BMRB Entry 17027
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17027
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Citation: Lyukmanova, Ekaterina; Shenkarev, Zakhar; Shulepko, Mikhail; Mineev, Konstantin; Kasheverov, Dieter; Filkin, Igor; Krivolapova, Sergey Yu; Janickova, Alexandra; Dolezal, Helena; Dolgikh, Vladimir; Arseniev, Dmitry; Bertrand, Alexander; Tsetlin, Daniel; Kirpichnikov, Victor. "NMR Structure and Action on Nicotinic Acetylcholine Receptors of Water-soluble Domain of Human LYNX1." J. Biol. Chem. 286, 10618-10627 (2011).
PubMed: 21252236
Assembly members:
Lynx1, polymer, 74 residues, Formula weight is not available
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):
Lynx1: MLDCHVCAYNGDNCFNPMRC
PAMVAYCMTTRTYYTPTRMK
VSKSCVPRCFETVYDGYSKH
ASTTSCCQYDLCNG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 40 |
| 15N chemical shifts | 79 |
| 1H chemical shifts | 458 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Lynx1 | 1 |
Entities:
Entity 1, Lynx1 74 residues - Formula weight is not available
| 1 | MET | LEU | ASP | CYS | HIS | VAL | CYS | ALA | TYR | ASN | ||||
| 2 | GLY | ASP | ASN | CYS | PHE | ASN | PRO | MET | ARG | CYS | ||||
| 3 | PRO | ALA | MET | VAL | ALA | TYR | CYS | MET | THR | THR | ||||
| 4 | ARG | THR | TYR | TYR | THR | PRO | THR | ARG | MET | LYS | ||||
| 5 | VAL | SER | LYS | SER | CYS | VAL | PRO | ARG | CYS | PHE | ||||
| 6 | GLU | THR | VAL | TYR | ASP | GLY | TYR | SER | LYS | HIS | ||||
| 7 | ALA | SER | THR | THR | SER | CYS | CYS | GLN | TYR | ASP | ||||
| 8 | LEU | CYS | ASN | GLY |
Samples:
sample_1: Lynx1, [U-99% 15N], 0.5 mM; acetic acid 20 mM; sodium azide 1 mM; H2O 90%; D2O 10%
sample_2: Lynx1 1.0 mM; acetic acid 20 mM; sodium azide 1 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 21 mM; pH: 5.3; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHB | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_2 | isotropic | sample_conditions_1 |
Software:
CARA v1.8.3, Keller and Wuthrich - chemical shift assignment
NMR spectrometers:
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| GB | AAK01642 AAR00319 AAV74279 AAV74324 EAW82301 |
| REF | NP_001012437 NP_001028116 NP_001266926 NP_803252 NP_803429 |
| SP | Q5IS42 Q5IS87 |
| AlphaFold | Q5IS42 Q5IS87 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
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or all simulated peaks