BMRB Entry 19365
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19365
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Title: Solution structure of Lipid Transfer Protein from Lentil Lens Culinaris PubMed: 23998937
Deposition date: 2013-07-16 Original release date: 2013-09-30
Authors: Gizatullina, Albina; Mineev, Konstantin; Shenkarev, Zakhar
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).
Assembly members:
Lipid Transfer Protein, polymer, 93 residues, 9299.741 Da.
Natural source: Common Name: lentil Taxonomy ID: 3864 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Lens Culinaris
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Lipid Transfer Protein: AISCGAVTSDLSPCLTYLTG
GPGPSPQCCGGVKKLLAAAN
TTPDRQAACNCLKSAAGSIT
KLNTNNAAALPGKCGVNIPY
KISTTTNCNTVKF
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 271 |
| 15N chemical shifts | 97 |
| 1H chemical shifts | 615 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Lipid Transfer Protein | 1 |
Entities:
Entity 1, Lipid Transfer Protein 93 residues - 9299.741 Da.
| 1 | ALA | ILE | SER | CYS | GLY | ALA | VAL | THR | SER | ASP | ||||
| 2 | LEU | SER | PRO | CYS | LEU | THR | TYR | LEU | THR | GLY | ||||
| 3 | GLY | PRO | GLY | PRO | SER | PRO | GLN | CYS | CYS | GLY | ||||
| 4 | GLY | VAL | LYS | LYS | LEU | LEU | ALA | ALA | ALA | ASN | ||||
| 5 | THR | THR | PRO | ASP | ARG | GLN | ALA | ALA | CYS | ASN | ||||
| 6 | CYS | LEU | LYS | SER | ALA | ALA | GLY | SER | ILE | THR | ||||
| 7 | LYS | LEU | ASN | THR | ASN | ASN | ALA | ALA | ALA | LEU | ||||
| 8 | PRO | GLY | LYS | CYS | GLY | VAL | ASN | ILE | PRO | TYR | ||||
| 9 | LYS | ILE | SER | THR | THR | THR | ASN | CYS | ASN | THR | ||||
| 10 | VAL | LYS | PHE |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D DQF-COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNHB | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_3 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_3 | isotropic | sample_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
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts