+Open data
-Basic information
Entry | Database: PDB / ID: 1a6j | ||||||
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Title | NITROGEN REGULATORY BACTERIAL PROTEIN IIA-NITROGEN | ||||||
Components | NITROGEN REGULATORY IIA PROTEIN | ||||||
Keywords | PHOSPHOTRANSFERASE SYSTEM / NITROGEN REGULATION | ||||||
Function / homology | Function and homology information regulation of monoatomic ion transmembrane transporter activity / protein-N(PI)-phosphohistidine-sugar phosphotransferase activity / phosphoenolpyruvate-dependent sugar phosphotransferase system / enzyme inhibitor activity / protein kinase activator activity / : / kinase activity / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / MIR / Resolution: 2.35 Å | ||||||
Authors | Bordo, D. / Van Montfort, R. / Pijning, T. / Kalk, K.H. / Reizer, J. / Saier, M.H. / Dijkstra, B.W. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1998 Title: The three-dimensional structure of the nitrogen regulatory protein IIANtr from Escherichia coli. Authors: Bordo, D. / van Monfort, R.L. / Pijning, T. / Kalk, K.H. / Reizer, J. / Saier Jr., M.H. / Dijkstra, B.W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1a6j.cif.gz | 71.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1a6j.ent.gz | 54.5 KB | Display | PDB format |
PDBx/mmJSON format | 1a6j.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1a6j_validation.pdf.gz | 447.4 KB | Display | wwPDB validaton report |
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Full document | 1a6j_full_validation.pdf.gz | 451.1 KB | Display | |
Data in XML | 1a6j_validation.xml.gz | 13.9 KB | Display | |
Data in CIF | 1a6j_validation.cif.gz | 18.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a6/1a6j ftp://data.pdbj.org/pub/pdb/validation_reports/a6/1a6j | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 17981.541 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12/W3110 / Cellular location: CYTOPLASM / Production host: Escherichia coli (E. coli) References: UniProt: P69829, protein-Npi-phosphohistidine-sugar phosphotransferase #2: Chemical | #3: Chemical | ChemComp-SO4 / | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 53 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.5 Details: PROTEIN CRYSTALLIZED WITH THE HANGING DROP SETUP. RESERVOIR CONTAINING 1.8 M AMMONIUM SULPHATE, 1 MM SODIUM AZIDE, 2MM DTT AND 0.1 M BES-NAOH, PH 7.5. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS Density % sol: 53 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 300 K |
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Diffraction source | Source: ROTATING ANODE / Type: ELLIOTT GX-21 / Wavelength: 1.5418 |
Detector | Type: MACSCIENCE / Detector: IMAGE PLATE / Date: Jun 15, 1995 |
Radiation | Monochromator: CU / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.35→30 Å / Num. obs: 14482 / % possible obs: 89 % / Observed criterion σ(I): 2 / Redundancy: 5.4 % / Biso Wilson estimate: 32 Å2 / Rmerge(I) obs: 0.05 / Rsym value: 0.06 / Net I/σ(I): 14 |
Reflection shell | Resolution: 2.35→2.43 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.06 / Mean I/σ(I) obs: 5 / Rsym value: 0.2 / % possible all: 75 |
Reflection | *PLUS Num. measured all: 104938 |
Reflection shell | *PLUS % possible obs: 75 % / Rmerge(I) obs: 0.2 |
-Processing
Software |
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Refinement | Method to determine structure: MIR / Resolution: 2.35→40 Å / Rfactor Rfree error: 0.01 / Data cutoff high absF: 10000000 / Data cutoff low absF: 0 / Isotropic thermal model: 0 / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 24 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.24 Å / Luzzati d res low obs: 5 Å / Luzzati sigma a obs: 0.22 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.35→40 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.35→2.46 Å / Rfactor Rfree error: 0.042 / Total num. of bins used: 8
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Xplor file |
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