BMRB Entry 16831
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16831
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Title: Solution structure of C-domain of Lsr2 PubMed: 20133735
Deposition date: 2010-04-02 Original release date: 2010-05-11
Authors: Li, Yifei; Xia, Bin
Citation: Gordon, Blair; Li, Yifei; Wang, Linru; Sintsova, Anna; van Bakel, Harm; Tian, Songhai; Navarre, William Wiley; Xia, Bin; Liu, Jun. "Lsr2 is a nucleoid-associated protein that targets AT-rich sequences and virulence genes in Mycobacterium tuberculosis." Proc. Natl. Acad. Sci. U.S.A. 107, 5154-5159 (2010).
Assembly members:
Lsr2C, polymer, 55 residues, Formula weight is not available
Natural source: Common Name: Mycobacterium tuberculosis Taxonomy ID: 1773 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycobacterium tuberculosis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Lsr2C: SGSGRGRGAIDREQSAAIRE
WARRNGHNVSTRGRIPADVI
DAYHAATLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 196 |
| 15N chemical shifts | 54 |
| 1H chemical shifts | 292 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Lsr2C | 1 |
Entities:
Entity 1, Lsr2C 55 residues - Formula weight is not available
| 1 | SER | GLY | SER | GLY | ARG | GLY | ARG | GLY | ALA | ILE | ||||
| 2 | ASP | ARG | GLU | GLN | SER | ALA | ALA | ILE | ARG | GLU | ||||
| 3 | TRP | ALA | ARG | ARG | ASN | GLY | HIS | ASN | VAL | SER | ||||
| 4 | THR | ARG | GLY | ARG | ILE | PRO | ALA | ASP | VAL | ILE | ||||
| 5 | ASP | ALA | TYR | HIS | ALA | ALA | THR | LEU | GLU | HIS | ||||
| 6 | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: Lsr2C, [U-13C; U-15N], 0.8 mM; H2O 90%; D2O 10%; PBS Na+ 50 mM; NaCl 50 mM
sample_conditions_1: ionic strength: 100 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
AMBER v9, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Duggan, Legge, Dyson & Wright, Johnson, One Moon Scientific - chemical shift assignment, data analysis, processing
NMR spectrometers:
- Bruker Avance 500 MHz
Related Database Links:
| PDB | |
| DBJ | BAH27935 BAL67717 BAN29552 BAQ07815 GAA43492 |
| EMBL | CAA37572 CAC29742 CAL73651 CAR70327 CCC28679 |
| GB | AAA25351 AAK48061 AAS02777 ABK67018 ABL06215 |
| REF | NP_218114 NP_301294 NP_857267 WP_003419513 WP_003875617 |
| SP | P24094 P65649 P9WIP6 P9WIP7 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts