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Database: PDB
Entry: 1PFK
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HEADER    TRANSFERASE(PHOSPHOTRANSFERASE)         25-JAN-88   1PFK              
TITLE     CRYSTAL STRUCTURE OF THE COMPLEX OF PHOSPHOFRUCTOKINASE FROM          
TITLE    2 ESCHERICHIA COLI WITH ITS REACTION PRODUCTS                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHOFRUCTOKINASE;                                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 2.7.1.11;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 CELL_LINE: 293;                                                      
SOURCE   5 EXPRESSION_SYSTEM_STRAIN: 293                                        
KEYWDS    TRANSFERASE(PHOSPHOTRANSFERASE)                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.SHIRAKIHARA,P.R.EVANS                                               
REVDAT   6   13-JUL-11 1PFK    1       VERSN                                    
REVDAT   5   24-FEB-09 1PFK    1       VERSN                                    
REVDAT   4   15-OCT-92 1PFK    1       SEQRES                                   
REVDAT   3   15-JUL-90 1PFK    1       REMARK                                   
REVDAT   2   19-APR-89 1PFK    1       JRNL                                     
REVDAT   1   09-JAN-89 1PFK    0                                                
JRNL        AUTH   Y.SHIRAKIHARA,P.R.EVANS                                      
JRNL        TITL   CRYSTAL STRUCTURE OF THE COMPLEX OF PHOSPHOFRUCTOKINASE FROM 
JRNL        TITL 2 ESCHERICHIA COLI WITH ITS REACTION PRODUCTS.                 
JRNL        REF    J.MOL.BIOL.                   V. 204   973 1988              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   2975709                                                      
JRNL        DOI    10.1016/0022-2836(88)90056-3                                 
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   W.R.RYPNIEWSKI,P.R.EVANS                                     
REMARK   1  TITL   CRYSTAL STRUCTURE OF UNLIGANDED PHOSPHOFRUCTOKINASE FROM     
REMARK   1  TITL 2 ESCHERICHIA COLI                                             
REMARK   1  REF    J.MOL.BIOL.                   V. 207   805 1989              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   P.R.EVANS,G.W.FARRANTS,M.C.LAWRENCE                          
REMARK   1  TITL   CRYSTALLOGRAPHIC STRUCTURE OF ALLOSTERICALLY INHIBITED       
REMARK   1  TITL 2 PHOSPHOFRUCTOKINASE AT 7 ANGSTROMS RESOLUTION                
REMARK   1  REF    J.MOL.BIOL.                   V. 191   713 1986              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   H.W.HELLINGA,P.R.EVANS                                       
REMARK   1  TITL   NUCLEOTIDE SEQUENCE AND HIGH-LEVEL EXPRESSION OF THE MAJOR   
REMARK   1  TITL 2 ESCHERICHIA COLI PHOSPHOFRUCTOKINASE                         
REMARK   1  REF    EUR.J.BIOCHEM.                V. 149   363 1985              
REMARK   1  REFN                   ISSN 0014-2956                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   P.R.EVANS,G.W.FARRANTS,P.J.HUDSON                            
REMARK   1  TITL   PHOSPHOFRUCTOKINASE. STRUCTURE AND CONTROL                   
REMARK   1  REF    PHILOS.TRANS.R.SOC.LONDON,    V. 293    53 1981              
REMARK   1  REF  2 SER.B                                                        
REMARK   1  REFN                   ISSN 0080-4622                               
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   P.R.EVANS,P.J.HUDSON                                         
REMARK   1  TITL   STRUCTURE AND CONTROL OF PHOSPHOFRUCTOKINASE FROM BACILLUS   
REMARK   1  TITL 2 STEAROTHERMOPHILUS                                           
REMARK   1  REF    NATURE                        V. 279   500 1979              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1 REFERENCE 6                                                          
REMARK   1  AUTH   P.R.EVANS,P.J.HUDSON                                         
REMARK   1  TITL   THE THREE-DIMENSIONAL STRUCTURE OF PHOSPHOFRUCTOKINASE FROM  
REMARK   1  TITL 2 BACILLUS STEAROTHERMOPHILUS                                  
REMARK   1  REF    PROC.FEBS MEET.               V.  52   349 1978              
REMARK   1  REFN                   ISSN 0071-4402                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROLSQ                                               
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 100.00                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
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 + TEST SET) : 0.165                           
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  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
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            : 4866                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 152                                     
REMARK   3   SOLVENT ATOMS            : 277                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 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  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.008 ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : 0.030 ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1PFK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
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   (%): 53.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
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       56.15000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.70000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       56.15000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.70000            
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 300 REMARK: THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT CONTAINS TWO SUBUNITS   
REMARK 300 OF THE TETRAMER.  THESE SUBUNITS HAVE BEEN ASSIGNED CHAIN            
REMARK 300 IDENTIFIERS *A* AND *B* AND HAVE DIFFERENT CONFORMATIONS.            
REMARK 300 CHAIN A IS A *CLOSED* SUBUNIT WITH THE MG++ ION BRIDGING             
REMARK 300 THE TWO PRODUCTS.  CHAIN B IS AN *OPEN* SUBUNIT WITH THE             
REMARK 300 MG++ BOUND TO ADP ONLY.  THERE ARE TWO WATER CHAINS, ONE             
REMARK 300 CORRESPONDING TO EACH SUBUNIT, AND EQUIVALENT WATER                  
REMARK 300 MOLECULES IN EACH CHAIN HAVE BEEN ASSIGNED THE SAME RESIDUE          
REMARK 300 NUMBER.  THE TETRAMER CAN BE COMPLETED FROM THE DIMER IN             
REMARK 300 THIS ENTRY BY ROTATING 180 DEGREES ABOUT Z                           
REMARK 300 (I.E. -X, -Y, Z).  THE STORED ORTHOGONAL CRYSTALLOGRAPHIC            
REMARK 300 COORDINATES IN THIS ENTRY MAY BE CONVERTED TO THE MOLECULAR          
REMARK 300 PQR FRAME (WITH THE MOLECULAR DIADS ALONG P,Q,R) BY THE              
REMARK 300 TRANSFORMATION                                                       
REMARK 300       0.87831   0.47808   0.00000               0.00000              
REMARK 300       0.00000   0.00000  -1.00000              -2.71300              
REMARK 300      -0.47808   0.87831   0.00000               0.00000              
REMARK 300                                                                      
REMARK 300 THE TRANSFORMATION SPECIFIED ON THE *MTRIX* RECORDS BELOW            
REMARK 300 WILL YIELD APPROXIMATE COORDINATES FOR THE B CHAIN WHEN              
REMARK 300 APPLIED TO THE A CHAIN.  IT WILL ALSO YIELD APPROXIMATE              
REMARK 300 COORDINATES FOR THE A CHAIN WHEN APPLIED TO THE B CHAIN.             
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 23490 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 41100 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -194.0 KCAL/MOL                       
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 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
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     LYS A 214    CD   CE   NZ                                        
REMARK 470     LYS A 236    CG   CD   CE   NZ                                   
REMARK 470     LYS B 236    CD   CE   NZ                                        
REMARK 470     LYS B 304    CG   CD   CE   NZ                                   
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   NZ   LYS A   316     O    HOH A   427              2.12            
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    ARG A  48   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ASP A  59   CB  -  CG  -  OD1 ANGL. DEV. =  10.5 DEGREES          
REMARK 500    ASP A  59   CB  -  CG  -  OD2 ANGL. DEV. =  -7.2 DEGREES          
REMARK 500    ARG A  63   CD  -  NE  -  CZ  ANGL. DEV. =  12.3 DEGREES          
REMARK 500    ARG A  63   NE  -  CZ  -  NH1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ARG A  63   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG A  72   CD  -  NE  -  CZ  ANGL. DEV. =  12.1 DEGREES          
REMARK 500    ARG A  72   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A  77   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    ARG A  77   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ASP A  78   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG A  82   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG A  82   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ARG A  92   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ASP A 127   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG A 152   NE  -  CZ  -  NH1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG A 154   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG A 198   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    ARG A 198   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    GLU A 241   CA  -  CB  -  CG  ANGL. DEV. =  13.4 DEGREES          
REMARK 500    ARG A 243   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG A 243   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG A 252   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A 261   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A 282   NE  -  CZ  -  NH1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP B  12   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP B  53   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG B  54   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ARG B  54   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    ARG B  63   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ARG B  72   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG B  77   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG B 162   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG B 162   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG B 171   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG B 243   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ASP B 260   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    TRP B 311   CA  -  CB  -  CG  ANGL. DEV. =  12.1 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    ILE A   1       98.33     74.16                                   
REMARK 500    THR A 125      140.42   -170.08                                   
REMARK 500    ARG A 171      -95.60     75.73                                   
REMARK 500    CYS A 225     -172.30   -176.98                                   
REMARK 500    LYS A 308       47.61    -92.64                                   
REMARK 500    ILE B   1      108.89     77.75                                   
REMARK 500    PHE B  76      -19.96    -46.97                                   
REMARK 500    THR B 125      138.20    175.14                                   
REMARK 500    ARG B 171      -92.84     59.72                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 407        DISTANCE =  5.24 ANGSTROMS                       
REMARK 525    HOH B 414        DISTANCE =  5.17 ANGSTROMS                       
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 ADP A 324 AND ADP B 324 ARE THE PRODUCTS OF THE CATALYTIC            
REMARK 600 REACTION ATP + F6P --> ADP + F-1,6-DP.  ADP A 326 AND                
REMARK 600 ADP B 326 ARE THE ALLOSTERIC ACTIVATORS.                             
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 325  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 FBP A 323   O2P                                                    
REMARK 620 2 HOH A 417   O    72.3                                              
REMARK 620 3 ASP A 103   OD2 146.2 102.4                                        
REMARK 620 4 ADP A 324   O2B  91.3 159.9  84.8                                  
REMARK 620 5 HOH A 386   O   111.0  95.3 102.6 101.5                            
REMARK 620 6 HOH A 402   O    73.5  78.9  72.8  85.4 171.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 327  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A 185   O                                                      
REMARK 620 2 ADP A 326   O2B  90.6                                              
REMARK 620 3 ADP A 326   O1A 173.5  86.5                                        
REMARK 620 4 HOH A 368   O    86.9  81.7  98.4                                  
REMARK 620 5 GLU A 187   OE1 103.4 159.7  81.0  84.4                            
REMARK 620 6 HOH A 369   O    80.7  97.0  94.0 167.5  99.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 325  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP B 324   O2B                                                    
REMARK 620 2 HOH B 419   O   106.9                                              
REMARK 620 3 ADP B 324   O1A  81.4  91.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 327  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 187   OE1                                                    
REMARK 620 2 GLU B 187   OE2  44.6                                              
REMARK 620 3 ADP B 326   O2B 177.4 132.9                                        
