HEADER LYASE 28-OCT-04 1WAU
TITLE STRUCTURE OF KDPG ALDOLASE E45N MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KHG/KDPG ALDOLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 4-HYDROXY-2-OXOGLUTARATE ALDOLASE, 2-KETO-4-HYDROXYGLUTARATE
COMPND 5 ALDOLASE, KHG-ALDOLASE, 2-DEHYDRO-3-DEOXY-PHOSPHOGLUCONATE ALDOLASE,
COMPND 6 PHOSPHO-2-DEHYDRO-3-DEOXYGLUCONATE ALDOLASE, PHOSPHO-2-KETO-3-
COMPND 7 DEOXYGLUCONATE ALDOLASE, 2-KETO-3-DEOXY-6-PHOSPHOGLUCONATE ALDOLASE;
COMPND 8 EC: 4.1.2.14, 4.1.3.16;
COMPND 9 ENGINEERED: YES;
COMPND 10 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: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET30B
KEYWDS KDPG ALDOLASE, ESCHERICHIA COLI, LYASE, E45N MUTANT, MULTIFUNCTIONAL
KEYWDS 2 ENZYME
EXPDTA X-RAY DIFFRACTION
AUTHOR A.B.MERKEL,J.H.NAISMITH
REVDAT 6 13-DEC-23 1WAU 1 REMARK
REVDAT 5 05-JUL-17 1WAU 1 REMARK
REVDAT 4 13-JUL-11 1WAU 1 VERSN
REVDAT 3 24-FEB-09 1WAU 1 VERSN
REVDAT 2 22-MAR-06 1WAU 1 JRNL REMARK
REVDAT 1 18-JAN-06 1WAU 0
JRNL AUTH S.W.B.FULLERTON,J.S.GRIFFITHS,A.B.MERKEL,M.CHERIYAN,
JRNL AUTH 2 N.J.WYMER,M.J.HUTCHINS,C.A.FIERKE,E.J.TOONE,J.H.NAISMITH
JRNL TITL MECHANISM OF THE CLASS I KDPG ALDOLASE.
JRNL REF BIOORG.MED.CHEM. V. 14 3002 2006
JRNL REFN ISSN 0968-0896
JRNL PMID 16403639
JRNL DOI 10.1016/J.BMC.2005.12.022
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0007
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 91.29
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 7816
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600
REMARK 3 FREE R VALUE TEST SET COUNT : 380
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.88
REMARK 3 REFLECTION IN BIN (WORKING SET) : 569
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3200
REMARK 3 BIN FREE R VALUE SET COUNT : 23
REMARK 3 BIN FREE R VALUE : 0.4590
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1565
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 102
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 65.16
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.56000
REMARK 3 B22 (A**2) : 1.56000
REMARK 3 B33 (A**2) : -2.34000
REMARK 3 B12 (A**2) : 0.78000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.595
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.326
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.274
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 25.119
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1597 ; 0.028 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2175 ; 2.311 ; 1.999
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 212 ; 6.903 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 51 ;41.271 ;24.706
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 265 ;21.709 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;16.093 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 262 ; 0.136 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1167 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 904 ; 0.303 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1114 ; 0.324 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 119 ; 0.359 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 64 ; 0.569 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 12 ; 0.441 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1092 ; 1.001 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1702 ; 1.713 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 578 ; 2.897 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 473 ; 4.743 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 200
REMARK 3 ORIGIN FOR THE GROUP (A): -36.0048 -19.3135 9.4543
REMARK 3 T TENSOR
REMARK 3 T11: -0.0725 T22: -0.0848
REMARK 3 T33: -0.0887 T12: 0.0261
REMARK 3 T13: 0.0059 T23: 0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 0.8646 L22: 1.3020
REMARK 3 L33: 0.7354 L12: 0.7431
REMARK 3 L13: -0.1001 L23: 0.2246
REMARK 3 S TENSOR
REMARK 3 S11: -0.0153 S12: 0.0373 S13: -0.0576
REMARK 3 S21: -0.0565 S22: 0.0432 S23: -0.1462
REMARK 3 S31: -0.0389 S32: 0.0177 S33: -0.0280
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 1WAU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-OCT-04.
