BMRB Entry 51959

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51959

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Title:
minor conformation of s1.1 domain of sA from Bacillus subtilis
Deposition date:
2023-05-10
Original release date:
2023-06-09
Authors:
Tuzincin, David
Citation:

Citation: Tuzincin, David; Padrta, Petr; Sanderova, Hana; Rabatinova, Alzebeta; Bendova, Katerina; Krasny, Libor; Zidek, Lukas; Kaderavek, Pavel. "Characterisation of a transitionally occupied state and thermal unfolding of domain 1.1 of sA factor of RNA polymerase from Bacillus subtilis"  Proteins 91, 1276-1287 (2023).
PubMed: 37350110

Assembly members:

Assembly members:
entity_1, polymer, 79 residues, 9379.02 Da.

Natural source:

Natural source:   Common Name: Bacillus subtilis   Taxonomy ID: 1423   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus subtilis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: ADKQTHETELTFDQVKEQLT ESGKKRGVLTYEEIAERMSS FEIESDQMDEYYEFLGEQGV ELISENEETEDLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts284
15N chemical shifts150
1H chemical shifts149

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1sigma1.11

Entities:

Entity 1, sigma1.1 79 residues - 9379.02 Da.

This protein sequence is a fragment (2-72) of sA primary transcription factor. The initial methionine at position 1 is N-terminally cleaved. Sequence numbering in our case begins with 1 ALA, 2 ASP, ... Residues 72-73 represent non-native residues inserted because of the restriction enzyme (XhoI) used for cloning. Residues 74-79 represent a non-native affinity tag.

1   ALAASPLYSGLNTHRHISGLUTHRGLULEU
2   THRPHEASPGLNVALLYSGLUGLNLEUTHR
3   GLUSERGLYLYSLYSARGGLYVALLEUTHR
4   TYRGLUGLUILEALAGLUARGMETSERSER
5   PHEGLUILEGLUSERASPGLNMETASPGLU
6   TYRTYRGLUPHELEUGLYGLUGLNGLYVAL
7   GLULEUILESERGLUASNGLUGLUTHRGLU
8   ASPLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: sigma1.1, [U-99% 13C; U-99% 15N], 1 mM; D2O 10%; H2O 90%; sodium phosphate 20 mM; sodium chloride 10 mM; sodium azide 3 mM

sample_2: sigma1.1, [U-99% 15N], 0.8 mM; H2O 100%; sodium phosphate 20 mM; sodium chloride 10 mM; sodium azide 3 mM

sample_3: sigma1.1, [U-15N; U-2H; 99%] + specific labeling of 13C pro-S methyls, 0.8 mM; H2O 100%; sodium phosphate 20 mM; sodium chloride 10 mM; sodium azide 3 mM

sample_4: sigma1.1, [U-15N; U-2H; 99%], 0.8 mM; H2O 100%; sodium phosphate 20 mM; sodium chloride 10 mM; sodium azide 3 mM

sample_5: sigma1.1, selectively labeled C-alpha positions except for Val, Leu, Ile,, 0.8 mM; D2O 100%; sodium phosphate 20 mM; sodium chloride 10 mM; sodium azide 3 mM

sample_conditions_1: pH: 6.6; pressure: 1 atm; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
13CO CESTsample_1isotropicsample_conditions_1
13CA CESTsample_5isotropicsample_conditions_1
HACACONNH 13 CA CESTsample_1isotropicsample_conditions_1
1HN CESTsample_3isotropicsample_conditions_1
1HN CESTsample_2isotropicsample_conditions_1
15N CESTsample_2isotropicsample_conditions_1
15N CPMGsample_1isotropicsample_conditions_1
15N CPMGsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

GLOVE v2.4 - chemical shift calculation from CPMG dispersion profiles

ChemEx v2021.4.0.dev6 - chemical shift calculation from CPMG and CEST profiles

NMRFAM-SPARKY - chemical shift assignment

NMR spectrometers:

  • Bruker DRX 950 MHz
  • Bruker DRX 850 MHz
  • Bruker DRX 700 MHz
  • Bruker DRX 600 MHz

Related Database Links:

UNP P06224

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