BMRB Entry 52729

Title:
Single Alpha-Helix in the postsynaptic Drebrin protein
Deposition date:
2024-11-28
Original release date:
2025-04-08
Authors:
Varga, Soma; Permi, Perttu; Gaspari, Zoltan
Citation:

Citation: Varga, Soma; Peterfia, Balint Ferenc; Dudola, Daniel; Farkas, Viktor; Jeffries, Cy; Permi, Perttu; Gaspari, Zoltan. "Dynamic Interchange of Local Residue-Residue Interactions in the Largely Extended Single Alpha-Helix in Drebrin"  Biochem. J. ., .-. (2025).
PubMed: 40192062

Assembly members:

Assembly members:
entity_1, polymer, 74 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: pET-15b

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts281
15N chemical shifts66
1H chemical shifts131

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Drebrin SAH1

Entities:

Entity 1, Drebrin SAH 74 residues - Formula weight is not available

1   GLYSERHISMETLYSASPPROMETLYSARG
2   ILEASNARGGLUGLNPHETRPGLUGLNALA
3   LYSLYSGLUGLUGLULEUARGLYSGLUGLU
4   GLUARGLYSLYSALALEUASPGLUARGLEU
5   ARGPHEGLUGLNGLUARGMETGLUGLNGLU
6   ARGGLNGLUGLNGLUGLUARGGLUARGARG
7   TYRARGGLUARGGLUGLNGLNILEGLUGLU
8   HISARGARGLYS

Samples:

sample_1: Drebrin SAH, [U-100% 13C; U-100% 15N], 0.34 mM; DSS 0.1 mM; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 0.1 mM

sample_conditions_1: ionic strength: 0.07 M; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1D 1Hsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D iHNCOsample_1isotropicsample_conditions_1
3D (H)CC(CO)NHsample_1isotropicsample_conditions_1
3D H(CC)(CO)NHsample_1isotropicsample_conditions_1
4D (HACA)N(CA)CONHsample_1isotropicsample_conditions_1

Software:

TOPSPIN - collection

CcpNMR - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

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