[English] 日本語
Yorodumi- PDB-1fr0: SOLUTION STRUCTURE OF THE HISTIDINE-CONTAINING PHOSPHOTRANSFER DO... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1fr0 | ||||||
---|---|---|---|---|---|---|---|
Title | SOLUTION STRUCTURE OF THE HISTIDINE-CONTAINING PHOSPHOTRANSFER DOMAIN OF ANAEROBIC SENSOR KINASE ARCB FROM ESCHERICHIA COLI. | ||||||
Components | ARCB | ||||||
Keywords | TRANSFERASE / four-helix bundle motif / anaerobic sensor kinase | ||||||
Function / homology | Function and homology information peptidyl-histidine phosphorylation / plasma membrane => GO:0005886 / response to oxygen levels / histidine kinase / phosphorelay sensor kinase activity / phosphoprotein phosphatase activity / protein autophosphorylation / regulation of DNA-templated transcription / signal transduction / ATP binding ...peptidyl-histidine phosphorylation / plasma membrane => GO:0005886 / response to oxygen levels / histidine kinase / phosphorelay sensor kinase activity / phosphoprotein phosphatase activity / protein autophosphorylation / regulation of DNA-templated transcription / signal transduction / ATP binding / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Ikegami, T. / Okada, T. / Ohki, I. / Hirayama, J. / Mizuno, T. / Shirakawa, M. | ||||||
Citation | Journal: Biochemistry / Year: 2001 Title: Solution structure and dynamic character of the histidine-containing phosphotransfer domain of anaerobic sensor kinase ArcB from Escherichia coli. Authors: Ikegami, T. / Okada, T. / Ohki, I. / Hirayama, J. / Mizuno, T. / Shirakawa, M. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1fr0.cif.gz | 1.1 MB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1fr0.ent.gz | 957.2 KB | Display | PDB format |
PDBx/mmJSON format | 1fr0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1fr0_validation.pdf.gz | 346.2 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1fr0_full_validation.pdf.gz | 642.4 KB | Display | |
Data in XML | 1fr0_validation.xml.gz | 103.6 KB | Display | |
Data in CIF | 1fr0_validation.cif.gz | 133.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fr/1fr0 ftp://data.pdbj.org/pub/pdb/validation_reports/fr/1fr0 | HTTPS FTP |
-Related structure data
Related structure data | |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 14013.939 Da / Num. of mol.: 1 Fragment: THE HISTIDINE-CONTAINING PHOSPHOTRANSFER (HPT) DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: PSU2DH / Production host: Escherichia coli (E. coli) References: UniProt: P22763, UniProt: P0AEC3*PLUS, Transferases; Transferring phosphorus-containing groups; Phosphotransferases with a nitrogenous group as acceptor |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
| ||||||||||||||||||||||||
NMR details | Text: The structure was determined using triple-resonance NMR spectroscopy. |
-Sample preparation
Details |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Sample conditions | Ionic strength: 100mM / pH: 6.5 / Pressure: ambient / Temperature: 310 K | |||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
|
---|
-Processing
NMR software |
| ||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: simulated annealing / Software ordinal: 1 Details: The structures are based on a total of 1348 restraints, 1188 are NOE-derived distance constraints, 83 dihedral angle restraints,77 distance restraints from hydrogen bonds. | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 30 |