HEADER LYASE 26-JAN-03 1NRX
TITLE CRYSTAL STRUCTURE OF 3-DEHYDROQUINATE SYNTHASE (DHQS) IN COMPLEX WITH
TITLE 2 ZN2+ AND NAD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-DEHYDROQUINATE SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DHQS;
COMPND 5 EC: 4.2.3.4;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: EMERICELLA NIDULANS;
SOURCE 3 ORGANISM_TAXID: 162425;
SOURCE 4 GENE: AROMA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: GLW38 (AROB-);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PTRC99A;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PTR51
KEYWDS SHIKIMATE PATHWAY, AROMATIC AMINO ACID BIOSYNTHESIS, DHQS, CLOSED
KEYWDS 2 FORM, FORM F, DOMAIN MOVEMENT, CYCLASE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.E.NICHOLS,J.REN,H.K.LAMB,A.R.HAWKINS,D.K.STAMMERS
REVDAT 3 25-OCT-23 1NRX 1 REMARK LINK
REVDAT 2 24-FEB-09 1NRX 1 VERSN
REVDAT 1 18-MAR-03 1NRX 0
JRNL AUTH C.E.NICHOLS,J.REN,H.K.LAMB,A.R.HAWKINS,D.K.STAMMERS
JRNL TITL LIGAND-INDUCED CONFORMATIONAL CHANGES AND A MECHANISM FOR
JRNL TITL 2 DOMAIN CLOSURE IN ASPERGILLUS NIDULANS DEHYDROQUINATE
JRNL TITL 3 SYNTHASE
JRNL REF J.MOL.BIOL. V. 327 129 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 12614613
JRNL DOI 10.1016/S0022-2836(03)00086-X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.E.NICHOLS,J.REN,H.LAMB,F.HALDANE,A.R.HAWKINS,D.K.STAMMERS
REMARK 1 TITL IDENTIFICATION OF MANY CRYSTAL FORMS OF ASPERGILLUS NIDULANS
REMARK 1 TITL 2 DEHYDROQUINATE SYNTHASE
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 57 306 2001
REMARK 1 REFN ISSN 0907-4449
REMARK 1 DOI 10.1107/S0907444900019429
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.36
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2090059.220
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.7
REMARK 3 NUMBER OF REFLECTIONS : 19328
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) : 0.200
REMARK 3 FREE R VALUE : 0.294
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 940
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.010
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.00
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1718
REMARK 3 BIN R VALUE (WORKING SET) : 0.3110
REMARK 3 BIN FREE R VALUE : 0.3740
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 89
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.040
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5825
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 104
REMARK 3 SOLVENT ATOMS : 225
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 59.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.14000
REMARK 3 B22 (A**2) : 4.13000
REMARK 3 B33 (A**2) : -3.99000
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) : 0.34
REMARK 3 ESD FROM SIGMAA (A) : 0.50
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) : 0.51
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.68
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.780
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 : 0.27
REMARK 3 BSOL : 15.60
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.PARAM
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 1NRX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-FEB-03.
