BMRB Entry 28040

Title:
Backbone and CB Chemical Shift Assignments of the Methanocaldococcus jannaschii Spt5-KOW domain
Deposition date:
2019-11-11
Original release date:
2023-01-09
Authors:
Zuber, Philipp; Schweimer, Kristian; Knauer, Stefan
Citation:

Citation: Zuber, Philipp; Daviter, Tina; Heissmann, Ramona; Persau, Ulrike; Schweimer, Kristian; Knauer, Stefan. "Structural and thermodynamic analyses of the beta-to-alpha transformation in RfaH reveal principles of fold-switching proteins"  Elife 11, e76630-e76630 (2022).
PubMed: 36255050

Assembly members:

Assembly members:
MjSpt5-KOW, polymer, 69 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: 2190   Superkingdom: Archaea   Kingdom: not available   Genus/species: Methanocaldococcus jannaschii

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETGb1a

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts189
15N chemical shifts62
1H chemical shifts62

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MjSpt5-KOW1

Entities:

Entity 1, MjSpt5-KOW 69 residues - Formula weight is not available

Residues 1-4 result from an engineered TEV-protease cleavage site; residues 5-69 correspond to residues 83-147 of MjSpt5

1   GLYALAMETGLYLYSLYSILEILEGLUASN
2   ILEGLULYSGLYASPVALVALGLUILEILE
3   ALAGLYPROPHELYSGLYGLUARGALALYS
4   VALILEARGVALASPLYSHISLYSGLUGLU
5   VALTHRLEUGLULEUGLUASNALAALAVAL
6   PROILEPROILETHRLEUPROVALGLUGLY
7   VALLYSILEVALSERLYSHISLYSASP

Samples:

sample_1: MjSpt5-KOW, [U-99% 13C; U-99% 15N], 1 mM; potassium phosphate 20 mM; sodium chloride 100 mM; EDTA 1 mM

sample_conditions_1: ionic strength: 0.139 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C ctHSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1

Software:

TOPSPIN vv3.5 pl5, Bruker Biospin - collection

NMRViewJ vv9.2.0-b2, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Ascend Aeon 900 MHz

Related Database Links:

UNP Q57818
AlphaFold Q57818

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