REMARK 620 4 ADP B 326   O1A  88.6 102.5  92.1                                  
REMARK 620 5 HOH B 369   O    99.8  55.7  77.7 101.2                            
REMARK 620 6 HOH B 370   O    80.0 121.0 102.4  92.8 166.0                      
REMARK 620 7 GLY B 185   O    88.9  82.6  90.8 169.8  88.9  77.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FBP A 323                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FBP B 323                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 325                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 327                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 325                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 327                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 324                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 326                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 324                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 326                 
DBREF  1PFK A    0   319  UNP    P0A796   K6PF1_ECOLI      1    320             
DBREF  1PFK B    0   319  UNP    P0A796   K6PF1_ECOLI      1    320             
SEQRES   1 A  320  MET ILE LYS LYS ILE GLY VAL LEU THR SER GLY GLY ASP          
SEQRES   2 A  320  ALA PRO GLY MET ASN ALA ALA ILE ARG GLY VAL VAL ARG          
SEQRES   3 A  320  SER ALA LEU THR GLU GLY LEU GLU VAL MET GLY ILE TYR          
SEQRES   4 A  320  ASP GLY TYR LEU GLY LEU TYR GLU ASP ARG MET VAL GLN          
SEQRES   5 A  320  LEU ASP ARG TYR SER VAL SER ASP MET ILE ASN ARG GLY          
SEQRES   6 A  320  GLY THR PHE LEU GLY SER ALA ARG PHE PRO GLU PHE ARG          
SEQRES   7 A  320  ASP GLU ASN ILE ARG ALA VAL ALA ILE GLU ASN LEU LYS          
SEQRES   8 A  320  LYS ARG GLY ILE ASP ALA LEU VAL VAL ILE GLY GLY ASP          
SEQRES   9 A  320  GLY SER TYR MET GLY ALA MET ARG LEU THR GLU MET GLY          
SEQRES  10 A  320  PHE PRO CYS ILE GLY LEU PRO GLY THR ILE ASP ASN ASP          
SEQRES  11 A  320  ILE LYS GLY THR ASP TYR THR ILE GLY PHE PHE THR ALA          
SEQRES  12 A  320  LEU SER THR VAL VAL GLU ALA ILE ASP ARG LEU ARG ASP          
SEQRES  13 A  320  THR SER SER SER HIS GLN ARG ILE SER VAL VAL GLU VAL          
SEQRES  14 A  320  MET GLY ARG TYR CYS GLY ASP LEU THR LEU ALA ALA ALA          
SEQRES  15 A  320  ILE ALA GLY GLY CYS GLU PHE VAL VAL VAL PRO GLU VAL          
SEQRES  16 A  320  GLU PHE SER ARG GLU ASP LEU VAL ASN GLU ILE LYS ALA          
SEQRES  17 A  320  GLY ILE ALA LYS GLY LYS LYS HIS ALA ILE VAL ALA ILE          
SEQRES  18 A  320  THR GLU HIS MET CYS ASP VAL ASP GLU LEU ALA HIS PHE          
SEQRES  19 A  320  ILE GLU LYS GLU THR GLY ARG GLU THR ARG ALA THR VAL          
SEQRES  20 A  320  LEU GLY HIS ILE GLN ARG GLY GLY SER PRO VAL PRO TYR          
SEQRES  21 A  320  ASP ARG ILE LEU ALA SER ARG MET GLY ALA TYR ALA ILE          
SEQRES  22 A  320  ASP LEU LEU LEU ALA GLY TYR GLY GLY ARG CYS VAL GLY          
SEQRES  23 A  320  ILE GLN ASN GLU GLN LEU VAL HIS HIS ASP ILE ILE ASP          
SEQRES  24 A  320  ALA ILE GLU ASN MET LYS ARG PRO PHE LYS GLY ASP TRP          
SEQRES  25 A  320  LEU ASP CYS ALA LYS LYS LEU TYR                              
SEQRES   1 B  320  MET ILE LYS LYS ILE GLY VAL LEU THR SER GLY GLY ASP          
SEQRES   2 B  320  ALA PRO GLY MET ASN ALA ALA ILE ARG GLY VAL VAL ARG          
SEQRES   3 B  320  SER ALA LEU THR GLU GLY LEU GLU VAL MET GLY ILE TYR          
SEQRES   4 B  320  ASP GLY TYR LEU GLY LEU TYR GLU ASP ARG MET VAL GLN          
SEQRES   5 B  320  LEU ASP ARG TYR SER VAL SER ASP MET ILE ASN ARG GLY          
SEQRES   6 B  320  GLY THR PHE LEU GLY SER ALA ARG PHE PRO GLU PHE ARG          
SEQRES   7 B  320  ASP GLU ASN ILE ARG ALA VAL ALA ILE GLU ASN LEU LYS          
SEQRES   8 B  320  LYS ARG GLY ILE ASP ALA LEU VAL VAL ILE GLY GLY ASP          
SEQRES   9 B  320  GLY SER TYR MET GLY ALA MET ARG LEU THR GLU MET GLY          
SEQRES  10 B  320  PHE PRO CYS ILE GLY LEU PRO GLY THR ILE ASP ASN ASP          
SEQRES  11 B  320  ILE LYS GLY THR ASP TYR THR ILE GLY PHE PHE THR ALA          
SEQRES  12 B  320  LEU SER THR VAL VAL GLU ALA ILE ASP ARG LEU ARG ASP          
SEQRES  13 B  320  THR SER SER SER HIS GLN ARG ILE SER VAL VAL GLU VAL          
SEQRES  14 B  320  MET GLY ARG TYR CYS GLY ASP LEU THR LEU ALA ALA ALA          
SEQRES  15 B  320  ILE ALA GLY GLY CYS GLU PHE VAL VAL VAL PRO GLU VAL          
SEQRES  16 B  320  GLU PHE SER ARG GLU ASP LEU VAL ASN GLU ILE LYS ALA          
SEQRES  17 B  320  GLY ILE ALA LYS GLY LYS LYS HIS ALA ILE VAL ALA ILE          
SEQRES  18 B  320  THR GLU HIS MET CYS ASP VAL ASP GLU LEU ALA HIS PHE          
SEQRES  19 B  320  ILE GLU LYS GLU THR GLY ARG GLU THR ARG ALA THR VAL          
SEQRES  20 B  320  LEU GLY HIS ILE GLN ARG GLY GLY SER PRO VAL PRO TYR          
SEQRES  21 B  320  ASP ARG ILE LEU ALA SER ARG MET GLY ALA TYR ALA ILE          
SEQRES  22 B  320  ASP LEU LEU LEU ALA GLY TYR GLY GLY ARG CYS VAL GLY          
SEQRES  23 B  320  ILE GLN ASN GLU GLN LEU VAL HIS HIS ASP ILE ILE ASP          
SEQRES  24 B  320  ALA ILE GLU ASN MET LYS ARG PRO PHE LYS GLY ASP TRP          
SEQRES  25 B  320  LEU ASP CYS ALA LYS LYS LEU TYR                              
HET    FBP  A 323      20                                                       
HET    FBP  B 323      20                                                       
HET     MG  A 325       1                                                       
HET     MG  A 327       1                                                       
HET     MG  B 325       1                                                       
HET     MG  B 327       1                                                       
HET    ADP  A 324      27                                                       
HET    ADP  A 326      27                                                       
HET    ADP  B 324      27                                                       
HET    ADP  B 326      27                                                       
HETNAM     FBP BETA-FRUCTOSE-1,6-DIPHOSPHATE                                    
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETSYN     FBP FRUCTOSE-1,6-BISPHOSPHATE                                        
FORMUL   3  FBP    2(C6 H14 O12 P2)                                             
FORMUL   5   MG    4(MG 2+)                                                     
FORMUL   9  ADP    4(C10 H15 N5 O10 P2)                                         
FORMUL  13  HOH   *277(H2 O)                                                    
HELIX    1  1A GLY A   15  GLU A   30  13/10 END                          16    
HELIX    2  2A GLY A   40  ASP A   47  13/10 BEGINNING AND END             8    
HELIX    3 4AA PHE A   73  ASP A   78  5                                   6    
HELIX    4  4A ASP A   78  GLY A   93  13/10 END                          16    
HELIX    5  5A GLY A  102  GLY A  116  1                                  15    
HELIX    6  6A GLY A  138  HIS A  160  1                                  23    
HELIX    7  7A THR A  177  GLY A  185  1                                   9    
HELIX    8  8A SER A  197  GLY A  212  13/10 BEGINNING AND END            16    
HELIX    9  9A ASP A  226  GLY A  239  1                                  14    
HELIX   10 10A GLY A  248  ARG A  252  5                                   5    
HELIX   11 11A VAL A  257  GLY A  278  13/10 END                          22    
HELIX   12 12A ASP A  295  ASN A  302  1                                   8    
HELIX   13 13A LYS A  308  TYR A  319  1                                  12    
HELIX   14  1B GLY B   15  GLU B   30  13/10 END                          16    
HELIX   15  2B GLY B   40  ASP B   47  13/10 BEGINNING AND END             8    
HELIX   16 4AB PHE B   73  ASP B   78  5                                   6    
HELIX   17  4B ASP B   78  GLY B   93  13/10 END                          16    
HELIX   18  5B GLY B  102  GLY B  116  1                                  15    
HELIX   19  6B GLY B  138  HIS B  160  1                                  23    
HELIX   20  7B THR B  177  GLY B  185  1                                   9    
HELIX   21  8B SER B  197  GLY B  212  13/10 BEGINNING AND END            16    
HELIX   22  9B ASP B  226  GLY B  239  1                                  14    
HELIX   23 10B GLY B  248  ARG B  252  5                                   5    
HELIX   24 11B VAL B  257  GLY B  278  13/10 END                          22    
HELIX   25 12B ASP B  295  ASN B  302  1                                   8    
HELIX   26 13B LYS B  308  TYR B  319  1                                  12    
SHEET    1 S1A 7 ARG A  48  LEU A  52  0                                        
SHEET    2 S1A 7 GLU A  33  TYR A  38 -1  O  GLY A  36   N  VAL A  50           
SHEET    3 S1A 7 LYS A   2  SER A   9  1  O  VAL A   6   N  ILE A  37           
SHEET    4 S1A 7 ALA A  96  GLY A 101  1  O  VAL A  98   N  LEU A   7           
SHEET    5 S1A 7 PRO A 118  LEU A 122  1  O  ILE A 120   N  VAL A  99           
SHEET    6 S1A 7 GLY A 281  GLN A 287  1  O  ARG A 282   N  GLY A 121           
SHEET    7 S1A 7 GLN A 290  ASP A 295 -1  O  HIS A 294   N  CYS A 283           
SHEET    1 S2A 4 PHE A 188  VAL A 190  0                                        
SHEET    2 S2A 4 ALA A 216  THR A 221  1  O  ALA A 219   N  VAL A 190           
SHEET    3 S2A 4 ARG A 162  VAL A 168  1  O  VAL A 166   N  ILE A 220           
SHEET    4 S2A 4 GLU A 241  LEU A 247  1  O  THR A 245   N  GLU A 167           
SHEET    1 S1B 7 ARG B  48  LEU B  52  0                                        
SHEET    2 S1B 7 GLU B  33  TYR B  38 -1  O  GLY B  36   N  VAL B  50           
SHEET    3 S1B 7 LYS B   2  SER B   9  1  O  VAL B   6   N  ILE B  37           
SHEET    4 S1B 7 ALA B  96  GLY B 101  1  O  VAL B  98   N  LEU B   7           
SHEET    5 S1B 7 PRO B 118  LEU B 122  1  O  ILE B 120   N  VAL B  99           
SHEET    6 S1B 7 GLY B 281  GLN B 287  1  O  ARG B 282   N  GLY B 121           
SHEET    7 S1B 7 GLN B 290  ASP B 295 -1  O  HIS B 294   N  CYS B 283           
SHEET    1 S2B 4 PHE B 188  VAL B 190  0                                        
SHEET    2 S2B 4 ALA B 216  THR B 221  1  O  ALA B 219   N  VAL B 190           
SHEET    3 S2B 4 ARG B 162  VAL B 168  1  O  VAL B 166   N  ILE B 220           
SHEET    4 S2B 4 GLU B 241  LEU B 247  1  O  THR B 245   N  GLU B 167           
LINK         O2P FBP A 323                MG    MG A 325     1555   1555  2.04  
LINK        MG    MG A 325                 O   HOH A 417     1555   1555  2.38  
LINK        MG    MG A 325                 OD2 ASP A 103     1555   1555  1.95  
LINK        MG    MG A 325                 O2B ADP A 324     1555   1555  2.19  
LINK        MG    MG A 325                 O   HOH A 386     1555   1555  2.25  
LINK        MG    MG A 325                 O   HOH A 402     1555   1555  2.43  
LINK        MG    MG A 327                 O   GLY A 185     1555   1555  2.25  
LINK        MG    MG A 327                 O2B ADP A 326     1555   1555  2.17  
LINK        MG    MG A 327                 O1A ADP A 326     1555   1555  2.42  
LINK        MG    MG A 327                 O   HOH A 368     1555   1555  1.96  
LINK        MG    MG A 327                 OE1 GLU A 187     1555   1555  2.14  
LINK        MG    MG A 327                 O   HOH A 369     1555   1555  1.91  
LINK        MG    MG B 325                 O2B ADP B 324     1555   1555  2.72  
LINK        MG    MG B 325                 O   HOH B 419     1555   1555  2.37  
LINK        MG    MG B 325                 O1A ADP B 324     1555   1555  2.26  
LINK        MG    MG B 327                 OE1 GLU B 187     1555   1555  2.21  
LINK        MG    MG B 327                 OE2 GLU B 187     1555   1555  3.08  
LINK        MG    MG B 327                 O2B ADP B 326     1555   1555  2.23  
LINK        MG    MG B 327                 O1A ADP B 326     1555   1555  2.15  
LINK        MG    MG B 327                 O   HOH B 369     1555   1555  2.17  
LINK        MG    MG B 327                 O   HOH B 370     1555   1555  2.05  
LINK        MG    MG B 327                 O   GLY B 185     1555   1555  2.30  
SITE     1 AC1 20 GLY A  11  ARG A  72  THR A 125  ASP A 127                    
SITE     2 AC1 20 MET A 169  GLY A 170  ARG A 171  GLU A 222                    
SITE     3 AC1 20 HIS A 249  ARG A 252  ADP A 324   MG A 325                    
SITE     4 AC1 20 HOH A 330  HOH A 351  HOH A 402  HOH A 417                    
SITE     5 AC1 20 HOH A 430  HOH A 447  ARG B 162  ARG B 243                    
SITE     1 AC2 18 ARG A 162  ARG A 243  GLY B  11  THR B 125                    
SITE     2 AC2 18 ASP B 127  MET B 169  GLY B 170  ARG B 171                    
SITE     3 AC2 18 GLU B 222  HIS B 249  ARG B 252  ADP B 324                    
SITE     4 AC2 18 HOH B 331  HOH B 352  HOH B 387  HOH B 403                    
SITE     5 AC2 18 HOH B 447  HOH B 448                                          
SITE     1 AC3  6 ASP A 103  FBP A 323  ADP A 324  HOH A 386                    
SITE     2 AC3  6 HOH A 402  HOH A 417                                          
SITE     1 AC4  5 GLY A 185  GLU A 187  ADP A 326  HOH A 368                    
SITE     2 AC4  5 HOH A 369                                                     
SITE     1 AC5  3 ASP B 103  ADP B 324  HOH B 419                               
SITE     1 AC6  5 GLY B 185  GLU B 187  ADP B 326  HOH B 369                    
SITE     2 AC6  5 HOH B 370                                                     
SITE     1 AC7 19 GLY A  10  GLY A  11  TYR A  41  ARG A  72                    
SITE     2 AC7 19 PHE A  73  PHE A  76  ARG A  77  GLY A 102                    
SITE     3 AC7 19 ASP A 103  GLY A 104  SER A 105  MET A 107                    
SITE     4 AC7 19 GLY A 108  FBP A 323   MG A 325  HOH A 351                    
SITE     5 AC7 19 HOH A 365  HOH A 386  HOH A 465                               
SITE     1 AC8 19 ARG A 154  SER A 158  GLY A 185  GLU A 187                    
SITE     2 AC8 19 GLY A 212  LYS A 213  LYS A 214  HIS A 215                    
SITE     3 AC8 19  MG A 327  HOH A 368  HOH A 369  HOH A 467                    
SITE     4 AC8 19 ARG B  21  ARG B  25  ARG B  54  TYR B  55                    
SITE     5 AC8 19 SER B  58  ASP B  59  HOH B 420                               
SITE     1 AC9 16 SER B   9  TYR B  41  ARG B  72  PHE B  73                    
SITE     2 AC9 16 PRO B  74  PHE B  76  ARG B  77  GLY B 102                    
SITE     3 AC9 16 ASP B 103  GLY B 104  SER B 105  MET B 107                    
SITE     4 AC9 16 GLY B 108  FBP B 323   MG B 325  HOH B 366                    
SITE     1 BC1 19 ARG A  21  ARG A  25  ARG A  54  TYR A  55                    
SITE     2 BC1 19 SER A  58  ASP A  59  HOH A 419  ARG B 154                    
SITE     3 BC1 19 SER B 158  GLY B 185  GLU B 187  GLY B 212                    
SITE     4 BC1 19 LYS B 213  LYS B 214  HIS B 215   MG B 327                    
SITE     5 BC1 19 HOH B 328  HOH B 369  HOH B 370                               
CRYST1  112.300   85.400   77.100  90.00  90.00  90.00 P 21 21 2     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      0.008905  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011710  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012970        0.00000                         
MTRIX1   1  0.542870  0.839820  0.000000        0.00000    1                    
MTRIX2   1  0.839820 -0.542870  0.000000        0.00000    1                    
MTRIX3   1  0.000000  0.000000 -1.000000       -5.42690    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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