REMARK 100 THE DEPOSITION ID IS D_1000018151.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-FEB-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
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 : 19328
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
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 (%) : 93.6
REMARK 200 DATA REDUNDANCY : 2.850
REMARK 200 R MERGE (I) : 0.10800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.9900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.19
REMARK 200 R MERGE FOR SHELL (I) : 0.35400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.550
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 1DQS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG6000, DMSO, HEPES, PH 8.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 36.20000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 74.50000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.75000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 74.50000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.20000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.75000
REMARK 290 SMTRY3 4 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 300 REMARK: THE CRYSTALLOGRAPHIC DIMER IS EQUIVALENT TO THE BIOLOGICAL
REMARK 300 DIMER
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
REMARK 350 TOTAL BURIED SURFACE AREA: 6050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -185.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 MET A 1
REMARK 465 SER A 2
REMARK 465 ASN A 3
REMARK 465 GLU A 229
REMARK 465 GLU A 258
REMARK 465 ARG A 259
REMARK 465 GLU A 260
REMARK 465 LYS A 356
REMARK 465 LYS A 357
REMARK 465 ASN A 358
REMARK 465 ASP A 359
REMARK 465 GLY A 360
REMARK 465 PRO A 393
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 GLU B 258
REMARK 465 ARG B 259
REMARK 465 GLU B 260
REMARK 465 LYS B 356
REMARK 465 LYS B 357
REMARK 465 ASN B 358
REMARK 465 ASP B 359
REMARK 465 GLY B 360
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 ARG A 77 CG CD NE CZ NH1 NH2
REMARK 470 GLY A 228 O
REMARK 470 ASP A 257 O
REMARK 470 ASP A 355 O
REMARK 470 ALA A 392 O
REMARK 470 ARG B 77 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 257 O
REMARK 470 ASP B 355 O
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 ARG A 12 120.72 -177.62
REMARK 500 SER A 14 -15.02 -152.52
REMARK 500 ASP A 18 179.33 170.19
REMARK 500 TYR A 25 -63.95 178.86
REMARK 500 SER A 32 -64.83 -92.33
REMARK 500 CYS A 34 56.71 -94.57
REMARK 500 ASN A 46 -75.60 -51.67
REMARK 500 SER A 49 -28.17 -38.97
REMARK 500 PHE A 59 -70.00 -69.88
REMARK 500 LYS A 61 -85.51 -51.34
REMARK 500 GLN A 87 -71.66 -60.22
REMARK 500 ASP A 146 -87.16 -158.55
REMARK 500 SER A 147 -27.01 -29.85
REMARK 500 PRO A 158 -7.90 -51.85
REMARK 500 SER A 202 -52.73 -131.86
REMARK 500 ALA A 214 -77.15 -36.45
REMARK 500 GLU A 233 108.58 -53.95
REMARK 500 LEU A 263 -26.94 -37.89
REMARK 500 ILE A 334 -77.74 -61.00
REMARK 500 ARG A 335 98.68 -59.35
REMARK 500 LYS A 336 -45.20 167.58
REMARK 500 ALA A 339 100.71 -43.87
REMARK 500 LEU A 354 -4.63 -59.04
REMARK 500 LYS A 362 -45.89 -136.44
REMARK 500 LYS A 363 102.66 90.59
REMARK 500 ILE A 371 107.64 -55.86
REMARK 500 THR A 377 35.35 -93.60
REMARK 500 ARG A 378 178.61 178.26
REMARK 500 ARG B 12 146.26 -176.94
REMARK 500 SER B 14 -48.77 -159.29
REMARK 500 ASP B 18 -178.40 171.30
REMARK 500 TYR B 25 -64.23 179.21
REMARK 500 ILE B 31 -9.01 -59.52
REMARK 500 SER B 32 -63.24 -94.07
REMARK 500 CYS B 34 57.31 -95.04
REMARK 500 ASN B 46 -74.08 -53.79
REMARK 500 SER B 49 -30.03 -38.84
REMARK 500 LYS B 61 -83.28 -52.95
REMARK 500 ALA B 63 -70.50 -61.86
REMARK 500 ASP B 146 -87.12 -156.83
REMARK 500 SER B 147 -28.33 -29.61
REMARK 500 PRO B 158 -7.66 -52.72
REMARK 500 SER B 202 -52.80 -130.88
REMARK 500 GLU B 233 109.16 -53.72
REMARK 500 THR B 338 72.00 -152.94
REMARK 500 THR B 377 37.92 -94.24
REMARK 500 ARG B 378 178.32 177.54
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 B1601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 194 OE2
REMARK 620 2 HIS B 271 NE2 73.6
REMARK 620 3 HIS B 287 NE2 116.2 83.7
REMARK 620 N 1 2
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 1601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 623
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 625
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 626
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 627
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
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
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 COFACTOR
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 AND REDUCED COFACTOR
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 AND REDUCED CO-FACTOR
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 CARBAPHOSPHONATE, CRYSTAL FORM H, CLOSED FORM
REMARK 900 WITH CO-FACTOR ANALOGUE AND SUBSTRATE ANALOGUE
DBREF 1NRX A 1 393 UNP P07547 ARO1_EMENI 1 393
DBREF 1NRX B 1 393 UNP P07547 ARO1_EMENI 1 393
SEQRES 1 A 393 MET SER ASN PRO THR LYS ILE SER ILE LEU GLY ARG GLU
SEQRES 2 A 393 SER ILE ILE ALA ASP PHE GLY LEU TRP ARG ASN TYR VAL
SEQRES 3 A 393 ALA LYS ASP LEU ILE SER ASP CYS SER SER THR THR TYR
SEQRES 4 A 393 VAL LEU VAL THR ASP THR ASN ILE GLY SER ILE TYR THR
SEQRES 5 A 393 PRO SER PHE GLU GLU ALA PHE ARG LYS ARG ALA ALA GLU
SEQRES 6 A 393 ILE THR PRO SER PRO ARG LEU LEU ILE TYR ASN ARG PRO
SEQRES 7 A 393 PRO GLY GLU VAL SER LYS SER ARG GLN THR LYS ALA ASP
