BMRB Entry 51087
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51087
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Title: Backbone chemical shift assignment and dynamics of N-terminal domain of ClpB from Francisella tularensis type VI secretion system PubMed: 34985724
Deposition date: 2021-09-17 Original release date: 2021-09-23
Authors: Mushtaq, Ameeq
Citation: Mushtaq, Ameeq Ul; Aden, Jorgen; Alam, Athar; Sjostedt, Anders; Grobner, Gerhard. "Backbone chemical shift assignment and dynamics of the N-terminal domain of ClpB from Francisella tularensis type VI secretion system" Biomol. NMR Assign. 16, 75-79 (2022).
Assembly members:
entity_1, polymer, 156 residues, 17114.35 Da.
Natural source: Common Name: Francisella tularensis Taxonomy ID: 263 Superkingdom: Bacteria Kingdom: not available Genus/species: Francisella tularensis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-His1a
Entity Sequences (FASTA):
entity_1: MNINKFTIKLQEALAEAQSY
AFQQKATEFTSAHILKALLE
QNDSVAISILSVCGVNIQNF
IKAVNDMVDSVAVLSGEGNP
QVTPSRDLIATLHKMQELAN
KNGDEFISSEVFLLASLEDK
SLTGLYNKFGITKEKLTKAV
NDYRGGEKVSSQNQED
- assigned_chemical_shifts
- heteronucl_NOEs
- heteronucl_T1_relaxation
- heteronucl_T2_relaxation
| Data type | Count |
| 13C chemical shifts | 406 |
| 15N chemical shifts | 135 |
| 1H chemical shifts | 135 |
| T1 relaxation values | 131 |
| T2 relaxation values | 131 |
| heteronuclear NOE values | 132 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NTD ClpB | 1 |
Entities:
Entity 1, NTD ClpB 156 residues - 17114.35 Da.
NTD ClpB (1-156)
| 1 | MET | ASN | ILE | ASN | LYS | PHE | THR | ILE | LYS | LEU | ||||
| 2 | GLN | GLU | ALA | LEU | ALA | GLU | ALA | GLN | SER | TYR | ||||
| 3 | ALA | PHE | GLN | GLN | LYS | ALA | THR | GLU | PHE | THR | ||||
| 4 | SER | ALA | HIS | ILE | LEU | LYS | ALA | LEU | LEU | GLU | ||||
| 5 | GLN | ASN | ASP | SER | VAL | ALA | ILE | SER | ILE | LEU | ||||
| 6 | SER | VAL | CYS | GLY | VAL | ASN | ILE | GLN | ASN | PHE | ||||
| 7 | ILE | LYS | ALA | VAL | ASN | ASP | MET | VAL | ASP | SER | ||||
| 8 | VAL | ALA | VAL | LEU | SER | GLY | GLU | GLY | ASN | PRO | ||||
| 9 | GLN | VAL | THR | PRO | SER | ARG | ASP | LEU | ILE | ALA | ||||
| 10 | THR | LEU | HIS | LYS | MET | GLN | GLU | LEU | ALA | ASN | ||||
| 11 | LYS | ASN | GLY | ASP | GLU | PHE | ILE | SER | SER | GLU | ||||
| 12 | VAL | PHE | LEU | LEU | ALA | SER | LEU | GLU | ASP | LYS | ||||
| 13 | SER | LEU | THR | GLY | LEU | TYR | ASN | LYS | PHE | GLY | ||||
| 14 | ILE | THR | LYS | GLU | LYS | LEU | THR | LYS | ALA | VAL | ||||
| 15 | ASN | ASP | TYR | ARG | GLY | GLY | GLU | LYS | VAL | SER | ||||
| 16 | SER | GLN | ASN | GLN | GLU | ASP |
Samples:
sample_1: NTD ClpB (1-156), [U-99% 13C; U-99% 15N], 1.7 mM; NaPi 20 mM; NaCl 20 mM
sample_2: NTD ClpB (1-156), [U-99% 15N], 1.7 mM; NaPi 20 mM; NaCl 20 mM
sample_conditions_1: pH: 6.5; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCANH | 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 HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| T1/R1 relaxation | sample_1 | isotropic | sample_conditions_1 |
| T2/R2 relaxation | sample_1 | isotropic | sample_conditions_1 |
| 1H-15N heteronoe | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.6 - collection
NMRPipe v10.6 - processing
CcpNMR v2.4.2 - data analysis
NMRFAM-SPARKY v1.470 - data analysis
NMR spectrometers:
- Bruker AVANCE III 850 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts