HEADER LYASE 25-AUG-04 1XAH
TITLE CRYSTAL STRUCTURE OF STAPHLYOCOCCUS AUREUS 3-DEHYDROQUINATE SYNTHASE
TITLE 2 (DHQS) IN COMPLEX WITH ZN2+ AND NAD+
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-DEHYDROQUINATE SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: SADHQS;
COMPND 5 EC: 4.2.3.4;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280;
SOURCE 4 GENE: AROB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3 PLYSS);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMUT27
KEYWDS SHIKIMATE PATHWAY, AROMATIC AMINO ACID BIOSYNTHESIS, DHQS, SADHQS,
KEYWDS 2 OPEN FORM, FORM B, DOMAIN MOVEMENT, CYCLASE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.E.NICHOLS,J.REN,K.LESLIE,B.DHALIWAL,M.LOCKYER,I.CHARLES,
AUTHOR 2 A.R.HAWKINS,D.K.STAMMERS
REVDAT 4 23-AUG-23 1XAH 1 REMARK LINK
REVDAT 3 24-FEB-09 1XAH 1 VERSN
REVDAT 2 22-MAR-05 1XAH 1 JRNL
REVDAT 1 01-MAR-05 1XAH 0
JRNL AUTH C.E.NICHOLS,J.REN,K.LESLIE,B.DHALIWAL,M.LOCKYER,I.CHARLES,
JRNL AUTH 2 A.R.HAWKINS,D.K.STAMMERS
JRNL TITL COMPARISON OF LIGAND INDUCED CONFORMATIONAL CHANGES AND
JRNL TITL 2 DOMAIN CLOSURE MECHANISMS, BETWEEN PROKARYOTIC AND
JRNL TITL 3 EUKARYOTIC DEHYDROQUINATE SYNTHASES.
JRNL REF J.MOL.BIOL. V. 343 533 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15465043
JRNL DOI 10.1016/J.JMB.2004.08.039
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.18
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2449728.300
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 34989
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 SET) : 0.210
REMARK 3 FREE R VALUE : 0.281
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 3475
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.24
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1588
REMARK 3 BIN R VALUE (WORKING SET) : 0.3410
REMARK 3 BIN FREE R VALUE : 0.3300
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 8.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 140
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.028
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5230
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 90
REMARK 3 SOLVENT ATOMS : 176
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.22000
REMARK 3 B22 (A**2) : 5.22000
REMARK 3 B33 (A**2) : -10.43000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.31
REMARK 3 ESD FROM SIGMAA (A) : 0.42
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.39
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.39
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.700
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 80.61
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : LIG.PAR
