BMRB Entry 50782

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50782

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Title:
MqsA Residues 1-34
Deposition date:
2021-02-19
Original release date:
2022-04-15
Authors:
Vos, Margaret; Peti, Wolfgang; Page, Rebecca
Citation:

Citation: Vos, Margaret; Piraino, Benjamin; LaBreck, Christopher; Rahmani, Negar; Trebino, Catherine; Schoenle, Marta; Peti, Wolfgang; Camberg, Jodi; Page, Rebecca. "Degradation of the E. coli antitoxin MqsA by the proteolytic complex ClpXP is regulated by zinc occupancy and oxidation"  J. Biol. Chem. 298, 101557-101557 (2022).
PubMed: 34974059

Assembly members:

Assembly members:
entity_1, polymer, 36 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GHMKCPVCHQGEMVSGIKDI PYTFRGRKTVLKGIHG

Data sets:
Data typeCount
13C chemical shifts51
15N chemical shifts28
1H chemical shifts28

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MqsA 1-341

Entities:

Entity 1, MqsA 1-34 36 residues - Formula weight is not available

GH are cloning artifacts; MqsA sequence starts with MTD

1   GLYHISMETLYSCYSPROVALCYSHISGLN
2   GLYGLUMETVALSERGLYILELYSASPILE
3   PROTYRTHRPHEARGGLYARGLYSTHRVAL
4   LEULYSGLYILEHISGLY

Samples:

sample_1: MqsA Residues 1-34, [U-99% 15N], 100 uM; sodium phosphate 20 mM; sodium chloride 50 mM; TCEP 0.5 mM

sample_2: MqsA Residues 1-34, [U-99% 15N, U-99% 13C], 85 uM; sodium phosphate 20 mM; sodium chloride 50 mM; TCEP 0.5 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

TOPSPIN v4.1.1 - collection, data analysis

CARA v1.9 - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE NEO 600 MHz
  • Bruker AVANCE NEO 800 MHz

Related Database Links:

NCBI Q46864

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