[English] 日本語
![](img/lk-miru.gif)
- PDB-1jem: NMR STRUCTURE OF HISTIDINE PHOSPHORYLATED FORM OF THE PHOSPHOCARR... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1jem | ||||||
---|---|---|---|---|---|---|---|
Title | NMR STRUCTURE OF HISTIDINE PHOSPHORYLATED FORM OF THE PHOSPHOCARRIER HISTIDINE CONTAINING PROTEIN FROM BACILLUS SUBTILIS, NMR, 25 STRUCTURES | ||||||
![]() | HISTIDINE CONTAINING PROTEIN | ||||||
![]() | PHOSPHOTRANSFERASE / HISTIDINE CONTAINING PROTEIN / PHOSPHOHISTIDINE / PTS | ||||||
Function / homology | ![]() regulation of carbohydrate utilization / phosphoenolpyruvate-dependent sugar phosphotransferase system / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR | ||||||
![]() | Jones, B.E. / Rajagopal, P. / Klevit, R.E. | ||||||
![]() | ![]() Title: Phosphorylation on histidine is accompanied by localized structural changes in the phosphocarrier protein, HPr from Bacillus subtilis. Authors: Jones, B.E. / Rajagopal, P. / Klevit, R.E. #1: ![]() Title: Structural Consequences of Histidine Phosphorylation: NMR Characterization of the Phosphohistidine Form of Histidine-Containing Protein from Bacillus Subtilis and Escherichia Coli Authors: Rajagopal, P. / Waygood, E.B. / Klevit, R.E. #2: ![]() Title: Solution Structure of the Phosphocarrier Protein Hpr from Bacillus Subtilis by Two-Dimensional NMR Spectroscopy Authors: Wittekind, M. / Rajagopal, P. / Branchini, B.R. / Reizer, J. / Saier Junior, M.H. / Klevit, R.E. #3: ![]() Title: Sequence-Specific 1H NMR Resonance Assignments of Bacillus Subtilis Hpr: Use of Spectra Obtained from Mutants to Resolve Spectral Overlap Authors: Wittekind, M. / Reizer, J. / Klevit, R.E. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 610.8 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 534.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 347.4 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 498.4 KB | Display | |
Data in XML | ![]() | 37.5 KB | Display | |
Data in CIF | ![]() | 61 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
Components
#1: Protein | Mass: 9115.053 Da / Num. of mol.: 1 / Mutation: M51V Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
---|
-
Sample preparation
Sample conditions | pH: 6.9 / Temperature: 303 K |
---|---|
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker DMX 500 / Manufacturer: Bruker / Model: DMX 500 / Field strength: 500.13 MHz |
---|
-
Processing
Software |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR software |
| ||||||||||||
NMR ensemble | Conformer selection criteria: LOWEST ENERGY / Conformers calculated total number: 50 / Conformers submitted total number: 25 |