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Yorodumi- PDB-1qaw: Regulatory Features of the TRP Operon and the Crystal Structure o... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1qaw | ||||||
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Title | Regulatory Features of the TRP Operon and the Crystal Structure of the TRP RNA-Binding Attenuation Protein from Bacillus Stearothermophilus. | ||||||
Components | TRP RNA-BINDING ATTENUATION PROTEIN | ||||||
Keywords | RNA BINDING PROTEIN / CIRCULAR ASSEMBLY / 11-FOLD SYMMETRY / RNA-BINDING PROTEIN | ||||||
Function / homology | Function and homology information DNA-templated transcription termination / regulation of DNA-templated transcription / RNA binding / identical protein binding Similarity search - Function | ||||||
Biological species | Geobacillus stearothermophilus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.5 Å | ||||||
Authors | Chen, X.-P. / Antson, A.A. / Yang, M. / Baumann, C. / Dodson, E.J. / Dodson, G.G. / Gollnick, P. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1999 Title: Regulatory features of the trp operon and the crystal structure of the trp RNA-binding attenuation protein from Bacillus stearothermophilus. Authors: Chen, X. / Antson, A.A. / Yang, M. / Li, P. / Baumann, C. / Dodson, E.J. / Dodson, G.G. / Gollnick, P. #1: Journal: Nature / Year: 1995 Title: The Structure of Trp RNA-Binding Attenuation Protein Authors: Antson, A.A. / Otridge, J. / Brzozowski, A.M. / Dodson, E.J. / Dodson, G.G. / Wilson, K.S. / Smith, T.M. / Yang, M. / Kurecki, T. / Gollnick, P. #2: Journal: J.Mol.Biol. / Year: 1994 Title: 11-Fold Symmetry of the Trp RNA-Binding Attenuation Protein (Trap)from Bacillus Subtilis Determined by X-Ray Analysis Authors: Antson, A.A. / Brzozowski, A.M. / Dodson, E.J. / Dauter, Z. / Wilson, K.S. / Kurecki, T. / Otridge, J. / Gollnick, P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1qaw.cif.gz | 165.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1qaw.ent.gz | 131 KB | Display | PDB format |
PDBx/mmJSON format | 1qaw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qa/1qaw ftp://data.pdbj.org/pub/pdb/validation_reports/qa/1qaw | HTTPS FTP |
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-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: 8257.377 Da / Num. of mol.: 11 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Geobacillus stearothermophilus (bacteria) Plasmid: PTZSTMTRB / References: UniProt: Q9X6J6 #2: Chemical | ChemComp-TRP / #3: Water | ChemComp-HOH / | Sequence details | THE NUCLEOTIDE | |
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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: 3.16 Å3/Da / Density % sol: 61.08 % | |||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.8 Details: L-tryptophan, K-Phosphate, Na-Phosphate, PEG 2000 monomethyl ether, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 291K | |||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 18 ℃ / Details: d | |||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: BW7B / Wavelength: 0.89 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jan 1, 1996 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.89 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→15 Å / Num. all: 36584 / Num. obs: 36543 / % possible obs: 90.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4 % / Biso Wilson estimate: 31.8 Å2 / Rmerge(I) obs: 0.089 / Net I/σ(I): 14.2 |
Reflection shell | Resolution: 2.5→2.54 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.487 / Num. unique all: 1776 / % possible all: 90 |
Reflection shell | *PLUS % possible obs: 90 % |
-Processing
Software |
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Refinement | Resolution: 2.5→15 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.5→15 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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