HEADER ALDOLASE (CLASS II) 30-JUN-00 1E48
TITLE L-FUCULOSE 1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT
TITLE 2 E73Q/Y113F/Y209F
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-E73Q/Y113F/Y209F;
SOURCE 8 OTHER_DETAILS: E73Q, Y113F, AND Y209F MUTATIONS PERFORMED WITH
SOURCE 9 PHOSPHOROTHIOATE METHOD USING M13MP19
KEYWDS ALDOLASE (CLASS II), BACTERIAL L-FUCOSE METABOLISM, CLEAVAGE OF L-
KEYWDS 2 FUCULOSE 1-PHOSPHATE TO DIHYDROXYACETONE PHOSPHATE AND L-
KEYWDS 3 LACTALDEHYDE, MUTANT STRUCTURE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.C.JOERGER,G.E.SCHULZ
REVDAT 6 30-JAN-19 1E48 1 REMARK
REVDAT 5 12-JUL-17 1E48 1
REVDAT 4 05-JUL-17 1E48 1 REMARK
REVDAT 3 24-FEB-09 1E48 1 VERSN
REVDAT 2 18-JUL-03 1E48 1 REMARK
REVDAT 1 06-NOV-00 1E48 0
JRNL AUTH A.C.JOERGER,C.MUELLER-DIECKMANN,G.E.SCHULZ
JRNL TITL STRUCTURES OF L-FUCULOSE-1-PHOSPHATE ALDOLASE MUTANTS
JRNL TITL 2 OUTLINING MOTIONS DURING CATALYSIS
JRNL REF J.MOL.BIOL. V. 303 531 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 11054289
JRNL DOI 10.1006/JMBI.2000.4153
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.C.JOERGER,C.GOSSE,W.-D.FESSNER,G.E.SCHULZ
REMARK 1 TITL CATALYTIC ACTION OF FUCULOSE 1-PHOSPHATE ALDOLASE (CLASS II)
REMARK 1 TITL 2 AS DERIVED BY STRUCTURE-DIRECTED MUTAGENESIS
REMARK 1 REF BIOCHEMISTRY V. 39 6033 2000
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 10821675
REMARK 1 DOI 10.1021/BI9927686
REMARK 1 REFERENCE 2
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 3
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. 1.97 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) : 1.97
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 13420
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) : 0.171
REMARK 3 FREE R VALUE : 0.221
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 : 1592
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 110
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.60
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): 0.180
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.170
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.040
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.550
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.011 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.033 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.034 ; 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: THE 9 C-TERMINAL RESIDUES (LYS207 - GLU
REMARK 3 215) WERE NOT SEEN IN THE DENSITY MAPS
REMARK 4
REMARK 4 1E48 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-JUN-00.
REMARK 100 THE DEPOSITION ID IS D_1290005093.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-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 : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : MULTIWIRE SIEMENS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13420
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.970
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 (%) : 96.0
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.97
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.04
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.19000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.000
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 (%): 39.00
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 46.85000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 46.85000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 46.85000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 46.85000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 46.85000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 46.85000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 46.85000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 46.85000
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 46.85000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 46.85000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 -46.85000
REMARK 350 BIOMT2 3 -1.000000 0.000000 0.000000 46.85000
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 93.70000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 CHAIN P ENGINEERED MUTATION GLU73GLN, TYR113PHE, TYR209PHE
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 LYS P 207
REMARK 465 THR P 208
REMARK 465 PHE P 209
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: 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 O3 13P P 302 ZN ZN P 303 1.68
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 P 8 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG P 75 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ASP P 86 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 TYR P 181 CB - CG - CD2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 TYR P 181 CB - CG - CD1 ANGL. DEV. = -4.7 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 THR P 26 63.58 34.17
REMARK 500 GLN P 35 -129.88 53.14
REMARK 500 ILE P 45 116.70 -23.81
REMARK 500 HIS P 155 -73.19 -146.16
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 303 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS P 92 NE2
REMARK 620 2 HIS P 94 NE2 107.7
REMARK 620 3 HIS P 155 NE2 100.7 100.1
REMARK 620 4 13P P 302 O2 145.4 91.8 103.7
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN S 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME S 314
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 13P S 600
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3FUA RELATED DB: PDB
REMARK 900 L-FUCULOSE-1-PHOSPHATE ALDOLASE CRYSTAL FORM K
REMARK 900 RELATED ID: 2FUA RELATED DB: PDB
REMARK 900 L-FUCULOSE 1-PHOSPHATE ALDOLASE CRYSTAL FORM T WITH COBALT
REMARK 900 RELATED ID: 1FUA RELATED DB: PDB
REMARK 900 L-FUCULOSE 1-PHOSPHATE ALDOLASE CRYSTAL FORM T
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 900 RELATED ID: 1DZU RELATED DB: PDB
REMARK 900 L-FUCULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT T26A
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: 4FUA RELATED DB: PDB
REMARK 900 L-FUCULOSE-1-PHOSPHATE ALDOLASE COMPLEX WITH PGH
REMARK 900 RELATED ID: 1E46 RELATED DB: PDB
REMARK 900 L-FUCULOSE 1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT E73S
REMARK 900 RELATED ID: 1E47 RELATED DB: PDB
REMARK 900 L-FUCULOSE 1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT E73Q
REMARK 900 RELATED ID: 1E49 RELATED DB: PDB
REMARK 900 L-FUCULOSE 1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT N29L/
REMARK 900 S71A
REMARK 900 RELATED ID: 1E4A RELATED DB: PDB
REMARK 900 L-FUCULOSE 1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT DEL(27)
REMARK 900 RELATED ID: 1E4B RELATED DB: PDB
REMARK 900 L-FUCULOSE 1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT N29Q
REMARK 900 RELATED ID: 1E4C RELATED DB: PDB
REMARK 900 L-FUCULOSE 1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT S71Q
DBREF 1E48 P 1 215 UNP P11550 FUCA_ECOLI 1 215
SEQADV 1E48 GLN P 73 UNP P11550 GLU 73 ENGINEERED MUTATION
SEQADV 1E48 PHE P 113 UNP P11550 TYR 113 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 THR
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 GLN 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 PHE 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 PHE GLY LEU ARG ILE GLU GLU
HET BME P 301 4
HET 13P P 302 10
HET ZN P 303 1
HETNAM BME BETA-MERCAPTOETHANOL
HETNAM 13P 1,3-DIHYDROXYACETONEPHOSPHATE
HETNAM ZN ZINC ION
FORMUL 2 BME C2 H6 O S
FORMUL 3 13P C3 H7 O6 P
FORMUL 4 ZN ZN 2+
FORMUL 5 HOH *110(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 GLN P 73 ARG P 84 1 12
HELIX 5 5 ALA P 95 ASN P 105 1 11
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 THR P 188 1 26
HELIX 9 9 SER P 195 PHE P 206 1 12
SHEET 1 A 7 VAL P 56 ILE P 58 0
SHEET 2 A 7 GLY P 37 ILE P 40 -1 O MET P 38 N ILE P 58
SHEET 3 A 7 ASN P 29 TYR P 34 -1 O VAL P 32 N LEU P 39
SHEET 4 A 7 ALA P 89 ASN P 93 -1 O VAL P 90 N SER P 31
SHEET 5 A 7 GLY P 156 GLU P 161 -1 O LEU P 157 N ASN P 93
SHEET 6 A 7 ALA P 149 LEU P 152 -1 O THR P 150 N ILE P 158
SHEET 7 A 7 CYS P 125 ALA P 126 1 N ALA P 126 O LEU P 151
LINK SG CYS P 14 S2 BME P 301 1555 1555 2.04
LINK NE2 HIS P 92 ZN ZN P 303 1555 1555 2.07
LINK NE2 HIS P 94 ZN ZN P 303 1555 1555 2.10
LINK NE2 HIS P 155 ZN ZN P 303 1555 1555 2.15
LINK O2 13P P 302 ZN ZN P 303 1555 1555 2.55
CISPEP 1 ASP P 189 PRO P 190 0 5.65
SITE 1 AC1 5 GLN P 73 HIS P 92 HIS P 94 HIS P 155
SITE 2 AC1 5 13P P 302
SITE 1 AC2 5 CYS P 14 GLY P 28 HOH P 434 HOH P 409
SITE 2 AC2 5 HOH P 439
SITE 1 AC3 12 ALA P 27 ASN P 29 THR P 43 SER P 71
SITE 2 AC3 12 SER P 72 GLN P 73 HIS P 92 HIS P 94
SITE 3 AC3 12 ZN P 303 HOH P 439 HOH P 413 HOH P 446
CRYST1 93.700 93.700 43.200 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 0.010672 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010672 0.000000 0.00000
SCALE3 0.000000 0.000000 0.023148 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
