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Yorodumi- PDB-2asr: THE THREE-DIMENSIONAL STRUCTURE OF THE ASPARTATE RECEPTOR FROM ES... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2asr | ||||||
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Title | THE THREE-DIMENSIONAL STRUCTURE OF THE ASPARTATE RECEPTOR FROM ESCHERICHIA COLI | ||||||
Components | ASPARTATE RECEPTORMethyl-accepting chemotaxis proteins | ||||||
Keywords | CHEMOTAXIS | ||||||
Function / homology | Function and homology information detection of chemical stimulus / methyl accepting chemotaxis protein complex / protein histidine kinase binding / positive regulation of post-translational protein modification / cell tip / regulation of chemotaxis / signal complex assembly / cellular response to amino acid stimulus / protein homooligomerization / chemotaxis ...detection of chemical stimulus / methyl accepting chemotaxis protein complex / protein histidine kinase binding / positive regulation of post-translational protein modification / cell tip / regulation of chemotaxis / signal complex assembly / cellular response to amino acid stimulus / protein homooligomerization / chemotaxis / transmembrane signaling receptor activity / signal transduction / protein homodimerization activity / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.3 Å | ||||||
Authors | Bowie, J.U. / Pakula, A.A. / Simon, M.I. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 1995 Title: The three-dimensional structure of the aspartate receptor from Escherichia coli. Authors: Bowie, J.U. / Pakula, A.A. / Simon, M.I. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2asr.cif.gz | 42.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2asr.ent.gz | 29.6 KB | Display | PDB format |
PDBx/mmJSON format | 2asr.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/as/2asr ftp://data.pdbj.org/pub/pdb/validation_reports/as/2asr | 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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Atom site foot note | 1: THE ELECTRON DENSITY IS WEAK AND BROKEN FOR RESIDUES 77 -81 AND THESE RESIDUES ARE INCLUDED IN THE MODEL MERELY FOR COMPLETENESS. THEIR COORDINATES ARE POORLY DEFINED. | ||||||||
Components on special symmetry positions |
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-Components
#1: Protein | Mass: 16277.374 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / References: UniProt: P07017 | ||
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#2: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 5.83 Å3/Da / Density % sol: 78.89 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal | *PLUS Density % sol: 70 % | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.3 Å / Num. obs: 15309 / % possible obs: 86.2 % / Observed criterion σ(F): 1 / Num. measured all: 46244 / Rmerge F obs: 0.076 |
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Reflection shell | *PLUS % possible obs: 65 % / Mean I/σ(I) obs: 4.1 |
-Processing
Software |
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Refinement | Resolution: 2.3→8 Å / σ(F): 1 Details: THE ELECTRON DENSITY IS WEAK AND BROKEN FOR RESIDUES 77 -81 AND THESE RESIDUES ARE INCLUDED IN THE MODEL MERELY FOR COMPLETENESS. THEIR COORDINATES ARE POORLY DEFINED.
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Refinement step | Cycle: LAST / Resolution: 2.3→8 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.203 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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