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Database: PDB
Entry: 7AT1
LinkDB: 7AT1
Original site: 7AT1 
HEADER    TRANSFERASE (CARBAMOYL-P,ASPARTATE)     22-SEP-89   7AT1              
TITLE     CRYSTAL STRUCTURES OF ASPARTATE CARBAMOYLTRANSFERASE LIGATED WITH     
TITLE    2 PHOSPHONOACETAMIDE, MALONATE, AND CTP OR ATP AT 2.8-ANGSTROMS        
TITLE    3 RESOLUTION AND NEUTRAL P*H                                           
CAVEAT     7AT1    GLC E 2 HAS WRONG CHIRALITY AT ATOM C1 GLC E 2 HAS WRONG     
CAVEAT   2 7AT1    CHIRALITY AT ATOM C3 GLC F 2 HAS WRONG CHIRALITY AT ATOM C1  
CAVEAT   3 7AT1    GLC F 2 HAS WRONG CHIRALITY AT ATOM C3                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ASPARTATE CARBAMOYLTRANSFERASE (R STATE), CATALYTIC CHAIN; 
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 EC: 2.1.3.2;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN;           
COMPND   8 CHAIN: B, D;                                                         
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 MOL_ID: 2;                                                           
SOURCE   5 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   6 ORGANISM_TAXID: 562                                                  
KEYWDS    TRANSFERASE (CARBAMOYL-P, ASPARTATE)                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.E.GOUAUX,R.C.STEVENS,W.N.LIPSCOMB                                   
REVDAT   7   06-MAR-24 7AT1    1       HETSYN                                   
REVDAT   6   29-JUL-20 7AT1    1       CAVEAT COMPND REMARK SEQADV              
REVDAT   6 2                   1       HET    HETNAM FORMUL LINK                
REVDAT   6 3                   1       SITE   ATOM                              
REVDAT   5   29-NOV-17 7AT1    1       REMARK HELIX                             
REVDAT   4   13-JUL-11 7AT1    1       VERSN                                    
REVDAT   3   24-FEB-09 7AT1    1       VERSN                                    
REVDAT   2   01-APR-03 7AT1    1       JRNL                                     
REVDAT   1   15-OCT-90 7AT1    0                                                
JRNL        AUTH   J.E.GOUAUX,R.C.STEVENS,W.N.LIPSCOMB                          
JRNL        TITL   CRYSTAL STRUCTURES OF ASPARTATE CARBAMOYLTRANSFERASE LIGATED 
JRNL        TITL 2 WITH PHOSPHONOACETAMIDE, MALONATE, AND CTP OR ATP AT 2.8-A   
JRNL        TITL 3 RESOLUTION AND NEUTRAL PH.                                   
JRNL        REF    BIOCHEMISTRY                  V.  29  7702 1990              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   2271529                                                      
JRNL        DOI    10.1021/BI00485A020                                          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   R.C.STEVENS,J.E.GOUAUX,W.N.LIPSCOMB                          
REMARK   1  TITL   STRUCTURAL CONSEQUENCES OF EFFECTOR BINDING TO THE T STATE   
REMARK   1  TITL 2 OF ASPARTATE CARBAMOYLTRANSFERASE. CRYSTAL STRUCTURES OF THE 
REMARK   1  TITL 3 UNLIGATED AND ATP-, AND CTP-COMPLEXED ENZYMES AT             
REMARK   1  TITL 4 2.6-ANGSTROMS RESOLUTION                                     
REMARK   1  REF    BIOCHEMISTRY                  V.  29  7691 1990              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   J.E.GOUAUX,W.N.LIPSCOMB                                      
REMARK   1  TITL   CRYSTAL STRUCTURES OF PHOSPHONOACETAMIDE LIGATED T AND       
REMARK   1  TITL 2 PHOSPHONOACETAMIDE AND MALONATE LIGATED R STATES OF          
REMARK   1  TITL 3 ASPARTATE CARBAMOYLTRANSFERASE AT 2.8-ANGSTROMS RESOLUTION   
REMARK   1  TITL 4 AND NEUTRAL PH                                               
REMARK   1  REF    BIOCHEMISTRY                  V.  29   389 1990              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   J.E.GOUAUX,W.N.LIPSCOMB,S.A.MIDDLETON,E.R.KANTROWITZ         
REMARK   1  TITL   STRUCTURE OF A SINGLE AMINO ACID MUTANT OF ASPARTATE         
REMARK   1  TITL 2 CARBAMOYLTRANSFERASE AT 2.5-ANGSTROMS RESOLUTION.            
REMARK   1  TITL 3 IMPLICATIONS FOR THE COOPERATIVE MECHANISM                   
REMARK   1  REF    BIOCHEMISTRY                  V.  28  1798 1989              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   J.E.GOUAUX,W.N.LIPSCOMB                                      
REMARK   1  TITL   STRUCTURAL TRANSITIONS IN CRYSTALS OF NATIVE ASPARTATE       
REMARK   1  TITL 2 CARBAMOYLTRANSFERASE                                         
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  86   845 1989              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   H.KE,W.N.LIPSCOMB,Y.CHO,R.B.HONZATKO                         
REMARK   1  TITL   COMPLEX OF N-PHOSPHONACETYL-L-ASPARTATE WITH ASPARTATE       
REMARK   1  TITL 2 CARBAMOYLTRANSFERASE. X-RAY REFINEMENT, ANALYSIS OF          
REMARK   1  TITL 3 CONFORMATIONAL CHANGES AND CATALYTIC AND ALLOSTERIC          
REMARK   1  TITL 4 MECHANISMS                                                   
REMARK   1  REF    J.MOL.BIOL.                   V. 204   725 1988              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 6                                                          
REMARK   1  AUTH   E.R.KANTROWITZ,W.N.LIPSCOMB                                  
REMARK   1  TITL   ESCHERICHIA COLI ASPARTATE TRANSCARBAMYLASE. THE RELATION    
REMARK   1  TITL 2 BETWEEN STRUCTURE AND FUNCTION                               
REMARK   1  REF    SCIENCE                       V. 241   669 1988              
REMARK   1  REFN                   ISSN 0036-8075                               
REMARK   1 REFERENCE 7                                                          
REMARK   1  AUTH   J.E.GOUAUX,W.N.LIPSCOMB                                      
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF CARBAMOYL PHOSPHATE AND       
REMARK   1  TITL 2 SUCCINATE BOUND TO ASPARTATE CARBAMOYLTRANSFERASE            
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  85  4205 1988              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1 REFERENCE 8                                                          
REMARK   1  AUTH   K.H.KIM,Z.PAN,R.B.HONZATKO,H.KE,W.N.LIPSCOMB                 
REMARK   1  TITL   STRUCTURAL ASYMMETRY IN THE CTP-LIGANDED FORM OF ASPARTATE   
REMARK   1  TITL 2 CARBAMOYLTRANSFERASE FROM ESCHERICHIA COLI                   
REMARK   1  REF    J.MOL.BIOL.                   V. 196   853 1987              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 9                                                          
REMARK   1  AUTH   K.L.KRAUSE,K.W.VOLZ,W.N.LIPSCOMB                             
REMARK   1  TITL   2.5 ANGSTROMS STRUCTURE OF ASPARTATE CARBAMOYLTRANSFERASE    
REMARK   1  TITL 2 COMPLEXED WITH THE BISUBSTRATE ANALOG                        
REMARK   1  TITL 3 N-(PHOSPHONACETYL)-L-ASPARTATE                               
REMARK   1  REF    J.MOL.BIOL.                   V. 193   527 1987              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 10                                                         
REMARK   1  AUTH   J.E.GOUAUX,K.L.KRAUSE,W.N.LIPSCOMB                           
REMARK   1  TITL   THE CATALYTIC MECHANISM OF ESCHERICHIA COLI ASPARTATE        
REMARK   1  TITL 2 CARBAMOYLTRANSFERASE. A MOLECULAR MODELLING STUDY            
REMARK   1  REF    BIOCHEM.BIOPHYS.RES.COMMUN.   V. 142   893 1987              
REMARK   1  REFN                   ISSN 0006-291X                               
REMARK   1 REFERENCE 11                                                         
REMARK   1  AUTH   K.L.KRAUSE,K.W.VOLZ,W.N.LIPSCOMB                             
REMARK   1  TITL   STRUCTURE AT 2.9-ANGSTROMS RESOLUTION OF ASPARTATE           
REMARK   1  TITL 2 CARBAMOYLTRANSFERASE COMPLEXED WITH THE BISUBSTRATE ANALOGUE 
REMARK   1  TITL 3 N-(PHOSPHONACETYL)-L-ASPARTATE                               
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  82  1643 1985              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1 REFERENCE 12                                                         
REMARK   1  AUTH   H.KE,R.B.HONZATKO,W.N.LIPSCOMB                               
REMARK   1  TITL   STRUCTURE OF UNLIGATED ASPARTATE CARBAMOYLTRANSFERASE OF     
REMARK   1  TITL 2 ESCHERICHIA COLI AT 2.6-ANGSTROMS RESOLUTION                 
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  81  4037 1984              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1 REFERENCE 13                                                         
REMARK   1  AUTH   R.B.HONZATKO,J.L.CRAWFORD,H.L.MONACO,J.E.LADNER,             
REMARK   1  AUTH 2 B.F.P.EDWARDS,D.R.EVANS,S.G.WARREN,D.C.WILEY,R.C.LADNER,     
REMARK   1  AUTH 3 W.N.LIPSCOMB                                                 
REMARK   1  TITL   CRYSTAL AND MOLECULAR STRUCTURES OF NATIVE AND CTP-LIGANDED  
REMARK   1  TITL 2 ASPARTATE CARBAMOYLTRANSFERASE FROM ESCHERICHIA COLI         
REMARK   1  REF    J.MOL.BIOL.                   V. 160   219 1982              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 14                                                         
REMARK   1  AUTH   R.B.HONZATKO,W.N.LIPSCOMB                                    
REMARK   1  TITL   INTERACTIONS OF PHOSPHATE LIGANDS WITH ESCHERICHIA COLI      
REMARK   1  TITL 2 ASPARTATE CARBAMOYLTRANSFERASE IN THE CRYSTALLINE STATE      
REMARK   1  REF    J.MOL.BIOL.                   V. 160   265 1982              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 15                                                         
REMARK   1  AUTH   R.B.HONZATKO,W.N.LIPSCOMB                                    
REMARK   1  TITL   INTERACTIONS OF METAL-NUCLEOTIDE COMPLEXES WITH ASPARTATE    
REMARK   1  TITL 2 CARBAMOYLTRANSFERASE IN THE CRYSTALLINE STATE                
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  79  7171 1982              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1 REFERENCE 16                                                         
REMARK   1  AUTH   J.E.LADNER,J.P.KITCHELL,R.B.HONZATKO,H.M.KE,K.W.VOLZ,        
REMARK   1  AUTH 2 A.J.KALB(GILBOA),R.C.LADNER,W.N.LIPSCOMB                     
REMARK   1  TITL   GROSS QUATERNARY CHANGES IN ASPARTATE CARBAMOYLTRANSFERASE   
REMARK   1  TITL 2 ARE INDUCED BY THE BINDING OF                                
REMARK   1  TITL 3 N-(PHOSPHONACETYL)-L-ASPARTATE. A 3.5-ANGSTROMS RESOLUTION   
REMARK   1  TITL 4 STUDY                                                        
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  79  3125 1982              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1 REFERENCE 17                                                         
REMARK   1  AUTH   R.B.HONZATKO,H.L.MONACO,W.N.LIPSCOMB                         
REMARK   1  TITL   A 3.0-ANGSTROMS RESOLUTION STUDY OF NUCLEOTIDE COMPLEXES     
REMARK   1  TITL 2 WITH ASPARTATE CARBAMOYLTRANSFERASE                          
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  76  5105 1979              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1 REFERENCE 18                                                         
REMARK   1  AUTH   H.L.MONACO,J.L.CRAWFORD,W.N.LIPSCOMB                         
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURES OF ASPARTATE                    
REMARK   1  TITL 2 CARBAMOYLTRANSFERASE FROM ESCHERICHIA COLI AND OF ITS        
REMARK   1  TITL 3 COMPLEX WITH CYTIDINE TRIPHOSPHATE                           
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  75  5276 1978              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1 REFERENCE 19                                                         
REMARK   1  AUTH   W.N.LIPSCOMB,B.F.P.EDWARDS,D.R.EVANS,S.C.PASTRA-LANDIS       
REMARK   1  TITL   BINDING SITE AT 5.5 ANGSTROMS RESOLUTION OF CYTIDINE         
REMARK   1  TITL 2 TRIPHOSPHATE, THE ALLOSTERIC INHIBITOR OF ASPARTATE          
REMARK   1  TITL 3 TRANSCARBAMYLASE FROM ESCHERICHIA COLI. RELATION TO          
REMARK   1  TITL 4 MECHANISMS OF CONTROL                                        
REMARK   1  EDIT   M.SUNDARALINGAM, S.T.RAO                                     
REMARK   1  REF    STRUCTURE AND CONFORMATION             333 1975              
REMARK   1  REF  2 OF NUCLEIC ACIDS AND                                         
REMARK   1  REF  3 PROTEIN-NUCLEIC ACID                                         
REMARK   1  REF  4 INTERACTIONS : PROCEEDINGS                                   
REMARK   1  REF  5 OF THE FOURTH ANNUAL HARRY                                   
REMARK   1  REF  6 STEENBOCK SYMPOSIUM, JUNE                                    
REMARK   1  REF  7 16-19, 1974, MADISON,                                        
REMARK   1  REF  8 WISCONSIN                                                    
REMARK   1  PUBL   UNIVERSITY PARK PRESS,BALTIMORE                              
REMARK   1  REFN                                                                
REMARK   1 REFERENCE 20                                                         
REMARK   1  AUTH   S.G.WARREN,B.F.P.EDWARDS,D.R.EVANS,D.C.WILEY,W.N.LIPSCOMB    
REMARK   1  TITL   ASPARTATE TRANSCARBAMOYLASE FROM ESCHERICHIA COLI. ELECTRON  
REMARK   1  TITL 2 DENSITY AT 5.5 ANGSTROMS RESOLUTION                          
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  70  1117 1973              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 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 SET) : 0.183                           
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   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7106                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 63                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
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  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.017                           
REMARK   3   BOND ANGLES            (DEGREES) : 3.500                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 7AT1 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_1000179882.                                   
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   (%): 62.68                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: THE CRYSTALS WERE GROWN IN A SOLUTION    
REMARK 280  OF PHOSPHONACETAMIDE (PAM) AND MALONATE (MAL) AT PH 5.8. THEY       
REMARK 280  WERE THEN SOAKED IN A SOLUTION CONTAINING PAM, MAL, AND ATP AT      
REMARK 280  PH 7.0.                                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  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 NON-CRYSTALLOGRAPHIC TWO-FOLD AXIS, WHICH IS SPECIFIED   
REMARK 300 ON THE *MTRIX* RECORDS BELOW, RELATES THE *A* AND *B*                
REMARK 300 CHAINS TO THE *C* AND *D* CHAINS.                                    
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: DODECAMERIC                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC                
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 33650 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 101400 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -112.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
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 -0.500000 -0.866025  0.000000      122.50000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000       61.25000            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000      106.08811            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     ASP B     4                                                      
REMARK 465     ASN B     5                                                      
REMARK 465     LYS B     6                                                      
REMARK 465     LEU B     7                                                      
REMARK 465     MET D     1                                                      
REMARK 465     THR D     2                                                      
REMARK 465     HIS D     3                                                      
REMARK 465     ASP D     4                                                      
REMARK 465     ASN D     5                                                      
REMARK 465     LYS D     6                                                      
REMARK 465     LEU D     7                                                      
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   O4   GLC E     1     O5   GLC E     2              2.15            
REMARK 500   O4   GLC F     1     O5   GLC F     2              2.15            
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    HIS A  41   NE2   HIS A  41   CD2    -0.067                       
REMARK 500    HIS A  64   NE2   HIS A  64   CD2    -0.071                       
REMARK 500    HIS A 106   NE2   HIS A 106   CD2    -0.074                       
REMARK 500    HIS A 134   NE2   HIS A 134   CD2    -0.067                       
REMARK 500    HIS A 212   NE2   HIS A 212   CD2    -0.067                       
REMARK 500    HIS A 265   NE2   HIS A 265   CD2    -0.076                       
REMARK 500    HIS A 282   NE2   HIS A 282   CD2    -0.076                       
REMARK 500    HIS B 117   NE2   HIS B 117   CD2    -0.073                       
REMARK 500    HIS B 147   NE2   HIS B 147   CD2    -0.076                       
REMARK 500    HIS C   8   NE2   HIS C   8   CD2    -0.068                       
REMARK 500    HIS C  64   NE2   HIS C  64   CD2    -0.083                       
REMARK 500    HIS C 156   NE2   HIS C 156   CD2    -0.079                       
REMARK 500    HIS C 170   NE2   HIS C 170   CD2    -0.068                       
REMARK 500    HIS C 212   NE2   HIS C 212   CD2    -0.070                       
REMARK 500    HIS C 255   NE2   HIS C 255   CD2    -0.070                       
REMARK 500    HIS C 265   NE2   HIS C 265   CD2    -0.070                       
REMARK 500    HIS C 282   NE2   HIS C 282   CD2    -0.072                       
REMARK 500    HIS D  20   NE2   HIS D  20   CD2    -0.074                       
REMARK 500    HIS D 117   NE2   HIS D 117   CD2    -0.070                       
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  54   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG A  54   NE  -  CZ  -  NH2 ANGL. DEV. =   4.9 DEGREES          
REMARK 500    ARG A  56   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ARG A  56   NE  -  CZ  -  NH2 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    ARG A  65   NE  -  CZ  -  NH2 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    TYR A  98   CB  -  CG  -  CD2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    MET A 104   CG  -  SD  -  CE  ANGL. DEV. = -11.3 DEGREES          
REMARK 500    ARG A 105   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ARG A 105   NE  -  CZ  -  NH2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    TYR A 165   CB  -  CG  -  CD1 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    TRP A 209   CD1 -  CG  -  CD2 ANGL. DEV. =   5.3 DEGREES          
REMARK 500    ARG A 234   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG A 250   NE  -  CZ  -  NH2 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG A 269   CB  -  CG  -  CD  ANGL. DEV. = -16.7 DEGREES          
REMARK 500    TRP A 284   CD1 -  CG  -  CD2 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    TRP A 284   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    ARG A 296   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG A 296   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG A 306   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    VAL A 309   CA  -  C   -  N   ANGL. DEV. = -13.4 DEGREES          
REMARK 500    VAL A 309   O   -  C   -  N   ANGL. DEV. =  10.6 DEGREES          
REMARK 500    ARG B  55   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG B  96   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ALA B 152   CA  -  C   -  N   ANGL. DEV. = -13.8 DEGREES          
REMARK 500    TYR C  98   CB  -  CG  -  CD2 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500    ARG C 105   NE  -  CZ  -  NH2 ANGL. DEV. =   5.3 DEGREES          
REMARK 500    ARG C 151   NE  -  CZ  -  NH2 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ARG C 183   NE  -  CZ  -  NH2 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    TRP C 209   CD1 -  CG  -  CD2 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    TRP C 209   CB  -  CG  -  CD1 ANGL. DEV. =  -8.3 DEGREES          
REMARK 500    TRP C 209   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ARG C 234   NE  -  CZ  -  NH2 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    MET C 261   CG  -  SD  -  CE  ANGL. DEV. = -10.5 DEGREES          
REMARK 500    TRP C 284   CD1 -  CG  -  CD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    TRP C 284   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    ARG D  14   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG D  85   NE  -  CZ  -  NH2 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ARG D 102   NE  -  CZ  -  NH2 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ASN D 105   N   -  CA  -  C   ANGL. DEV. =  16.9 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    GLN A   6        9.44     50.01                                   
REMARK 500    THR A  53      -74.03   -126.84                                   
REMARK 500    ARG A  54      -82.53    -46.05                                   
REMARK 500    ASN A 132      -79.47    -94.32                                   
REMARK 500    HIS A 134       75.46   -150.92                                   
REMARK 500    PRO A 237      -36.00    -36.54                                   
REMARK 500    ALA A 259        0.71    -63.72                                   
REMARK 500    LEU A 267      157.74     66.17                                   
REMARK 500    VAL A 270      -94.24   -116.67                                   
REMARK 500    VAL B   9     -138.55     51.09                                   
REMARK 500    LYS B  13      -75.34    -66.27                                   
REMARK 500    GLN B  24      -55.73     96.87                                   
REMARK 500    LYS B  34       49.28    -65.49                                   
REMARK 500    ASN B  47       67.11     60.38                                   
REMARK 500    ASN B  88       71.44     31.05                                   
REMARK 500    ASN B 105      -43.47     70.47                                   
REMARK 500    ARG B 130      -81.04   -100.39                                   
REMARK 500    ALA B 131       25.69   -159.16                                   
REMARK 500    ASN B 132      -62.05   -178.81                                   
REMARK 500    ASP B 133     -169.51   -120.13                                   
REMARK 500    TYR B 140      -70.54    -81.76                                   
REMARK 500    ALA B 152      173.85     60.41                                   
REMARK 500    GLN C  35       72.14   -116.16                                   
REMARK 500    THR C  53      -70.74   -102.56                                   
REMARK 500    ALA C  77      -29.46    -39.28                                   
REMARK 500    ASN C 132      -77.49    -80.25                                   
REMARK 500    HIS C 134       73.05   -153.68                                   
REMARK 500    LEU C 267      155.47     70.60                                   
REMARK 500    VAL C 270     -128.38   -115.01                                   
REMARK 500    GLU D  10      179.99     86.54                                   
REMARK 500    GLN D  24      -26.98     73.22                                   
REMARK 500    SER D  50       83.02   -158.22                                   
REMARK 500    GLU D  68      -59.67    -27.31                                   
REMARK 500    TYR D  89      -10.95     60.17                                   
REMARK 500    ASN D 105       16.87     34.88                                   
REMARK 500    PRO D 120       67.41    -59.99                                   
REMARK 500    ASP D 133     -167.65   -173.69                                   
REMARK 500    TYR D 140      -67.98    -92.81                                   
REMARK 500    ALA D 152       96.39    -61.79                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A   5         0.09    SIDE CHAIN                              
REMARK 500    TYR A 240         0.09    SIDE CHAIN                              
REMARK 500    TYR B  89         0.07    SIDE CHAIN                              
REMARK 500    TYR C 165         0.08    SIDE CHAIN                              
REMARK 500    TYR C 226         0.08    SIDE CHAIN                              
REMARK 500    PHE D  27         0.09    SIDE CHAIN                              
REMARK 500    TYR D  77         0.10    SIDE CHAIN                              
REMARK 500    TYR D  89         0.10    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 THERE ARE NO ATP COORDINATES FOR THE D CHAIN BECAUSE THERE           
REMARK 600 WAS NOT SUFFICIENT DENSITY TO BUILD THE MOLECULE INTO THE            
REMARK 600 ELECTRON DENSITY MAPS.                                               
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     GLC E    2                                                       
REMARK 610     GLC F    2                                                       
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                              ZN B 154  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 109   SG                                                     
REMARK 620 2 CYS B 114   SG  121.2                                              
REMARK 620 3 CYS B 138   SG  115.7 105.8                                        
REMARK 620 4 CYS B 141   SG  103.0 107.5 101.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 154  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 109   SG                                                     
REMARK 620 2 CYS D 114   SG  121.9                                              
REMARK 620 3 CYS D 138   SG  110.2 105.9                                        
REMARK 620 4 CYS D 141   SG  105.3 110.9 100.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: PMA                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: BINDING SITES OF COMBINED *PCT* AND *MAL*          
REMARK 800  MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF      
REMARK 800  SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE    
REMARK 800  IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN.                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ZNB                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: zn binding site                                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ATB                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: ALLOSTERIC BINDING SITE                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PMC                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: BINDING SITES OF COMBINED *PCT* AND *MAL*          
REMARK 800  MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF      
REMARK 800  SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE    
REMARK 800  IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN.                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ZND                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: zn binding site                                    
DBREF  7AT1 A    1   310  UNP    P0A786   PYRB_ECOLI       1    310             
DBREF  7AT1 B    2   153  UNP    P0A7F3   PYRI_ECOLI       1    152             
DBREF  7AT1 C    1   310  UNP    P0A786   PYRB_ECOLI       1    310             
DBREF  7AT1 D    2   153  UNP    P0A7F3   PYRI_ECOLI       1    152             
SEQADV 7AT1 GLN A   60  UNP  P0A786    GLU    60 CONFLICT                       
SEQADV 7AT1 GLN A  147  UNP  P0A786    GLU   147 CONFLICT                       
SEQADV 7AT1 GLU A  149  UNP  P0A786    GLN   149 CONFLICT                       
SEQADV 7AT1 GLU A  196  UNP  P0A786    GLN   196 CONFLICT                       
SEQADV 7AT1 GLY B    8  UNP  P0A7F3    GLN     7 CONFLICT                       
SEQADV 7AT1 GLN C   60  UNP  P0A786    GLU    60 CONFLICT                       
SEQADV 7AT1 GLN C  147  UNP  P0A786    GLU   147 CONFLICT                       
SEQADV 7AT1 GLU C  149  UNP  P0A786    GLN   149 CONFLICT                       
SEQADV 7AT1 GLU C  196  UNP  P0A786    GLN   196 CONFLICT                       
SEQADV 7AT1 GLY D    8  UNP  P0A7F3    GLN     7 CONFLICT                       
SEQRES   1 A  310  ALA ASN PRO LEU TYR GLN LYS HIS ILE ILE SER ILE ASN          
SEQRES   2 A  310  ASP LEU SER ARG ASP ASP LEU ASN LEU VAL LEU ALA THR          
SEQRES   3 A  310  ALA ALA LYS LEU LYS ALA ASN PRO GLN PRO GLU LEU LEU          
SEQRES   4 A  310  LYS HIS LYS VAL ILE ALA SER CYS PHE PHE GLU ALA SER          
SEQRES   5 A  310  THR ARG THR ARG LEU SER PHE GLN THR SER MET HIS ARG          
SEQRES   6 A  310  LEU GLY ALA SER VAL VAL GLY PHE SER ASP SER ALA ASN          
SEQRES   7 A  310  THR SER LEU GLY LYS LYS GLY GLU THR LEU ALA ASP THR          
SEQRES   8 A  310  ILE SER VAL ILE SER THR TYR VAL ASP ALA ILE VAL MET          
SEQRES   9 A  310  ARG HIS PRO GLN GLU GLY ALA ALA ARG LEU ALA THR GLU          
SEQRES  10 A  310  PHE SER GLY ASN VAL PRO VAL LEU ASN ALA GLY ASP GLY          
SEQRES  11 A  310  SER ASN GLN HIS PRO THR GLN THR LEU LEU ASP LEU PHE          
SEQRES  12 A  310  THR ILE GLN GLN THR GLU GLY ARG LEU ASP ASN LEU HIS          
SEQRES  13 A  310  VAL ALA MET VAL GLY ASP LEU LYS TYR GLY ARG THR VAL          
SEQRES  14 A  310  HIS SER LEU THR GLN ALA LEU ALA LYS PHE ASP GLY ASN          
SEQRES  15 A  310  ARG PHE TYR PHE ILE ALA PRO ASP ALA LEU ALA MET PRO          
SEQRES  16 A  310  GLU TYR ILE LEU ASP MET LEU ASP GLU LYS GLY ILE ALA          
SEQRES  17 A  310  TRP SER LEU HIS SER SER ILE GLU GLU VAL MET ALA GLU          
SEQRES  18 A  310  VAL ASP ILE LEU TYR MET THR ARG VAL GLN LYS GLU ARG          
SEQRES  19 A  310  LEU ASP PRO SER GLU TYR ALA ASN VAL LYS ALA GLN PHE          
SEQRES  20 A  310  VAL LEU ARG ALA SER ASP LEU HIS ASN ALA LYS ALA ASN          
SEQRES  21 A  310  MET LYS VAL LEU HIS PRO LEU PRO ARG VAL ASP GLU ILE          
SEQRES  22 A  310  ALA THR ASP VAL ASP LYS THR PRO HIS ALA TRP TYR PHE          
SEQRES  23 A  310  GLN GLN ALA GLY ASN GLY ILE PHE ALA ARG GLN ALA LEU          
SEQRES  24 A  310  LEU ALA LEU VAL LEU ASN ARG ASP LEU VAL LEU                  
SEQRES   1 B  153  MET THR HIS ASP ASN LYS LEU GLY VAL GLU ALA ILE LYS          
SEQRES   2 B  153  ARG GLY THR VAL ILE ASP HIS ILE PRO ALA GLN ILE GLY          
SEQRES   3 B  153  PHE LYS LEU LEU SER LEU PHE LYS LEU THR GLU THR ASP          
SEQRES   4 B  153  GLN ARG ILE THR ILE GLY LEU ASN LEU PRO SER GLY GLU          
SEQRES   5 B  153  MET GLY ARG LYS ASP LEU ILE LYS ILE GLU ASN THR PHE          
SEQRES   6 B  153  LEU SER GLU ASP GLN VAL ASP GLN LEU ALA LEU TYR ALA          
SEQRES   7 B  153  PRO GLN ALA THR VAL ASN ARG ILE ASP ASN TYR GLU VAL          
SEQRES   8 B  153  VAL GLY LYS SER ARG PRO SER LEU PRO GLU ARG ILE ASP          
SEQRES   9 B  153  ASN VAL LEU VAL CYS PRO ASN SER ASN CYS ILE SER HIS          
SEQRES  10 B  153  ALA GLU PRO VAL SER SER SER PHE ALA VAL ARG LYS ARG          
SEQRES  11 B  153  ALA ASN ASP ILE ALA LEU LYS CYS LYS TYR CYS GLU LYS          
SEQRES  12 B  153  GLU PHE SER HIS ASN VAL VAL LEU ALA ASN                      
SEQRES   1 C  310  ALA ASN PRO LEU TYR GLN LYS HIS ILE ILE SER ILE ASN          
SEQRES   2 C  310  ASP LEU SER ARG ASP ASP LEU ASN LEU VAL LEU ALA THR          
SEQRES   3 C  310  ALA ALA LYS LEU LYS ALA ASN PRO GLN PRO GLU LEU LEU          
SEQRES   4 C  310  LYS HIS LYS VAL ILE ALA SER CYS PHE PHE GLU ALA SER          
SEQRES   5 C  310  THR ARG THR ARG LEU SER PHE GLN THR SER MET HIS ARG          
SEQRES   6 C  310  LEU GLY ALA SER VAL VAL GLY PHE SER ASP SER ALA ASN          
SEQRES   7 C  310  THR SER LEU GLY LYS LYS GLY GLU THR LEU ALA ASP THR          
SEQRES   8 C  310  ILE SER VAL ILE SER THR TYR VAL ASP ALA ILE VAL MET          
SEQRES   9 C  310  ARG HIS PRO GLN GLU GLY ALA ALA ARG LEU ALA THR GLU          
SEQRES  10 C  310  PHE SER GLY ASN VAL PRO VAL LEU ASN ALA GLY ASP GLY          
SEQRES  11 C  310  SER ASN GLN HIS PRO THR GLN THR LEU LEU ASP LEU PHE          
SEQRES  12 C  310  THR ILE GLN GLN THR GLU GLY ARG LEU ASP ASN LEU HIS          
SEQRES  13 C  310  VAL ALA MET VAL GLY ASP LEU LYS TYR GLY ARG THR VAL          
SEQRES  14 C  310  HIS SER LEU THR GLN ALA LEU ALA LYS PHE ASP GLY ASN          
SEQRES  15 C  310  ARG PHE TYR PHE ILE ALA PRO ASP ALA LEU ALA MET PRO          
SEQRES  16 C  310  GLU TYR ILE LEU ASP MET LEU ASP GLU LYS GLY ILE ALA          
SEQRES  17 C  310  TRP SER LEU HIS SER SER ILE GLU GLU VAL MET ALA GLU          
SEQRES  18 C  310  VAL ASP ILE LEU TYR MET THR ARG VAL GLN LYS GLU ARG          
SEQRES  19 C  310  LEU ASP PRO SER GLU TYR ALA ASN VAL LYS ALA GLN PHE          
SEQRES  20 C  310  VAL LEU ARG ALA SER ASP LEU HIS ASN ALA LYS ALA ASN          
SEQRES  21 C  310  MET LYS VAL LEU HIS PRO LEU PRO ARG VAL ASP GLU ILE          
SEQRES  22 C  310  ALA THR ASP VAL ASP LYS THR PRO HIS ALA TRP TYR PHE          
SEQRES  23 C  310  GLN GLN ALA GLY ASN GLY ILE PHE ALA ARG GLN ALA LEU          
SEQRES  24 C  310  LEU ALA LEU VAL LEU ASN ARG ASP LEU VAL LEU                  
SEQRES   1 D  153  MET THR HIS ASP ASN LYS LEU GLY VAL GLU ALA ILE LYS          
SEQRES   2 D  153  ARG GLY THR VAL ILE ASP HIS ILE PRO ALA GLN ILE GLY          
SEQRES   3 D  153  PHE LYS LEU LEU SER LEU PHE LYS LEU THR GLU THR ASP          
SEQRES   4 D  153  GLN ARG ILE THR ILE GLY LEU ASN LEU PRO SER GLY GLU          
SEQRES   5 D  153  MET GLY ARG LYS ASP LEU ILE LYS ILE GLU ASN THR PHE          
SEQRES   6 D  153  LEU SER GLU ASP GLN VAL ASP GLN LEU ALA LEU TYR ALA          
SEQRES   7 D  153  PRO GLN ALA THR VAL ASN ARG ILE ASP ASN TYR GLU VAL          
SEQRES   8 D  153  VAL GLY LYS SER ARG PRO SER LEU PRO GLU ARG ILE ASP          
SEQRES   9 D  153  ASN VAL LEU VAL CYS PRO ASN SER ASN CYS ILE SER HIS          
SEQRES  10 D  153  ALA GLU PRO VAL SER SER SER PHE ALA VAL ARG LYS ARG          
SEQRES  11 D  153  ALA ASN ASP ILE ALA LEU LYS CYS LYS TYR CYS GLU LYS          
SEQRES  12 D  153  GLU PHE SER HIS ASN VAL VAL LEU ALA ASN                      
HET    GLC  E   1       1                                                       
HET    GLC  E   2       6                                                       
HET    GLC  F   1       1                                                       
HET    GLC  F   2       6                                                       
HET    PCT  A 311       8                                                       
HET     ZN  B 154       1                                                       
HET    ATP  B 155      31                                                       
HET    PCT  C 311       8                                                       
HET     ZN  D 154       1                                                       
HETNAM     GLC ALPHA-D-GLUCOPYRANOSE                                            
HETNAM     PCT PHOSPHONOACETAMIDE                                               
HETNAM      ZN ZINC ION                                                         
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETSYN     GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE                              
FORMUL   5  GLC    4(C6 H12 O6)                                                 
FORMUL   7  PCT    2(C2 H6 N O4 P)                                              
FORMUL   8   ZN    2(ZN 2+)                                                     
FORMUL   9  ATP    C10 H16 N5 O13 P3                                            
HELIX    1 H1A ARG A   17  ALA A   32  1                                  16    
HELIX    2 H2A THR A   53  LEU A   66  1                                  14    
HELIX    3 H3A ALA A   89  VAL A   99  1                                  11    
HELIX    4 H4A ALA A  111  SER A  119  1                                   9    
HELIX    5 H5A PRO A  135  GLU A  149  1                                  15    
HELIX    6 H6A ARG A  167  PHE A  179  1                                  13    
HELIX    7 H7A GLU A  196  LYS A  205  1                                  10    
HELIX    8 H8A ILE A  215  ALA A  220  1                                   6    
HELIX    9 H0A ALA A  251  ASN A  256  1                                   6    
HELIX   10 HEA THR A  275  LYS A  279  1                                   5    
HELIX   11 HTA TYR A  285  LEU A  304  1                                  20    
HELIX   12 H1B ILE B   25  PHE B   33  1                                   9    
HELIX   13 H2B ASP B   69  TYR B   77  5ENDS TYPE 1                        9    
HELIX   14 H3B HIS B  147  VAL B  150  1                                   4    
HELIX   15 H1C ARG C   17  ALA C   32  1                                  16    
HELIX   16 H2C THR C   53  LEU C   66  1                                  14    
HELIX   17 H3C ALA C   89  VAL C   99  1                                  11    
HELIX   18 H4C ALA C  111  SER C  119  1                                   9    
HELIX   19 H5C PRO C  135  GLU C  149  1                                  15    
HELIX   20 H6C ARG C  167  PHE C  179  1                                  13    
HELIX   21 H7C GLU C  196  LYS C  205  1                                  10    
HELIX   22 H8C ILE C  215  ALA C  220  1                                   6    
HELIX   23 H0C ALA C  251  ASN C  256  1                                   6    
HELIX   24 HEC THR C  275  LYS C  279  1                                   5    
HELIX   25 HTC TYR C  285  LEU C  304  1                                  20    
HELIX   26 H1D ILE D   25  PHE D   33  1                                   9    
HELIX   27 H2D ASP D   69  TYR D   77  5ENDS TYPE 1                        9    