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : LIG.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : WATER_REP.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XAH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-NOV-04.
REMARK 100 THE DEPOSITION ID IS D_1000030139.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAY-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 4
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC MULTILAYER OPTICS
REMARK 200 OPTICS : OSMIC MULTILAYER
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34989
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 12.50
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.2200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.24
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 11.20
REMARK 200 R MERGE FOR SHELL (I) : 0.55900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.380
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1NR5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, KCL, PH 8.0, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43
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,X,Z+3/4
REMARK 290 4555 Y,-X,Z+1/4
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 116.43500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 174.65250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 58.21750
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: MONOMERIC
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 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 ASP A 52
REMARK 465 ILE A 53
REMARK 465 LEU A 54
REMARK 465 SER A 55
REMARK 465 TYR A 56
REMARK 465 GLU A 57
REMARK 465 MET A 297
REMARK 465 ILE A 298
REMARK 465 THR A 299
REMARK 465 ASP A 300
REMARK 465 LEU A 301
REMARK 465 ASP A 302
REMARK 465 PHE A 303
REMARK 465 GLU A 304
REMARK 465 THR A 305
REMARK 465 LEU A 306
REMARK 465 TYR A 307
REMARK 465 GLN A 308
REMARK 465 TYR A 309
REMARK 465 MET A 310
REMARK 465 LEU A 311
REMARK 465 SER A 312
REMARK 465 ASP A 313
REMARK 465 LYS A 314
REMARK 465 LYS A 315
REMARK 465 ASN A 316
REMARK 465 ASP A 317
REMARK 465 LYS A 318
REMARK 465 GLN A 319
REMARK 465 PHE A 353
REMARK 465 LYS A 354
REMARK 465 ASP B 52
REMARK 465 ILE B 53
REMARK 465 LEU B 54
REMARK 465 SER B 55
REMARK 465 TYR B 56
REMARK 465 GLU B 57
REMARK 465 MET B 297
REMARK 465 ILE B 298
REMARK 465 THR B 299
REMARK 465 ASP B 300
REMARK 465 LEU B 301
REMARK 465 ASP B 302
REMARK 465 PHE B 303
REMARK 465 GLU B 304
REMARK 465 SER B 312
REMARK 465 ASP B 313
REMARK 465 LYS B 314
REMARK 465 LYS B 315
REMARK 465 ASN B 316
REMARK 465 ASP B 317
REMARK 465 LYS B 318
REMARK 465 GLN B 319
REMARK 465 PHE B 353
REMARK 465 LYS B 354
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 A 6 59.23 -118.92
REMARK 500 LEU A 28 -28.37 -30.51
REMARK 500 GLN A 30 23.99 -79.33
REMARK 500 PRO A 65 167.18 -49.95
REMARK 500 HIS A 87 72.30 30.50
REMARK 500 VAL A 117 -169.64 -108.88
REMARK 500 ASN A 146 66.81 18.49
REMARK 500 ALA A 247 -75.81 -70.17
REMARK 500 LYS A 253 37.41 39.29
REMARK 500 LEU A 274 -71.07 -70.57
REMARK 500 LEU A 295 71.03 -103.17
REMARK 500 MET A 323 133.70 173.93
REMARK 500 ASN B 10 68.73 60.66
REMARK 500 THR B 26 -17.09 -49.27
REMARK 500 LEU B 28 -24.15 -34.30
REMARK 500 GLN B 30 25.68 -75.10
REMARK 500 ASP B 32 -72.44 -59.74
REMARK 500 HIS B 86 20.04 -79.80
REMARK 500 HIS B 87 70.57 38.64
REMARK 500 ASN B 91 40.62 -106.55
REMARK 500 VAL B 117 -166.46 -114.41
REMARK 500 ASN B 146 71.00 23.07
REMARK 500 LEU B 161 -9.48 -58.12
REMARK 500 ALA B 247 -71.73 -71.52
REMARK 500 LYS B 253 39.73 38.04
REMARK 500 LEU B 295 55.94 -107.22
REMARK 500 MET B 323 131.73 -172.31
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 ZN A 600 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 178 OE1
REMARK 620 2 HIS A 242 NE2 81.3
REMARK 620 3 HIS A 256 NE2 86.9 97.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 178 OE1
REMARK 620 2 HIS B 242 NE2 82.0
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1NR5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 3-DEHYDROQUINATE SYNTHASE (DHQS) IN COMPLEX
REMARK 900 WITH ZN2+, NAD+ AND CARBAPHOSPHONATE, CRYSTAL FORM C, CLOSED FORM
REMARK 900 WITH COFACTOR AND SUBSTRATE ANALOGUE
REMARK 900 RELATED ID: 1NRX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 3-DEHYDROQUINATE SYNTHASE (DHQS) IN COMPLEX
REMARK 900 WITH ZN2+ AND NAD+, CRYSTAL FORM F, OPEN FORM WITH COFACTOR
REMARK 900 RELATED ID: 1NVE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 3-DEHYDROQUINATE SYNTHASE (DHQS) IN COMPLEX
REMARK 900 WITH ZN2+ AND NAD+, CRYSTAL FORM E, OPEN FORM WITH CO-FACTOR
REMARK 900 RELATED ID: 1NVD RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 3-DEHYDROQUINATE SYNTHASE (DHQS) IN COMPLEX
REMARK 900 WITH ZN2+ AND CARBAPHOSPHONATE, CRYSTAL FORM B, CLOSED FORM WITH
REMARK 900 SUBSTRATE ANALOGUE
REMARK 900 RELATED ID: 1NVB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 3-DEHYDROQUINATE SYNTHASE (DHQS) IN COMPLEX
REMARK 900 WITH ZN2+ AND CARBAPHOSPHONATE, CRYSTAL FORM C, CLOSED FORM WITH
REMARK 900 SUBSTRATE ANALOGUE
REMARK 900 RELATED ID: 1NUA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 3-DEHYDROQUINATE SYNTHASE (DHQS) IN COMPLEX
REMARK 900 WITH ZN2+, APO, CRYSTAL FORM D, OPEN FORM
REMARK 900 RELATED ID: 1NVA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 3-DEHYDROQUINATE SYNTHASE (DHQS) IN COMPLEX
REMARK 900 WITH ZN2+ AND ADP, CRYSTAL FORM D, OPEN FORM WITH CO-FACTOR ANALOGUE
REMARK 900 RELATED ID: 1NVF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 3-DEHYDROQUINATE SYNTHASE (DHQS) IN COMPLEX
REMARK 900 WITH ZN2+, ADP AND CBP, CRYSTAL FORM H, CLOSED FORM WITH CO-FACTOR
REMARK 900 ANALOGUE AND SUBSTRATE ANALOGUE
REMARK 900 RELATED ID: 1XAG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF STAPHLYOCOCCUS AUREUS 3-DEHYDROQUINATE
REMARK 900 SYNTHASE (DHQS) IN COMPLEX WITH ZN2+ AND CAR
REMARK 900 RELATED ID: 1XAI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF STAPHLYOCOCCUS AUREUS 3-DEHYDROQUINATE
REMARK 900 SYNTHASE (DHQS) IN COMPLEX WITH ZN2+, NAD+ AND CARBAPHOSPHONATE
REMARK 900 RELATED ID: 1XAJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF STAPHLYOCOCCUS AUREUS 3-DEHYDROQUINATE
REMARK 900 SYNTHASE (DHQS) IN COMPLEX WITH ZN2+, NAD+ AND CARBAPHOSPHONATE
REMARK 900 RELATED ID: 1XAL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF STAPHLYOCOCCUS AUREUS 3-DEHYDROQUINATE
REMARK 900 SYNTHASE (DHQS) IN COMPLEX WITH ZN2+, NAD+ AND CARBAPHOSPHONATE
REMARK 900 (SOAK)
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THESE CONFLICTS REFLECT CLONAL VARIATION FROM DATABASE SEQUENCE.
DBREF 1XAH A 1 354 UNP Q6GGU4 AROB_STAAR 1 354
DBREF 1XAH B 1 354 UNP Q6GGU4 AROB_STAAR 1 354
SEQADV 1XAH LYS A 22 UNP Q6GGU4 ASP 22 SEE REMARK 999
SEQADV 1XAH TYR A 23 UNP Q6GGU4 HIS 23 SEE REMARK 999
SEQADV 1XAH GLY A 25 UNP Q6GGU4 SER 25 SEE REMARK 999
SEQADV 1XAH LEU A 28 UNP Q6GGU4 ILE 28 SEE REMARK 999
SEQADV 1XAH ASN A 29 UNP Q6GGU4 ASP 29 SEE REMARK 999
SEQADV 1XAH LEU A 36 UNP Q6GGU4 ILE 36 SEE REMARK 999
SEQADV 1XAH TYR A 41 UNP Q6GGU4 HIS 41 SEE REMARK 999
SEQADV 1XAH ASN A 48 UNP Q6GGU4 ASP 48 SEE REMARK 999
SEQADV 1XAH VAL A 109 UNP Q6GGU4 ILE 109 SEE REMARK 999
SEQADV 1XAH LYS A 170 UNP Q6GGU4 GLU 170 SEE REMARK 999
SEQADV 1XAH VAL A 226 UNP Q6GGU4 ILE 226 SEE REMARK 999
SEQADV 1XAH SER A 282 UNP Q6GGU4 ASN 282 SEE REMARK 999
SEQADV 1XAH MET A 326 UNP Q6GGU4 ILE 326 SEE REMARK 999
SEQADV 1XAH LYS B 22 UNP Q6GGU4 ASP 22 SEE REMARK 999
SEQADV 1XAH TYR B 23 UNP Q6GGU4 HIS 23 SEE REMARK 999
SEQADV 1XAH GLY B 25 UNP Q6GGU4 SER 25 SEE REMARK 999
SEQADV 1XAH LEU B 28 UNP Q6GGU4 ILE 28 SEE REMARK 999
SEQADV 1XAH ASN B 29 UNP Q6GGU4 ASP 29 SEE REMARK 999
SEQADV 1XAH LEU B 36 UNP Q6GGU4 ILE 36 SEE REMARK 999
SEQADV 1XAH TYR B 41 UNP Q6GGU4 HIS 41 SEE REMARK 999
SEQADV 1XAH ASN B 48 UNP Q6GGU4 ASP 48 SEE REMARK 999
SEQADV 1XAH VAL B 109 UNP Q6GGU4 ILE 109 SEE REMARK 999
SEQADV 1XAH LYS B 170 UNP Q6GGU4 GLU 170 SEE REMARK 999
