BMRB Entry 50240

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50240

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Title:
Molecular Basis for the Adaptive Evolution of Environment Sensing by H-NS Proteins
Deposition date:
2020-04-20
Original release date:
2021-08-11
Authors:
Kharchenko, Vladlena; Jaremko, Lukasz
Citation:

Citation: Zhao, Xiaochuan; Shahul Hameed, Umar; Kharchenko, Vladlena; Liao, Chenyi; Huser, Franceline; Remington, Jacob; Radhakrishnan, Anand; Jaremko, Mariusz; Jaremko, Lukasz; Arold, Stefan; Li, Jianing. "Molecular basis for the adaptive evolution of environment-sensing by H-NS proteins"  eLife 10, e57467-e57467 (2021).
PubMed: 33410747

Assembly members:

Assembly members:
entity_1, polymer, 60 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Salmonella typhimurium   Taxonomy ID: 90371   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Salmonella enterica

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX6P-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPLGSGTKAKRAARPAKYSY VDENGETKTWTGQGRTPAVI KKAMEEQGKQLEDFLIKELE

Data sets:
Data typeCount
13C chemical shifts171
15N chemical shifts53
1H chemical shifts117

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 60 residues - Formula weight is not available

1   GLYPROLEUGLYSERGLYTHRLYSALALYS
2   ARGALAALAARGPROALALYSTYRSERTYR
3   VALASPGLUASNGLYGLUTHRLYSTHRTRP
4   THRGLYGLNGLYARGTHRPROALAVALILE
5   LYSLYSALAMETGLUGLUGLNGLYLYSGLN
6   LEUGLUASPPHELEUILELYSGLULEUGLU

Samples:

sample_1: H-NS C-terminal 84-137 complex, [U-100% 13C; U-100% 15N], 200 uM; H-NS N-terminal 1-57 1.5 mM; sodium chloride 50 mM; Bis-Tris pH6.5 20 mM; sodium azide 0.002%

sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D (H)CACOsample_1isotropicsample_conditions_1
2D (H)CACBCOsample_1isotropicsample_conditions_1
2D (H)CANCOsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1

Software:

CARA - chemical shift assignment

NMR spectrometers:

  • Bruker NEO 700 MHz

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