BMRB Entry 27605
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27605
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Gutmans, Daniel; Whittaker, Sara B-M; Asiani, Karishma; Atkinson, R Andrew; Oregioni, Alain; Pfuhl, Mark. "Controlling the dynamics of the Nek2 leucine zipper by engineering of "kinetic" disulphide bonds." PLoS ONE 14, e0210352-e0210352 (2019).
PubMed: 30707691
Assembly members:
LZ2, polymer, 49 residues, 5700 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: pLEICS-07
Entity Sequences (FASTA):
LZ2: GAMASSPVLSELKLKEIQLQ
ERERALKAREERLEQKEQEL
AVRERLACD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 224 |
| 15N chemical shifts | 98 |
| 1H chemical shifts | 522 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | monomer 1 conformer A | 1 |
| 2 | monomer 2 conformer A | 1 |
| 3 | monomer 1 conformer B | 1 |
| 4 | monomer 2 conformer B | 1 |
Entities:
Entity 1, monomer 1 conformer A 49 residues - 5700 Da.
residues 295-298 are leftover of the his-tag. The real sequence starts at S299
| 1 | GLY | ALA | MET | ALA | SER | SER | PRO | VAL | LEU | SER | ||||
| 2 | GLU | LEU | LYS | LEU | LYS | GLU | ILE | GLN | LEU | GLN | ||||
| 3 | GLU | ARG | GLU | ARG | ALA | LEU | LYS | ALA | ARG | GLU | ||||
| 4 | GLU | ARG | LEU | GLU | GLN | LYS | GLU | GLN | GLU | LEU | ||||
| 5 | ALA | VAL | ARG | GLU | ARG | LEU | ALA | CYS | ASP |
Samples:
sample_1: LZ2, [U-98% 15N], 1 ± 0.05 mM; NaCl 50 mM
sample_2: LZ2, [U-95% 13C; U-90% 15N], 1 ± 0.05 mM; NaCl 50 mM
sample_conditions_1: ionic strength: 0.05 M; pH: 7.2; 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 HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HNHB | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.1, Bruker Biospin - processing
CCPN_Analysis v2.4, CCPN - chemical shift assignment, data analysis, peak picking
NMR spectrometers:
- Bruker Avance 900 MHz
- Bruker Avance 700 MHz
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks