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Yorodumi- PDB-1m1g: Crystal Structure of Aquifex aeolicus N-utilization substance G (... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1m1g | ||||||
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Title | Crystal Structure of Aquifex aeolicus N-utilization substance G (NusG), Space Group P2(1) | ||||||
Components | Transcription antitermination protein nusG | ||||||
Keywords | TRANSCRIPTION / Transcription termination / Antitermination / KOW domain / RNP motif / Immunoglobulin fold / Nucleic acid interaction / protein-protein interaction | ||||||
Function / homology | Function and homology information transcription elongation-coupled chromatin remodeling / regulation of DNA-templated transcription elongation / transcription antitermination / DNA-templated transcription termination / cytosol Similarity search - Function | ||||||
Biological species | Aquifex aeolicus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Steiner, T. / Kaiser, J.T. / Marinkovic, S. / Huber, R. / Wahl, M.C. | ||||||
Citation | Journal: Embo J. / Year: 2002 Title: Crystal structures of transcription factor NusG in light of its nucleic acid- and protein-binding activities Authors: Steiner, T. / Kaiser, J.T. / Marinkovic, S. / Huber, R. / Wahl, M.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1m1g.cif.gz | 223.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1m1g.ent.gz | 184.8 KB | Display | PDB format |
PDBx/mmJSON format | 1m1g.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/m1/1m1g ftp://data.pdbj.org/pub/pdb/validation_reports/m1/1m1g | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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3 |
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4 |
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5 |
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6 |
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Unit cell |
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Details | The biological assembly is a monomer |
-Components
#1: Protein | Mass: 28041.703 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Aquifex aeolicus (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: O67757 #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 48.76 % | |||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 8.2 Details: PEG 3000, sodium chloride, pH 8.2, Vapor diffusion, sitting drop, temperature 291K | |||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 18 ℃ | |||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Details: mirrors |
Radiation | Monochromator: graphite / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→30 Å / Num. obs: 69671 / % possible obs: 94.9 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Redundancy: 3.3 % / Rsym value: 0.08 / Net I/σ(I): 8.9 |
Reflection shell | Resolution: 2→2.1 Å / Mean I/σ(I) obs: 1.6 / Rsym value: 0.406 / % possible all: 79.2 |
Reflection | *PLUS Rmerge(I) obs: 0.08 |
Reflection shell | *PLUS % possible obs: 79.2 % / Rmerge(I) obs: 0.406 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2→30 Å / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber / Details: Refmac 5 was also used in refinement
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Refinement step | Cycle: LAST / Resolution: 2→30 Å
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Refine LS restraints |
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Refinement | *PLUS | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: o_bond_d / Dev ideal: 0.008 | |||||||||||||||||||||||||
LS refinement shell | *PLUS Rfactor Rfree: 0.439 / Rfactor Rwork: 0.415 |