HEADER OXIDOREDUCTASE (NAD(A)-CHOH(D)) 12-OCT-95 1GRP
TITLE REGULATORY AND CATALYTIC MECHANISMS IN ESCHERICHIA COLI ISOCITRATE
TITLE 2 DEHYDROGENASE: MULTIPLE ROLES FOR N115
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ISOCITRATE DEHYDROGENASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.1.1.42;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562
KEYWDS OXIDOREDUCTASE, NADP, PHOSPHORYLATION, GLYOXYLATE BYPASS,
KEYWDS 2 OXIDOREDUCTASE (NAD(A)-CHOH(D))
EXPDTA X-RAY DIFFRACTION
AUTHOR J.A.GROBLER,J.H.HURLEY
REVDAT 6 07-FEB-24 1GRP 1 REMARK
REVDAT 5 03-NOV-21 1GRP 1 REMARK SEQADV LINK
REVDAT 4 29-NOV-17 1GRP 1 HELIX
REVDAT 3 13-JUL-11 1GRP 1 VERSN
REVDAT 2 24-FEB-09 1GRP 1 VERSN
REVDAT 1 03-APR-96 1GRP 0
JRNL AUTH R.CHEN,J.A.GROBLER,J.H.HURLEY,A.M.DEAN
JRNL TITL SECOND-SITE SUPPRESSION OF REGULATORY PHOSPHORYLATION IN
JRNL TITL 2 ESCHERICHIA COLI ISOCITRATE DEHYDROGENASE.
JRNL REF PROTEIN SCI. V. 5 287 1996
JRNL REFN ISSN 0961-8368
JRNL PMID 8745407
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.H.HURLEY,A.M.DEAN,P.E.THORSNESS,D.E.KOSHLAND JUNIOR,
REMARK 1 AUTH 2 R.M.STROUD
REMARK 1 TITL REGULATION OF ISOCITRATE DEHYDROGENASE BY PHOSPHORYLATION
REMARK 1 TITL 2 INVOLVES NO LONG-RANGE CONFORMATIONAL CHANGE IN THE FREE
REMARK 1 TITL 3 ENZYME
REMARK 1 REF J.BIOL.CHEM. V. 265 3599 1990
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.H.HURLEY,A.M.DEAN,J.L.SOHL,D.E.KOSHLAND JUNIOR,R.M.STROUD
REMARK 1 TITL REGULATION OF AN ENZYME BY PHOSPHORYLATION AT THE ACTIVE
REMARK 1 TITL 2 SITE
REMARK 1 REF SCIENCE V. 249 1012 1990
REMARK 1 REFN ISSN 0036-8075
REMARK 1 REFERENCE 3
REMARK 1 AUTH J.H.HURLEY,P.E.THORSNESS,V.RAMALINGAM,N.H.HELMERS,
REMARK 1 AUTH 2 D.E.KOSHLAND JUNIOR,R.M.STROUD
REMARK 1 TITL STRUCTURE OF A BACTERIAL ENZYME REGULATED BY
REMARK 1 TITL 2 PHOSPHORYLATION, ISOCITRATE DEHYDROGENASE
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 86 8635 1989
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 25689
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3150
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 2.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1GRP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000173680.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28004
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.11800
REMARK 200 R SYM (I) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 75.30000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 52.55000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 52.55000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 112.95000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 52.55000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 52.55000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 37.65000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 52.55000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 52.55000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 112.95000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 52.55000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 52.55000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 37.65000
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 75.30000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 7610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 KCAL/MOL
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 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 GLU A 2
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN A 10 CG CD OE1 NE2
REMARK 470 GLN A 17 CG CD OE1 NE2
REMARK 470 ASN A 18 CG OD1 ND2
REMARK 470 LYS A 20 CG CD CE NZ
REMARK 470 ASP A 81 CG OD1 OD2
REMARK 470 GLU A 182 CG CD OE1 OE2
REMARK 470 LYS A 186 CG CD CE NZ
REMARK 470 GLU A 204 CG CD OE1 OE2
REMARK 470 ASP A 259 CG OD1 OD2
REMARK 470 LYS A 273 CG CD CE NZ
REMARK 470 GLU A 331 CG CD OE1 OE2
REMARK 470 LYS A 344 CG CD CE NZ
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 HIS A 143 NE2 HIS A 143 CD2 -0.073
REMARK 500 HIS A 193 NE2 HIS A 193 CD2 -0.076
REMARK 500 HIS A 229 NE2 HIS A 229 CD2 -0.073
REMARK 500 HIS A 339 NE2 HIS A 339 CD2 -0.069
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 TRP A 65 CD1 - CG - CD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 TRP A 65 CE2 - CD2 - CG ANGL. DEV. = -5.8 DEGREES
REMARK 500 TRP A 83 CD1 - CG - CD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 TRP A 83 CE2 - CD2 - CG ANGL. DEV. = -6.2 DEGREES
REMARK 500 TRP A 83 CG - CD2 - CE3 ANGL. DEV. = 5.5 DEGREES
REMARK 500 TRP A 165 CD1 - CG - CD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 TRP A 165 CE2 - CD2 - CG ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG A 189 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 TRP A 244 CD1 - CG - CD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 TRP A 244 CE2 - CD2 - CG ANGL. DEV. = -5.8 DEGREES
REMARK 500 TRP A 263 CD1 - CG - CD2 ANGL. DEV. = 5.3 DEGREES
REMARK 500 TRP A 263 CE2 - CD2 - CG ANGL. DEV. = -5.2 DEGREES
REMARK 500 TRP A 369 CD1 - CG - CD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 TRP A 369 CE2 - CD2 - CG ANGL. DEV. = -5.2 DEGREES
REMARK 500 MET A 380 CG - SD - CE ANGL. DEV. = -12.0 DEGREES
REMARK 500 VAL A 389 N - CA - CB 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 ASN A 18 80.40 53.07
REMARK 500 ARG A 96 -47.31 70.82
REMARK 500 SER A 113 119.49 -38.64
REMARK 500 ASP A 148 80.05 -157.39
REMARK 500 GLU A 157 -143.13 -124.06
REMARK 500 ASP A 158 -169.36 67.54
REMARK 500 ASP A 221 75.21 18.39
REMARK 500 LYS A 230 53.73 -111.32
REMARK 500 THR A 237 -69.11 -122.47
REMARK 500 ASP A 259 67.41 34.13
REMARK 500 ARG A 292 58.17 -143.35
REMARK 500 ASP A 297 -97.00 -148.39
REMARK 500 ALA A 342 63.77 36.31
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 MG A 417 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 283 OD2
REMARK 620 2 ASP A 307 OD1 70.6
REMARK 620 3 ASP A 311 OD1 94.5 120.0
REMARK 620 4 ICT A 418 O2 132.0 77.0 132.7
REMARK 620 5 ICT A 418 O7 74.5 81.0 152.2 66.1
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 MG A 417
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ICT A 418
DBREF 1GRP A 1 416 UNP P08200 IDH_ECOLI 1 416
SEQADV 1GRP LEU A 115 UNP P08200 ASN 115 ENGINEERED MUTATION
SEQADV 1GRP ASP A 192 UNP P08200 GLU 192 CONFLICT
SEQRES 1 A 416 MET GLU SER LYS VAL VAL VAL PRO ALA GLN GLY LYS LYS
SEQRES 2 A 416 ILE THR LEU GLN ASN GLY LYS LEU ASN VAL PRO GLU ASN
SEQRES 3 A 416 PRO ILE ILE PRO TYR ILE GLU GLY ASP GLY ILE GLY VAL
SEQRES 4 A 416 ASP VAL THR PRO ALA MET LEU LYS VAL VAL ASP ALA ALA
SEQRES 5 A 416 VAL GLU LYS ALA TYR LYS GLY GLU ARG LYS ILE SER TRP
SEQRES 6 A 416 MET GLU ILE TYR THR GLY GLU LYS SER THR GLN VAL TYR
SEQRES 7 A 416 GLY GLN ASP VAL TRP LEU PRO ALA GLU THR LEU ASP LEU
SEQRES 8 A 416 ILE ARG GLU TYR ARG VAL ALA ILE LYS GLY PRO LEU THR
SEQRES 9 A 416 THR PRO VAL GLY GLY GLY ILE ARG SER LEU LEU VAL ALA
SEQRES 10 A 416 LEU ARG GLN GLU LEU ASP LEU TYR ILE CYS LEU ARG PRO
SEQRES 11 A 416 VAL ARG TYR TYR GLN GLY THR PRO SER PRO VAL LYS HIS
SEQRES 12 A 416 PRO GLU LEU THR ASP MET VAL ILE PHE ARG GLU ASN SER
SEQRES 13 A 416 GLU ASP ILE TYR ALA GLY ILE GLU TRP LYS ALA ASP SER
SEQRES 14 A 416 ALA ASP ALA GLU LYS VAL ILE LYS PHE LEU ARG GLU GLU
SEQRES 15 A 416 MET GLY VAL LYS LYS ILE ARG PHE PRO ASP HIS CYS GLY
SEQRES 16 A 416 ILE GLY ILE LYS PRO CYS SER GLU GLU GLY THR LYS ARG
SEQRES 17 A 416 LEU VAL ARG ALA ALA ILE GLU TYR ALA ILE ALA ASN ASP
SEQRES 18 A 416 ARG ASP SER VAL THR LEU VAL HIS LYS GLY ASN ILE MET
SEQRES 19 A 416 LYS PHE THR GLU GLY ALA PHE LYS ASP TRP GLY TYR GLN
SEQRES 20 A 416 LEU ALA ARG GLU GLU PHE GLY GLY GLU LEU ILE ASP GLY
SEQRES 21 A 416 GLY PRO TRP LEU LYS VAL LYS ASN PRO ASN THR GLY LYS
SEQRES 22 A 416 GLU ILE VAL ILE LYS ASP VAL ILE ALA ASP ALA PHE LEU
SEQRES 23 A 416 GLN GLN ILE LEU LEU ARG PRO ALA GLU TYR ASP VAL ILE
SEQRES 24 A 416 ALA CYS MET ASN LEU ASN GLY ASP TYR ILE SER ASP ALA
SEQRES 25 A 416 LEU ALA ALA GLN VAL GLY GLY ILE GLY ILE ALA PRO GLY
SEQRES 26 A 416 ALA ASN ILE GLY ASP GLU CYS ALA LEU PHE GLU ALA THR
SEQRES 27 A 416 HIS GLY THR ALA PRO LYS TYR ALA GLY GLN ASP LYS VAL
SEQRES 28 A 416 ASN PRO GLY SER ILE ILE LEU SER ALA GLU MET MET LEU
SEQRES 29 A 416 ARG HIS MET GLY TRP THR GLU ALA ALA ASP LEU ILE VAL
SEQRES 30 A 416 LYS GLY MET GLU GLY ALA ILE ASN ALA LYS THR VAL THR
SEQRES 31 A 416 TYR ASP PHE GLU ARG LEU MET ASP GLY ALA LYS LEU LEU
SEQRES 32 A 416 LYS CYS SER GLU PHE GLY ASP ALA ILE ILE GLU ASN MET
HET MG A 417 1
HET ICT A 418 13
HETNAM MG MAGNESIUM ION
HETNAM ICT ISOCITRIC ACID
FORMUL 2 MG MG 2+
FORMUL 3 ICT C6 H8 O7
HELIX 1 HA ILE A 37 LYS A 58 5 22
HELIX 2 HB THR A 70 TYR A 78 1 9
HELIX 3 HC PRO A 85 TYR A 95 1 11
HELIX 4 HD SER A 113 LEU A 124 1 12
HELIX 5 HE1 PRO A 144 LEU A 146 5 3
HELIX 6 HE2 ASP A 158 ALA A 161 5 4
HELIX 7 HE ASP A 168 MET A 183 1 16
HELIX 8 HF GLU A 203 ARG A 222 1 20
HELIX 9 HG LYS A 235 PHE A 253 1 19
HELIX 10 HH ILE A 281 LEU A 291 1 11
HELIX 11 HH1 PRO A 293 GLU A 295 5 3
HELIX 12 HI ASN A 303 VAL A 317 1 15
HELIX 13 HJ PRO A 353 MET A 367 1 15
HELIX 14 HK TRP A 369 THR A 388 1 20
HELIX 15 HL THR A 390 MET A 397 1 8
HELIX 16 HM LYS A 404 ASN A 415 1 12
SHEET 1 A 2 THR A 15 GLN A 17 0
SHEET 2 A 2 LYS A 20 ASN A 22 -1 N ASN A 22 O THR A 15
SHEET 1 S112 ARG A 61 ILE A 68 0
SHEET 2 S112 GLU A 25 ILE A 32 1 N ILE A 29 O SER A 64
SHEET 3 S112 ARG A 96 LYS A 100 1 N ILE A 99 O PRO A 30
SHEET 4 S112 ALA A 333 GLU A 336 1 N ALA A 333 O ALA A 98
SHEET 5 S112 GLY A 325 ILE A 328 -1 N ASN A 327 O LEU A 334
SHEET 6 S112 TYR A 125 ARG A 132 -1 N LEU A 128 O ALA A 326
SHEET 7 S112 THR A 147 ARG A 153 -1 N ARG A 153 O CYS A 127
SHEET 8 S112 ASP A 297 MET A 302 1 N ILE A 299 O VAL A 150
SHEET 9 S112 SER A 224 HIS A 229 1 N THR A 226 O VAL A 298
SHEET 10 S112 LYS A 273 VAL A 280 1 N VAL A 276 O VAL A 225
SHEET 11 S112 LEU A 264 LYS A 267 -1 N VAL A 266 O ILE A 275
SHEET 12 S112 GLY A 254 GLU A 256 -1
SHEET 1 C 2 THR A 388 THR A 390 0
SHEET 2 C 2 LYS A 401 LEU A 403 1 N LYS A 401 O VAL A 389
SHEET 1 S2 2 ILE A 163 ALA A 167 0
SHEET 2 S2 2 HIS A 193 SER A 202 -1
LINK OD2 ASP A 283 MG MG A 417 7555 1555 2.55
LINK OD1 ASP A 307 MG MG A 417 1555 1555 2.47
LINK OD1 ASP A 311 MG MG A 417 1555 1555 3.12
LINK MG MG A 417 O2 ICT A 418 1555 1555 2.37
LINK MG MG A 417 O7 ICT A 418 1555 1555 2.47
CISPEP 1 GLY A 261 PRO A 262 0 5.16
SITE 1 AC1 4 ASP A 283 ASP A 307 ASP A 311 ICT A 418
SITE 1 AC2 11 SER A 113 LEU A 115 ARG A 119 ARG A 129
SITE 2 AC2 11 ARG A 153 TYR A 160 LYS A 230 ILE A 233
SITE 3 AC2 11 ASP A 283 ASP A 307 MG A 417
CRYST1 105.100 105.100 150.600 90.00 90.00 90.00 P 43 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 0.009515 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009515 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006640 0.00000
(ATOM LINES ARE NOT SHOWN.)
END