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Database: PDB
Entry: 1DZU
LinkDB: 1DZU
Original site: 1DZU 
HEADER    LYASE (ALDEHYDE)                        07-MAR-00   1DZU              
TITLE     L-FUCULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT T26A     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: L-FUCULOSE-1-PHOSPHATE ALDOLASE;                           
COMPND   3 CHAIN: P;                                                            
COMPND   4 EC: 4.1.2.17;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: JM 105;                                    
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PKKFA2-T26A;                              
SOURCE   8 OTHER_DETAILS: T26A SUBSTITUTION PERFORMED WITH PHOSPHOROTHIOATE     
SOURCE   9 METHOD USING M13MP19                                                 
KEYWDS    LYASE (ALDEHYDE), ALDOLASE (CLASS II), BACTERIAL L-FUCOSE METABOLISM, 
KEYWDS   2 CLEAVAGE OF L-FUCULOSE-1-PHOSPHATE TO DIHYDROXYACETONEPHOSPHATE AND  
KEYWDS   3 L-LACTALDEHYDE, MUTANT STRUCTURE                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.C.JOERGER,G.E.SCHULZ                                                
REVDAT   6   30-JAN-19 1DZU    1       REMARK                                   
REVDAT   5   05-JUL-17 1DZU    1       REMARK                                   
REVDAT   4   24-FEB-09 1DZU    1       VERSN                                    
REVDAT   3   20-JUL-00 1DZU    1       SEQRES                                   
REVDAT   2   09-JUN-00 1DZU    1       FORMUL                                   
REVDAT   1   02-JUN-00 1DZU    0                                                
JRNL        AUTH   A.C.JOERGER,C.GOSSE,W.-D.FESSNER,G.E.SCHULZ                  
JRNL        TITL   CATALYTIC ACTION OF FUCULOSE 1-PHOSPHATE ALDOLASE (CLASS II) 
JRNL        TITL 2 AS DERIVED FROM STRUCTURE-DIRECTED MUTAGENESIS               
JRNL        REF    BIOCHEMISTRY                  V.  39  6033 2000              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   10821675                                                     
JRNL        DOI    10.1021/BI9927686                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.K.DREYER,G.E.SCHULZ                                        
REMARK   1  TITL   CATALYTIC MECHANISM OF THE METAL-DEPENDENT FUCULOSE ALDOLASE 
REMARK   1  TITL 2 FROM ESCHERICHIA COLI AS DERIVED FROM THE STRUCTURE          
REMARK   1  REF    J.MOL.BIOL.                   V. 259   458 1996              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  PMID   8676381                                                      
REMARK   1  DOI    10.1006/JMBI.1996.0332                                       
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   M.K.DREYER,G.E.SCHULZ                                        
REMARK   1  TITL   THE SPATIAL STRUCTURE OF THE CLASS II L-FUCULOSE-1-PHOSPHATE 
REMARK   1  TITL 2 ALDOLASE FROM ESCHERICHIA COLI                               
REMARK   1  REF    J.MOL.BIOL.                   V. 231   549 1993              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  PMID   8515438                                                      
REMARK   1  DOI    10.1006/JMBI.1993.1307                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.09 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.09                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 87.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 10121                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.150                           
REMARK   3   FREE R VALUE                     : 0.207                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1619                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 15                                      
REMARK   3   SOLVENT ATOMS            : 108                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.10                          
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.280         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.200         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.070         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.900         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.009 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.031 ; 0.040               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.032 ; 0.050               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1DZU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-MAR-00.                  
REMARK 100 THE DEPOSITION ID IS D_1290004649.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-FEB-96                          
REMARK 200  TEMPERATURE           (KELVIN) : 293.0                              
REMARK 200  PH                             : 8.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH2R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS X-1000 CCD                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10121                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.090                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 10.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 87.0                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.09                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 78.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.15000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS GROWN FROM AMMONIUM SULFATE     
REMARK 280  AT PH 8.0,VAPOUR DIFFUSION, HANGING DROP, CONDITIONS CLOSE TO       
REMARK 280  THE ONES REPORTED FOR THE WILD-TYPE, SEE PDB ID 1FUA FOR FURTHER    
REMARK 280  DETAILS, PH 8.00, VAPOR DIFFUSION, HANGING DROP                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y+1/2,X+1/2,Z                                          
REMARK 290       4555   Y+1/2,-X+1/2,Z                                          
REMARK 290       5555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       6555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       46.90000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       46.90000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       46.90000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       46.90000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       46.90000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       46.90000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       46.90000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       46.90000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
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                                                                      
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P                                     
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       46.90000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000       46.90000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000  1.000000  0.000000      -46.90000            
REMARK 350   BIOMT2   3 -1.000000  0.000000  0.000000       46.90000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000       93.80000            
REMARK 350   BIOMT3   4  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 P2050  LIES ON A SPECIAL POSITION.                          
