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
MolProbity Validation Chart

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Title:
Solution structure of C-domain of Lsr2
Deposition date:
2010-04-02
Original release date:
2010-05-11
Authors:
Li, Yifei; Xia, Bin
Citation:

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).
PubMed: 20133735

Assembly members:

Assembly members:
Lsr2C, polymer, 55 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Mycobacterium tuberculosis   Taxonomy ID: 1773   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Mycobacterium tuberculosis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21d

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Lsr2C: SGSGRGRGAIDREQSAAIRE WARRNGHNVSTRGRIPADVI DAYHAATLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts196
15N chemical shifts54
1H chemical shifts292

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Lsr2C1

Entities:

Entity 1, Lsr2C 55 residues - Formula weight is not available

1   SERGLYSERGLYARGGLYARGGLYALAILE
2   ASPARGGLUGLNSERALAALAILEARGGLU
3   TRPALAARGARGASNGLYHISASNVALSER
4   THRARGGLYARGILEPROALAASPVALILE
5   ASPALATYRHISALAALATHRLEUGLUHIS
6   HISHISHISHISHIS

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_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
AlphaFold P24094 P65649 P9WIP6 P9WIP7

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks