BMRB Entry 28039

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28039

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Title:
Backbone and CB Chemical Shift Assignments for the hSpt5-KOW5 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:
hSpt5-KOW5, polymer, 59 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hSpt5-KOW5: GAMGRRDNELIGQTVRISQG PYKGYIGVVKDATESTARVE LHSTCQTISVDRQRLTTVG

Data sets:
Data typeCount
13C chemical shifts160
15N chemical shifts54
1H chemical shifts54

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1monomer 11

Entities:

Entity 1, monomer 1 59 residues - Formula weight is not available

Residues 1-3 result from an engineered TEV-protease cleavage site; residues 3 -5 correspond to residues 699-754 of hSpt5

1   GLYALAMETGLYARGARGASPASNGLULEU
2   ILEGLYGLNTHRVALARGILESERGLNGLY
3   PROTYRLYSGLYTYRILEGLYVALVALLYS
4   ASPALATHRGLUSERTHRALAARGVALGLU
5   LEUHISSERTHRCYSGLNTHRILESERVAL
6   ASPARGGLNARGLEUTHRTHRVALGLY

Samples:

sample_1: hSpt5-KOW5, [U-99% 13C; U-99% 15N], 0.85 mM; sodium 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
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C ctHSQCsample_1isotropicsample_conditions_1

Software:

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

TOPSPIN vv3.5 pl5, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

UNP O00267
AlphaFold Q99639

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