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Database: PDB
Entry: 1JQN
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HEADER    LYASE                                   07-AUG-01   1JQN              
TITLE     CRYSTAL STRUCTURE OF E.COLI PHOSPHOENOLPYRUVATE CARBOXYLASE           
TITLE    2 IN COMPLEX WITH MN2+ AND DCDP                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHOENOLPYRUVATE CARBOXYLASE;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PEPCASE, PEPC;                                              
COMPND   5 EC: 4.1.1.31;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: ESCHERICHIA COLI;                                              
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: F15                                        
KEYWDS    BETA BARREL, MN2+ AND DCDP COMPLEX, LYASE                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.MATSUMURA,Y.KAI                                                     
REVDAT   2   24-FEB-09 1JQN    1       VERSN                                    
REVDAT   1   14-JAN-03 1JQN    0                                                
JRNL        AUTH   H.MATSUMURA,Y.XIE,S.SHIRAKATA,T.INOUE,T.YOSHINAGA,           
JRNL        AUTH 2 Y.UENO,K.IZUI,Y.KAI                                          
JRNL        TITL   CRYSTAL STRUCTURES OF C4 FORM MAIZE AND QUATERNARY           
JRNL        TITL 2 COMPLEX OF E. COLI PHOSPHOENOLPYRUVATE                       
JRNL        TITL 3 CARBOXYLASES.                                                
JRNL        REF    STRUCTURE                     V.  10  1721 2002              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   12467579                                                     
JRNL        DOI    10.1016/S0969-2126(02)00913-9                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   H.MATSUMURA,M.TERADA,S.SHIRAKATA,T.INOUE,                    
REMARK   1  AUTH 2 T.YOSHINAGA,K.IZUI,Y.KAI                                     
REMARK   1  TITL   PLAUSIBLE PHOSPHOENOLPYRUVATE BINDING SITE                   
REMARK   1  TITL 2 REVEALED BY 2.6 A STRUCTURE OF MN2+-BOUND                    
REMARK   1  TITL 3 PHOSPHOENOLPYRUVATE CARBOXYLASE FROM ESCHERICHIA             
REMARK   1  TITL 4 COLI.                                                        
REMARK   1  REF    FEBS LETT.                    V. 458    93 1999              
REMARK   1  REFN                   ISSN 0014-5793                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   Y.KAI,H.MATSUMURA,T.INOUE,K.TERADA,Y.NAGARA,                 
REMARK   1  AUTH 2 T.YOSHINAGA,A.KIHARA,K.TSUMURA,K.IZUI                        
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF PHOSPHOENOLPYRUVATE           
REMARK   1  TITL 2 CARBOXYLASE: A PROPOSED MECHANISM FOR ALLOSTERIC             
REMARK   1  TITL 3 INHIBITION                                                   
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  96   823 1999              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   H.MATSUMURA,T.NAGATA,M.TERADA,S.SHIRAKATA,T.INOUE,           
REMARK   1  AUTH 2 T.YOSHINAGA,Y.UENO,H.SAZE,K.IZUI,Y.KAI                       
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION            
REMARK   1  TITL 2 STUDIES OF C4-FORM PHOSPHOENOLPYRUVATE CARBOXYLASE           
REMARK   1  TITL 3 FROM MAIZE DIFFRACTION STUDIES OF C4-FORM                    
REMARK   1  TITL 4 PHOSPHOENOLPYRUVATE CARBOXYLASE FROM MAIZE.                  
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  55  1937 1999              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 45753                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2292                            
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) : 2.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.50                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 66.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3570                       
REMARK   3   BIN FREE R VALUE                    : 0.3700                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 300                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.021                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6881                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 22                                      
REMARK   3   SOLVENT ATOMS            : 194                                     
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) : 0.31                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.56                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
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) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.10                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 20.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.79                            
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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 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 1JQN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-AUG-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB014075.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-NOV-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-18B                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : WEISSENBERG                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45789                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 11.300                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.2                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.05800                            
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) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.43                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 61.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG300, TRIS-HCL, MNCL2, DCDP, PH        
REMARK 280  8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 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,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
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        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  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       58.97500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      124.53000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       41.56000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       58.97500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      124.53000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       41.56000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       58.97500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      124.53000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       41.56000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       58.97500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      124.53000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       41.56000            
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 BIOLOGICAL ASSEMBLY IS A TETRAMER GENERATED FROM         
REMARK 300 MONOMER IN THE ASSYMMETRIC UNIT BY D2 SYMMETRY.                      