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 CHAIN P ENGINEERED MUTATION THR26ALA                                 
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     GLY P   210                                                      
REMARK 465     LEU P   211                                                      
REMARK 465     ARG P   212                                                      
REMARK 465     ILE P   213                                                      
REMARK 465     GLU P   214                                                      
REMARK 465     GLU P   215                                                      
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    ASP P  12   CB  -  CG  -  OD1 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ARG P  33   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ARG P  33   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    GLU P  66   OE1 -  CD  -  OE2 ANGL. DEV. =   8.5 DEGREES          
REMARK 500    LEU P 157   CA  -  CB  -  CG  ANGL. DEV. =  16.5 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 P  23       61.47   -109.22                                   
REMARK 500    GLN P  35     -130.85     56.84                                   
REMARK 500    HIS P 155      -72.55   -152.10                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN P 999  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU P  73   OE2                                                    
REMARK 620 2 HIS P  92   NE2  94.3                                              
REMARK 620 3 HIS P  94   NE2 112.5 111.0                                        
REMARK 620 4 HIS P 155   NE2 132.6 104.1 101.1                                  
REMARK 620 5 GLU P  73   OE1  53.9  96.5 150.9  80.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN P 999                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 P 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 P 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME P 314                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1FUA   RELATED DB: PDB                                   
REMARK 900 L-FUCULOSE 1-PHOSPHATE ALDOLASE CRYSTAL FORM T                       
REMARK 900 RELATED ID: 2FUA   RELATED DB: PDB                                   
REMARK 900 L-FUCULOSE 1-PHOSPHATE ALDOLASE CRYSTAL FORM T WITH COBALT           
REMARK 900 RELATED ID: 3FUA   RELATED DB: PDB                                   
REMARK 900 L-FUCULOSE 1-PHOSPHATE ALDOLASE CRYSTAL FORM K                       
REMARK 900 RELATED ID: 4FUA   RELATED DB: PDB                                   
REMARK 900 L-FUCULOSE 1-PHOSPHATE ALDOLASE COMPLEX WITH PGH                     
REMARK 900 RELATED ID: 1DZV   RELATED DB: PDB                                   
REMARK 900 L-FUCULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT Y113F/  
REMARK 900 Y209F                                                                
REMARK 900 RELATED ID: 1DZW   RELATED DB: PDB                                   
REMARK 900 L-FUCULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT F131A   
REMARK 900 RELATED ID: 1DZX   RELATED DB: PDB                                   
REMARK 900 L-FUCULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT R212A   
REMARK 900 RELATED ID: 1DZY   RELATED DB: PDB                                   
REMARK 900 L-FUCULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT E214A   
REMARK 900 RELATED ID: 1DZZ   RELATED DB: PDB                                   
REMARK 900 L-FUCULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT Y113F   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE C-TERMINAL RESIDUES 210-215 ARE DISORDERED IN THE CRYSTAL        
DBREF  1DZU P    1   215  UNP    P11550   FUCA_ECOLI       1    215             
SEQADV 1DZU ALA P   26  UNP  P11550    THR    26 ENGINEERED MUTATION            
SEQRES   1 P  215  MET GLU ARG ASN LYS LEU ALA ARG GLN ILE ILE ASP THR          
SEQRES   2 P  215  CYS LEU GLU MET THR ARG LEU GLY LEU ASN GLN GLY ALA          
SEQRES   3 P  215  ALA GLY ASN VAL SER VAL ARG TYR GLN ASP GLY MET LEU          
SEQRES   4 P  215  ILE THR PRO THR GLY ILE PRO TYR GLU LYS LEU THR GLU          
SEQRES   5 P  215  SER HIS ILE VAL PHE ILE ASP GLY ASN GLY LYS HIS GLU          
SEQRES   6 P  215  GLU GLY LYS LEU PRO SER SER GLU TRP ARG PHE HIS MET          
SEQRES   7 P  215  ALA ALA TYR GLN SER ARG PRO ASP ALA ASN ALA VAL VAL          