SEQADV 1XAH VAL B 226 UNP Q6GGU4 ILE 226 SEE REMARK 999
SEQADV 1XAH SER B 282 UNP Q6GGU4 ASN 282 SEE REMARK 999
SEQADV 1XAH MET B 326 UNP Q6GGU4 ILE 326 SEE REMARK 999
SEQRES 1 A 354 MET LYS LEU GLN THR THR TYR PRO SER ASN ASN TYR PRO
SEQRES 2 A 354 ILE TYR VAL GLU HIS GLY ALA ILE LYS TYR ILE GLY THR
SEQRES 3 A 354 TYR LEU ASN GLN PHE ASP GLN SER PHE LEU LEU ILE ASP
SEQRES 4 A 354 GLU TYR VAL ASN GLN TYR PHE ALA ASN LYS PHE ASP ASP
SEQRES 5 A 354 ILE LEU SER TYR GLU ASN VAL HIS LYS VAL ILE ILE PRO
SEQRES 6 A 354 ALA GLY GLU LYS THR LYS THR PHE GLU GLN TYR GLN GLU
SEQRES 7 A 354 THR LEU GLU TYR ILE LEU SER HIS HIS VAL THR ARG ASN
SEQRES 8 A 354 THR ALA ILE ILE ALA VAL GLY GLY GLY ALA THR GLY ASP
SEQRES 9 A 354 PHE ALA GLY PHE VAL ALA ALA THR LEU LEU ARG GLY VAL
SEQRES 10 A 354 HIS PHE ILE GLN VAL PRO THR THR ILE LEU ALA HIS ASP
SEQRES 11 A 354 SER SER VAL GLY GLY LYS VAL GLY ILE ASN SER LYS GLN
SEQRES 12 A 354 GLY LYS ASN LEU ILE GLY ALA PHE TYR ARG PRO THR ALA
SEQRES 13 A 354 VAL ILE TYR ASP LEU ASP PHE LEU LYS THR LEU PRO PHE
SEQRES 14 A 354 LYS GLN ILE LEU SER GLY TYR ALA GLU VAL TYR LYS HIS
SEQRES 15 A 354 ALA LEU LEU ASN GLY GLU SER ALA THR GLN ASP ILE GLU
SEQRES 16 A 354 GLN HIS PHE LYS ASP ARG GLU ILE LEU GLN SER LEU ASN
SEQRES 17 A 354 GLY MET ASP LYS TYR ILE ALA LYS GLY ILE GLU THR LYS
SEQRES 18 A 354 LEU ASP ILE VAL VAL ALA ASP GLU LYS GLU GLN GLY VAL
SEQRES 19 A 354 ARG LYS PHE LEU ASN LEU GLY HIS THR PHE GLY HIS ALA
SEQRES 20 A 354 VAL GLU TYR TYR HIS LYS ILE PRO HIS GLY HIS ALA VAL
SEQRES 21 A 354 MET VAL GLY ILE ILE TYR GLN PHE ILE VAL ALA ASN ALA
SEQRES 22 A 354 LEU PHE ASP SER LYS HIS ASP ILE SER HIS TYR ILE GLN
SEQRES 23 A 354 TYR LEU ILE GLN LEU GLY TYR PRO LEU ASP MET ILE THR
SEQRES 24 A 354 ASP LEU ASP PHE GLU THR LEU TYR GLN TYR MET LEU SER
SEQRES 25 A 354 ASP LYS LYS ASN ASP LYS GLN GLY VAL GLN MET VAL LEU
SEQRES 26 A 354 MET ARG GLN PHE GLY ASP ILE VAL VAL GLN HIS VAL ASP
SEQRES 27 A 354 GLN LEU THR LEU GLN HIS ALA CYS GLU GLN LEU LYS THR
SEQRES 28 A 354 TYR PHE LYS
SEQRES 1 B 354 MET LYS LEU GLN THR THR TYR PRO SER ASN ASN TYR PRO
SEQRES 2 B 354 ILE TYR VAL GLU HIS GLY ALA ILE LYS TYR ILE GLY THR
SEQRES 3 B 354 TYR LEU ASN GLN PHE ASP GLN SER PHE LEU LEU ILE ASP
SEQRES 4 B 354 GLU TYR VAL ASN GLN TYR PHE ALA ASN LYS PHE ASP ASP
SEQRES 5 B 354 ILE LEU SER TYR GLU ASN VAL HIS LYS VAL ILE ILE PRO
SEQRES 6 B 354 ALA GLY GLU LYS THR LYS THR PHE GLU GLN TYR GLN GLU
SEQRES 7 B 354 THR LEU GLU TYR ILE LEU SER HIS HIS VAL THR ARG ASN
SEQRES 8 B 354 THR ALA ILE ILE ALA VAL GLY GLY GLY ALA THR GLY ASP
SEQRES 9 B 354 PHE ALA GLY PHE VAL ALA ALA THR LEU LEU ARG GLY VAL
SEQRES 10 B 354 HIS PHE ILE GLN VAL PRO THR THR ILE LEU ALA HIS ASP
SEQRES 11 B 354 SER SER VAL GLY GLY LYS VAL GLY ILE ASN SER LYS GLN
SEQRES 12 B 354 GLY LYS ASN LEU ILE GLY ALA PHE TYR ARG PRO THR ALA
SEQRES 13 B 354 VAL ILE TYR ASP LEU ASP PHE LEU LYS THR LEU PRO PHE
SEQRES 14 B 354 LYS GLN ILE LEU SER GLY TYR ALA GLU VAL TYR LYS HIS
SEQRES 15 B 354 ALA LEU LEU ASN GLY GLU SER ALA THR GLN ASP ILE GLU
SEQRES 16 B 354 GLN HIS PHE LYS ASP ARG GLU ILE LEU GLN SER LEU ASN
SEQRES 17 B 354 GLY MET ASP LYS TYR ILE ALA LYS GLY ILE GLU THR LYS
SEQRES 18 B 354 LEU ASP ILE VAL VAL ALA ASP GLU LYS GLU GLN GLY VAL
SEQRES 19 B 354 ARG LYS PHE LEU ASN LEU GLY HIS THR PHE GLY HIS ALA
SEQRES 20 B 354 VAL GLU TYR TYR HIS LYS ILE PRO HIS GLY HIS ALA VAL
SEQRES 21 B 354 MET VAL GLY ILE ILE TYR GLN PHE ILE VAL ALA ASN ALA
SEQRES 22 B 354 LEU PHE ASP SER LYS HIS ASP ILE SER HIS TYR ILE GLN
SEQRES 23 B 354 TYR LEU ILE GLN LEU GLY TYR PRO LEU ASP MET ILE THR
SEQRES 24 B 354 ASP LEU ASP PHE GLU THR LEU TYR GLN TYR MET LEU SER
SEQRES 25 B 354 ASP LYS LYS ASN ASP LYS GLN GLY VAL GLN MET VAL LEU
SEQRES 26 B 354 MET ARG GLN PHE GLY ASP ILE VAL VAL GLN HIS VAL ASP
SEQRES 27 B 354 GLN LEU THR LEU GLN HIS ALA CYS GLU GLN LEU LYS THR
SEQRES 28 B 354 TYR PHE LYS
HET ZN A 600 1
HET NAD A 400 44
HET ZN B 601 1
HET NAD B 401 44
HETNAM ZN ZINC ION
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 NAD 2(C21 H27 N7 O14 P2)
FORMUL 7 HOH *176(H2 O)
HELIX 1 1 GLY A 19 ILE A 21 5 3
HELIX 2 2 LYS A 22 ASN A 29 1 8
HELIX 3 3 GLU A 40 ASP A 51 1 12
HELIX 4 4 ALA A 66 LYS A 71 5 6
HELIX 5 5 THR A 72 SER A 85 1 14
HELIX 6 6 GLY A 99 LEU A 113 1 15
HELIX 7 7 LEU A 114 GLY A 116 5 3
HELIX 8 8 LEU A 127 SER A 132 1 6
HELIX 9 9 ASP A 162 LEU A 167 5 6
HELIX 10 10 PRO A 168 GLY A 187 1 20
HELIX 11 11 GLY A 187 PHE A 198 1 12
HELIX 12 12 ASP A 200 LEU A 207 1 8
HELIX 13 13 GLY A 209 ASP A 228 1 20
HELIX 14 14 GLY A 233 LEU A 240 5 8
HELIX 15 15 HIS A 242 LYS A 253 1 12
HELIX 16 16 PRO A 255 PHE A 275 1 21
HELIX 17 17 ASP A 280 GLY A 292 1 13
HELIX 18 18 ASP A 338 TYR A 352 1 15
HELIX 19 19 GLY B 19 TYR B 23 5 5
HELIX 20 20 ILE B 24 ASN B 29 1 6
HELIX 21 21 GLU B 40 ASP B 51 1 12
HELIX 22 22 ALA B 66 LYS B 71 5 6
HELIX 23 23 THR B 72 SER B 85 1 14
HELIX 24 24 GLY B 99 LEU B 113 1 15
HELIX 25 25 LEU B 114 GLY B 116 5 3
HELIX 26 26 LEU B 127 SER B 132 1 6
HELIX 27 27 ASP B 162 LEU B 167 5 6
HELIX 28 28 PRO B 168 GLY B 187 1 20
HELIX 29 29 GLY B 187 PHE B 198 1 12
HELIX 30 30 ASP B 200 LEU B 207 1 8
HELIX 31 31 GLY B 209 ASP B 228 1 20
HELIX 32 32 GLY B 233 LEU B 240 5 8
HELIX 33 33 GLY B 241 LYS B 253 1 13
HELIX 34 34 PRO B 255 ASP B 276 1 22
HELIX 35 35 ASP B 280 GLY B 292 1 13
