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Database: PDB
Entry: 2ZJ4
LinkDB: 2ZJ4
Original site: 2ZJ4 
HEADER    TRANSFERASE                             29-FEB-08   2ZJ4              
TITLE     ISOMERASE DOMAIN OF HUMAN GLUCOSE:FRUCTOSE-6-PHOSPHATE                
TITLE    2 AMIDOTRANSFERASE                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE                          
COMPND   3 AMINOTRANSFERASE [ISOMERIZING] 1;                                    
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: SIS(SUGAR ISOMERASE) DOMAINS, UNP RESIDUES 332-            
COMPND   6 699;                                                                 
COMPND   7 SYNONYM: GLUTAMINE:FRUCTOSE 6 PHOSPHATE AMIDOTRANSFERASE 1,          
COMPND   8 HEXOSEPHOSPHATE AMINOTRANSFERASE 1, D-FRUCTOSE-6-PHOSPHATE           
COMPND   9 AMIDOTRANSFERASE 1, GFAT 1, GFAT1;                                   
COMPND  10 EC: 2.6.1.16;                                                        
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)CODON+RIL;                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET23                                     
KEYWDS    GLUCOSAMINE-6-PHOSPHATE SYNTHASE, ALDOSE/KETOSE ISOMERASE,            
KEYWDS   2 CRYSTAL STRUCTURE, ROSSMANN-LIKE FOLD, TRANSFERASE,                  
KEYWDS   3 ALTERNATIVE SPLICING, AMINOTRANSFERASE, GLUTAMINE                    
KEYWDS   4 AMIDOTRANSFERASE, PHOSPHOPROTEIN                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.NAKAISHI,M.BANDO,K.KONDO,H.TSUGE                                    
REVDAT   1   13-JAN-09 2ZJ4    0                                                
JRNL        AUTH   Y.NAKAISHI,M.BANDO,H.SHIMIZU,K.WATANABE,F.GOTO,              
JRNL        AUTH 2 H.TSUGE,K.KONDO,M.KOMATSU                                    
JRNL        TITL   STRUCTURAL ANALYSIS OF HUMAN                                 
JRNL        TITL 2 GLUTAMINE:FRUCTOSE-6-PHOSPHATE AMIDOTRANSFERASE, A           
JRNL        TITL 3 KEY REGULATOR IN TYPE 2 DIABETES                             
JRNL        REF    FEBS LETT.                    V. 583   163 2009              
JRNL        REFN                   ISSN 0014-5793                               
JRNL        PMID   19059404                                                     
JRNL        DOI    10.1016/J.FEBSLET.2008.11.041                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 21357                          
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 + TEST SET) : 0.160                           
REMARK   3   R VALUE            (WORKING SET) : 0.158                           
REMARK   3   FREE R VALUE                     : 0.208                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1144                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1560                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.46                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1460                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 87                           
REMARK   3   BIN FREE R VALUE                    : 0.2170                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2863                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 16                                      
REMARK   3   SOLVENT ATOMS            : 267                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.57                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : 0.01000                                              
REMARK   3    B33 (A**2) : -0.02000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.212         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.180         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.105         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.982         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.915                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2920 ; 0.021 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2003 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3937 ; 1.778 ; 1.983       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4906 ; 1.454 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   364 ; 6.404 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   124 ;32.790 ;23.871       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   555 ;15.697 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;20.724 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   464 ; 0.121 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3173 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   562 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   584 ; 0.230 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1997 ; 0.196 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1380 ; 0.171 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1404 ; 0.088 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   178 ; 0.185 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    15 ; 0.187 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    61 ; 0.289 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    32 ; 0.240 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2368 ; 1.437 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   742 ; 0.238 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2940 ; 1.612 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1246 ; 3.106 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   997 ; 4.334 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 2ZJ4 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-MAR-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB028036.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-AUG-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL32B2                             
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                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS V                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22501                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.530                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2ZJ3                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.79                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% ISOPORPANOL, 0.04M TRIS, 0.08M       
REMARK 280  AMMONIUM ACETATE, 12% GLYCEROL 10-FOLD EXCESS OF 2-DEOXY-2-         
REMARK 280  AMINOGLUCITOL-6-PHOSPHATE, PH 8.50, VAPOR DIFFUSION, HANGING        
REMARK 280  DROP, TEMPERATURE 277K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       3555   -Y,X+1/2,Z+1/4                                          
REMARK 290       4555   Y+1/2,-X,Z+3/4                                          
REMARK 290       5555   -X+1/2,Y,-Z+3/4                                         
REMARK 290       6555   X,-Y+1/2,-Z+1/4                                         
REMARK 290       7555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X,-Y,Z                                                 
REMARK 290      11555   -Y+1/2,X,Z+3/4                                          
REMARK 290      12555   Y,-X+1/2,Z+1/4                                          
REMARK 290      13555   -X,Y+1/2,-Z+1/4                                         
REMARK 290      14555   X+1/2,-Y,-Z+3/4                                         
REMARK 290      15555   Y,X,-Z                                                  
REMARK 290      16555   -Y+1/2,-X+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       39.46350            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       39.46350            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      138.66150            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       39.46350            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       69.33075            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       39.46350            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      207.99225            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       39.46350            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      207.99225            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       39.46350            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       69.33075            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000       39.46350            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       39.46350            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      138.66150            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       39.46350            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       39.46350            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      138.66150            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       39.46350            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000      207.99225            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       39.46350            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       69.33075            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       39.46350            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       69.33075            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       39.46350            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      207.99225            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       39.46350            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       39.46350            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      138.66150            
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 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: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26330 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 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  0.000000 -1.000000  0.000000       78.92700            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000       78.92700            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 883  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 887  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 929  LIES ON A SPECIAL POSITION.                          
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   306                                                      
REMARK 465     HIS A   307                                                      
REMARK 465     HIS A   308                                                      
REMARK 465     HIS A   309                                                      
REMARK 465     HIS A   310                                                      
REMARK 465     HIS A   311                                                      
REMARK 465     HIS A   312                                                      
REMARK 465     GLN A   313                                                      
REMARK 465     GLN A   314                                                      
REMARK 465     ILE A   315                                                      
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   722     O    HOH A   844              2.08            
REMARK 500   O    HOH A   877     O    HOH A   922              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    MET A 396   CG    MET A 396   SD      0.165                       
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 502   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    ARG A 502   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    ARG A 594   NE  -  CZ  -  NH2 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 663   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.0 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    ASN A 319      -25.38    108.30                                   
REMARK 500    ARG A 342      -50.53   -129.43                                   
REMARK 500    SER A 420      117.54   -161.55                                   
REMARK 500    THR A 474      -82.58   -132.69                                   
REMARK 500    ASP A 595     -164.96   -127.48                                   
REMARK 500    GLN A 612        4.82     80.74                                   
REMARK 500    VAL A 679      -78.63   -112.08                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    HIS A 547         0.06    SIDE_CHAIN                              
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 A 845        DISTANCE =  5.15 ANGSTROMS                       
REMARK 525    HOH A 910        DISTANCE =  5.41 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AGP A 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2ZJ3   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH ALPHA-D-GLUCOSE-6-PHOSPHATE          
DBREF  2ZJ4 A  313   680  UNP    Q06210   GFPT1_HUMAN    332    699             
SEQADV 2ZJ4 MET A  306  UNP  Q06210              EXPRESSION TAG                 
SEQADV 2ZJ4 HIS A  307  UNP  Q06210              EXPRESSION TAG                 
SEQADV 2ZJ4 HIS A  308  UNP  Q06210              EXPRESSION TAG                 
SEQADV 2ZJ4 HIS A  309  UNP  Q06210              EXPRESSION TAG                 
SEQADV 2ZJ4 HIS A  310  UNP  Q06210              EXPRESSION TAG                 
SEQADV 2ZJ4 HIS A  311  UNP  Q06210              EXPRESSION TAG                 
SEQADV 2ZJ4 HIS A  312  UNP  Q06210              EXPRESSION TAG                 
SEQRES   1 A  375  MET HIS HIS HIS HIS HIS HIS GLN GLN ILE MET LYS GLY          
SEQRES   2 A  375  ASN PHE SER SER PHE MET GLN LYS GLU ILE PHE GLU GLN          
SEQRES   3 A  375  PRO GLU SER VAL VAL ASN THR MET ARG GLY ARG VAL ASN          
SEQRES   4 A  375  PHE ASP ASP TYR THR VAL ASN LEU GLY GLY LEU LYS ASP          
SEQRES   5 A  375  HIS ILE LYS GLU ILE GLN ARG CYS ARG ARG LEU ILE LEU          
SEQRES   6 A  375  ILE ALA CYS GLY THR SER TYR HIS ALA GLY VAL ALA THR          
SEQRES   7 A  375  ARG GLN VAL LEU GLU GLU LEU THR GLU LEU PRO VAL MET          
SEQRES   8 A  375  VAL GLU LEU ALA SER ASP PHE LEU ASP ARG ASN THR PRO          
SEQRES   9 A  375  VAL PHE ARG ASP ASP VAL CYS PHE PHE LEU SER GLN SER          
SEQRES  10 A  375  GLY GLU THR ALA ASP THR LEU MET GLY LEU ARG TYR CYS          
SEQRES  11 A  375  LYS GLU ARG GLY ALA LEU THR VAL GLY ILE THR ASN THR          
SEQRES  12 A  375  VAL GLY SER SER ILE SER ARG GLU THR ASP CYS GLY VAL          
SEQRES  13 A  375  HIS ILE ASN ALA GLY PRO GLU ILE GLY VAL ALA SER THR          
SEQRES  14 A  375  LYS ALA TYR THR SER GLN PHE VAL SER LEU VAL MET PHE          
SEQRES  15 A  375  ALA LEU MET MET CYS ASP ASP ARG ILE SER MET GLN GLU          
SEQRES  16 A  375  ARG ARG LYS GLU ILE MET LEU GLY LEU LYS ARG LEU PRO          
SEQRES  17 A  375  ASP LEU ILE LYS GLU VAL LEU SER MET ASP ASP GLU ILE          
SEQRES  18 A  375  GLN LYS LEU ALA THR GLU LEU TYR HIS GLN LYS SER VAL          
SEQRES  19 A  375  LEU ILE MET GLY ARG GLY TYR HIS TYR ALA THR CYS LEU          
SEQRES  20 A  375  GLU GLY ALA LEU LYS ILE LYS GLU ILE THR TYR MET HIS          
SEQRES  21 A  375  SER GLU GLY ILE LEU ALA GLY GLU LEU LYS HIS GLY PRO          
SEQRES  22 A  375  LEU ALA LEU VAL ASP LYS LEU MET PRO VAL ILE MET ILE          
SEQRES  23 A  375  ILE MET ARG ASP HIS THR TYR ALA LYS CYS GLN ASN ALA          
SEQRES  24 A  375  LEU GLN GLN VAL VAL ALA ARG GLN GLY ARG PRO VAL VAL          
SEQRES  25 A  375  ILE CYS ASP LYS GLU ASP THR GLU THR ILE LYS ASN THR          
SEQRES  26 A  375  LYS ARG THR ILE LYS VAL PRO HIS SER VAL ASP CYS LEU          
SEQRES  27 A  375  GLN GLY ILE LEU SER VAL ILE PRO LEU GLN LEU LEU ALA          
SEQRES  28 A  375  PHE HIS LEU ALA VAL LEU ARG GLY TYR ASP VAL ASP PHE          
SEQRES  29 A  375  PRO ARG ASN LEU ALA LYS SER VAL THR VAL GLU                  
HET    AGP  A   1      16                                                       
HETNAM     AGP 2-DEOXY-2-AMINO GLUCITOL-6-PHOSPHATE                             
FORMUL   2  AGP    C6 H16 N O8 P                                                
FORMUL   3  HOH   *267(H2 O)                                                    
HELIX    1   1 SER A  322  GLU A  330  1                                   9    
HELIX    2   2 GLU A  330  ARG A  340  1                                  11    
HELIX    3   3 LEU A  352  LYS A  356  5                                   5    
HELIX    4   4 HIS A  358  CYS A  365  1                                   8    
HELIX    5   5 CYS A  373  GLU A  392  1                                  20    
HELIX    6   6 ALA A  400  ARG A  406  1                                   7    
HELIX    7   7 THR A  425  ARG A  438  1                                  14    
HELIX    8   8 SER A  451  THR A  457  1                                   7    
HELIX    9   9 THR A  474  CYS A  492  1                                  19    
HELIX   10  10 ARG A  495  SER A  497  5                                   3    
HELIX   11  11 MET A  498  SER A  521  1                                  24    
HELIX   12  12 MET A  522  TYR A  534  1                                  13    
HELIX   13  13 ARG A  544  TYR A  546  5                                   3    
HELIX   14  14 HIS A  547  TYR A  563  1                                  17    
HELIX   15  15 GLY A  572  VAL A  582  5                                  11    
HELIX   16  16 THR A  597  ARG A  611  1                                  15    
HELIX   17  17 ASP A  623  THR A  630  1                                   8    
HELIX   18  18 LEU A  643  VAL A  649  1                                   7    
HELIX   19  19 VAL A  649  GLY A  664  1                                  16    
SHEET    1   A 2 VAL A 343  ASN A 344  0                                        
SHEET    2   A 2 THR A 349  VAL A 350 -1  O  THR A 349   N  ASN A 344           
SHEET    1   B 5 VAL A 395  LEU A 399  0                                        
SHEET    2   B 5 ARG A 367  ALA A 372  1  N  LEU A 370   O  MET A 396           
SHEET    3   B 5 ASP A 414  SER A 420  1  O  PHE A 417   N  ILE A 371           
SHEET    4   B 5 LEU A 441  THR A 446  1  O  ILE A 445   N  PHE A 418           
SHEET    5   B 5 CYS A 459  HIS A 462  1  O  VAL A 461   N  GLY A 444           
SHEET    1   C 5 HIS A 565  LEU A 570  0                                        
SHEET    2   C 5 SER A 538  GLY A 543  1  N  ILE A 541   O  ILE A 569           
SHEET    3   C 5 VAL A 588  ILE A 591  1  O  ILE A 589   N  MET A 542           
SHEET    4   C 5 VAL A 616  ASP A 620  1  O  ILE A 618   N  MET A 590           
SHEET    5   C 5 THR A 633  VAL A 636  1  O  VAL A 636   N  CYS A 619           
SITE     1 AC1 19 GLY A 374  THR A 375  SER A 376  SER A 420                    
SITE     2 AC1 19 GLN A 421  SER A 422  THR A 425  VAL A 471                    
SITE     3 AC1 19 ALA A 472  SER A 473  LYS A 557  GLU A 560                    
SITE     4 AC1 19 HIS A 576  HOH A 685  HOH A 692  HOH A 696                    
SITE     5 AC1 19 HOH A 700  HOH A 702  HOH A 728                               
CRYST1   78.927   78.927  277.323  90.00  90.00  90.00 I 41 2 2     16          
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      0.012670  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012670  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003606        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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