALA ALA MET LYS LYS ALA GLY VAL PRO CYS          
SEQRES  11 A  449  VAL PRO GLY SER ASP GLY PRO LEU GLY ASP ASP MET ASP          
SEQRES  12 A  449  LYS ASN ARG ALA ILE ALA LYS ARG ILE GLY TYR PRO VAL          
SEQRES  13 A  449  ILE ILE LYS ALA SER GLY GLY GLY GLY GLY ARG GLY MET          
SEQRES  14 A  449  ARG VAL VAL ARG GLY ASP ALA GLU LEU ALA GLN SER ILE          
SEQRES  15 A  449  SER MET THR ARG ALA GLU ALA LYS ALA ALA PHE SER ASN          
SEQRES  16 A  449  ASP MET VAL TYR MET GLU LYS TYR LEU GLU ASN PRO ARG          
SEQRES  17 A  449  HIS VAL GLU ILE GLN VAL LEU ALA ASP GLY GLN GLY ASN          
SEQRES  18 A  449  ALA ILE TYR LEU ALA GLU ARG ASP CYS SER MET GLN ARG          
SEQRES  19 A  449  ARG HIS GLN LYS VAL VAL GLU GLU ALA PRO ALA PRO GLY          
SEQRES  20 A  449  ILE THR PRO GLU LEU ARG ARG TYR ILE GLY GLU ARG CYS          
SEQRES  21 A  449  ALA LYS ALA CYS VAL ASP ILE GLY TYR ARG GLY ALA GLY          
SEQRES  22 A  449  THR PHE GLU PHE LEU PHE GLU ASN GLY GLU PHE TYR PHE          
SEQRES  23 A  449  ILE GLU MET ASN THR ARG ILE GLN VAL GLU HIS PRO VAL          
SEQRES  24 A  449  THR GLU MET ILE THR GLY VAL ASP LEU ILE LYS GLU GLN          
SEQRES  25 A  449  LEU ARG ILE ALA ALA GLY GLN PRO LEU SER ILE LYS GLN          
SEQRES  26 A  449  GLU GLU VAL HIS VAL ARG GLY HIS ALA VAL GLU CYS ARG          
SEQRES  27 A  449  ILE ASN ALA GLU ASP PRO ASN THR PHE LEU PRO SER PRO          
SEQRES  28 A  449  GLY LYS ILE THR ARG PHE HIS ALA PRO GLY GLY PHE GLY          
SEQRES  29 A  449  VAL ARG TRP GLU SER HIS ILE TYR ALA GLY TYR THR VAL          
SEQRES  30 A  449  PRO PRO TYR TYR ASP SER MET ILE GLY LYS LEU ILE CYS          
SEQRES  31 A  449  TYR GLY GLU ASN ARG ASP VAL ALA ILE ALA ARG MET LYS          
SEQRES  32 A  449  ASN ALA LEU GLN GLU LEU ILE ILE ASP GLY ILE LYS THR          
SEQRES  33 A  449  ASN VAL ASP LEU GLN ILE ARG ILE MET ASN ASP GLU ASN          
SEQRES  34 A  449  PHE GLN HIS GLY GLY THR ASN ILE HIS TYR LEU GLU LYS          
SEQRES  35 A  449  LYS LEU GLY LEU GLN GLU LYS                                  
SEQRES   1 B  449  MET LEU ASP LYS ILE VAL ILE ALA ASN ARG GLY GLU ILE          
SEQRES   2 B  449  ALA LEU ARG ILE LEU ARG ALA CYS LYS GLU LEU GLY ILE          
SEQRES   3 B  449  LYS THR VAL ALA VAL HIS SER SER ALA ASP ARG ASP LEU          
SEQRES   4 B  449  LYS HIS VAL LEU LEU ALA ASP GLU THR VAL CYS ILE GLY          
SEQRES   5 B  449  PRO ALA PRO SER VAL LYS SER TYR LEU ASN ILE PRO ALA          
SEQRES   6 B  449  ILE ILE SER ALA ALA GLU ILE THR GLY ALA VAL ALA ILE          
SEQRES   7 B  449  HIS PRO GLY TYR GLY PHE LEU SER GLU ASN ALA ASN PHE          
SEQRES   8 B  449  ALA GLU GLN VAL GLU ARG SER GLY PHE ILE PHE ILE GLY          
SEQRES   9 B  449  PRO LYS ALA GLU THR ILE ARG LEU MET GLY ASP LYS VAL          
SEQRES  10 B  449  SER ALA ILE ALA ALA MET LYS LYS ALA GLY VAL PRO CYS          
SEQRES  11 B  449  VAL PRO GLY SER ASP GLY PRO LEU GLY ASP ASP MET ASP          
SEQRES  12 B  449  LYS ASN ARG ALA ILE ALA LYS ARG ILE GLY TYR PRO VAL          
SEQRES  13 B  449  ILE ILE LYS ALA SER GLY GLY GLY GLY GLY ARG GLY MET          
SEQRES  14 B  449  ARG VAL VAL ARG GLY ASP ALA GLU LEU ALA GLN SER ILE          
SEQRES  15 B  449  SER MET THR ARG ALA GLU ALA LYS ALA ALA PHE SER ASN          
SEQRES  16 B  449  ASP MET VAL TYR MET GLU LYS TYR LEU GLU ASN PRO ARG          
SEQRES  17 B  449  HIS VAL GLU ILE GLN VAL LEU ALA ASP GLY GLN GLY ASN          
SEQRES  18 B  449  ALA ILE TYR LEU ALA GLU ARG ASP CYS SER MET GLN ARG          
SEQRES  19 B  449  ARG HIS GLN LYS VAL VAL GLU GLU ALA PRO ALA PRO GLY          
SEQRES  20 B  449  ILE THR PRO GLU LEU ARG ARG TYR ILE GLY GLU ARG CYS          
SEQRES  21 B  449  ALA LYS ALA CYS VAL ASP ILE GLY TYR ARG GLY ALA GLY          
SEQRES  22 B  449  THR PHE GLU PHE LEU PHE GLU ASN GLY GLU PHE TYR PHE          
SEQRES  23 B  449  ILE GLU MET ASN THR ARG ILE GLN VAL GLU HIS PRO VAL          
SEQRES  24 B  449  THR GLU MET ILE THR GLY VAL ASP LEU ILE LYS GLU GLN          
SEQRES  25 B  449  LEU ARG ILE ALA ALA GLY GLN PRO LEU SER ILE LYS GLN          
SEQRES  26 B  449  GLU GLU VAL HIS VAL ARG GLY HIS ALA VAL GLU CYS ARG          
SEQRES  27 B  449  ILE ASN ALA GLU ASP PRO ASN THR PHE LEU PRO SER PRO          
SEQRES  28 B  449  GLY LYS ILE THR ARG PHE HIS ALA PRO GLY GLY PHE GLY          
SEQRES  29 B  449  VAL ARG TRP GLU SER HIS ILE TYR ALA GLY TYR THR VAL          
SEQRES  30 B  449  PRO PRO TYR TYR ASP SER MET ILE GLY LYS LEU ILE CYS          
SEQRES  31 B  449  TYR GLY GLU ASN ARG ASP VAL ALA ILE ALA ARG MET LYS          
SEQRES  32 B  449  ASN ALA LEU GLN GLU LEU ILE ILE ASP GLY ILE LYS THR          
SEQRES  33 B  449  ASN VAL ASP LEU GLN ILE ARG ILE MET ASN ASP GLU ASN          
SEQRES  34 B  449  PHE GLN HIS GLY GLY THR ASN ILE HIS TYR LEU GLU LYS          
SEQRES  35 B  449  LYS LEU GLY LEU GLN GLU LYS                                  
HET    PO4  A 953       5                                                       
HET    PO4  B 954       5                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   3  PO4    2(O4 P 3-)                                                   
FORMUL   5  HOH   *116(H2 O)                                                    
HELIX    1  H1 GLU A   12  CYS A   21  1                                  10    
HELIX    2  H2 LYS A   40  LEU A   44  1                                   5    
HELIX    3  H3 ILE A   63  ALA A   70  1                                   8    
HELIX    4  H4 ALA A   89  SER A   98  1                                  10    
HELIX    5  H5 ALA A  107  ALA A  126  1                                  20    
HELIX    6  H6 MET A  142  ILE A  152  1                                  11    
HELIX    7  H7 ASP A  175  ALA A  187  1                                  13    
HELIX    8  H8 PRO A  250  ASP A  266  1                                  17    
HELIX    9  H9 PRO A  298  THR A  304  1                                   7    
HELIX   10 H10 LEU A  308  ARG A  314  1                                   7    
HELIX   11 H11 ARG A  395  GLU A  408  1                                  14    
HELIX   12 H12 VAL A  418  ASN A  426  1                                   9    
HELIX   13 H13 GLU A  428  HIS A  432  1                                   5    
HELIX   14 H14 TYR A  439  LEU A  446  1                                   8    
HELIX   15 H15 GLU B   12  CYS B   21  1                                  10    
HELIX   16 H16 LYS B   40  LEU B   44  1                                   5    
HELIX   17 H17 ILE B   63  ALA B   70  1                                   8    
HELIX   18 H18 ALA B   89  SER B   98  1                                  10    
HELIX   19 H19 ALA B  107  ALA B  126  1                                  20    
HELIX   20 H20 MET B  142  ILE B  152  1                                  11    
HELIX   21 H21 ASP B  175  ALA B  187  1                                  13    
HELIX   22 H22 PRO B  250  ASP B  266  1                                  17    
HELIX   23 H23 PRO B  298  THR B  304  1                                   7    
HELIX   24 H24 LEU B  308  ARG B  314  1                                   7    
HELIX   25 H25 ARG B  395  GLU B  408  1                                  14    
HELIX   26 H26 VAL B  418  ASN B  426  1                                   9    
HELIX   27 H27 GLU B  428  HIS B  432  1                                   5    
HELIX   28 H28 TYR B  439  LEU B  446  1                                   8    
SHEET    1 S1A 5 PHE A 100  ILE A 103  0                                        
SHEET    2 S1A 5 ALA A  77  HIS A  79  1                                        
SHEET    3 S1A 5 LYS A   4  ILE A   7  1                                        
SHEET    4 S1A 5 ILE A  26  HIS A  32  1                                        
SHEET    5 S1A 5 GLU A  47  GLY A  52  1                                        
SHEET    1 S2A 3 GLY A 168  VAL A 172  0                                        
SHEET    2 S2A 3 TYR A 154  LYS A 159 -1                                        
SHEET    3 S2A 3 MET A 197  LEU A 204 -1                                        
SHEET    1 S3A 8 PHE A 284  ILE A 293  0                                        
SHEET    2 S3A 8 TYR A 269  PHE A 279 -1                                        
SHEET    3 S3A 8 ASN A 206  ALA A 216 -1                                        
SHEET    4 S3A 8 ASN A 221  ASP A 229 -1                                        
SHEET    5 S3A 8 VAL A 240  PRO A 244 -1                                        
SHEET    6 S3A 8 HIS A 333  ALA A 341 -1                                        
SHEET    7 S3A 8 MET A 384  GLY A 392 -1                                        
SHEET    8 S3A 8 VAL A 365  SER A 369 -1                                        
SHEET    1 S4A 3 THR A 376  PRO A 378  0                                        
SHEET    2 S4A 3 LYS A 353  GLY A 361 -1                                        
SHEET    3 S4A 3 LEU A 409  THR A 416 -1                                        
SHEET    1 S1B 5 PHE B 100  ILE B 103  0                                        
SHEET    2 S1B 5 ALA B  77  HIS B  79  1                                        
SHEET    3 S1B 5 LYS B   4  ILE B   7  1                                        
SHEET    4 S1B 5 ILE B  26  HIS B  32  1                                        
SHEET    5 S1B 5 GLU B  47  GLY B  52  1                                        
SHEET    1 S2B 3 ARG B 170  VAL B 172  0                                        
SHEET    2 S2B 3 TYR B 154  LYS B 159 -1                                        
SHEET    3 S2B 3 TYR B 199  LEU B 204 -1                                        
SHEET    1 S3B 8 PHE B 284  ILE B 293  0                                        
SHEET    2 S3B 8 TYR B 269  PHE B 279 -1                                        
SHEET    3 S3B 8 ASN B 206  ALA B 216 -1                                        
SHEET    4 S3B 8 ASN B 221  ASP B 229 -1                                        
SHEET    5 S3B 8 VAL B 240  PRO B 244 -1                                        
SHEET    6 S3B 8 HIS B 333  ALA B 341 -1                                        
SHEET    7 S3B 8 MET B 384  GLY B 392 -1                                        
SHEET    8 S3B 8 VAL B 365  SER B 369 -1                                        
SHEET    1 S4B 3 THR B 376  PRO B 378  0                                        
SHEET    2 S4B 3 LYS B 353  GLY B 361 -1                                        
SHEET    3 S4B 3 LEU B 409  THR B 416 -1                                        
CISPEP   1 TYR A  154    PRO A  155          0         1.48                     
CISPEP   2 ALA A  243    PRO A  244          0        -2.59                     
CISPEP   3 TYR B  154    PRO B  155          0         0.68                     
CISPEP   4 ALA B  243    PRO B  244          0        -0.14                     
SITE     1 AC1  7 LYS A 238  ARG A 292  GLN A 294  VAL A 295                    
SITE     2 AC1  7 GLU A 296  ARG A 338  HOH A 972                               
SITE     1 AC2  6 LYS B 238  ARG B 292  GLN B 294  VAL B 295                    
SITE     2 AC2  6 GLU B 296  ARG B 338                                          
CRYST1   61.900   96.100  180.600  90.00  90.00  90.00 P 21 21 21    8          
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      0.016155  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010406  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005537        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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