HELIX   28 H3D HIS D  147  VAL D  150  1                                   4    
SHEET    1 C1A 5 LYS A   7  ILE A   9  0                                        
SHEET    2 C1A 5 PRO A 123  ALA A 127  1                                        
SHEET    3 C1A 5 ALA A 101  HIS A 106  1                                        
SHEET    4 C1A 5 LYS A  42  PHE A  48  1                                        
SHEET    5 C1A 5 ALA A  68  SER A  74  1                                        
SHEET    1 C2A 6 ALA A 208  HIS A 212  0                                        
SHEET    2 C2A 6 ASN A 182  ALA A 188  1                                        
SHEET    3 C2A 6 LEU A 155  VAL A 160  1                                        
SHEET    4 C2A 6 ILE A 224  VAL A 230  1                                        
SHEET    5 C2A 6 LYS A 262  HIS A 265  1                                        
SHEET    6 C2A 6 PRO A 281  ALA A 283  1                                        
SHEET    1 R1B 5 ARG B  41  LEU B  46  0                                        
SHEET    2 R1B 5 ARG B  55  GLU B  62 -1                                        
SHEET    3 R1B 5 ARG B  14  ASP B  19 -1                                        
SHEET    4 R1B 5 THR B  82  ASP B  87 -1                                        
SHEET    5 R1B 5 GLY B  93  PRO B  97 -1                                        
SHEET    1 R2B 4 GLU B 101  ASP B 104  0                                        
SHEET    2 R2B 4 SER B 123  LYS B 129 -1                                        
SHEET    3 R2B 4 ILE B 134  CYS B 138 -1                                        
SHEET    4 R2B 4 LYS B 143  SER B 146 -1                                        
SHEET    1 C1C 5 LYS C   7  ILE C   9  0                                        
SHEET    2 C1C 5 PRO C 123  ALA C 127  1                                        
SHEET    3 C1C 5 ALA C 101  HIS C 106  1                                        
SHEET    4 C1C 5 LYS C  42  PHE C  48  1                                        
SHEET    5 C1C 5 ALA C  68  SER C  74  1                                        
SHEET    1 C2C 6 ALA C 208  HIS C 212  0                                        
SHEET    2 C2C 6 ASN C 182  ALA C 188  1                                        
SHEET    3 C2C 6 LEU C 155  VAL C 160  1                                        
SHEET    4 C2C 6 ILE C 224  VAL C 230  1                                        
SHEET    5 C2C 6 LYS C 262  HIS C 265  1                                        
SHEET    6 C2C 6 PRO C 281  ALA C 283  1                                        
SHEET    1 R1D 5 ARG D  41  LEU D  46  0                                        
SHEET    2 R1D 5 ARG D  55  GLU D  62 -1                                        
SHEET    3 R1D 5 ARG D  14  ASP D  19 -1                                        
SHEET    4 R1D 5 THR D  82  ASP D  87 -1                                        
SHEET    5 R1D 5 GLY D  93  PRO D  97 -1                                        
SHEET    1 R2D 4 GLU D 101  ASP D 104  0                                        
SHEET    2 R2D 4 SER D 123  LYS D 129 -1                                        
SHEET    3 R2D 4 ILE D 134  CYS D 138 -1                                        
SHEET    4 R2D 4 LYS D 143  SER D 146 -1                                        
LINK         O4  GLC E   1                 C1  GLC E   2     1555   1555  1.24  
LINK         O4  GLC F   1                 C1  GLC F   2     1555   1555  1.22  
LINK         SG  CYS B 109                ZN    ZN B 154     1555   1555  2.33  
LINK         SG  CYS B 114                ZN    ZN B 154     1555   1555  2.35  
LINK         SG  CYS B 138                ZN    ZN B 154     1555   1555  2.34  
LINK         SG  CYS B 141                ZN    ZN B 154     1555   1555  2.31  
LINK         SG  CYS D 109                ZN    ZN D 154     1555   1555  2.36  
LINK         SG  CYS D 114                ZN    ZN D 154     1555   1555  2.32  
LINK         SG  CYS D 138                ZN    ZN D 154     1555   1555  2.38  
LINK         SG  CYS D 141                ZN    ZN D 154     1555   1555  2.32  
CISPEP   1 LEU A  267    PRO A  268          0        -4.81                     
CISPEP   2 LEU C  267    PRO C  268          0        -5.34                     
SITE     1 PMA 10 ARG A  54  THR A  55  ARG A 105  HIS A 134                    
SITE     2 PMA 10 GLN A 137  ARG A 167  ARG A 229  GLN A 231                    
SITE     3 PMA 10 PRO A 266  LEU A 267                                          
SITE     1 ZNB  4 CYS B 109  CYS B 114  CYS B 138  CYS B 141                    
SITE     1 ATB 12 GLY B   8  VAL B   9  GLU B  10  ALA B  11                    
SITE     2 ATB 12 ILE B  12  ASP B  19  HIS B  20  LYS B  56                    
SITE     3 ATB 12 LYS B  60  ASN B  84  TYR B  89  LYS B  94                    
SITE     1 PMC 10 ARG C  54  THR C  55  ARG C 105  HIS C 134                    
SITE     2 PMC 10 GLN C 137  ARG C 167  ARG C 229  GLN C 231                    
SITE     3 PMC 10 PRO C 266  LEU C 267                                          
SITE     1 ZND  4 CYS D 109  CYS D 114  CYS D 138  CYS D 141                    
CRYST1  122.500  122.500  156.500  90.00  90.00 120.00 P 3 2 1      12          
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      0.008163  0.004713  0.000000        0.00000                         
SCALE2      0.000000  0.009426  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006390        0.00000                         
MTRIX1   1 -0.109515 -0.993509  0.030771      102.21250    1                    
MTRIX2   1 -0.993693  0.108679 -0.027637       92.59020    1                    
MTRIX3   1  0.024113 -0.033603 -0.999144       80.22470    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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