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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      117.95000            
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 350   BIOMT1   3 -1.000000  0.000000  0.000000       58.97500            
REMARK 350   BIOMT2   3  0.000000 -1.000000  0.000000      124.53000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000       41.56000            
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000       58.97500            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000      124.53000            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000       41.56000            
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 A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     ALA A   701                                                      
REMARK 465     LYS A   702                                                      
REMARK 465     ARG A   703                                                      
REMARK 465     ARG A   704                                                      
REMARK 465     PRO A   705                                                      
REMARK 465     THR A   706                                                      
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     GLU A 190    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 443    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 305   CD    GLU A 305   OE1     0.101                       
REMARK 500    GLU A 305   CD    GLU A 305   OE2     0.108                       
REMARK 500    GLU A 306   CD    GLU A 306   OE1     0.079                       
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    ALA A  26      -77.38    -44.89                                   
REMARK 500    ASN A  49       97.31    -68.10                                   
REMARK 500    ASP A 165       14.76     55.24                                   
REMARK 500    THR A 188       72.17   -102.66                                   
REMARK 500    SER A 212      -47.05   -145.58                                   
REMARK 500    MET A 292      152.33    -46.06                                   
REMARK 500    GLU A 306       -8.30     70.29                                   
REMARK 500    LEU A 339      139.01   -170.53                                   
REMARK 500    PRO A 342     -172.30    -60.94                                   
REMARK 500    THR A 347       -8.87   -141.18                                   
REMARK 500    CYS A 366       27.71    -70.15                                   
REMARK 500    MET A 368       43.64   -147.24                                   
REMARK 500    LEU A 390      -61.32     78.84                                   
REMARK 500    GLN A 446       72.59   -115.15                                   
REMARK 500    LYS A 478      -36.61   -131.69                                   
REMARK 500    TYR A 621       20.19   -140.37                                   
REMARK 500    PRO A 687       33.04    -86.98                                   
REMARK 500    MET A 727       19.26     58.08                                   
REMARK 500    TRP A 731      -19.94   -154.73                                   
REMARK 500    LEU A 732      -42.38    -22.88                                   
REMARK 500    MET A 819       70.46     42.19                                   
REMARK 500    ARG A 880     -134.85     56.11                                   
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 A1045        DISTANCE =  5.62 ANGSTROMS                       
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                              MN A 902  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 506   OE1                                                    
REMARK 620 2 ASP A 543   OD1  84.0                                              
REMARK 620 3 DCO A 901   O2   93.1  73.1                                        
REMARK 620 4 DCO A 901   O3  162.5 111.6  99.0                                  
REMARK 620 5 HOH A1095   O    74.1  77.2 148.7 100.8                            
