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- PDB-2asr: THE THREE-DIMENSIONAL STRUCTURE OF THE ASPARTATE RECEPTOR FROM ES... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2asr | ||||||
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Title | THE THREE-DIMENSIONAL STRUCTURE OF THE ASPARTATE RECEPTOR FROM ESCHERICHIA COLI | ||||||
![]() | ASPARTATE RECEPTOR | ||||||
![]() | CHEMOTAXIS | ||||||
Function / homology | ![]() detection of chemical stimulus / methyl accepting chemotaxis protein complex / positive regulation of post-translational protein modification / protein histidine kinase binding / cell tip / regulation of chemotaxis / signal complex assembly / cellular response to amino acid stimulus / protein homooligomerization / transmembrane signaling receptor activity ...detection of chemical stimulus / methyl accepting chemotaxis protein complex / positive regulation of post-translational protein modification / protein histidine kinase binding / cell tip / regulation of chemotaxis / signal complex assembly / cellular response to amino acid stimulus / protein homooligomerization / transmembrane signaling receptor activity / chemotaxis / signal transduction / protein homodimerization activity / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Bowie, J.U. / Pakula, A.A. / Simon, M.I. | ||||||
![]() | ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 42.2 KB | Display | ![]() |
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PDB format | ![]() | 29.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 419.8 KB | Display | ![]() |
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Full document | ![]() | 422.8 KB | Display | |
Data in XML | ![]() | 9 KB | Display | |
Data in CIF | ![]() | 11.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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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.) ![]() ![]() | ||
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#2: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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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 |
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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: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.203 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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