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Database: PDB
Entry: 1EX2
LinkDB: 1EX2
Original site: 1EX2 
HEADER    STRUCTURAL GENOMICS                     28-APR-00   1EX2              
TITLE     CRYSTAL STRUCTURE OF BACILLUS SUBTILIS MAF PROTEIN                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN MAF;                                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PQE30                                     
KEYWDS    B. SUBTILIS PROTEIN MAF, STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE  
KEYWDS   2 INITIATIVE, MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.MINASOV,M.TEPLOVA,G.C.STEWART,E.V.KOONIN,W.F.ANDERSON,M.EGLI,       
AUTHOR   2 MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG)                        
REVDAT   5   29-JUL-20 1EX2    1       COMPND REMARK HET    HETNAM              
REVDAT   5 2                   1       FORMUL LINK   SITE   ATOM                
REVDAT   4   24-FEB-09 1EX2    1       VERSN                                    
REVDAT   3   18-JAN-05 1EX2    1       JRNL   AUTHOR KEYWDS REMARK              
REVDAT   2   28-JUN-00 1EX2    1       SOURCE                                   
REVDAT   1   14-JUN-00 1EX2    0                                                
JRNL        AUTH   G.MINASOV,M.TEPLOVA,G.C.STEWART,E.V.KOONIN,W.F.ANDERSON,     
JRNL        AUTH 2 M.EGLI                                                       
JRNL        TITL   FUNCTIONAL IMPLICATIONS FROM CRYSTAL STRUCTURES OF THE       
JRNL        TITL 2 CONSERVED BACILLUS SUBTILIS PROTEIN MAF WITH AND WITHOUT     
JRNL        TITL 3 DUTP.                                                        
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V.  97  6328 2000              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   10841541                                                     
JRNL        DOI    10.1073/PNAS.97.12.6328                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 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, R.A. AND HUBER, R.                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 91.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 40372                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM, 10% OF THE OBSERVED     
REMARK   3                                      DATA                            
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 4068                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2926                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 38                                      
REMARK   3   SOLVENT ATOMS            : 305                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.400                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  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: MAXIMUM LIKELIHOOD TARGET USING           
REMARK   3  AMPLITUDES                                                          
REMARK   4                                                                      
REMARK   4 1EX2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAY-00.                  
REMARK 100 THE DEPOSITION ID IS D_1000010982.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-SEP-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 5ID-B                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1004                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43834                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.06800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.92                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44900                            
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: NULL                         
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.54                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 8000, 0.1M TRIS-HCL, PH 8.5,      
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295.0K                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       31.33000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       46.97000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.00500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       46.97000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.33000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.00500            
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER CONSTRUCTED FROM CHAINS   
REMARK 300 A AND B                                                              
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 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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 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     ASP A   186                                                      
REMARK 465     ILE A   187                                                      
REMARK 465     ARG A   188                                                      
REMARK 465     ALA A   189                                                      
REMARK 465     ASP B   186                                                      
REMARK 465     ILE B   187                                                      
REMARK 465     ARG B   188                                                      
REMARK 465     ALA B   189                                                      
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    ARG A  38      -15.84    -49.07                                   
REMARK 500    HIS A 114      135.89   -170.77                                   
REMARK 500    HIS B 114      134.94   -170.70                                   
REMARK 500    MET B 144       -4.09    -57.04                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: APC121   RELATED DB: TARGETDB                            
DBREF  1EX2 A    1   189  UNP    Q02169   MAF_BACSU        1    189             
DBREF  1EX2 B    1   189  UNP    Q02169   MAF_BACSU        1    189             
SEQRES   1 A  189  MET THR LYS PRO LEU ILE LEU ALA SER GLN SER PRO ARG          
SEQRES   2 A  189  ARG LYS GLU LEU LEU ASP LEU LEU GLN LEU PRO TYR SER          
SEQRES   3 A  189  ILE ILE VAL SER GLU VAL GLU GLU LYS LEU ASN ARG ASN          
SEQRES   4 A  189  PHE SER PRO GLU GLU ASN VAL GLN TRP LEU ALA LYS GLN          
SEQRES   5 A  189  LYS ALA LYS ALA VAL ALA ASP LEU HIS PRO HIS ALA ILE          
SEQRES   6 A  189  VAL ILE GLY ALA ASP THR MET VAL CYS LEU ASP GLY GLU          
SEQRES   7 A  189  CYS LEU GLY LYS PRO GLN ASP GLN GLU GLU ALA ALA SER          
SEQRES   8 A  189  MET LEU ARG ARG LEU SER GLY ARG SER HIS SER VAL ILE          
SEQRES   9 A  189  THR ALA VAL SER ILE GLN ALA GLU ASN HIS SER GLU THR          
SEQRES  10 A  189  PHE TYR ASP LYS THR GLU VAL ALA PHE TRP SER LEU SER          
SEQRES  11 A  189  GLU GLU GLU ILE TRP THR TYR ILE GLU THR LYS GLU PRO          
SEQRES  12 A  189  MET ASP LYS ALA GLY ALA TYR GLY ILE GLN GLY ARG GLY          
SEQRES  13 A  189  ALA LEU PHE VAL LYS LYS ILE ASP GLY ASP TYR TYR SER          
SEQRES  14 A  189  VAL MET GLY LEU PRO ILE SER LYS THR MET ARG ALA LEU          
SEQRES  15 A  189  ARG HIS PHE ASP ILE ARG ALA                                  
SEQRES   1 B  189  MET THR LYS PRO LEU ILE LEU ALA SER GLN SER PRO ARG          
SEQRES   2 B  189  ARG LYS GLU LEU LEU ASP LEU LEU GLN LEU PRO TYR SER          
SEQRES   3 B  189  ILE ILE VAL SER GLU VAL GLU GLU LYS LEU ASN ARG ASN          
SEQRES   4 B  189  PHE SER PRO GLU GLU ASN VAL GLN TRP LEU ALA LYS GLN          
SEQRES   5 B  189  LYS ALA LYS ALA VAL ALA ASP LEU HIS PRO HIS ALA ILE          
SEQRES   6 B  189  VAL ILE GLY ALA ASP THR MET VAL CYS LEU ASP GLY GLU          
SEQRES   7 B  189  CYS LEU GLY LYS PRO GLN ASP GLN GLU GLU ALA ALA SER          
SEQRES   8 B  189  MET LEU ARG ARG LEU SER GLY ARG SER HIS SER VAL ILE          
SEQRES   9 B  189  THR ALA VAL SER ILE GLN ALA GLU ASN HIS SER GLU THR          
SEQRES  10 B  189  PHE TYR ASP LYS THR GLU VAL ALA PHE TRP SER LEU SER          
SEQRES  11 B  189  GLU GLU GLU ILE TRP THR TYR ILE GLU THR LYS GLU PRO          
SEQRES  12 B  189  MET ASP LYS ALA GLY ALA TYR GLY ILE GLN GLY ARG GLY          
SEQRES  13 B  189  ALA LEU PHE VAL LYS LYS ILE ASP GLY ASP TYR TYR SER          
SEQRES  14 B  189  VAL MET GLY LEU PRO ILE SER LYS THR MET ARG ALA LEU          
SEQRES  15 B  189  ARG HIS PHE ASP ILE ARG ALA                                  
HET    GLC  C   1      11                                                       
HET    FRU  C   2      12                                                       
HET    PO4  A 201       5                                                       
HET    PO4  A 203       5                                                       
HET    PO4  B 202      10                                                       
HETNAM     GLC ALPHA-D-GLUCOPYRANOSE                                            
HETNAM     FRU BETA-D-FRUCTOFURANOSE                                            
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   3  GLC    C6 H12 O6                                                    
FORMUL   3  FRU    C6 H12 O6                                                    
FORMUL   4  PO4    3(O4 P 3-)                                                   
FORMUL   7  HOH   *305(H2 O)                                                    
HELIX    1   1 SER A   11  LEU A   20  1                                  10    
HELIX    2   2 SER A   41  HIS A   61  1                                  21    
HELIX    3   3 ASP A   85  SER A   97  1                                  13    
HELIX    4   4 SER A  130  GLU A  139  1                                  10    
HELIX    5   5 GLU A  142  LYS A  146  5                                   5    
HELIX    6   6 GLN A  153  LEU A  158  5                                   6    
HELIX    7   7 ASP A  166  GLY A  172  1                                   7    
HELIX    8   8 PRO A  174  ARG A  183  1                                  10    
HELIX    9   9 SER B   11  ASP B   19  1                                   9    
HELIX   10  10 LEU B   20  GLN B   22  5                                   3    
HELIX   11  11 SER B   41  ASP B   59  1                                  19    
HELIX   12  12 ASP B   85  SER B   97  1                                  13    
HELIX   13  13 SER B  130  THR B  140  1                                  11    
HELIX   14  14 LYS B  141  LYS B  141  5                                   1    
HELIX   15  15 GLU B  142  LYS B  146  5                                   5    
HELIX   16  16 LYS B  146  TYR B  150  5                                   5    
HELIX   17  17 GLN B  153  LEU B  158  5                                   6    
HELIX   18  18 ASP B  166  GLY B  172  1                                   7    
HELIX   19  19 PRO B  174  ARG B  183  1                                  10    
SSBOND   1 CYS A   74    CYS A   79                          1555   1555  2.04  
SSBOND   2 CYS B   74    CYS B   79                          1555   1555  2.04  
LINK         C1  GLC C   1                 O2  FRU C   2     1555   1555  1.41  
CRYST1   62.660   86.010   93.940  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015959  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011627  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010645        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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