HEADER LYASE (ALDEHYDE) 07-MAR-00 1DZZ
TITLE L-FUCULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT Y113F
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: L-FUCULOSE PHOSPHATE ALDOLASE;
COMPND 3 CHAIN: P;
COMPND 4 SYNONYM: D-RIBULOSE-PHOSPHATE ALDOLASE,L-FUCULOSE-1-PHOSPHATE
COMPND 5 ALDOLASE;
COMPND 6 EC: 4.1.2.17;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: FUCA, FUCA_1, FUCA_2, A9R57_06860, ACU57_24310, AM464_05705,
SOURCE 5 AUQ13_17640, BANRA_01321, BANRA_04164, BANRA_04304, BHS87_15835,
SOURCE 6 BJJ90_05160, BUE81_06870, BVCMS12BK_05168, BVCMS2454_02072,
SOURCE 7 BVCMSHHP001_01136, BVCMSHHP056_02000, BVCMSKKP061_04411,
SOURCE 8 BVCMSKSP011_02414, BVCMSKSP024_03378, BVCMSKSP026_00082,
SOURCE 9 BVCMSKSP040_03336, BVCMSKSP045_02228, BVCMSKSP067_03660,
SOURCE 10 BVCMSNSNP027_02922, BVCMSNSP047_01577, BVCMSSINP012_00041,
SOURCE 11 BW690_04870, C4J69_11555, C9E25_03225, CV83915_03318, D2185_02685,
SOURCE 12 D3821_11040, D3Y67_10455, D9D20_04550, D9E35_20280, D9H68_17240,
SOURCE 13 DP258_16175, E5M00_06120, EAI52_12600, EC3234A_48C01090,
SOURCE 14 ECTO6_01047, EEP23_13950, EFB45_09210, EL75_0893, EL79_0895,
SOURCE 15 EL80_0898, EPS71_16910, EPT01_16955, ERS085365_02448,
SOURCE 16 ERS085366_03061, ERS085416_02919, ERS139211_02051, ERS150873_02024,
SOURCE 17 EXX32_11695, EXX39_16005, EXX71_16135, HMCMS184_04796,
SOURCE 18 NCTC11181_03256, NCTC13462_04786, NCTC8500_01060, NCTC9037_01222,
SOURCE 19 NCTC9045_01197, NCTC9058_00868, NCTC9062_02153, NCTC9706_03275,
SOURCE 20 RK56_023265, SAMEA3472047_00318, SAMEA3472080_03134,
SOURCE 21 SAMEA3484427_03277, SAMEA3484429_03394, SAMEA3752559_02974,
SOURCE 22 SAMEA3753300_01128, SK85_03044, WR15_06195;
SOURCE 23 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 24 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 25 EXPRESSION_SYSTEM_STRAIN: JM 105;
SOURCE 26 EXPRESSION_SYSTEM_PLASMID: PKKFA2-Y113F;
SOURCE 27 OTHER_DETAILS: Y113F SUBSTITUTION PERFORMED WITH PHOSPHOROTHIOATE
SOURCE 28 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 7 25-SEP-19 1DZZ 1 COMPND SOURCE DBREF SEQADV
REVDAT 7 2 1 LINK
REVDAT 6 30-JAN-19 1DZZ 1 REMARK
REVDAT 5 24-FEB-09 1DZZ 1 VERSN
REVDAT 4 21-FEB-02 1DZZ 1 HET HETNAM FORMUL SITE
REVDAT 4 2 1 HETATM
REVDAT 3 20-JUL-00 1DZZ 1 SEQRES
REVDAT 2 09-JUN-00 1DZZ 1 FORMUL
REVDAT 1 02-JUN-00 1DZZ 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. 1.92 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) : 1.92
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 : 13096
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) : 0.159
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 : 1608
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) : 28.00
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): 0.190
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.160
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.060
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.200
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.008 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.028 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.028 ; 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 1DZZ 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_1290004698.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUL-95
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 : SIEMENS XP-18H
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 : 13096
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.920
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 : 4.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04300
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) : 1.92
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.96
REMARK 200 COMPLETENESS FOR SHELL (%) : 63.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.18000
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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 46.85000
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 TYR113PHE
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 TYR 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: 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 GLU P 66 OE1 - CD - OE2 ANGL. DEV. = 7.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLN P 35 -128.32 52.74
REMARK 500 HIS P 155 -65.51 -150.49
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 89.4
REMARK 620 3 HIS P 94 NE2 119.9 105.8
REMARK 620 4 HIS P 155 NE2 133.5 99.4 101.5
REMARK 620 5 GLU P 73 OE1 52.4 101.9 151.3 81.2
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: 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: 1DZY RELATED DB: PDB
REMARK 900 L-FUCULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT E214A
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THR: THE 7 C-TERMINAL RESIDUES (TYR 209 - GLU 215) WERE NOT
REMARK 999 SEEN IN THE DENSITY MAPS
DBREF1 1DZZ P 1 215 UNP A0A037YR34_ECOLX
DBREF2 1DZZ P A0A037YR34 1 215
SEQADV 1DZZ PHE P 113 UNP A0A037YR3 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 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 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 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 THR P 208 1 14
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 2.00
LINK ZN ZN P 999 OE2 GLU P 73 1555 1555 2.46
LINK ZN ZN P 999 NE2 HIS P 92 1555 1555 2.19
LINK ZN ZN P 999 NE2 HIS P 94 1555 1555 2.21
LINK ZN ZN P 999 NE2 HIS P 155 1555 1555 2.22
LINK ZN ZN P 999 OE1 GLU P 73 1555 1555 2.53
CISPEP 1 ASP P 189 PRO P 190 0 6.49
SITE 1 AC1 4 GLU P 73 HIS P 92 HIS P 94 HIS P 155
SITE 1 AC2 8 THR P 26 ASN P 29 THR P 43 SER P 71
SITE 2 AC2 8 SER P 72 HOH P2008 HOH P2015 HOH P2106
SITE 1 AC3 8 HIS P 64 GLU P 66 GLY P 67 TRP P 74
SITE 2 AC3 8 ARG P 75 HOH P2035 HOH P2105 HOH P2107
SITE 1 AC4 4 CYS P 14 GLY P 28 HOH P2106 HOH P2108
CRYST1 93.700 93.700 42.600 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 0.023474 0.00000
(ATOM LINES ARE NOT SHOWN.)
END