[English] 日本語
Yorodumi- PDB-2lqj: Solution structure of the C-terminal domain of the MgtC protein f... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2lqj | ||||||
---|---|---|---|---|---|---|---|
Title | Solution structure of the C-terminal domain of the MgtC protein from Mycobacterium tuberculosis | ||||||
Components | Mg2+ transport protein | ||||||
Keywords | HYDROLASE / tuberculosis / ACT domain / membrane protein / regulation | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Mycobacterium tuberculosis (bacteria) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | closest to the average, model 1 | ||||||
Authors | Yang, M. / Yang, Y. / Labesse, G. / Blanc-Potard, A. | ||||||
Citation | Journal: J.Bacteriol. / Year: 2012 Title: The C-Terminal Domain of the Virulence Factor MgtC Is a Divergent ACT Domain. Authors: Yang, Y. / Labesse, G. / Carrere-Kremer, S. / Esteves, K. / Kremer, L. / Cohen-Gonsaud, M. / Blanc-Potard, A.B. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2lqj.cif.gz | 473 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2lqj.ent.gz | 399.1 KB | Display | PDB format |
PDBx/mmJSON format | 2lqj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2lqj_validation.pdf.gz | 460 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 2lqj_full_validation.pdf.gz | 567.7 KB | Display | |
Data in XML | 2lqj_validation.xml.gz | 27.6 KB | Display | |
Data in CIF | 2lqj_validation.cif.gz | 45.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lq/2lqj ftp://data.pdbj.org/pub/pdb/validation_reports/lq/2lqj | HTTPS FTP |
-Related structure data
Similar structure data | |
---|---|
Other databases |
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 10414.767 Da / Num. of mol.: 1 / Fragment: UNP residues 141-234 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mycobacterium tuberculosis (bacteria) / Strain: H37rv / Gene: mgtC, MT1859, Rv1811 / Production host: Escherichia coli (E. coli) / References: UniProt: O07221, EC: 3.6.3.1 |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Sample |
| ||||||||||||
Sample conditions | Ionic strength: 0.11 / pH: 4.6 / Pressure: ambient / Temperature: 293 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 700 MHz |
---|
-Processing
NMR software |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: simulated annealing / Software ordinal: 1 | |||||||||
NMR constraints | NOE constraints total: 1188 / NOE intraresidue total count: 240 / NOE long range total count: 380 / NOE medium range total count: 210 / NOE sequential total count: 358 / Protein chi angle constraints total count: 17 / Protein other angle constraints total count: 0 / Protein phi angle constraints total count: 69 / Protein psi angle constraints total count: 66 | |||||||||
NMR representative | Selection criteria: closest to the average | |||||||||
NMR ensemble | Average torsion angle constraint violation: 2.209 ° / Conformer selection criteria: target function / Conformers calculated total number: 200 / Conformers submitted total number: 15 / Maximum lower distance constraint violation: 0.2 Å / Maximum torsion angle constraint violation: 5 ° / Maximum upper distance constraint violation: 0.3 Å / Torsion angle constraint violation method: RECORD SCRIPTS | |||||||||
NMR ensemble rms | Distance rms dev: 0.0178 Å / Distance rms dev error: 0.012 Å |