HELIX 36 36 THR B 305 TYR B 309 5 5
HELIX 37 37 ASP B 338 TYR B 352 1 15
SHEET 1 A 7 LYS A 2 GLN A 4 0
SHEET 2 A 7 PRO A 13 GLU A 17 -1 O ILE A 14 N LEU A 3
SHEET 3 A 7 ALA A 156 ASP A 160 1 O VAL A 157 N TYR A 15
SHEET 4 A 7 HIS A 118 PRO A 123 1 N GLN A 121 O ILE A 158
SHEET 5 A 7 ALA A 93 GLY A 98 1 N ALA A 96 O ILE A 120
SHEET 6 A 7 SER A 34 ASP A 39 1 N PHE A 35 O ALA A 93
SHEET 7 A 7 VAL A 59 ILE A 64 1 O HIS A 60 N LEU A 36
SHEET 1 B 2 LYS A 136 ILE A 139 0
SHEET 2 B 2 ILE A 148 PHE A 151 -1 O ILE A 148 N ILE A 139
SHEET 1 C 2 VAL A 324 GLN A 328 0
SHEET 2 C 2 ASP A 331 VAL A 334 -1 O ASP A 331 N GLN A 328
SHEET 1 D 7 LYS B 2 GLN B 4 0
SHEET 2 D 7 PRO B 13 GLU B 17 -1 O ILE B 14 N LEU B 3
SHEET 3 D 7 ALA B 156 ASP B 160 1 O VAL B 157 N TYR B 15
SHEET 4 D 7 HIS B 118 PRO B 123 1 N GLN B 121 O ILE B 158
SHEET 5 D 7 ALA B 93 GLY B 98 1 N ALA B 96 O ILE B 120
SHEET 6 D 7 SER B 34 ASP B 39 1 N LEU B 37 O VAL B 97
SHEET 7 D 7 VAL B 59 ILE B 64 1 O HIS B 60 N LEU B 36
SHEET 1 E 2 LYS B 136 ILE B 139 0
SHEET 2 E 2 ILE B 148 PHE B 151 -1 O ILE B 148 N ILE B 139
SHEET 1 F 2 VAL B 324 GLN B 328 0
SHEET 2 F 2 ASP B 331 VAL B 334 -1 O ASP B 331 N GLN B 328
LINK OE1 GLU A 178 ZN ZN A 600 1555 1555 2.43
LINK NE2 HIS A 242 ZN ZN A 600 1555 1555 2.50
LINK NE2 HIS A 256 ZN ZN A 600 1555 1555 2.72
LINK OE1 GLU B 178 ZN ZN B 601 1555 1555 2.38
LINK NE2 HIS B 242 ZN ZN B 601 1555 1555 2.41
SITE 1 AC1 5 ASP A 130 GLU A 178 HIS A 242 HIS A 256
SITE 2 AC1 5 NAD A 400
SITE 1 AC2 5 ASP B 130 GLU B 178 HIS B 242 HIS B 256
SITE 2 AC2 5 NAD B 401
SITE 1 AC3 32 ASP A 39 TYR A 41 VAL A 42 TYR A 45
SITE 2 AC3 32 PHE A 46 GLY A 67 GLU A 68 LYS A 71
SITE 3 AC3 32 GLY A 99 GLY A 100 ALA A 101 ASP A 104
SITE 4 AC3 32 THR A 124 THR A 125 LEU A 127 ASP A 130
SITE 5 AC3 32 SER A 131 LYS A 136 LYS A 145 ASN A 146
SITE 6 AC3 32 PHE A 163 THR A 166 LEU A 167 GLN A 171
SITE 7 AC3 32 LYS A 221 HIS A 256 ZN A 600 HOH A 609
SITE 8 AC3 32 HOH A 615 HOH A 616 HOH A 670 GLN B 286
SITE 1 AC4 29 GLN A 286 ASP B 39 TYR B 41 VAL B 42
SITE 2 AC4 29 TYR B 45 PHE B 46 GLY B 67 GLU B 68
SITE 3 AC4 29 LYS B 71 GLY B 99 GLY B 100 ALA B 101
SITE 4 AC4 29 ASP B 104 THR B 124 THR B 125 LEU B 127
SITE 5 AC4 29 ASP B 130 SER B 131 LYS B 136 LYS B 145
SITE 6 AC4 29 ASN B 146 PHE B 163 THR B 166 LEU B 167
SITE 7 AC4 29 GLN B 171 LYS B 221 ZN B 601 HOH B 611
SITE 8 AC4 29 HOH B 633
CRYST1 55.260 55.260 232.870 90.00 90.00 90.00 P 43 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 0.018096 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018096 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004294 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
