BMRB Entry 19365

Title:
Solution structure of Lipid Transfer Protein from Lentil Lens Culinaris
Deposition date:
2013-07-16
Original release date:
2013-09-30
Authors:
Gizatullina, Albina; Mineev, Konstantin; Shenkarev, Zakhar
Citation:

Citation: Gizatullina, Albina; Finkina, Ekaterina; Mineev, Konstantin; Melnikova, Daria; Bogdanov, Ivan; Telezhinskaya, Irina; Balandin, Sergey; Shenkarev, Zakhar; Arseniev, Alexander; Ovchinnikova, Tatiana. "Recombinant production and solution structure of lipid transfer protein from lentil Lens culinaris."  Biochem. Biophys. Res. Commun. 439, 427-432 (2013).
PubMed: 23998937

Assembly members:

Assembly members:
Lipid Transfer Protein, polymer, 93 residues, 9299.741 Da.

Natural source:

Natural source:   Common Name: lentil   Taxonomy ID: 3864   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Lens Culinaris

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-His8-TrxL-Lc-LTP2

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts271
15N chemical shifts97
1H chemical shifts615

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Lipid Transfer Protein1

Entities:

Entity 1, Lipid Transfer Protein 93 residues - 9299.741 Da.

1   ALAILESERCYSGLYALAVALTHRSERASP
2   LEUSERPROCYSLEUTHRTYRLEUTHRGLY
3   GLYPROGLYPROSERPROGLNCYSCYSGLY
4   GLYVALLYSLYSLEULEUALAALAALAASN
5   THRTHRPROASPARGGLNALAALACYSASN
6   CYSLEULYSSERALAALAGLYSERILETHR
7   LYSLEUASNTHRASNASNALAALAALALEU
8   PROGLYLYSCYSGLYVALASNILEPROTYR
9   LYSILESERTHRTHRTHRASNCYSASNTHR
10   VALLYSPHE

Samples:

sample_1: Lc-LTP2, [U-100% 15N], 1.4 mM; D2O 100%

sample_2: Lc-LTP2, [U-100% 15N], 1.4 mM; H2O 95%; D2O 5%

sample_3: Lc-LTP2, [U-100% 13C; U-100% 15N], 1.0 – 1.5 mM; H2O, natural source, 95%; D2O, natural source, 5%

sample_conditions_1: ionic strength: 0 M; pH: 5.6; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D DQF-COSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
3D HNHBsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1

Software:

XEASY, Keller and Wuthrich - chemical shift assignment, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - data analysis, structure solution

TALOS, Cornilescu, Delaglio and Bax - refinement

Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Tho - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
GB AAX35807 AAX35810 AAX35811
SP A0AT29 A0AT32 A0AT33
AlphaFold A0AT33 A0AT29 A0AT32

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