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- PDB-1zg5: NarL complexed to narG-89 promoter palindromic tail-to-tail DNA site -
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Open data
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Basic information
Entry | Database: PDB / ID: 1zg5 | ||||||
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Title | NarL complexed to narG-89 promoter palindromic tail-to-tail DNA site | ||||||
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![]() | TRANSCRIPTION/DNA / ![]() ![]() | ||||||
Function / homology | ![]() DNA-binding transcription repressor activity / phosphorelay signal transduction system / nitrate assimilation / ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Maris, A.E. / Kaczor-Grzeskowiak, M. / Ma, Z. / Kopka, M.L. / Gunsalus, R.P. / Dickerson, R.E. | ||||||
![]() | ![]() Title: Primary and Secondary Modes of DNA Recognition by the NarL Two-Component Response Regulator. Authors: Maris, A.E. / Kaczor-Grzeskowiak, M. / Ma, Z. / Kopka, M.L. / Gunsalus, R.P. / Dickerson, R.E. #1: ![]() Title: Dimerization allows DNA target site recognition by the NarL response regulator Authors: Maris, A.E. / Sawaya, M.R. / Kaczor-Grzeskowiak, M. / Jarvis, M.R. / Bearson, S.M.D. / Kopka, M.L. / Schroeder, I. / Gunsalus, R.P. / Dickerson, R.E. #2: ![]() Title: Structure of the Escherichia coli response regulator NarL Authors: Baikalov, I. / Schroeder, I. / Kaczor-Grzeskowiak, M. / Grzeskowiak, K. / Gunsalus, R.P. / Dickerson, R.E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 120.6 KB | Display | ![]() |
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PDB format | ![]() | 89.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1zg1C ![]() 1je8S C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Details | The biological unit is a dimer bound to DNA. There are two biological units in the asymmetric unit (chains A, B, C & D and chains E, F, G & H) |
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Components
#1: DNA chain | Mass: 6134.967 Da / Num. of mol.: 4 / Source method: obtained synthetically / Details: solid phase synthesis #2: Protein | Mass: 9827.909 Da / Num. of mol.: 4 / Fragment: DNA binding domain (residues 147-216) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() #3: Chemical | ChemComp-SO4 / ![]() #4: Water | ChemComp-HOH / | ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.7 Å3/Da / Density % sol: 54.2 % |
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Crystal grow![]() | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: Ammonium sulfate, pH 7.5, vapor diffusion, hanging drop, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Mar 11, 2001 |
Radiation | Protocol: SINGLE WAVELENGTH / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2.2→50 Å / Num. all: 34483 / Num. obs: 34483 / % possible obs: 99.5 % / Observed criterion σ(I): -3 / Redundancy: 4.2 % / Biso Wilson estimate: 52.2 Å2 / Rmerge(I) obs: 0.104 / Rsym value: 0.131 / Χ2: 1.948 / Net I/σ(I): 16.4 |
Reflection shell | Resolution: 2.2→2.25 Å / % possible obs: 96.4 % / Redundancy: 3.4 % / Rmerge(I) obs: 0.687 / Mean I/σ(I) obs: 2.9 / Num. measured obs: 2194 / Num. unique all: 2194 / Rsym value: 0.954 / Χ2: 4.303 / % possible all: 96.4 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: PDB ENTRY 1JE8 Resolution: 2.3→20 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Bsol: 38.791 Å2 | |||||||||||||||||||||||||
Displacement parameters | Biso mean: 40.426 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.3→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.3→2.44 Å / Rfactor Rfree error: 0.025
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Xplor file |
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