BMRB Entry 52979

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52979

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Title:
Backbone 1H, 13C and 15N chemical shift assignment for human E3 ubiquitin-protein ligase SH3RF1 intrinsically disordered region (315-380)
Deposition date:
2025-03-24
Original release date:
2025-11-05
Authors:
Kjaer, Lenette; Bessa, Luiza; Delaforge, Elise; Jensen, Malene
Citation:

Citation: Kjaer, Lenette; Bessa, Luiza; Delaforge, Elise; Jensen, Malene. "Hierarchical folding-upon-binding of an intrinsically disordered protein"  Nat. Commun. ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 70 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: pEsprit

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GHMWSQASQNRHSMEISPPV LISSSNPTAAARISELSGLS CSAPSQVHISTTGLIVTPPP SSPVTTGPSF

Data sets:
Data typeCount
13C chemical shifts185
15N chemical shifts59
1H chemical shifts59

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1POSH 315-3801

Entities:

Entity 1, POSH 315-380 70 residues - Formula weight is not available

1   GLYHISMETTRPSERGLNALASERGLNASN
2   ARGHISSERMETGLUILESERPROPROVAL
3   LEUILESERSERSERASNPROTHRALAALA
4   ALAARGILESERGLULEUSERGLYLEUSER
5   CYSSERALAPROSERGLNVALHISILESER
6   THRTHRGLYLEUILEVALTHRPROPROPRO
7   SERSERPROVALTHRTHRGLYPROSERPHE

Samples:

sample_1: POSH 315-380, [U-13C; U-15N], 500 uM; sodium phosphate 50 mM; sodium chloride 150 mM; magnesium chloride 5 mM; DTT 10 mM

sample_conditions_1: ionic strength: 0.215 M; pH: 6; pressure: 1 atm; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCOCACBsample_1isotropicsample_conditions_1

Software:

NMRPipe - processing

SPARKY - peak picking

MARS - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 700 MHz

Related Database Links:

UNP Q7Z6J0

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