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Yorodumi- PDB-1fwp: CHEY-BINDING DOMAIN OF CHEA (RESIDUES 159-227), NMR, MINIMIZED AV... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1fwp | ||||||
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Title | CHEY-BINDING DOMAIN OF CHEA (RESIDUES 159-227), NMR, MINIMIZED AVERAGE STRUCTURE | ||||||
Components | CHEA | ||||||
Keywords | CHEMOTAXIS / KINASE / SIGNAL TRANSDUCTION | ||||||
Function / homology | Function and homology information negative regulation of protein modification process / methyl accepting chemotaxis protein complex / positive regulation of post-translational protein modification / bacterial-type flagellum-dependent swimming motility / regulation of bacterial-type flagellum-dependent cell motility / aerotaxis / protein histidine kinase activity / regulation of chemotaxis / thermotaxis / histidine kinase ...negative regulation of protein modification process / methyl accepting chemotaxis protein complex / positive regulation of post-translational protein modification / bacterial-type flagellum-dependent swimming motility / regulation of bacterial-type flagellum-dependent cell motility / aerotaxis / protein histidine kinase activity / regulation of chemotaxis / thermotaxis / histidine kinase / phosphorelay sensor kinase activity / phosphorelay signal transduction system / establishment of localization in cell / chemotaxis / phosphorylation / signal transduction / ATP binding / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR | ||||||
Authors | Mcevoy, M.M. / Dahlquist, F.W. | ||||||
Citation | Journal: Biochemistry / Year: 1996 Title: Structure and dynamics of a CheY-binding domain of the chemotaxis kinase CheA determined by nuclear magnetic resonance spectroscopy. Authors: McEvoy, M.M. / Muhandiram, D.R. / Kay, L.E. / Dahlquist, F.W. #1: Journal: Biochemistry / Year: 1995 Title: Nuclear Magnetic Resonance Assignments and Global Fold of a Chey-Binding Domain in Chea, the Chemotaxis-Specific Kinase of Escherichia Coli Authors: Mcevoy, M.M. / Zhou, H. / Roth, A.F. / Lowry, D.F. / Morrison, T.B. / Kay, L.E. / Dahlquist, F.W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1fwp.cif.gz | 31.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fwp.ent.gz | 23.7 KB | Display | PDB format |
PDBx/mmJSON format | 1fwp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fw/1fwp ftp://data.pdbj.org/pub/pdb/validation_reports/fw/1fwp | 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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NMR ensembles |
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-Components
#1: Protein | Mass: 15019.027 Da / Num. of mol.: 1 / Fragment: CHEY-BINDING DOMAIN, RESIDUES 159 - 227 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: CHEA (RESIDUES 124-257) / Plasmid: PTM22 / Gene (production host): CHEA (RESIDUES 124-257) / Production host: TAC PROMOTER / References: UniProt: P07363 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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-Sample preparation
Sample conditions | pH: 6.5 / Temperature: 303 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-Processing
Software |
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NMR software | Name: X-PLOR / Developer: BRUNGER / Classification: refinement | ||||||||
NMR ensemble | Conformers submitted total number: 1 |