BMRB Entry 26613
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26613
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Title: Periplasmic chaperone Skp from E. coli in 8 m Urea PubMed: 33087350
Deposition date: 2015-07-15 Original release date: 2020-08-30
Authors: Burmann, Bjoern; Hiller, Sebastian
Citation: Mas, Guillaume; Burmann, Bjorn; Sharpe, Timothy; Claudi, Beatrice; Bumann, Dirk; Hiller, Sebastian. "Regulation of chaperone function by coupled folding and oligomerization" Sci. Adv. 6, eabc5822-eabc5822 (2020).
Assembly members:
Skp, polymer, 162 residues, Formula weight is not available
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28b
Entity Sequences (FASTA):
Skp: MGSSHHHHHHSSGLVPRGSH
MADKIAIVNMGSLFQQVAQK
TGVSNTLENEFKGRASELQR
METDLQAKMKKLQSMKAGSD
RTKLEKDVMAQRQTFAQKAQ
AFEQDRARRSNEERGKLVTR
IQTAVKSVANSQDIDLVVDA
NAVAYNSSDVKDITADVLKQ
VK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 417 |
| 15N chemical shifts | 141 |
| 1H chemical shifts | 141 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Skp | 1 |
Entities:
Entity 1, Skp 162 residues - Formula weight is not available
His-tag including thrombin-cleavage site (residues -20 - 0) followed by mature Skp (residues 1 - 141)
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | ||||
| 3 | MET | ALA | ASP | LYS | ILE | ALA | ILE | VAL | ASN | MET | ||||
| 4 | GLY | SER | LEU | PHE | GLN | GLN | VAL | ALA | GLN | LYS | ||||
| 5 | THR | GLY | VAL | SER | ASN | THR | LEU | GLU | ASN | GLU | ||||
| 6 | PHE | LYS | GLY | ARG | ALA | SER | GLU | LEU | GLN | ARG | ||||
| 7 | MET | GLU | THR | ASP | LEU | GLN | ALA | LYS | MET | LYS | ||||
| 8 | LYS | LEU | GLN | SER | MET | LYS | ALA | GLY | SER | ASP | ||||
| 9 | ARG | THR | LYS | LEU | GLU | LYS | ASP | VAL | MET | ALA | ||||
| 10 | GLN | ARG | GLN | THR | PHE | ALA | GLN | LYS | ALA | GLN | ||||
| 11 | ALA | PHE | GLU | GLN | ASP | ARG | ALA | ARG | ARG | SER | ||||
| 12 | ASN | GLU | GLU | ARG | GLY | LYS | LEU | VAL | THR | ARG | ||||
| 13 | ILE | GLN | THR | ALA | VAL | LYS | SER | VAL | ALA | ASN | ||||
| 14 | SER | GLN | ASP | ILE | ASP | LEU | VAL | VAL | ASP | ALA | ||||
| 15 | ASN | ALA | VAL | ALA | TYR | ASN | SER | SER | ASP | VAL | ||||
| 16 | LYS | ASP | ILE | THR | ALA | ASP | VAL | LEU | LYS | GLN | ||||
| 17 | VAL | LYS |
Samples:
sample_1: Skp, [U-13C; U-15N; U-2H], 0.6 mM; D2O 10%; DSS 50 uM; MES 25 mM; NaCl 150 mM; urea 8 M; H2O 90%
sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 288.15 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 5D APSY HNCOCACB | sample_1 | isotropic | sample_conditions_1 |
| 4D APSY HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.0, Bruker Biospin, Guntert, Herrmann and Wuthrich, Keller and Wuthrich - chemical shift assignment, collection, processing
NMR spectrometers:
- Bruker Ascend 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts