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Database: PDB
Entry: 1E58
LinkDB: 1E58
Original site: 1E58 
HEADER    ISOMERASE                               19-JUL-00   1E58              
TITLE     E.COLI COFACTOR-DEPENDENT PHOSPHOGLYCERATE MUTASE                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHOGLYCERATE MUTASE;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 5.4.2.1;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12;                                                         
SOURCE   5 GENE: PGM1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET3A                                     
KEYWDS    PHOSPHOHISTIDINE, GLYCOLYSIS AND GLUCONEOGENESIS,                     
KEYWDS   2 PHOSPHOGLYCERATE MUTASE, ISOMERASE                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.S.BOND,W.N.HUNTER                                                   
REVDAT   2   24-FEB-09 1E58    1       VERSN                                    
REVDAT   1   20-MAR-01 1E58    0                                                
JRNL        AUTH   C.S.BOND,M.F.WHITE,W.N.HUNTER                                
JRNL        TITL   HIGH RESOLUTION STRUCTURE OF THE                             
JRNL        TITL 2 PHOSPHOHISTIDINE-ACTIVATED FORM OF ESCHERICHIA               
JRNL        TITL 3 COLI COFACTOR-DEPENDENT PHOSPHOGLYCERATE MUTASE.             
JRNL        REF    J.BIOL.CHEM.                  V. 276  3247 2001              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   11038361                                                     
JRNL        DOI    10.1074/JBC.M007318200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   COMPLETENESS FOR RANGE        (%) : 83.0                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R                         
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.1209                 
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.121                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.168                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 3.0                    
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 65026                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.1195                 
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 62531                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 2065                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 15                                            
REMARK   3   SOLVENT ATOMS      : 425                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 2434.16                 
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 1977.00                 
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 17                      
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 22606                   
REMARK   3   NUMBER OF RESTRAINTS                     : 27457                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.014                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.030                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.0314                  
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.079                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.085                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.076                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.005                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.042                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.080                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-2          
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: ANISOTROPIC SCALING APPLIED BY THE        
REMARK   3  METHOD OF PARKIN, MOEZZI & HOPE, J.APPL.CRYST.28 (1995)53-56        
REMARK   3  PHOSPHOHISTIDINE MODELLED AT 0.28 OCCUPANCY COUPLED TO A 0.72       
REMARK   3  OCCUPANCY HISTIDINE WITH THREE WATER MOLECULES                      
REMARK   4                                                                      
REMARK   4 1E58 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-JUL-00.                  
REMARK 100 THE PDBE ID CODE IS EBI-5176.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-SEP-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 105                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX9.6                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.89                               
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 : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 67122                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.25                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.0                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NONE                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 85.4                               
REMARK 200  DATA REDUNDANCY                : 2                                  
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.047                              
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 211                                
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 63                                 
REMARK 200  DATA REDUNDANCY IN SHELL       : 2                                  
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.071                              
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 11                                 
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: SHELX                                                 
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 51                                         
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL (PH 8.0),                
REMARK 280  200 MM LI2SO4, 20% PEG 4000                                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       30.78500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.50000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.78500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.50000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE:  1                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 1700 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27000 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.7 KCAL/MOL                         
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       61.57000            
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400  CATALYTIC ACTIVITY: 2-PHOSPHOGLYCERATE + 2,3-DIPHOSPHOGLYCERATE =   
REMARK 400  3-PHOSPHOGLYCERATE + 2,3-DIPHOSPHOGLYCERATE.                        
REMARK 400  PATHWAY: GLYCOLYSIS.                                                
REMARK 400  SIMILARITY: BELONGS TO THE PHOSPHOGLYCERATE MUTASE FAMILY.          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A   248                                                      
REMARK 465     LYS A   249                                                      
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   O    HOH A  2262  -  O    HOH A  2272              2.04            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500                                                                      
REMARK 500   O    HOH A  2262     O    HOH A  2407     4456      2.09           
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  20   CD  -  NE  -  CZ  ANGL. DEV. =   9.7 DEGREES          
REMARK 500    ARG A  20   NE  -  CZ  -  NH2 ANGL. DEV. =   5.1 DEGREES          
REMARK 500    ARG A  89   CD  -  NE  -  CZ  ANGL. DEV. =  10.1 DEGREES          
REMARK 500    ARG A  89   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    ARG A 115   NE  -  CZ  -  NH1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG A 115   NH1 -  CZ  -  NH2 ANGL. DEV. =  -7.6 DEGREES          
REMARK 500    ARG A 116   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG A 171   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500 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    GLU A  88      152.30    -49.99                                   
REMARK 500    THR A 167      -57.26   -126.18                                   
REMARK 500    ALA A 182     -138.81   -149.79                                   
REMARK 500    ASP A 218     -167.60    -79.77                                   
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 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A3001                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1E59   RELATED DB: PDB                                   
REMARK 900  E.COLI COFACTOR-DEPENDENT PHOSPHOGLYCERATE MUTASE                   
REMARK 900  COMPLEXED WITH VANADATE                                             
DBREF  1E58 A    1   249  UNP    P62707   GPMA_ECOLI       1    249             
SEQRES   1 A  249  ALA VAL THR LYS LEU VAL LEU VAL ARG NEP GLY GLU SER          
SEQRES   2 A  249  GLN TRP ASN LYS GLU ASN ARG PHE THR GLY TRP TYR ASP          
SEQRES   3 A  249  VAL ASP LEU SER GLU LYS GLY VAL SER GLU ALA LYS ALA          
SEQRES   4 A  249  ALA GLY LYS LEU LEU LYS GLU GLU GLY TYR SER PHE ASP          
SEQRES   5 A  249  PHE ALA TYR THR SER VAL LEU LYS ARG ALA ILE HIS THR          
SEQRES   6 A  249  LEU TRP ASN VAL LEU ASP GLU LEU ASP GLN ALA TRP LEU          
SEQRES   7 A  249  PRO VAL GLU LYS SER TRP LYS LEU ASN GLU ARG HIS TYR          
SEQRES   8 A  249  GLY ALA LEU GLN GLY LEU ASN LYS ALA GLU THR ALA GLU          
SEQRES   9 A  249  LYS TYR GLY ASP GLU GLN VAL LYS GLN TRP ARG ARG GLY          
SEQRES  10 A  249  PHE ALA VAL THR PRO PRO GLU LEU THR LYS ASP ASP GLU          
SEQRES  11 A  249  ARG TYR PRO GLY HIS ASP PRO ARG TYR ALA LYS LEU SER          
SEQRES  12 A  249  GLU LYS GLU LEU PRO LEU THR GLU SER LEU ALA LEU THR          
SEQRES  13 A  249  ILE ASP ARG VAL ILE PRO TYR TRP ASN GLU THR ILE LEU          
SEQRES  14 A  249  PRO ARG MET LYS SER GLY GLU ARG VAL ILE ILE ALA ALA          
SEQRES  15 A  249  HIS GLY ASN SER LEU ARG ALA LEU VAL LYS TYR LEU ASP          
SEQRES  16 A  249  ASN MET SER GLU GLU GLU ILE LEU GLU LEU ASN ILE PRO          
SEQRES  17 A  249  THR GLY VAL PRO LEU VAL TYR GLU PHE ASP GLU ASN PHE          
SEQRES  18 A  249  LYS PRO LEU LYS ARG TYR TYR LEU GLY ASN ALA ASP GLU          
SEQRES  19 A  249  ILE ALA ALA LYS ALA ALA ALA VAL ALA ASN GLN GLY LYS          
SEQRES  20 A  249  ALA LYS                                                      
MODRES 1E58 NEP A   10  HIS  N1-PHOSPHONOHISTIDINE                              
HET    NEP  A  10      19                                                       
HET    SO4  A1001       5                                                       
HET    SO4  A1002       5                                                       
HET     CL  A3001       1                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM     NEP N1-PHOSPHONOHISTIDINE                                            
FORMUL   2  SO4    2(O4 S 2-)                                                   
FORMUL   3   CL    CL 1-                                                        
FORMUL   4  NEP    C6 H10 N3 O5 P                                               
FORMUL   5  HOH   *425(H2 O1)                                                   
HELIX    1   1 SER A   13  GLU A   18  1                                   6    
HELIX    2   2 SER A   30  GLU A   47  1                                  18    
HELIX    3   3 LEU A   59  ASP A   74  1                                  16    
HELIX    4   4 TRP A   84  ASN A   87  5                                   4    
HELIX    5   5 TYR A   91  GLN A   95  5                                   5    
HELIX    6   6 ASN A   98  GLY A  107  1                                  10    
HELIX    7   7 GLY A  107  GLY A  117  1                                  11    
HELIX    8   8 TYR A  132  ASP A  136  5                                   5    
HELIX    9   9 ASP A  136  ALA A  140  5                                   5    
HELIX   10  10 SER A  152  THR A  167  1                                  16    
HELIX   11  11 THR A  167  SER A  174  1                                   8    
HELIX   12  12 HIS A  183  ASP A  195  1                                  13    
HELIX   13  13 SER A  198  LEU A  205  1                                   8    
HELIX   14  14 ASN A  231  ALA A  239  1                                   9    
SHEET    1   A 6 VAL A  80  LYS A  82  0                                        
SHEET    2   A 6 PHE A  53  THR A  56  1  N  ALA A  54   O  GLU A  81           
SHEET    3   A 6 VAL A 178  ALA A 182  1  N  ILE A 179   O  PHE A  53           
SHEET    4   A 6 THR A   3  ARG A   9  1  N  VAL A   6   O  VAL A 178           
SHEET    5   A 6 LEU A 213  PHE A 217 -1  N  PHE A 217   O  THR A   3           
SHEET    6   A 6 PRO A 223  TYR A 228 -1  N  TYR A 227   O  VAL A 214           
LINK         C   ARG A   9                 N   NEP A  10     1555   1555  1.35  
LINK         C   NEP A  10                 N   GLY A  11     1555   1555  1.33  
SITE     1 AC1 15 NEP A  10  ARG A  20  PHE A  21  THR A  22                    
SITE     2 AC1 15 GLY A  23  ARG A  61  GLU A  88  TYR A  91                    
SITE     3 AC1 15 HOH A2033  HOH A2211  HOH A2339  HOH A2417                    
SITE     4 AC1 15 HOH A2418  HOH A2421  HOH A2424                               
SITE     1 AC2  9 TYR A  91  ARG A 115  ARG A 116  HOH A2367                    
SITE     2 AC2  9 HOH A2418  HOH A2419  HOH A2420  HOH A2421                    
SITE     3 AC2  9 HOH A2422                                                     
SITE     1 AC3  2 TRP A  67  LYS A  82                                          
CRYST1   61.570  113.000   40.260  90.00  90.00  90.00 P 21 21 2     4          
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      0.016242  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008850  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.024839        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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