BMRB Entry 34532
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34532
MolProbity Validation Chart
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NMR-STAR v3 text file.
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Title: NMR structure of water-soluble domain of human Lynx2 (Lypd1) protein PubMed: 33019770
Deposition date: 2020-07-16 Original release date: 2021-01-06
Authors: Kocharovskaya, M.; Paramonov, A.; Lyukmanova, E.; Shenkarev, Z.
Citation: Paramonov, Alexander; Kocharovskaya, Milita; Tsarev, Andrey; Kulbatskii, Dmitrii; Loktyushov, Eugene; Shulepko, Mikhail; Kirpichnikov, Mikhail; Lyukmanova, Ekaterina; Shenkarev, Zakhar. "Structural Diversity and Dynamics of Human Three-Finger Proteins Acting on Nicotinic Acetylcholine Receptors" Int. J. Mol. Sci. 21, 7280-7280 (2020).
Assembly members:
entity_1, polymer, 86 residues, 9390.756 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-22b(+)
Entity Sequences (FASTA):
entity_1: MIQCYQCEEFQLNNDCSSPE
FIVNCTVNVQDMCQKEVMEQ
SAGIMYRKSCASSAACLIAS
AGYQSFCSPGKLNSVCISCC
NTPLCN
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 313 |
| 15N chemical shifts | 86 |
| 1H chemical shifts | 512 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 86 residues - 9390.756 Da.
| 1 | MET | ILE | GLN | CYS | TYR | GLN | CYS | GLU | GLU | PHE | ||||
| 2 | GLN | LEU | ASN | ASN | ASP | CYS | SER | SER | PRO | GLU | ||||
| 3 | PHE | ILE | VAL | ASN | CYS | THR | VAL | ASN | VAL | GLN | ||||
| 4 | ASP | MET | CYS | GLN | LYS | GLU | VAL | MET | GLU | GLN | ||||
| 5 | SER | ALA | GLY | ILE | MET | TYR | ARG | LYS | SER | CYS | ||||
| 6 | ALA | SER | SER | ALA | ALA | CYS | LEU | ILE | ALA | SER | ||||
| 7 | ALA | GLY | TYR | GLN | SER | PHE | CYS | SER | PRO | GLY | ||||
| 8 | LYS | LEU | ASN | SER | VAL | CYS | ILE | SER | CYS | CYS | ||||
| 9 | ASN | THR | PRO | LEU | CYS | ASN |
Samples:
sample_1: Lynx2, [U-98% 13C; U-98% 15N], 0.25 ± 0.03 mM
sample_conditions_1: ionic strength: 10 mM; pH: 6.7; pressure: 1 atm; temperature: 318 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N-TOCSY-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N-NOESY-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C-HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHB | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C TROSY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v3.98.13, Guntert, Mumenthaler and Wuthrich - refinement
TopSpin, Bruker Biospin - collection
CARA v1.8, Keller and Wuthrich - chemical shift assignment
MddNMR, V. Orekhov, V. Jaravine, M. Mayzel, K. Kazimierczuk, Swedish NMR Center, University of Gothenburg - processing
NMR spectrometers:
- Bruker AVANCE III 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts