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Yorodumi- PDB-1ew0: CRYSTAL STRUCTURE ANALYSIS OF THE SENSOR DOMAIN OF RMFIXL(FERROUS... -
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-Basic information
Entry | Database: PDB / ID: 1ew0 | ||||||
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Title | CRYSTAL STRUCTURE ANALYSIS OF THE SENSOR DOMAIN OF RMFIXL(FERROUS FORM) | ||||||
Components | FIXL | ||||||
Keywords | TRANSFERASE / OXYGEN SENSOR / HEME PROTEIN / HISTIDINE KINASE / RHIZOBIUM MELILOTI | ||||||
Function / homology | Function and homology information nitrogen fixation / histidine kinase / phosphorelay sensor kinase activity / regulation of DNA-templated transcription / ATP binding / metal ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | Sinorhizobium meliloti (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.4 Å | ||||||
Authors | Miyatake, H. / Mukai, M. / Park, S.-Y. / Adachi, S. / Tamura, K. / Nakamura, H. / Nakamura, K. / Tsuchiya, T. / Iizuka, T. / Shiro, Y. | ||||||
Citation | Journal: J.MOL.BIOL. / Year: 2000 Title: Sensory mechanism of oxygen sensor FixL from Rhizobium meliloti: crystallographic, mutagenesis and resonance Raman spectroscopic studies Authors: Miyatake, H. / Mukai, M. / Park, S.-Y. / Adachi, S. / Tamura, K. / Nakamura, H. / Nakamura, K. / Tsuchiya, T. / Iizuka, T. / Shiro, Y. #1: Journal: ACTA CRYSTALLOGR.,SECT.D / Year: 1999 Title: Dynamic light-scattering and preliminary crystallographic studies of the sensor domain of the haem-based oxygen sensor FixL from Rhizobium meliloti. Authors: Miyatake, H. / Kanai, M. / Adachi, S. / Nakamura, H. / Tamura, K. / Tanida, H. / Tsuchiya, T. / Iizuka, T. / Shiro, Y. #2: Journal: J.Biol.Chem. / Year: 1999 Title: Iron coordination structure of oxygen sensor FixL characterized by Fe K-edge EXAFS and resonance Raman spectroscopy Authors: Miyatake, H. / Mukai, M. / Adachi, S. / Nakamura, H. / Tamura, K. / Iizuka, T. / Shiro, Y. / Strange, R.W. / Hasnain, S.S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ew0.cif.gz | 41.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ew0.ent.gz | 27.9 KB | Display | PDB format |
PDBx/mmJSON format | 1ew0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ew/1ew0 ftp://data.pdbj.org/pub/pdb/validation_reports/ew/1ew0 | 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
#1: Protein | Mass: 14522.385 Da / Num. of mol.: 1 / Fragment: SENSOR DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Sinorhizobium meliloti (bacteria) / Plasmid: PET-14B / Production host: Escherichia coli (E. coli) References: UniProt: P10955, Transferases; Transferring phosphorus-containing groups; Phosphotransferases with a nitrogenous group as acceptor |
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#2: Chemical | ChemComp-HEM / |
#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: 1.86 Å3/Da / Density % sol: 33.7 % | |||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 4.6 Details: PEG 4000, acetic acid/NaOH, ammonium acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K | |||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / pH: 4.5 | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL44B2 / Wavelength: 0.7 |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Jun 10, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.7 Å / Relative weight: 1 |
Reflection | Resolution: 1.2→100 Å / Num. all: 165005 / Num. obs: 33489 / % possible obs: 92.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.93 % / Biso Wilson estimate: 19.2 Å2 / Rmerge(I) obs: 0.051 / Net I/σ(I): 28.7 |
Reflection shell | Resolution: 1.2→1.28 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.278 / Num. unique all: 4730 / % possible all: 84.4 |
Reflection | *PLUS Num. measured all: 165005 |
-Processing
Software |
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Refinement | Resolution: 1.4→20 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.4→20 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Version: 3.851 / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.4 Å / Lowest resolution: 20 Å / σ(F): 0 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS |