BMRB Entry 26321
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26321
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Title: Backbone resonance assignment of a LysM domain of a chitinase-A from Equisetum arvense PubMed: 35696910
Deposition date: 2021-10-05 Original release date: 2022-06-16
Authors: Kitaoku, Yoshihito; Ohnuma, Takayuki; Fukamizo, Tamo
Citation: Kitaoku, Yoshihito; Taira, Toki; Numata, Tomoyuki; Ohnuma, Takayuki; Fukamizo, Tamo. "Structure, mechanism, and phylogeny of LysM-chitinase conjugates specifically found in fern plants." Plant Sci. 321, 111310-. (2022).
Assembly members:
LysM, polymer, 50 residues, Formula weight is not available
Natural source: Common Name: not available Taxonomy ID: 3258 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Equisetum arvense
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pETBlue-1
Entity Sequences (FASTA):
LysM: ACTSYYTVKSGDICYNIAQT
YGIDVATLQSYNPGLQCDNL
QIGQQLCVAD
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 146 |
15N chemical shifts | 48 |
1H chemical shifts | 48 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | LysM | 1 |
Entities:
Entity 1, LysM 50 residues - Formula weight is not available
1 | ALA | CYS | THR | SER | TYR | TYR | THR | VAL | LYS | SER | |
2 | GLY | ASP | ILE | CYS | TYR | ASN | ILE | ALA | GLN | THR | |
3 | TYR | GLY | ILE | ASP | VAL | ALA | THR | LEU | GLN | SER | |
4 | TYR | ASN | PRO | GLY | LEU | GLN | CYS | ASP | ASN | LEU | |
5 | GLN | ILE | GLY | GLN | GLN | LEU | CYS | VAL | ALA | ASP |
Samples:
sample_1: LysM, [U-99% 13C; U-99% 15N], 151 uM; sodium acetate 20 mM; H2O 90%; D2O, U-2H, 10%
sample_conditions_1: ionic strength: 20 mM; pH: 5; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN - collection
NMRPipe - data analysis
NMRDraw - data analysis
NMRFAM-SPARKY - chemical shift assignment
NMR spectrometers:
- Bruker Avance 500 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts