HEADER DEHYDRATASE 11-JUN-02 1H05
TITLE 3-DEHYDROQUINATE DEHYDRATASE FROM MYCOBACTERIUM TUBERCULOSIS IN
TITLE 2 COMPLEX WITH SULPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-DEHYDROQUINATE DEHYDRATASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 3-DEHYDROQUINASE, TYPE 2 DHQASE;
COMPND 5 EC: 4.2.1.10;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET-15B;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: MPET
KEYWDS DEHYDRATASE, SHIKIMATE PATHWAY, ALPHA/BETA PROTEIN, LYASE, AROMATIC
KEYWDS 2 AMINO ACID BIOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR A.W.ROSZAK,J.R.COGGINS,A.J.LAPTHORN
REVDAT 4 13-DEC-23 1H05 1 REMARK
REVDAT 3 24-FEB-09 1H05 1 VERSN
REVDAT 2 05-DEC-02 1H05 1 AUTHOR
REVDAT 1 24-OCT-02 1H05 0
JRNL AUTH L.EVANS,A.W.ROSZAK,L.NOBLE,D.ROBINSON,P.CHALK,J.MATTHEWS,
JRNL AUTH 2 J.R.COGGINS,N.PRICE,A.J.LAPTHORN
JRNL TITL SPECIFICITY OF SUBSTRATE RECOGNITION BY TYPE II
JRNL TITL 2 DEHYDROQUINASES AS REVEALED BY BINDING OF POLYANIONS(1)
JRNL REF FEBS LETT. V. 530 24 2002
JRNL REFN ISSN 0014-5793
JRNL PMID 12387860
JRNL DOI 10.1016/S0014-5793(02)03346-X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.G.GOURLEY,A.K.SHRIVE,I.POLIKARPOV,T.KRELL,J.R.COGGINS,
REMARK 1 AUTH 2 A.R.HAWKINS,N.W.ISAACS,L.SAWYER
REMARK 1 TITL THE TWO TYPES OF 3-DEHYDROQUINASE HAVE DIFFERENT STRUCTURES
REMARK 1 TITL 2 BUT CATALYZE THE SAME OVERALL REACTION
REMARK 1 REF NAT.STRUCT.BIOL. V. 6 521 1999
REMARK 1 REFN ISSN 1072-8368
REMARK 1 PMID 10360352
REMARK 1 DOI 10.1038/9287
REMARK 2
REMARK 2 RESOLUTION. 1.50 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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.9
REMARK 3 NUMBER OF REFLECTIONS : 24274
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) : 0.139
REMARK 3 FREE R VALUE : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2427
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1045
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 200
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.10
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): 0.089
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.080
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
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 1H05 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-JUN-02.
REMARK 100 THE DEPOSITION ID IS D_1290009965.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-FEB-99
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX9.6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.87
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24274
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.9
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.03900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 32.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.83200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 2DHQ
REMARK 200
REMARK 200 REMARK: LOW COMPLETENESS AND REDUNDANCY IN HIGHEST RESOLUTION
REMARK 200 SHELL AS DATA WERE PROCESSED TO CORNERS OF CCD DETECTOR
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% MPD, 0.5M AMMONIUM SULPHATE 0.1M
REMARK 280 HEPES PH 7.5, PH 7.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 2 3
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 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 X,Y+1/2,Z+1/2
REMARK 290 14555 -X,-Y+1/2,Z+1/2
REMARK 290 15555 -X,Y+1/2,-Z+1/2
REMARK 290 16555 X,-Y+1/2,-Z+1/2
REMARK 290 17555 Z,X+1/2,Y+1/2
REMARK 290 18555 Z,-X+1/2,-Y+1/2
REMARK 290 19555 -Z,-X+1/2,Y+1/2
REMARK 290 20555 -Z,X+1/2,-Y+1/2
REMARK 290 21555 Y,Z+1/2,X+1/2
REMARK 290 22555 -Y,Z+1/2,-X+1/2
REMARK 290 23555 Y,-Z+1/2,-X+1/2
REMARK 290 24555 -Y,-Z+1/2,X+1/2
REMARK 290 25555 X+1/2,Y,Z+1/2
REMARK 290 26555 -X+1/2,-Y,Z+1/2
REMARK 290 27555 -X+1/2,Y,-Z+1/2
REMARK 290 28555 X+1/2,-Y,-Z+1/2
REMARK 290 29555 Z+1/2,X,Y+1/2
REMARK 290 30555 Z+1/2,-X,-Y+1/2
REMARK 290 31555 -Z+1/2,-X,Y+1/2
REMARK 290 32555 -Z+1/2,X,-Y+1/2
REMARK 290 33555 Y+1/2,Z,X+1/2
REMARK 290 34555 -Y+1/2,Z,-X+1/2
REMARK 290 35555 Y+1/2,-Z,-X+1/2
REMARK 290 36555 -Y+1/2,-Z,X+1/2
REMARK 290 37555 X+1/2,Y+1/2,Z
REMARK 290 38555 -X+1/2,-Y+1/2,Z
REMARK 290 39555 -X+1/2,Y+1/2,-Z
REMARK 290 40555 X+1/2,-Y+1/2,-Z
REMARK 290 41555 Z+1/2,X+1/2,Y
REMARK 290 42555 Z+1/2,-X+1/2,-Y
REMARK 290 43555 -Z+1/2,-X+1/2,Y
REMARK 290 44555 -Z+1/2,X+1/2,-Y
REMARK 290 45555 Y+1/2,Z+1/2,X
REMARK 290 46555 -Y+1/2,Z+1/2,-X
REMARK 290 47555 Y+1/2,-Z+1/2,-X
REMARK 290 48555 -Y+1/2,-Z+1/2,X
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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 63.31750
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 63.31750
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 63.31750
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 63.31750
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 63.31750
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 63.31750
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 63.31750
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 63.31750
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 63.31750
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 63.31750
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 63.31750
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 63.31750
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 63.31750
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 63.31750
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 63.31750
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 63.31750
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 63.31750
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 63.31750
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 63.31750
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 63.31750
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 63.31750
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 63.31750
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 63.31750
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 63.31750
REMARK 290 SMTRY1 25 1.000000 0.000000 0.000000 63.31750
REMARK 290 SMTRY2 25 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 25 0.000000 0.000000 1.000000 63.31750
REMARK 290 SMTRY1 26 -1.000000 0.000000 0.000000 63.31750
REMARK 290 SMTRY2 26 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 26 0.000000 0.000000 1.000000 63.31750
REMARK 290 SMTRY1 27 -1.000000 0.000000 0.000000 63.31750
REMARK 290 SMTRY2 27 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 27 0.000000 0.000000 -1.000000 63.31750
REMARK 290 SMTRY1 28 1.000000 0.000000 0.000000 63.31750
REMARK 290 SMTRY2 28 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 28 0.000000 0.000000 -1.000000 63.31750
REMARK 290 SMTRY1 29 0.000000 0.000000 1.000000 63.31750
REMARK 290 SMTRY2 29 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 29 0.000000 1.000000 0.000000 63.31750
REMARK 290 SMTRY1 30 0.000000 0.000000 1.000000 63.31750
REMARK 290 SMTRY2 30 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 30 0.000000 -1.000000 0.000000 63.31750
REMARK 290 SMTRY1 31 0.000000 0.000000 -1.000000 63.31750
REMARK 290 SMTRY2 31 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 31 0.000000 1.000000 0.000000 63.31750
REMARK 290 SMTRY1 32 0.000000 0.000000 -1.000000 63.31750
REMARK 290 SMTRY2 32 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 32 0.000000 -1.000000 0.000000 63.31750
REMARK 290 SMTRY1 33 0.000000 1.000000 0.000000 63.31750
REMARK 290 SMTRY2 33 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 33 1.000000 0.000000 0.000000 63.31750
REMARK 290 SMTRY1 34 0.000000 -1.000000 0.000000 63.31750
REMARK 290 SMTRY2 34 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 34 -1.000000 0.000000 0.000000 63.31750
REMARK 290 SMTRY1 35 0.000000 1.000000 0.000000 63.31750
REMARK 290 SMTRY2 35 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 35 -1.000000 0.000000 0.000000 63.31750
REMARK 290 SMTRY1 36 0.000000 -1.000000 0.000000 63.31750
REMARK 290 SMTRY2 36 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 36 1.000000 0.000000 0.000000 63.31750
REMARK 290 SMTRY1 37 1.000000 0.000000 0.000000 63.31750
REMARK 290 SMTRY2 37 0.000000 1.000000 0.000000 63.31750
REMARK 290 SMTRY3 37 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 38 -1.000000 0.000000 0.000000 63.31750
REMARK 290 SMTRY2 38 0.000000 -1.000000 0.000000 63.31750
REMARK 290 SMTRY3 38 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 39 -1.000000 0.000000 0.000000 63.31750
REMARK 290 SMTRY2 39 0.000000 1.000000 0.000000 63.31750
REMARK 290 SMTRY3 39 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 40 1.000000 0.000000 0.000000 63.31750
REMARK 290 SMTRY2 40 0.000000 -1.000000 0.000000 63.31750
REMARK 290 SMTRY3 40 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 41 0.000000 0.000000 1.000000 63.31750
REMARK 290 SMTRY2 41 1.000000 0.000000 0.000000 63.31750
REMARK 290 SMTRY3 41 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 42 0.000000 0.000000 1.000000 63.31750
REMARK 290 SMTRY2 42 -1.000000 0.000000 0.000000 63.31750
REMARK 290 SMTRY3 42 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 43 0.000000 0.000000 -1.000000 63.31750
REMARK 290 SMTRY2 43 -1.000000 0.000000 0.000000 63.31750
REMARK 290 SMTRY3 43 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 44 0.000000 0.000000 -1.000000 63.31750
REMARK 290 SMTRY2 44 1.000000 0.000000 0.000000 63.31750
REMARK 290 SMTRY3 44 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 45 0.000000 1.000000 0.000000 63.31750
REMARK 290 SMTRY2 45 0.000000 0.000000 1.000000 63.31750
REMARK 290 SMTRY3 45 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 46 0.000000 -1.000000 0.000000 63.31750
REMARK 290 SMTRY2 46 0.000000 0.000000 1.000000 63.31750
REMARK 290 SMTRY3 46 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 47 0.000000 1.000000 0.000000 63.31750
REMARK 290 SMTRY2 47 0.000000 0.000000 -1.000000 63.31750
REMARK 290 SMTRY3 47 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 48 0.000000 -1.000000 0.000000 63.31750
REMARK 290 SMTRY2 48 0.000000 0.000000 -1.000000 63.31750
REMARK 290 SMTRY3 48 1.000000 0.000000 0.000000 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: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
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 -1.000000 0.000000 0.000000 63.31750
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 63.31750
REMARK 350 BIOMT1 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 63.31750
REMARK 350 BIOMT3 3 0.000000 1.000000 0.000000 -63.31750
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 -63.31750
REMARK 350 BIOMT2 4 0.000000 0.000000 1.000000 63.31750
REMARK 350 BIOMT3 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 5 0.000000 0.000000 -1.000000 63.31750
REMARK 350 BIOMT2 5 -1.000000 0.000000 0.000000 126.63500
REMARK 350 BIOMT3 5 0.000000 1.000000 0.000000 -63.31750
REMARK 350 BIOMT1 6 0.000000 1.000000 0.000000 -63.31750
REMARK 350 BIOMT2 6 0.000000 0.000000 -1.000000 126.63500
REMARK 350 BIOMT3 6 -1.000000 0.000000 0.000000 63.31750
REMARK 350 BIOMT1 7 0.000000 0.000000 -1.000000 63.31750
REMARK 350 BIOMT2 7 1.000000 0.000000 0.000000 63.31750
REMARK 350 BIOMT3 7 0.000000 -1.000000 0.000000 126.63500
REMARK 350 BIOMT1 8 0.000000 -1.000000 0.000000 126.63500
REMARK 350 BIOMT2 8 0.000000 0.000000 1.000000 63.31750
REMARK 350 BIOMT3 8 -1.000000 0.000000 0.000000 63.31750
REMARK 350 BIOMT1 9 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 9 -1.000000 0.000000 0.000000 126.63500
REMARK 350 BIOMT3 9 0.000000 -1.000000 0.000000 126.63500
REMARK 350 BIOMT1 10 0.000000 -1.000000 0.000000 126.63500
REMARK 350 BIOMT2 10 0.000000 0.000000 -1.000000 126.63500
REMARK 350 BIOMT3 10 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 11 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 11 0.000000 -1.000000 0.000000 189.95250
REMARK 350 BIOMT3 11 0.000000 0.000000 -1.000000 63.31750
REMARK 350 BIOMT1 12 -1.000000 0.000000 0.000000 63.31750
REMARK 350 BIOMT2 12 0.000000 -1.000000 0.000000 189.95250
REMARK 350 BIOMT3 12 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 S SO4 A 202 LIES ON A SPECIAL POSITION.
REMARK 375 O1 SO4 A 202 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2031 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2045 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2127 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2150 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2178 LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400 CATALYZES TRANS-DEHYDRATION VIA AN ENOLATE
REMARK 400 INTERMEDIATE.
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 SER A 1
REMARK 465 GLU A 2
REMARK 465 GLU A 20
REMARK 465 PRO A 21
REMARK 465 ALA A 22
REMARK 465 VAL A 23
REMARK 465 TYR A 24
REMARK 465 GLY A 25
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 O HOH A 2003 O HOH A 2118 2.17
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 A 15 NH1 - CZ - NH2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ARG A 15 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 15 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ASP A 30 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 GLU A 31 OE1 - CD - OE2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 GLU A 31 CG - CD - OE1 ANGL. DEV. = 13.5 DEGREES
REMARK 500 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG A 38 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 50 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG A 50 NE - CZ - NH2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 ASP A 53 CB - CG - OD1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 GLU A 55 OE1 - CD - OE2 ANGL. DEV. = 12.5 DEGREES
REMARK 500 GLU A 92 CG - CD - OE2 ANGL. DEV. = -13.9 DEGREES
REMARK 500 ARG A 108 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG A 108 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ARG A 112 NH1 - CZ - NH2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ARG A 112 NE - CZ - NH2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 ARG A 113 NH1 - CZ - NH2 ANGL. DEV. = 9.6 DEGREES
REMARK 500 ARG A 113 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 113 NE - CZ - NH1 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ARG A 113 NE - CZ - NH2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 ARG A 113 O - C - N ANGL. DEV. = -11.6 DEGREES
REMARK 500 HIS A 114 CA - CB - CG ANGL. DEV. = -11.4 DEGREES
REMARK 500 LEU A 135 O - C - N ANGL. DEV. = -10.1 DEGREES
REMARK 500 HIS A 143 CA - CB - CG ANGL. DEV. = -11.0 DEGREES
REMARK 500 VAL A 144 CA - CB - CG2 ANGL. DEV. = 12.4 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 12 -4.14 77.47
REMARK 500 ARG A 108 -141.51 -119.65
REMARK 500 HIS A 143 51.34 -113.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2009 DISTANCE = 7.07 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 204
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2DHQ RELATED DB: PDB
REMARK 900 3-DEHYDROQUINATE DEHYDRATASE FROM MYCOBACTERIUM TUBERCULOSIS
DBREF 1H05 A 1 146 UNP P36918 AROQ_MYCTU 1 146
SEQRES 1 A 146 SER GLU LEU ILE VAL ASN VAL ILE ASN GLY PRO ASN LEU
SEQRES 2 A 146 GLY ARG LEU GLY ARG ARG GLU PRO ALA VAL TYR GLY GLY
SEQRES 3 A 146 THR THR HIS ASP GLU LEU VAL ALA LEU ILE GLU ARG GLU
SEQRES 4 A 146 ALA ALA GLU LEU GLY LEU LYS ALA VAL VAL ARG GLN SER
SEQRES 5 A 146 ASP SER GLU ALA GLN LEU LEU ASP TRP ILE HIS GLN ALA
SEQRES 6 A 146 ALA ASP ALA ALA GLU PRO VAL ILE LEU ASN ALA GLY GLY
SEQRES 7 A 146 LEU THR HIS THR SER VAL ALA LEU ARG ASP ALA CYS ALA
SEQRES 8 A 146 GLU LEU SER ALA PRO LEU ILE GLU VAL HIS ILE SER ASN
SEQRES 9 A 146 VAL HIS ALA ARG GLU GLU PHE ARG ARG HIS SER TYR LEU
SEQRES 10 A 146 SER PRO ILE ALA THR GLY VAL ILE VAL GLY LEU GLY ILE
SEQRES 11 A 146 GLN GLY TYR LEU LEU ALA LEU ARG TYR LEU ALA GLU HIS
SEQRES 12 A 146 VAL GLY THR
HET SO4 A 201 5
HET SO4 A 202 5
HET SO4 A 203 5
HET SO4 A 204 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 4(O4 S 2-)
FORMUL 6 HOH *200(H2 O)
HELIX 1 1 ASN A 12 LEU A 16 5 5
HELIX 2 2 THR A 28 LEU A 43 1 16
HELIX 3 3 SER A 54 ALA A 69 1 16
HELIX 4 4 ALA A 76 THR A 82 5 7
HELIX 5 5 SER A 83 GLU A 92 1 10
HELIX 6 6 ASN A 104 ARG A 108 5 5
HELIX 7 7 GLU A 109 HIS A 114 5 6
HELIX 8 8 LEU A 117 ALA A 121 5 5
HELIX 9 9 ILE A 130 HIS A 143 1 14
SHEET 1 AA 5 LYS A 46 GLN A 51 0
SHEET 2 AA 5 ILE A 4 ASN A 9 1 O VAL A 5 N VAL A 48
SHEET 3 AA 5 VAL A 72 ASN A 75 1 O ILE A 73 N ILE A 8
SHEET 4 AA 5 LEU A 97 HIS A 101 1 O ILE A 98 N LEU A 74
SHEET 5 AA 5 GLY A 123 VAL A 126 1 O GLY A 123 N GLU A 99
SITE 1 AC1 9 ARG A 19 ASN A 75 ILE A 102 SER A 103
SITE 2 AC1 9 HOH A2119 HOH A2191 HOH A2192 HOH A2193
SITE 3 AC1 9 HOH A2194
SITE 1 AC2 3 SER A 54 HOH A2095 HOH A2195
SITE 1 AC3 5 ARG A 50 TRP A 61 GLN A 64 HOH A2101
SITE 2 AC3 5 HOH A2197
SITE 1 AC4 6 ARG A 15 LEU A 16 GLY A 17 ARG A 19
SITE 2 AC4 6 HOH A2199 HOH A2200
CRYST1 126.635 126.635 126.635 90.00 90.00 90.00 F 2 3 48
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 0.007897 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007897 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007897 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