SEQRES   8 P  215  HIS ASN HIS ALA VAL HIS CYS THR ALA VAL SER ILE LEU          
SEQRES   9 P  215  ASN ARG SER ILE PRO ALA ILE HIS TYR MET ILE ALA ALA          
SEQRES  10 P  215  ALA GLY GLY ASN SER ILE PRO CYS ALA PRO TYR ALA THR          
SEQRES  11 P  215  PHE GLY THR ARG GLU LEU SER GLU HIS VAL ALA LEU ALA          
SEQRES  12 P  215  LEU LYS ASN ARG LYS ALA THR LEU LEU GLN HIS HIS GLY          
SEQRES  13 P  215  LEU ILE ALA CYS GLU VAL ASN LEU GLU LYS ALA LEU TRP          
SEQRES  14 P  215  LEU ALA HIS GLU VAL GLU VAL LEU ALA GLN LEU TYR LEU          
SEQRES  15 P  215  THR THR LEU ALA ILE THR ASP PRO VAL PRO VAL LEU SER          
SEQRES  16 P  215  ASP GLU GLU ILE ALA VAL VAL LEU GLU LYS PHE LYS THR          
SEQRES  17 P  215  TYR GLY LEU ARG ILE GLU GLU                                  
HET    SO4  P 300       5                                                       
HET    SO4  P 301       5                                                       
HET    BME  P 314       4                                                       
HET     ZN  P 999       1                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     BME BETA-MERCAPTOETHANOL                                             
HETNAM      ZN ZINC ION                                                         
FORMUL   2  SO4    2(O4 S 2-)                                                   
FORMUL   4  BME    C2 H6 O S                                                    
FORMUL   5   ZN    ZN 2+                                                        
FORMUL   6  HOH   *108(H2 O)                                                    
HELIX    1   1 GLU P    2  LEU P   20  1                                  19    
HELIX    2   2 PRO P   46  LEU P   50  5                                   5    
HELIX    3   3 THR P   51  ILE P   55  5                                   5    
HELIX    4   4 GLU P   73  ARG P   84  1                                  12    
HELIX    5   5 ALA P   95  LEU P  104  1                                  10    
HELIX    6   6 HIS P  112  GLY P  119  5                                   8    
HELIX    7   7 THR P  133  LEU P  144  1                                  12    
HELIX    8   8 ASN P  163  ALA P  186  1                                  24    
HELIX    9   9 SER P  195  TYR P  209  1                                  15    
SHEET    1   A 7 VAL P  56  ILE P  58  0                                        
SHEET    2   A 7 GLY P  37  ILE P  40 -1  N  ILE P  40   O  VAL P  56           
SHEET    3   A 7 ASN P  29  TYR P  34 -1  N  TYR P  34   O  GLY P  37           
SHEET    4   A 7 ALA P  89  ASN P  93 -1  N  HIS P  92   O  ASN P  29           
SHEET    5   A 7 GLY P 156  GLU P 161 -1  N  GLU P 161   O  ALA P  89           
SHEET    6   A 7 ALA P 149  LEU P 152 -1  N  LEU P 152   O  GLY P 156           
SHEET    7   A 7 PRO P 124  ALA P 126  1  N  PRO P 124   O  LEU P 151           
LINK         SG  CYS P  14                 S2  BME P 314     1555   1555  2.01  
LINK        ZN    ZN P 999                 OE2 GLU P  73     1555   1555  2.11  
LINK        ZN    ZN P 999                 NE2 HIS P  92     1555   1555  2.12  
LINK        ZN    ZN P 999                 NE2 HIS P  94     1555   1555  2.05  
LINK        ZN    ZN P 999                 NE2 HIS P 155     1555   1555  2.14  
LINK        ZN    ZN P 999                 OE1 GLU P  73     1555   1555  2.57  
CISPEP   1 ASP P  189    PRO P  190          0         4.20                     
SITE     1 AC1  5 GLU P  73  HIS P  92  HIS P  94  TYR P 113                    
SITE     2 AC1  5 HIS P 155                                                     
SITE     1 AC2  8 ASN P  29  THR P  43  SER P  71  SER P  72                    
SITE     2 AC2  8 HOH P2012  HOH P2013  HOH P2019  HOH P2022                    
SITE     1 AC3 10 HIS P  64  GLU P  66  GLY P  67  TRP P  74                    
SITE     2 AC3 10 ARG P  75  TYR P 209  HOH P2042  HOH P2105                    
SITE     3 AC3 10 HOH P2106  HOH P2107                                          
SITE     1 AC4  4 CYS P  14  GLY P  28  HOH P2013  HOH P2108                    
CRYST1   93.800   93.800   43.000  90.00  90.00  90.00 P 4 21 2      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010661  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010661  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.023256        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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