REMARK 620 6 HOH A1096   O    84.0 165.6 115.4  79.4  91.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 902                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ASP A 884                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DCO A 901                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1FIY   RELATED DB: PDB                                   
REMARK 900 1FIY CONTAINS THE NATIVE STRUCTURE OF E.COLI PEPC.                   
REMARK 900 RELATED ID: 1JQO   RELATED DB: PDB                                   
REMARK 900 1JQO CONTAINS THE STRUCTURE OF C4-FORM PHOSPHOENOLPYRUVATE           
REMARK 900 CARBOXYLASE FROM MAIZE                                               
DBREF  1JQN A    1   883  UNP    P00864   CAPP_ECOLI       1    883             
SEQRES   1 A  883  MET ASN GLU GLN TYR SER ALA LEU ARG SER ASN VAL SER          
SEQRES   2 A  883  MET LEU GLY LYS VAL LEU GLY GLU THR ILE LYS ASP ALA          
SEQRES   3 A  883  LEU GLY GLU HIS ILE LEU GLU ARG VAL GLU THR ILE ARG          
SEQRES   4 A  883  LYS LEU SER LYS SER SER ARG ALA GLY ASN ASP ALA ASN          
SEQRES   5 A  883  ARG GLN GLU LEU LEU THR THR LEU GLN ASN LEU SER ASN          
SEQRES   6 A  883  ASP GLU LEU LEU PRO VAL ALA ARG ALA PHE SER GLN PHE          
SEQRES   7 A  883  LEU ASN LEU ALA ASN THR ALA GLU GLN TYR HIS SER ILE          
SEQRES   8 A  883  SER PRO LYS GLY GLU ALA ALA SER ASN PRO GLU VAL ILE          
SEQRES   9 A  883  ALA ARG THR LEU ARG LYS LEU LYS ASN GLN PRO GLU LEU          
SEQRES  10 A  883  SER GLU ASP THR ILE LYS LYS ALA VAL GLU SER LEU SER          
SEQRES  11 A  883  LEU GLU LEU VAL LEU THR ALA HIS PRO THR GLU ILE THR          
SEQRES  12 A  883  ARG ARG THR LEU ILE HIS LYS MET VAL GLU VAL ASN ALA          
SEQRES  13 A  883  CYS LEU LYS GLN LEU ASP ASN LYS ASP ILE ALA ASP TYR          
SEQRES  14 A  883  GLU HIS ASN GLN LEU MET ARG ARG LEU ARG GLN LEU ILE          
SEQRES  15 A  883  ALA GLN SER TRP HIS THR ASP GLU ILE ARG LYS LEU ARG          
SEQRES  16 A  883  PRO SER PRO VAL ASP GLU ALA LYS TRP GLY PHE ALA VAL          
SEQRES  17 A  883  VAL GLU ASN SER LEU TRP GLN GLY VAL PRO ASN TYR LEU          
SEQRES  18 A  883  ARG GLU LEU ASN GLU GLN LEU GLU GLU ASN LEU GLY TYR          
SEQRES  19 A  883  LYS LEU PRO VAL GLU PHE VAL PRO VAL ARG PHE THR SER          
SEQRES  20 A  883  TRP MET GLY GLY ASP ARG ASP GLY ASN PRO ASN VAL THR          
SEQRES  21 A  883  ALA ASP ILE THR ARG HIS VAL LEU LEU LEU SER ARG TRP          
SEQRES  22 A  883  LYS ALA THR ASP LEU PHE LEU LYS ASP ILE GLN VAL LEU          
SEQRES  23 A  883  VAL SER GLU LEU SER MET VAL GLU ALA THR PRO GLU LEU          
SEQRES  24 A  883  LEU ALA LEU VAL GLY GLU GLU GLY ALA ALA GLU PRO TYR          
SEQRES  25 A  883  ARG TYR LEU MET LYS ASN LEU ARG SER ARG LEU MET ALA          
SEQRES  26 A  883  THR GLN ALA TRP LEU GLU ALA ARG LEU LYS GLY GLU GLU          
SEQRES  27 A  883  LEU PRO LYS PRO GLU GLY LEU LEU THR GLN ASN GLU GLU          
SEQRES  28 A  883  LEU TRP GLU PRO LEU TYR ALA CYS TYR GLN SER LEU GLN          
SEQRES  29 A  883  ALA CYS GLY MET GLY ILE ILE ALA ASN GLY ASP LEU LEU          
SEQRES  30 A  883  ASP THR LEU ARG ARG VAL LYS CYS PHE GLY VAL PRO LEU          
SEQRES  31 A  883  VAL ARG ILE ASP ILE ARG GLN GLU SER THR ARG HIS THR          
SEQRES  32 A  883  GLU ALA LEU GLY GLU LEU THR ARG TYR LEU GLY ILE GLY          
SEQRES  33 A  883  ASP TYR GLU SER TRP SER GLU ALA ASP LYS GLN ALA PHE          
SEQRES  34 A  883  LEU ILE ARG GLU LEU ASN SER LYS ARG PRO LEU LEU PRO          
SEQRES  35 A  883  ARG ASN TRP GLN PRO SER ALA GLU THR ARG GLU VAL LEU          
SEQRES  36 A  883  ASP THR CYS GLN VAL ILE ALA GLU ALA PRO GLN GLY SER          
SEQRES  37 A  883  ILE ALA ALA TYR VAL ILE SER MET ALA LYS THR PRO SER          
SEQRES  38 A  883  ASP VAL LEU ALA VAL HIS LEU LEU LEU LYS GLU ALA GLY          
SEQRES  39 A  883  ILE GLY PHE ALA MET PRO VAL ALA PRO LEU PHE GLU THR          
SEQRES  40 A  883  LEU ASP ASP LEU ASN ASN ALA ASN ASP VAL MET THR GLN          
SEQRES  41 A  883  LEU LEU ASN ILE ASP TRP TYR ARG GLY LEU ILE GLN GLY          
SEQRES  42 A  883  LYS GLN MET VAL MET ILE GLY TYR SER ASP SER ALA LYS          
SEQRES  43 A  883  ASP ALA GLY VAL MET ALA ALA SER TRP ALA GLN TYR GLN          
SEQRES  44 A  883  ALA GLN ASP ALA LEU ILE LYS THR CYS GLU LYS ALA GLY          
SEQRES  45 A  883  ILE GLU LEU THR LEU PHE HIS GLY ARG GLY GLY SER ILE          
SEQRES  46 A  883  GLY ARG GLY GLY ALA PRO ALA HIS ALA ALA LEU LEU SER          
SEQRES  47 A  883  GLN PRO PRO GLY SER LEU LYS GLY GLY LEU ARG VAL THR          
SEQRES  48 A  883  GLU GLN GLY GLU MET ILE ARG PHE LYS TYR GLY LEU PRO          
SEQRES  49 A  883  GLU ILE THR VAL SER SER LEU SER LEU TYR THR GLY ALA          
SEQRES  50 A  883  ILE LEU GLU ALA ASN LEU LEU PRO PRO PRO GLU PRO LYS          
SEQRES  51 A  883  GLU SER TRP ARG ARG ILE MET ASP GLU LEU SER VAL ILE          
SEQRES  52 A  883  SER CYS ASP VAL TYR ARG GLY TYR VAL ARG GLU ASN LYS          
SEQRES  53 A  883  ASP PHE VAL PRO TYR PHE ARG SER ALA THR PRO GLU GLN          
SEQRES  54 A  883  GLU LEU GLY LYS LEU PRO LEU GLY SER ARG PRO ALA LYS          
SEQRES  55 A  883  ARG ARG PRO THR GLY GLY VAL GLU SER LEU ARG ALA ILE          
SEQRES  56 A  883  PRO TRP ILE PHE ALA TRP THR GLN ASN ARG LEU MET LEU          
SEQRES  57 A  883  PRO ALA TRP LEU GLY ALA GLY THR ALA LEU GLN LYS VAL          
SEQRES  58 A  883  VAL GLU ASP GLY LYS GLN SER GLU LEU GLU ALA MET CYS          
SEQRES  59 A  883  ARG ASP TRP PRO PHE PHE SER THR ARG LEU GLY MET LEU          
SEQRES  60 A  883  GLU MET VAL PHE ALA LYS ALA ASP LEU TRP LEU ALA GLU          
SEQRES  61 A  883  TYR TYR ASP GLN ARG LEU VAL ASP LYS ALA LEU TRP PRO          
SEQRES  62 A  883  LEU GLY LYS GLU LEU ARG ASN LEU GLN GLU GLU ASP ILE          
SEQRES  63 A  883  LYS VAL VAL LEU ALA ILE ALA ASN ASP SER HIS LEU MET          
SEQRES  64 A  883  ALA ASP LEU PRO TRP ILE ALA GLU SER ILE GLN LEU ARG          
SEQRES  65 A  883  ASN ILE TYR THR ASP PRO LEU ASN VAL LEU GLN ALA GLU          
SEQRES  66 A  883  LEU LEU HIS ARG SER ARG GLN ALA GLU LYS GLU GLY GLN          
SEQRES  67 A  883  GLU PRO ASP PRO ARG VAL GLU GLN ALA LEU MET VAL THR          
SEQRES  68 A  883  ILE ALA GLY ILE ALA ALA GLY MET ARG ASN THR GLY              
HET     MN  A 902       1                                                       
HET    ASP  A 884       9                                                       
HET    DCO  A 901      12                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     ASP ASPARTIC ACID                                                    
HETNAM     DCO 3,3-DICHLORO-2-PHOSPHONOMETHYL-ACRYLIC ACID                      
FORMUL   2   MN    MN 2+                                                        
FORMUL   3  ASP    C4 H7 N O4                                                   
FORMUL   4  DCO    C4 H5 CL2 O5 P                                               
FORMUL   5  HOH   *194(H2 O)                                                    
HELIX    1   1 TYR A    5  LEU A   27  1                                  23    
HELIX    2   2 GLU A   29  ALA A   47  1                                  19    
HELIX    3   3 ASN A   49  ASN A   62  1                                  14    
HELIX    4   4 SER A   64  SER A   92  1                                  29    
HELIX    5   5 PRO A  101  ASN A  113  1                                  13    
HELIX    6   6 SER A  118  SER A  128  1                                  11    
HELIX    7   7 LEU A  147  ASP A  162  1                                  16    
HELIX    8   8 ALA A  167  THR A  188  1                                  22    
HELIX    9   9 SER A  197  LEU A  232  1                                  36    
HELIX   10  10 THR A  260  LEU A  290  1                                  31    
HELIX   11  11 THR A  296  GLY A  304  1                                   9    
HELIX   12  12 GLU A  310  LYS A  335  1                                  26    
HELIX   13  13 GLN A  348  CYS A  366  1                                  19    
HELIX   14  14 MET A  368  ASN A  373  1                                   6    
HELIX   15  15 GLY A  374  PHE A  386  1                                  13    
HELIX   16  16 SER A  399  LEU A  413  1                                  15    
HELIX   17  17 ASP A  417  TRP A  421  5                                   5    
HELIX   18  18 SER A  422  SER A  436  1                                  15    
HELIX   19  19 SER A  448  ALA A  464  1                                  17    
HELIX   20  20 THR A  479  GLU A  492  1                                  14    
HELIX   21  21 THR A  507  ILE A  531  1                                  25    
HELIX   22  22 GLY A  540  GLY A  572  1                                  33    
HELIX   23  23 GLY A  583  ARG A  587  5                                   5    
HELIX   24  24 GLY A  588  SER A  598  1                                  11    
HELIX   25  25 GLN A  613  GLU A  615  5                                   3    
HELIX   26  26 MET A  616  GLY A  622  1                                   7    
HELIX   27  27 LEU A  623  LEU A  644  1                                  22    
HELIX   28  28 LYS A  650  ARG A  673  1                                  24    
HELIX   29  29 ASP A  677  THR A  686  1                                  10    
HELIX   30  30 PRO A  687  LEU A  694  1                                   8    
HELIX   31  31 GLY A  708  LEU A  712  5                                   5    
HELIX   32  32 ARG A  713  ASN A  724  1                                  12    
HELIX   33  33 MET A  727  TRP A  731  5                                   5    
HELIX   34  34 GLY A  733  GLU A  743  1                                  11    
HELIX   35  35 LYS A  746  ALA A  774  1                                  29    
HELIX   36  36 ASP A  775  VAL A  787  1                                  13    
HELIX   37  37 LEU A  791  ALA A  813  1                                  23    
HELIX   38  38 LEU A  822  GLY A  857  1                                  36    
HELIX   39  39 ASP A  861  ARG A  880  1                                  20    
SHEET    1   A 9 LEU A 131  LEU A 135  0                                        
SHEET    2   A 9 VAL A 243  SER A 247  1  O  THR A 246   N  LEU A 135           
SHEET    3   A 9 ARG A 392  GLU A 398  1  O  ARG A 392   N  SER A 247           
SHEET    4   A 9 ILE A 469  SER A 475  1  O  VAL A 473   N  ILE A 395           
SHEET    5   A 9 VAL A 501  PHE A 505  1  O  ALA A 502   N  ILE A 474           
SHEET    6   A 9 LYS A 534  ILE A 539  1  O  MET A 538   N  PHE A 505           
SHEET    7   A 9 GLU A 574  HIS A 579  1  O  PHE A 578   N  VAL A 537           
SHEET    8   A 9 LEU A 608  GLU A 612  1  O  ARG A 609   N  HIS A 579           
SHEET    9   A 9 LEU A 131  LEU A 135  1  N  VAL A 134   O  VAL A 610           
LINK         OE1 GLU A 506                MN    MN A 902     1555   1555  2.11  
LINK         OD1 ASP A 543                MN    MN A 902     1555   1555  2.16  
LINK         O2  DCO A 901                MN    MN A 902     1555   1555  1.93  
LINK         O3  DCO A 901                MN    MN A 902     1555   1555  2.10  
LINK        MN    MN A 902                 O   HOH A1095     1555   1555  2.31  
LINK        MN    MN A 902                 O   HOH A1096     1555   1555  2.06  
SITE     1 AC1  5 GLU A 506  ASP A 543  DCO A 901  HOH A1095                    
SITE     2 AC1  5 HOH A1096                                                     
SITE     1 AC2  7 ARG A 587  MET A 769  LYS A 773  ARG A 832                    
SITE     2 AC2  7 ASN A 881  HOH A 928  HOH A1090                               
SITE     1 AC3 11 ARG A 396  GLU A 506  MET A 538  GLY A 540                    
SITE     2 AC3 11 ASP A 543  GLY A 580  ARG A 581  ARG A 699                    
SITE     3 AC3 11 ARG A 713   MN A 902  HOH A1096                               
CRYST1  117.950  249.060   83.120  90.00  90.00  90.00 I 2 2 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      0.008478  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004015  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012031        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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