BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 19901

Title: 1H, 13C, and 15N Chemical Shift Assignments for Thymosin alpha 1   PubMed: 25642593

Authors: Nepravishta, Ridvan; Mandaliti, Walter; Eliseo, Tommaso; Sinibaldi Vallebona, Paola; Garaci, Enrico; Paci, Maurizio

Citation: Nepravishta, Ridvan; Mandaliti, Walter; Eliseo, Tommaso; Sinibaldi Vallebona, Paola; Garaci, Enrico; Paci, Maurizio. "Thymosin alpha 1 inserts N terminus into model membranes assuming a helical conformation"  Expert Opin. Biol. Ther. 15, S71-S81 (2015).

Assembly members:
Thymosin_alpha_1_polypeptide, polymer, 29 residues, 3070.300 Da.

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

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
Thymosin_alpha_1_polypeptide: XSDAAVDTSSEITTKDLKEK KEVVEEAEN

Data sets:
Data typeCount
13C chemical shifts81
15N chemical shifts29
1H chemical shifts171

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Thymosin_alpha_1_polypeptide1

Entities:

Entity 1, Thymosin_alpha_1_polypeptide 29 residues - 3070.300 Da.

1   ACESERASPALAALAVALASPTHRSERSER
2   GLUILETHRTHRLYSASPLEULYSGLULYS
3   LYSGLUVALVALGLUGLUALAGLUASN

Samples:

sample_1: Thymosin alpha 1 polypeptide 8 mM; SDS, [U-100% 2H], 80 mM; H2O 90%; D2O 10%

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

NMRView v9.0.0-b110, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz

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