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Database: PDB
Entry: 1NT4
LinkDB: 1NT4
Original site: 1NT4 
HEADER    HYDROLASE                               28-JAN-03   1NT4              
TITLE     CRYSTAL STRUCTURE OF ESCHERICHIA COLI PERIPLASMIC GLUCOSE-1-          
TITLE    2 PHOSPHATASE H18A MUTANT COMPLEXED WITH GLUCOSE-1-PHOSPHATE           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUCOSE-1-PHOSPHATASE;                                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: G1PASE;                                                     
COMPND   5 EC: 3.1.3.10;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: AGP OR B1002;                                                  
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: SBS1572;                                   
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PBR322                                    
KEYWDS    ALPHA DOMAIN, ALPHA-BETA DOMAIN, OCCLUDED ACTIVE SITE,                
KEYWDS   2 ENZYME-SUBSTRATE COMPLEX, MONTREAL-KINGSTON BACTERIAL                
KEYWDS   3 STRUCTURAL GENOMICS INITIATIVE, BSGI, STRUCTURAL GENOMICS,           
KEYWDS   4 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.C.LEE,M.A.COTTRILL,C.W.FORSBERG,Z.JIA,MONTREAL-KINGSTON             
AUTHOR   2 BACTERIAL STRUCTURAL GENOMICS INITIATIVE (BSGI)                      
REVDAT   2   24-FEB-09 1NT4    1       VERSN                                    
REVDAT   1   13-JAN-04 1NT4    0                                                
JRNL        AUTH   D.C.LEE,M.A.COTTRILL,C.W.FORSBERG,Z.JIA                      
JRNL        TITL   FUNCTIONAL INSIGHTS REVEALED BY THE CRYSTAL                  
JRNL        TITL 2 STRUCTURES OF ESCHERICHIA COLI                               
JRNL        TITL 3 GLUCOSE-1-PHOSPHATASE.                                       
JRNL        REF    J.BIOL.CHEM.                  V. 278 31412 2003              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   12782623                                                     
JRNL        DOI    10.1074/JBC.M213154200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 91.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 26181                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.218                           
REMARK   3   FREE R VALUE                     : 0.284                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1388                            
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) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.49                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2180                       
REMARK   3   BIN FREE R VALUE                    : 0.2840                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 1388                         
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            : 6116                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 32                                      
REMARK   3   SOLVENT ATOMS            : 351                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.75                          
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) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.42                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
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 1NT4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-FEB-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB018176.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-FEB-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : F1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.2146, 1.2149, 1.3190             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27106                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.9                               
REMARK 200  DATA REDUNDANCY                : 3.450                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.27100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.07                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PEG 500 MME, PH        
REMARK 280  6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
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   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
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  1.000000  0.000000  0.000000       78.13150            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       45.10924            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       28.19167            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       78.13150            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       45.10924            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       28.19167            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       78.13150            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       45.10924            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       28.19167            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       90.21849            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       56.38333            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       90.21849            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       56.38333            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       90.21849            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       56.38333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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    ALA B  1018     O    ILE B  1316              2.12            
REMARK 500   O    LEU B  1020     O    LEU B  1049              2.13            
REMARK 500   O    ALA A    18     O    ILE A   316              2.15            
REMARK 500   ND1  HIS B  1289     O2P  G1P B  2001              2.15            
REMARK 500   O    TYR B  1088     O    HIS B  1115              2.18            
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    LEU A  49   CA  -  CB  -  CG  ANGL. DEV. =  14.8 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    ALA A  18      146.61     58.30                                   
REMARK 500    ASN A  19     -156.05    -95.45                                   
REMARK 500    PRO A  45     -168.59    -73.11                                   
REMARK 500    GLU A  78      -20.62   -178.26                                   
REMARK 500    CYS A  79      130.99     53.71                                   
REMARK 500    PRO A  82      -64.09    -16.72                                   
REMARK 500    SER A  91       27.69    -50.14                                   
REMARK 500    ASP A 111       60.70    126.87                                   
REMARK 500    ALA A 136      -45.82     69.36                                   
REMARK 500    PRO A 172       46.80    -77.95                                   
REMARK 500    ALA A 173      -32.65   -131.63                                   
REMARK 500    GLU A 176      -42.98    107.35                                   
REMARK 500    GLN A 178        7.90     48.65                                   
REMARK 500    ALA A 191       42.32   -167.67                                   
REMARK 500    SER A 233      130.40     81.54                                   
REMARK 500    ASP A 234     -148.88     27.56                                   
REMARK 500    GLN A 235       53.03   -100.70                                   
REMARK 500    LYS A 263      -48.00    -27.92                                   
REMARK 500    LYS A 271      -46.72    177.50                                   
REMARK 500    VAL A 274      -72.05   -126.39                                   
REMARK 500    ASP A 301       67.29     36.80                                   
REMARK 500    LYS A 329      -83.59    -38.38                                   
REMARK 500    ASN A 331       55.79    -62.54                                   
REMARK 500    SER A 343      177.94    -59.08                                   
REMARK 500    ALA A 350       68.18     60.36                                   
REMARK 500    THR B1002     -133.74   -136.12                                   
REMARK 500    TYR B1007       67.92     76.97                                   
REMARK 500    GLN B1008       98.35     62.98                                   
REMARK 500    THR B1050      147.50     78.53                                   
REMARK 500    GLU B1078        2.78   -167.01                                   
REMARK 500    CYS B1079      116.87     73.84                                   
REMARK 500    PRO B1081      151.74    -41.19                                   
REMARK 500    PRO B1082      -56.39    -20.78                                   
REMARK 500    TYR B1088      -97.61    -99.44                                   
REMARK 500    ALA B1089      133.45     86.43                                   
REMARK 500    SER B1091       45.68    -72.87                                   
REMARK 500    ASP B1111       63.27     77.08                                   
REMARK 500    ASP B1134       39.50    -78.92                                   
REMARK 500    ALA B1136      -64.88     67.91                                   
REMARK 500    THR B1156      -15.91    -39.06                                   
REMARK 500    ASP B1170       -8.08     77.13                                   
REMARK 500    LYS B1175       47.31    -93.01                                   
REMARK 500    GLU B1176      -22.74   -170.12                                   
REMARK 500    LYS B1177       14.38   -143.22                                   
REMARK 500    GLN B1178       55.91     32.91                                   
REMARK 500    LYS B1186     -105.76    -57.83                                   
REMARK 500    ASN B1187      115.32    117.48                                   
REMARK 500    ALA B1191       42.93   -154.44                                   
REMARK 500    PRO B1197       12.15    -60.70                                   
REMARK 500    ILE B1231      -80.63    -57.97                                   
REMARK 500    LYS B1232      -74.95     16.80                                   
REMARK 500    SER B1233      107.89    -23.77                                   
REMARK 500    ASP B1234     -154.99     46.99                                   
REMARK 500    GLN B1235       73.17   -104.53                                   
REMARK 500    VAL B1274      -59.80   -141.75                                   
REMARK 500    GLN B1306      118.65   -161.90                                   
REMARK 500    HIS B1326      101.31   -162.13                                   
REMARK 500    LYS B1329      -74.25    -49.25                                   
REMARK 500    SER B1343     -173.51    -61.77                                   
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 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A3246        DISTANCE =  5.44 ANGSTROMS                       
REMARK 525    HOH A3295        DISTANCE =  6.97 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G1P A 2000                
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G1P B 2001                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: AGP_ECOLI   RELATED DB: TARGETDB                         
DBREF  1NT4 A    1   391  UNP    P19926   AGP_ECOLI       23    413             
DBREF  1NT4 B 1001  1391  UNP    P19926   AGP_ECOLI       23    413             
SEQADV 1NT4 ALA A   18  UNP  P19926    HIS    40 ENGINEERED                     
SEQADV 1NT4 ALA B 1018  UNP  P19926    HIS    40 ENGINEERED                     
SEQRES   1 A  391  GLN THR VAL PRO GLU GLY TYR GLN LEU GLN GLN VAL LEU          
SEQRES   2 A  391  MET MET SER ARG ALA ASN LEU ARG ALA PRO LEU ALA ASN          
SEQRES   3 A  391  ASN GLY SER VAL LEU GLU GLN SER THR PRO ASN LYS TRP          
SEQRES   4 A  391  PRO GLU TRP ASP VAL PRO GLY GLY GLN LEU THR THR LYS          
SEQRES   5 A  391  GLY GLY VAL LEU GLU VAL TYR MET GLY HIS TYR MET ARG          
SEQRES   6 A  391  GLU TRP LEU ALA GLU GLN GLY MET VAL LYS SER GLY GLU          
SEQRES   7 A  391  CYS PRO PRO PRO TYR THR VAL TYR ALA TYR ALA ASN SER          
SEQRES   8 A  391  LEU GLN ARG THR VAL ALA THR ALA GLN PHE PHE ILE THR          
SEQRES   9 A  391  GLY ALA PHE PRO GLY CYS ASP ILE PRO VAL HIS HIS GLN          
SEQRES  10 A  391  GLU LYS MET GLY THR MET ASP PRO THR PHE ASN PRO VAL          
SEQRES  11 A  391  ILE THR ASP ASP SER ALA ALA PHE SER GLU GLN ALA VAL          
SEQRES  12 A  391  ALA ALA MET GLU LYS GLU LEU SER LYS LEU GLN LEU THR          
SEQRES  13 A  391  ASP SER TYR GLN LEU LEU GLU LYS ILE VAL ASN TYR LYS          
SEQRES  14 A  391  ASP SER PRO ALA CYS LYS GLU LYS GLN GLN CYS SER LEU          
SEQRES  15 A  391  VAL ASP GLY LYS ASN THR PHE SER ALA LYS TYR GLN GLN          
SEQRES  16 A  391  GLU PRO GLY VAL SER GLY PRO LEU LYS VAL GLY ASN SER          
SEQRES  17 A  391  LEU VAL ASP ALA PHE THR LEU GLN TYR TYR GLU GLY PHE          
SEQRES  18 A  391  PRO MET ASP GLN VAL ALA TRP GLY GLU ILE LYS SER ASP          
SEQRES  19 A  391  GLN GLN TRP LYS VAL LEU SER LYS LEU LYS ASN GLY TYR          
SEQRES  20 A  391  GLN ASP SER LEU PHE THR SER PRO GLU VAL ALA ARG ASN          
SEQRES  21 A  391  VAL ALA LYS PRO LEU VAL SER TYR ILE ASP LYS ALA LEU          
SEQRES  22 A  391  VAL THR ASP ARG THR SER ALA PRO LYS ILE THR VAL LEU          
SEQRES  23 A  391  VAL GLY HIS ASP SER ASN ILE ALA SER LEU LEU THR ALA          
SEQRES  24 A  391  LEU ASP PHE LYS PRO TYR GLN LEU HIS ASP GLN ASN GLU          
SEQRES  25 A  391  ARG THR PRO ILE GLY GLY LYS ILE VAL PHE GLN ARG TRP          
SEQRES  26 A  391  HIS ASP SER LYS ALA ASN ARG ASP LEU MET LYS ILE GLU          
SEQRES  27 A  391  TYR VAL TYR GLN SER ALA GLU GLN LEU ARG ASN ALA ASP          
SEQRES  28 A  391  ALA LEU THR LEU GLN ALA PRO ALA GLN ARG VAL THR LEU          