SEQRES 8 A 393 ILE GLU ASP TRP MET LEU SER GLN ASN PRO PRO CYS GLY
SEQRES 9 A 393 ARG ASP THR VAL VAL ILE ALA LEU GLY GLY GLY VAL ILE
SEQRES 10 A 393 GLY ASP LEU THR GLY PHE VAL ALA SER THR TYR MET ARG
SEQRES 11 A 393 GLY VAL ARG TYR VAL GLN VAL PRO THR THR LEU LEU ALA
SEQRES 12 A 393 MET VAL ASP SER SER ILE GLY GLY LYS THR ALA ILE ASP
SEQRES 13 A 393 THR PRO LEU GLY LYS ASN LEU ILE GLY ALA ILE TRP GLN
SEQRES 14 A 393 PRO THR LYS ILE TYR ILE ASP LEU GLU PHE LEU GLU THR
SEQRES 15 A 393 LEU PRO VAL ARG GLU PHE ILE ASN GLY MET ALA GLU VAL
SEQRES 16 A 393 ILE LYS THR ALA ALA ILE SER SER GLU GLU GLU PHE THR
SEQRES 17 A 393 ALA LEU GLU GLU ASN ALA GLU THR ILE LEU LYS ALA VAL
SEQRES 18 A 393 ARG ARG GLU VAL THR PRO GLY GLU HIS ARG PHE GLU GLY
SEQRES 19 A 393 THR GLU GLU ILE LEU LYS ALA ARG ILE LEU ALA SER ALA
SEQRES 20 A 393 ARG HIS LYS ALA TYR VAL VAL SER ALA ASP GLU ARG GLU
SEQRES 21 A 393 GLY GLY LEU ARG ASN LEU LEU ASN TRP GLY HIS SER ILE
SEQRES 22 A 393 GLY HIS ALA ILE GLU ALA ILE LEU THR PRO GLN ILE LEU
SEQRES 23 A 393 HIS GLY GLU CYS VAL ALA ILE GLY MET VAL LYS GLU ALA
SEQRES 24 A 393 GLU LEU ALA ARG HIS LEU GLY ILE LEU LYS GLY VAL ALA
SEQRES 25 A 393 VAL SER ARG ILE VAL LYS CYS LEU ALA ALA TYR GLY LEU
SEQRES 26 A 393 PRO THR SER LEU LYS ASP ALA ARG ILE ARG LYS LEU THR
SEQRES 27 A 393 ALA GLY LYS HIS CYS SER VAL ASP GLN LEU MET PHE ASN
SEQRES 28 A 393 MET ALA LEU ASP LYS LYS ASN ASP GLY PRO LYS LYS LYS
SEQRES 29 A 393 ILE VAL LEU LEU SER ALA ILE GLY THR PRO TYR GLU THR
SEQRES 30 A 393 ARG ALA SER VAL VAL ALA ASN GLU ASP ILE ARG VAL VAL
SEQRES 31 A 393 LEU ALA PRO
SEQRES 1 B 393 MET SER ASN PRO THR LYS ILE SER ILE LEU GLY ARG GLU
SEQRES 2 B 393 SER ILE ILE ALA ASP PHE GLY LEU TRP ARG ASN TYR VAL
SEQRES 3 B 393 ALA LYS ASP LEU ILE SER ASP CYS SER SER THR THR TYR
SEQRES 4 B 393 VAL LEU VAL THR ASP THR ASN ILE GLY SER ILE TYR THR
SEQRES 5 B 393 PRO SER PHE GLU GLU ALA PHE ARG LYS ARG ALA ALA GLU
SEQRES 6 B 393 ILE THR PRO SER PRO ARG LEU LEU ILE TYR ASN ARG PRO
SEQRES 7 B 393 PRO GLY GLU VAL SER LYS SER ARG GLN THR LYS ALA ASP
SEQRES 8 B 393 ILE GLU ASP TRP MET LEU SER GLN ASN PRO PRO CYS GLY
SEQRES 9 B 393 ARG ASP THR VAL VAL ILE ALA LEU GLY GLY GLY VAL ILE
SEQRES 10 B 393 GLY ASP LEU THR GLY PHE VAL ALA SER THR TYR MET ARG
SEQRES 11 B 393 GLY VAL ARG TYR VAL GLN VAL PRO THR THR LEU LEU ALA
SEQRES 12 B 393 MET VAL ASP SER SER ILE GLY GLY LYS THR ALA ILE ASP
SEQRES 13 B 393 THR PRO LEU GLY LYS ASN LEU ILE GLY ALA ILE TRP GLN
SEQRES 14 B 393 PRO THR LYS ILE TYR ILE ASP LEU GLU PHE LEU GLU THR
SEQRES 15 B 393 LEU PRO VAL ARG GLU PHE ILE ASN GLY MET ALA GLU VAL
SEQRES 16 B 393 ILE LYS THR ALA ALA ILE SER SER GLU GLU GLU PHE THR
SEQRES 17 B 393 ALA LEU GLU GLU ASN ALA GLU THR ILE LEU LYS ALA VAL
SEQRES 18 B 393 ARG ARG GLU VAL THR PRO GLY GLU HIS ARG PHE GLU GLY
SEQRES 19 B 393 THR GLU GLU ILE LEU LYS ALA ARG ILE LEU ALA SER ALA
SEQRES 20 B 393 ARG HIS LYS ALA TYR VAL VAL SER ALA ASP GLU ARG GLU
SEQRES 21 B 393 GLY GLY LEU ARG ASN LEU LEU ASN TRP GLY HIS SER ILE
SEQRES 22 B 393 GLY HIS ALA ILE GLU ALA ILE LEU THR PRO GLN ILE LEU
SEQRES 23 B 393 HIS GLY GLU CYS VAL ALA ILE GLY MET VAL LYS GLU ALA
SEQRES 24 B 393 GLU LEU ALA ARG HIS LEU GLY ILE LEU LYS GLY VAL ALA
SEQRES 25 B 393 VAL SER ARG ILE VAL LYS CYS LEU ALA ALA TYR GLY LEU
SEQRES 26 B 393 PRO THR SER LEU LYS ASP ALA ARG ILE ARG LYS LEU THR
SEQRES 27 B 393 ALA GLY LYS HIS CYS SER VAL ASP GLN LEU MET PHE ASN
SEQRES 28 B 393 MET ALA LEU ASP LYS LYS ASN ASP GLY PRO LYS LYS LYS
SEQRES 29 B 393 ILE VAL LEU LEU SER ALA ILE GLY THR PRO TYR GLU THR
SEQRES 30 B 393 ARG ALA SER VAL VAL ALA ASN GLU ASP ILE ARG VAL VAL
SEQRES 31 B 393 LEU ALA PRO
HET ZN A 600 1
HET CL A 606 1
HET CL A 608 1
HET CL A 609 1
HET CL A 610 1
HET CL A 612 1
HET CL A 613 1
HET CL A 626 1
HET NAD A 400 44
HET ZN B1601 1
HET CL B1604 1
HET CL B 607 1
HET CL B 616 1
HET CL B 619 1
HET CL B 623 1
HET CL B 625 1
HET CL B 627 1
HET NAD B 401 44
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 CL 14(CL 1-)
FORMUL 11 NAD 2(C21 H27 N7 O14 P2)
FORMUL 21 HOH *225(H2 O)
HELIX 1 1 TYR A 25 CYS A 34 1 10
HELIX 2 2 THR A 45 GLU A 65 1 21
HELIX 3 3 GLY A 80 LYS A 84 5 5
HELIX 4 4 SER A 85 GLN A 99 1 15
HELIX 5 5 GLY A 114 TYR A 128 1 15
HELIX 6 6 MET A 129 GLY A 131 5 3
HELIX 7 7 THR A 140 ASP A 146 1 7
HELIX 8 8 GLU A 178 LEU A 183 1 6
HELIX 9 9 PRO A 184 ILE A 201 1 18
HELIX 10 10 SER A 203 ARG A 223 1 21
HELIX 11 11 THR A 235 ALA A 256 1 22
HELIX 12 12 ARG A 264 TRP A 269 5 6
HELIX 13 13 GLY A 270 THR A 282 1 13
HELIX 14 14 LEU A 286 LEU A 305 1 20
HELIX 15 15 LYS A 309 TYR A 323 1 15
HELIX 16 16 ARG A 333 THR A 338 1 6
HELIX 17 17 SER A 344 LEU A 354 1 11
HELIX 18 18 ALA A 383 LEU A 391 1 9
HELIX 19 19 TYR B 25 CYS B 34 1 10
HELIX 20 20 THR B 45 GLU B 65 1 21
HELIX 21 21 GLY B 80 LYS B 84 5 5
HELIX 22 22 SER B 85 GLN B 99 1 15
HELIX 23 23 GLY B 114 TYR B 128 1 15
HELIX 24 24 MET B 129 GLY B 131 5 3
HELIX 25 25 THR B 140 ASP B 146 1 7
HELIX 26 26 GLU B 178 LEU B 183 1 6
HELIX 27 27 PRO B 184 ILE B 201 1 18
HELIX 28 28 SER B 203 ARG B 223 1 21
HELIX 29 29 THR B 235 ASP B 257 1 23
HELIX 30 30 GLY B 262 TRP B 269 5 8
HELIX 31 31 GLY B 270 THR B 282 1 13
HELIX 32 32 LEU B 286 LEU B 305 1 20
HELIX 33 33 LYS B 309 TYR B 323 1 15
HELIX 34 34 ASP B 331 LEU B 337 1 7
HELIX 35 35 SER B 344 LEU B 354 1 11
HELIX 36 36 ASN B 384 ALA B 392 1 9
SHEET 1 A 7 THR A 5 SER A 8 0
SHEET 2 A 7 GLU A 13 ASP A 18 -1 O ALA A 17 N THR A 5
SHEET 3 A 7 LYS A 172 ASP A 176 1 O ILE A 175 N ILE A 16
SHEET 4 A 7 ARG A 133 PRO A 138 1 N GLN A 136 O LYS A 172
SHEET 5 A 7 VAL A 108 GLY A 113 1 N ALA A 111 O VAL A 135
SHEET 6 A 7 THR A 38 ASP A 44 1 N VAL A 40 O ILE A 110
SHEET 7 A 7 ARG A 71 ARG A 77 1 O LEU A 73 N LEU A 41
SHEET 1 B 2 LYS A 152 THR A 157 0
SHEET 2 B 2 GLY A 160 ILE A 167 -1 O GLY A 160 N THR A 157
SHEET 1 C 2 LYS A 364 ILE A 365 0
SHEET 2 C 2 SER A 380 VAL A 381 -1 O SER A 380 N ILE A 365
SHEET 1 D 2 LEU A 368 ALA A 370 0
SHEET 2 D 2 THR A 373 PRO A 374 -1 O THR A 373 N ALA A 370
SHEET 1 E 7 THR B 5 SER B 8 0
SHEET 2 E 7 GLU B 13 ASP B 18 -1 O ALA B 17 N THR B 5
SHEET 3 E 7 LYS B 172 ASP B 176 1 O ILE B 175 N ILE B 16
SHEET 4 E 7 ARG B 133 PRO B 138 1 N GLN B 136 O LYS B 172
SHEET 5 E 7 VAL B 108 GLY B 113 1 N ALA B 111 O VAL B 135
SHEET 6 E 7 THR B 38 ASP B 44 1 N VAL B 40 O ILE B 110
SHEET 7 E 7 ARG B 71 ARG B 77 1 O LEU B 73 N LEU B 41
SHEET 1 F 2 LYS B 152 THR B 157 0
SHEET 2 F 2 GLY B 160 ILE B 167 -1 O GLY B 160 N THR B 157
SHEET 1 G 2 LYS B 362 ILE B 365 0
SHEET 2 G 2 SER B 380 ALA B 383 -1 O SER B 380 N ILE B 365
SHEET 1 H 2 LEU B 368 ALA B 370 0
SHEET 2 H 2 THR B 373 PRO B 374 -1 O THR B 373 N ALA B 370
LINK NE2 HIS A 287 ZN ZN A 600 1555 1555 2.77
LINK OE2 GLU B 194 ZN ZN B1601 1555 1555 2.59
LINK NE2 HIS B 271 ZN ZN B1601 1555 1555 2.73
LINK NE2 HIS B 287 ZN ZN B1601 1555 1555 2.60
CISPEP 1 THR A 67 PRO A 68 0 0.04
CISPEP 2 ASN A 100 PRO A 101 0 -0.28
CISPEP 3 THR A 282 PRO A 283 0 0.59
CISPEP 4 THR B 67 PRO B 68 0 -0.37
CISPEP 5 ASN B 100 PRO B 101 0 -0.29
CISPEP 6 THR B 282 PRO B 283 0 0.85
SITE 1 AC1 4 ASP A 146 GLU A 194 HIS A 271 HIS A 287
SITE 1 AC2 3 GLU B 194 HIS B 271 HIS B 287
SITE 1 AC3 1 ARG B 12
SITE 1 AC4 1 ARG A 12
SITE 1 AC5 3 ALA A 279 GLN A 347 ASN A 351
SITE 1 AC6 3 ARG A 130 HOH A 723 LYS B 152
SITE 1 AC7 1 LEU B 72
SITE 1 AC8 1 LYS B 309
SITE 1 AC9 1 GLN B 347
SITE 1 BC1 1 GLN A 99
SITE 1 BC2 2 THR B 282 LYS B 341
SITE 1 BC3 20 ASP A 44 ASN A 46 GLU A 81 LYS A 84
SITE 2 BC3 20 GLY A 114 GLY A 115 VAL A 116 ASP A 119
SITE 3 BC3 20 THR A 139 THR A 140 ASP A 146 SER A 147
SITE 4 BC3 20 LYS A 152 ASN A 162 PHE A 179 THR A 182
SITE 5 BC3 20 LEU A 183 GLU A 187 HOH A 635 HOH A 637
SITE 1 BC4 21 ASP B 44 ASN B 46 ILE B 47 GLU B 81
SITE 2 BC4 21 LYS B 84 GLY B 114 GLY B 115 VAL B 116
SITE 3 BC4 21 ASP B 119 THR B 139 THR B 140 ASP B 146
SITE 4 BC4 21 SER B 147 LYS B 152 ASN B 162 PHE B 179
SITE 5 BC4 21 THR B 182 LEU B 183 PRO B 184 GLU B 187
SITE 6 BC4 21 HOH B1703
CRYST1 72.400 83.500 149.000 90.00 90.00 90.00 P 21 21 21 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 0.013812 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011976 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006711 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
