[English] 日本語
Yorodumi- PDB-2mrl: Backbone 1H, 13C, and 15N Chemical Shift Assignments and NMR stru... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2mrl | ||||||
---|---|---|---|---|---|---|---|
Title | Backbone 1H, 13C, and 15N Chemical Shift Assignments and NMR structure for potential drug target from Burkholderia thailandensis E264 | ||||||
Components | Uncharacterized protein BTH I2711 | ||||||
Keywords | UNKNOWN FUNCTION / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease / SSGCID | ||||||
Function / homology | DNA polymerase; domain 1 - #610 / DNA polymerase; domain 1 / Orthogonal Bundle / Mainly Alpha / Uncharacterized protein Function and homology information | ||||||
Biological species | Burkholderia thailandensis E264 (bacteria) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Barnwal, R. / Varani, G. / Seattle Structural Genomics Center for Infectious Disease (SSGCID) | ||||||
Citation | Journal: To be Published Title: NMR structure for potential drug target from Burkholderia thailandensis E264 Authors: Barnwal, R. / Varani, G. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2mrl.cif.gz | 448.9 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2mrl.ent.gz | 378.2 KB | Display | PDB format |
PDBx/mmJSON format | 2mrl.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2mrl_validation.pdf.gz | 397 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 2mrl_full_validation.pdf.gz | 491.6 KB | Display | |
Data in XML | 2mrl_validation.xml.gz | 23.4 KB | Display | |
Data in CIF | 2mrl_validation.cif.gz | 35.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mr/2mrl ftp://data.pdbj.org/pub/pdb/validation_reports/mr/2mrl | HTTPS FTP |
-Related structure data
Similar structure data | |
---|---|
Other databases |
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 8133.304 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Burkholderia thailandensis E264 (bacteria) Strain: E264 / ATCC 700388 / DSM 13276 / CIP 106301 / Gene: BTH_I2711 / Production host: Escherichia coli (E. coli) / References: UniProt: Q2SV23 |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details | Contents: 7.2 mg/mL [U-95% 13C; U-95% 15N] protein BTH I2711, 95% H2O/5% D2O Solvent system: 95% H2O/5% D2O |
---|---|
Sample | Conc.: 7.2 mg/mL / Component: protein BTH_I2711 / Isotopic labeling: [U-95% 13C; U-95% 15N] |
Sample conditions | pH: 7 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
|
---|
-Processing
NMR software |
| |||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: torsion angle dynamics / Software ordinal: 1 | |||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | |||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 200 / Conformers submitted total number: 20 |