SEQRES  29 A  391  GLU LEU SER GLY CYS PRO ILE ASP ALA ASP GLY PHE CYS          
SEQRES  30 A  391  PRO MET ASP LYS PHE ASP SER VAL LEU ASN GLU ALA VAL          
SEQRES  31 A  391  LYS                                                          
SEQRES   1 B  391  GLN THR VAL PRO GLU GLY TYR GLN LEU GLN GLN VAL LEU          
SEQRES   2 B  391  MET MET SER ARG ALA ASN LEU ARG ALA PRO LEU ALA ASN          
SEQRES   3 B  391  ASN GLY SER VAL LEU GLU GLN SER THR PRO ASN LYS TRP          
SEQRES   4 B  391  PRO GLU TRP ASP VAL PRO GLY GLY GLN LEU THR THR LYS          
SEQRES   5 B  391  GLY GLY VAL LEU GLU VAL TYR MET GLY HIS TYR MET ARG          
SEQRES   6 B  391  GLU TRP LEU ALA GLU GLN GLY MET VAL LYS SER GLY GLU          
SEQRES   7 B  391  CYS PRO PRO PRO TYR THR VAL TYR ALA TYR ALA ASN SER          
SEQRES   8 B  391  LEU GLN ARG THR VAL ALA THR ALA GLN PHE PHE ILE THR          
SEQRES   9 B  391  GLY ALA PHE PRO GLY CYS ASP ILE PRO VAL HIS HIS GLN          
SEQRES  10 B  391  GLU LYS MET GLY THR MET ASP PRO THR PHE ASN PRO VAL          
SEQRES  11 B  391  ILE THR ASP ASP SER ALA ALA PHE SER GLU GLN ALA VAL          
SEQRES  12 B  391  ALA ALA MET GLU LYS GLU LEU SER LYS LEU GLN LEU THR          
SEQRES  13 B  391  ASP SER TYR GLN LEU LEU GLU LYS ILE VAL ASN TYR LYS          
SEQRES  14 B  391  ASP SER PRO ALA CYS LYS GLU LYS GLN GLN CYS SER LEU          
SEQRES  15 B  391  VAL ASP GLY LYS ASN THR PHE SER ALA LYS TYR GLN GLN          
SEQRES  16 B  391  GLU PRO GLY VAL SER GLY PRO LEU LYS VAL GLY ASN SER          
SEQRES  17 B  391  LEU VAL ASP ALA PHE THR LEU GLN TYR TYR GLU GLY PHE          
SEQRES  18 B  391  PRO MET ASP GLN VAL ALA TRP GLY GLU ILE LYS SER ASP          
SEQRES  19 B  391  GLN GLN TRP LYS VAL LEU SER LYS LEU LYS ASN GLY TYR          
SEQRES  20 B  391  GLN ASP SER LEU PHE THR SER PRO GLU VAL ALA ARG ASN          
SEQRES  21 B  391  VAL ALA LYS PRO LEU VAL SER TYR ILE ASP LYS ALA LEU          
SEQRES  22 B  391  VAL THR ASP ARG THR SER ALA PRO LYS ILE THR VAL LEU          
SEQRES  23 B  391  VAL GLY HIS ASP SER ASN ILE ALA SER LEU LEU THR ALA          
SEQRES  24 B  391  LEU ASP PHE LYS PRO TYR GLN LEU HIS ASP GLN ASN GLU          
SEQRES  25 B  391  ARG THR PRO ILE GLY GLY LYS ILE VAL PHE GLN ARG TRP          
SEQRES  26 B  391  HIS ASP SER LYS ALA ASN ARG ASP LEU MET LYS ILE GLU          
SEQRES  27 B  391  TYR VAL TYR GLN SER ALA GLU GLN LEU ARG ASN ALA ASP          
SEQRES  28 B  391  ALA LEU THR LEU GLN ALA PRO ALA GLN ARG VAL THR LEU          
SEQRES  29 B  391  GLU LEU SER GLY CYS PRO ILE ASP ALA ASP GLY PHE CYS          
SEQRES  30 B  391  PRO MET ASP LYS PHE ASP SER VAL LEU ASN GLU ALA VAL          
SEQRES  31 B  391  LYS                                                          
HET    G1P  A2000      16                                                       
HET    G1P  B2001      16                                                       
HETNAM     G1P ALPHA-D-GLUCOSE-1-PHOSPHATE                                      
FORMUL   3  G1P    2(C6 H13 O9 P)                                               
FORMUL   5  HOH   *351(H2 O)                                                    
HELIX    1   1 LEU A   24  ASN A   26  5                                   3    
HELIX    2   2 ASN A   27  SER A   34  1                                   8    
HELIX    3   3 THR A   50  GLN A   71  1                                  22    
HELIX    4   4 LEU A   92  PHE A  107  1                                  16    
HELIX    5   5 ALA A  136  LEU A  153  1                                  18    
HELIX    6   6 LEU A  155  ASN A  167  1                                  13    
HELIX    7   7 TYR A  168  SER A  171  5                                   4    
HELIX    8   8 GLY A  201  GLU A  219  1                                  19    
HELIX    9   9 GLN A  225  GLU A  230  5                                   6    
HELIX   10  10 GLN A  235  THR A  253  1                                  19    
HELIX   11  11 SER A  254  ALA A  262  1                                   9    
HELIX   12  12 ALA A  262  LEU A  273  1                                  12    
HELIX   13  13 HIS A  289  LEU A  300  1                                  12    
HELIX   14  14 SER A  343  ALA A  350  1                                   8    
HELIX   15  15 MET A  379  VAL A  390  1                                  12    
HELIX   16  16 LEU B 1024  ASN B 1026  5                                   3    
HELIX   17  17 ASN B 1027  SER B 1034  1                                   8    
HELIX   18  18 THR B 1050  GLN B 1071  1                                  22    
HELIX   19  19 LEU B 1092  PHE B 1107  1                                  16    
HELIX   20  20 ALA B 1136  SER B 1151  1                                  16    
HELIX   21  21 ASP B 1157  ASN B 1167  1                                  11    
HELIX   22  22 GLY B 1201  GLY B 1220  1                                  20    
HELIX   23  23 PRO B 1222  GLU B 1230  5                                   9    
HELIX   24  24 GLN B 1236  THR B 1253  1                                  18    
HELIX   25  25 SER B 1254  ALA B 1262  1                                   9    
HELIX   26  26 ALA B 1262  VAL B 1274  1                                  13    
HELIX   27  27 HIS B 1289  LEU B 1300  1                                  12    
HELIX   28  28 SER B 1343  ASN B 1349  1                                   7    
HELIX   29  29 MET B 1379  VAL B 1390  1                                  12    
SHEET    1   A 7 VAL A 114  HIS A 115  0                                        
SHEET    2   A 7 VAL A  85  ALA A  89  1  N  ALA A  87   O  HIS A 115           
SHEET    3   A 7 ILE A 283  VAL A 287  1  O  VAL A 285   N  TYR A  88           
SHEET    4   A 7 TYR A   7  SER A  16  1  N  SER A  16   O  LEU A 286           
SHEET    5   A 7 LYS A 319  ASP A 327 -1  O  PHE A 322   N  LEU A  13           
SHEET    6   A 7 ARG A 332  TYR A 341 -1  O  LEU A 334   N  TRP A 325           
SHEET    7   A 7 GLN A 360  THR A 363 -1  O  VAL A 362   N  TYR A 339           
SHEET    1   B 7 VAL A 114  HIS A 115  0                                        
SHEET    2   B 7 VAL A  85  ALA A  89  1  N  ALA A  87   O  HIS A 115           
SHEET    3   B 7 ILE A 283  VAL A 287  1  O  VAL A 285   N  TYR A  88           
SHEET    4   B 7 TYR A   7  SER A  16  1  N  SER A  16   O  LEU A 286           
SHEET    5   B 7 LYS A 319  ASP A 327 -1  O  PHE A 322   N  LEU A  13           
SHEET    6   B 7 ARG A 332  TYR A 341 -1  O  LEU A 334   N  TRP A 325           
SHEET    7   B 7 CYS A 377  PRO A 378 -1  O  CYS A 377   N  MET A 335           
SHEET    1   C 2 THR A 188  SER A 190  0                                        
SHEET    2   C 2 GLY A 198  SER A 200 -1  O  SER A 200   N  THR A 188           
SHEET    1   D 6 VAL B1085  ALA B1087  0                                        
SHEET    2   D 6 ILE B1283  GLY B1288  1  O  ILE B1283   N  TYR B1086           
SHEET    3   D 6 LEU B1009  ARG B1017  1  N  SER B1016   O  LEU B1286           
SHEET    4   D 6 LYS B1319  ASP B1327 -1  O  ARG B1324   N  GLN B1011           
SHEET    5   D 6 ARG B1332  TYR B1341 -1  O  LEU B1334   N  TRP B1325           
SHEET    6   D 6 GLN B1360  THR B1363 -1  O  VAL B1362   N  TYR B1339           
SHEET    1   E 6 VAL B1085  ALA B1087  0                                        
SHEET    2   E 6 ILE B1283  GLY B1288  1  O  ILE B1283   N  TYR B1086           
SHEET    3   E 6 LEU B1009  ARG B1017  1  N  SER B1016   O  LEU B1286           
SHEET    4   E 6 LYS B1319  ASP B1327 -1  O  ARG B1324   N  GLN B1011           
SHEET    5   E 6 ARG B1332  TYR B1341 -1  O  LEU B1334   N  TRP B1325           
SHEET    6   E 6 CYS B1377  PRO B1378 -1  O  CYS B1377   N  MET B1335           
SHEET    1   F 2 THR B1188  PHE B1189  0                                        
SHEET    2   F 2 VAL B1199  SER B1200 -1  O  SER B1200   N  THR B1188           
SSBOND   1 CYS A   79    CYS A  110                          1555   1555  2.02  
SSBOND   2 CYS A  174    CYS A  180                          1555   1555  2.04  
SSBOND   3 CYS A  369    CYS A  377                          1555   1555  2.03  
SSBOND   4 CYS B 1079    CYS B 1110                          1555   1555  2.05  
SSBOND   5 CYS B 1174    CYS B 1180                          1555   1555  2.03  
SSBOND   6 CYS B 1369    CYS B 1377                          1555   1555  2.03  
SITE     1 AC1  9 ARG A  17  ARG A  21  ARG A  94  GLU A 196                    
SITE     2 AC1  9 HIS A 289  ASP A 290  SER A 291  HOH A3102                    
SITE     3 AC1  9 HOH A3181                                                     
SITE     1 AC2  9 ARG B1017  ARG B1021  ARG B1094  GLU B1196                    
SITE     2 AC2  9 HIS B1289  ASP B1290  SER B1291  HOH B3210                    
SITE     3 AC2  9 HOH B3211                                                     
CRYST1  156.263  156.263   84.575  90.00  90.00 120.00 H 3          18          
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      0.006399  0.003695  0.000000        0.00000                         
SCALE2      0.000000  0.007389  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011824        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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