REMARK 100 THE DEPOSITION ID IS D_1290021436.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAR-04
REMARK 200 TEMPERATURE (KELVIN) : 100.0
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 MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15069
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 45.550
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : 1.700
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.8
REMARK 200 DATA REDUNDANCY IN SHELL : 1.70
REMARK 200 R MERGE FOR SHELL (I) : 0.46000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1EUA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M AMMONIUM SULPHATE, 15% PEG4000,
REMARK 280 10MM TRIS, PH8.0, PH 8.00
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 -105.19500
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 -52.59750
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 -91.10154
REMARK 350 BIOMT3 3 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 A2040 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2058 LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE GLU 45 ASN, CHAIN A
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 NZ LYS A 130 O HOH A 2072 1.75
REMARK 500 NZ LYS A 133 O HOH A 2074 1.79
REMARK 500 NZ LYS A 130 O HOH A 2070 1.79
REMARK 500 NZ LYS A 176 O HOH A 2089 1.80
REMARK 500 O HOH A 2070 O HOH A 2072 1.82
REMARK 500 OD2 ASP A 196 OD2 ASP A 198 1.85
REMARK 500 O4 SO4 A 1214 O HOH A 2098 1.85
REMARK 500 OD2 ASP A 196 OD1 ASP A 198 1.85
REMARK 500 O2 SO4 A 1214 O HOH A 2100 1.98
REMARK 500 CB ASP A 196 O HOH A 2093 1.98
REMARK 500 O4 SO4 A 1214 O HOH A 2102 2.00
REMARK 500 O3 SO4 A 1214 O HOH A 2102 2.07
REMARK 500 OD2 ASP A 196 CG ASP A 198 2.08
REMARK 500 S SO4 A 1214 O HOH A 2098 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD2 ASP A 196 OD2 ASP A 196 5556 1.41
REMARK 500 OE1 GLU A 98 OE1 GLU A 98 3445 1.84
REMARK 500 CG ASP A 196 OD2 ASP A 196 5556 1.93
REMARK 500 OD1 ASP A 196 OD2 ASP A 198 5556 1.94
REMARK 500 OD1 ASP A 198 OD2 ASP A 198 5556 2.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 51 CB GLU A 51 CG 0.187
REMARK 500 GLU A 98 CB GLU A 98 CG 0.146
REMARK 500 GLU A 98 CG GLU A 98 CD 0.124
REMARK 500 LYS A 130 CD LYS A 130 CE 0.155
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 GLU A 98 CB - CA - C ANGL. DEV. = 14.1 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 LYS A 2 -155.21 71.82
REMARK 500 ASN A 3 35.37 -91.15
REMARK 500 GLU A 51 -29.46 -19.13
REMARK 500 CYS A 52 31.68 -149.33
REMARK 500 VAL A 64 73.56 -107.63
REMARK 500 SER A 116 -34.62 -133.72
REMARK 500 LYS A 130 -7.32 -143.78
REMARK 500 ALA A 137 -74.79 -22.88
REMARK 500 GLU A 138 -78.04 -51.11
REMARK 500 ALA A 139 -44.52 -27.73
REMARK 500 ASN A 140 4.07 -63.12
REMARK 500 VAL A 143 -73.22 -45.00
REMARK 500 LYS A 212 -167.23 -113.73
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1214
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EUA RELATED DB: PDB
REMARK 900 SCHIFF BASE INTERMEDIATE IN KDPG ALDOLASE FROM ESCHERICHIA COLI
REMARK 900 RELATED ID: 1EUN RELATED DB: PDB
REMARK 900 STRUCTURE OF 2-KETO-3-DEOXY-6- PHOSPHOGLUCONATE ALDOLASE FROM
REMARK 900 ESCHERICHIA COLI
REMARK 900 RELATED ID: 1FQ0 RELATED DB: PDB
REMARK 900 KDPG ALDOLASE FROM ESCHERICHIA COLI
REMARK 900 RELATED ID: 1FWR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF KDPG ALDOLASE DOUBLE MUTANT K133Q/T161K
DBREF 1WAU A 1 213 UNP P10177 ALKH_ECOLI 1 213
SEQADV 1WAU ASN A 45 UNP P10177 GLU 45 ENGINEERED MUTATION
SEQRES 1 A 213 MET LYS ASN TRP LYS THR SER ALA GLU SER ILE LEU THR
SEQRES 2 A 213 THR GLY PRO VAL VAL PRO VAL ILE VAL VAL LYS LYS LEU
SEQRES 3 A 213 GLU HIS ALA VAL PRO MET ALA LYS ALA LEU VAL ALA GLY
SEQRES 4 A 213 GLY VAL ARG VAL LEU ASN VAL THR LEU ARG THR GLU CYS
SEQRES 5 A 213 ALA VAL ASP ALA ILE ARG ALA ILE ALA LYS GLU VAL PRO
SEQRES 6 A 213 GLU ALA ILE VAL GLY ALA GLY THR VAL LEU ASN PRO GLN
SEQRES 7 A 213 GLN LEU ALA GLU VAL THR GLU ALA GLY ALA GLN PHE ALA
SEQRES 8 A 213 ILE SER PRO GLY LEU THR GLU PRO LEU LEU LYS ALA ALA
SEQRES 9 A 213 THR GLU GLY THR ILE PRO LEU ILE PRO GLY ILE SER THR
SEQRES 10 A 213 VAL SER GLU LEU MET LEU GLY MET ASP TYR GLY LEU LYS
SEQRES 11 A 213 GLU PHE LYS PHE PHE PRO ALA GLU ALA ASN GLY GLY VAL
SEQRES 12 A 213 LYS ALA LEU GLN ALA ILE ALA GLY PRO PHE SER GLN VAL
SEQRES 13 A 213 ARG PHE CYS PRO THR GLY GLY ILE SER PRO ALA ASN TYR
SEQRES 14 A 213 ARG ASP TYR LEU ALA LEU LYS SER VAL LEU CYS ILE GLY
SEQRES 15 A 213 GLY SER TRP LEU VAL PRO ALA ASP ALA LEU GLU ALA GLY
SEQRES 16 A 213 ASP TYR ASP ARG ILE THR LYS LEU ALA ARG GLU ALA VAL
SEQRES 17 A 213 GLU GLY ALA LYS LEU
HET SO4 A1214 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 O4 S 2-
FORMUL 3 HOH *102(H2 O)
HELIX 1 1 SER A 7 THR A 13 1 7
HELIX 2 2 LYS A 25 GLU A 27 5 3
HELIX 3 3 HIS A 28 GLY A 39 1 12
HELIX 4 4 CYS A 52 VAL A 64 1 13
HELIX 5 5 ASN A 76 GLY A 87 1 12
HELIX 6 6 THR A 97 GLY A 107 1 11
HELIX 7 7 THR A 117 TYR A 127 1 11
HELIX 8 8 GLY A 141 ALA A 150 1 10
HELIX 9 9 ASN A 168 LEU A 175 1 8
HELIX 10 10 PRO A 188 ALA A 194 1 7
HELIX 11 11 ASP A 196 GLY A 210 1 15
SHEET 1 AA 4 ILE A 68 GLY A 72 0
SHEET 2 AA 4 VAL A 43 THR A 47 1 O LEU A 44 N GLY A 70
SHEET 3 AA 4 VAL A 17 ILE A 21 1 O PRO A 19 N ASN A 45
SHEET 4 AA 4 ILE A 181 GLY A 183 1 O ILE A 181 N VAL A 18
SHEET 1 AB 4 ALA A 91 SER A 93 0
SHEET 2 AB 4 LEU A 111 ILE A 115 1 O ILE A 112 N SER A 93
SHEET 3 AB 4 GLU A 131 PHE A 134 1 O LYS A 133 N ILE A 115
SHEET 4 AB 4 ARG A 157 PRO A 160 1 O ARG A 157 N PHE A 132
CISPEP 1 PHE A 135 PRO A 136 0 -4.61
SITE 1 AC1 8 GLY A 162 GLY A 163 ILE A 164 SER A 184
SITE 2 AC1 8 HOH A2098 HOH A2100 HOH A2101 HOH A2102
CRYST1 105.195 105.195 51.444 90.00 90.00 120.00 P 3 2 1 6
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 0.009506 0.005488 0.000000 0.00000
SCALE2 0.000000 0.010977 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019439 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
