BMRB Entry 25830
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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/BMR25830
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Title: Solution Structure of Lipid Transfer Protein From Pea Pisum Sativum PubMed: 27137920
Deposition date: 2015-09-30 Original release date: 2016-05-23
Authors: Paramonov, Alexander; Rumynskiy, Eugene; Bogdanov, Ivan; Ovchinnikova, Tatiana; Shenkarev, Zakhar
Citation: Bogdanov, Ivan; Shenkarev, Zakhar; Paramonov, Alexander; Rumynskiy, Eugene; Finkina, Ekaterina; Melnikova, Daria; Arseniev, Alexander; Ovchinnikova, Tatiana. "A novel lipid transfer protein from the pea Pisum sativum: isolation, recombinant expression, solution structure, antifungal activity, lipid binding, and allergenic properties" BMC Plant Biol. 16, 107-107 (2016).
Assembly members:
Ps-LTP1, polymer, 95 residues, 9546.055 Da.
Natural source: Common Name: pea Taxonomy ID: 3888 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Pisum sativum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Ps-LTP1: ALSCGTVSADLAPCVTYLQA
PNNASPPPPCCAGVKKLLAA
ATTTPDRQAACNCLKSAAGS
IPKLNTNNAAALPGKCGVSI
PYKISTSTNCNTVRF
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 379 |
| 15N chemical shifts | 96 |
| 1H chemical shifts | 623 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PS-LTP1 | 1 |
Entities:
Entity 1, PS-LTP1 95 residues - 9546.055 Da.
| 1 | ALA | LEU | SER | CYS | GLY | THR | VAL | SER | ALA | ASP | ||||
| 2 | LEU | ALA | PRO | CYS | VAL | THR | TYR | LEU | GLN | ALA | ||||
| 3 | PRO | ASN | ASN | ALA | SER | PRO | PRO | PRO | PRO | CYS | ||||
| 4 | CYS | ALA | GLY | VAL | LYS | LYS | LEU | LEU | ALA | ALA | ||||
| 5 | ALA | THR | THR | THR | PRO | ASP | ARG | GLN | ALA | ALA | ||||
| 6 | CYS | ASN | CYS | LEU | LYS | SER | ALA | ALA | GLY | SER | ||||
| 7 | ILE | PRO | LYS | LEU | ASN | THR | ASN | ASN | ALA | ALA | ||||
| 8 | ALA | LEU | PRO | GLY | LYS | CYS | GLY | VAL | SER | ILE | ||||
| 9 | PRO | TYR | LYS | ILE | SER | THR | SER | THR | ASN | CYS | ||||
| 10 | ASN | THR | VAL | ARG | PHE |
Samples:
sample_1: PS-LTP1, [U-98% 13C; U-98% 15N], 1 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 10 mM; pH: 5.5; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
Software:
CARA v1.8, Keller and Wuthrich - chemical shift assignment, chemical shift calculation, peak picking
TOPSPIN v2.1, Bruker Biospin - collection, processing
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Bruker Avance 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts