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Yorodumi- PDB-1bow: MULTIDRUG-BINDING DOMAIN OF TRANSCRIPTION ACTIVATOR BMRR (APO FORM) -
+Open data
-Basic information
Entry | Database: PDB / ID: 1bow | ||||||
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Title | MULTIDRUG-BINDING DOMAIN OF TRANSCRIPTION ACTIVATOR BMRR (APO FORM) | ||||||
Components | MULTIDRUG-EFFLUX TRANSPORTER 1 REGULATOR BMRR | ||||||
Keywords | TRANSCRIPTION ACTIVATOR / MULTIDRUG BINDING | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Bacillus subtilis (bacteria) | ||||||
Method | X-RAY DIFFRACTION / MIR / Resolution: 2.7 Å | ||||||
Authors | Zheleznova, E.E. / Markham, P.N. / Neyfakh, A.A. / Brennan, R.G. | ||||||
Citation | Journal: Cell(Cambridge,Mass.) / Year: 1999 Title: Structural basis of multidrug recognition by BmrR, a transcription activator of a multidrug transporter. Authors: Zheleznova, E.E. / Markham, P.N. / Neyfakh, A.A. / Brennan, R.G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1bow.cif.gz | 42.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1bow.ent.gz | 29.5 KB | Display | PDB format |
PDBx/mmJSON format | 1bow.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bo/1bow ftp://data.pdbj.org/pub/pdb/validation_reports/bo/1bow | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 18492.049 Da / Num. of mol.: 1 / Fragment: MULTIDRUG-BINDING DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus subtilis (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: P39075 |
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#2: Chemical | ChemComp-MN / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.78 Å3/Da / Density % sol: 67.43 % | ||||||||||||||||||||||||||||
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Crystal grow | pH: 8.5 / Details: pH 8.5 | ||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop / Details: Zheleznova, E.E., (1997) Protein Sci., 6, 2465. | ||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418 |
Detector | Type: ADSC / Detector: AREA DETECTOR |
Radiation | Monochromator: NI FILTER / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→24 Å / Num. obs: 8264 / % possible obs: 100 % / Observed criterion σ(I): 0 / Redundancy: 7.9 % / Rsym value: 0.06 / Net I/σ(I): 10.3 |
Reflection shell | Resolution: 2.7→2.8 Å / Mean I/σ(I) obs: 1.6 / % possible all: 100 |
Reflection | *PLUS Num. measured all: 65480 / Rmerge(I) obs: 0.06 |
Reflection shell | *PLUS % possible obs: 100 % |
-Processing
Software |
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Refinement | Method to determine structure: MIR / Resolution: 2.7→20 Å / Isotropic thermal model: TNT BCORREL / Cross valid method: RFREE / σ(F): 0 / Stereochemistry target values: TNT CSDX_PROTGEO
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Refinement step | Cycle: LAST / Resolution: 2.7→20 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Version: 5D / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rfree: 0.274 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |