BMRB Entry 51402
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51402
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Title: Bacillus subtilis SepF protein assembly (wild type) PubMed: 35799411
Deposition date: 2022-04-19 Original release date: 2022-07-11
Authors: Liu, Wenjing
Citation: Zhang, Chang; Liu, Wenjing; Deng, Jing; Ma, Shaojie; Chang, Ziwei; Yang, Jun. "Structural Insights into the Interaction between Bacillus subtilis SepF Assembly and FtsZ by Solid-State NMR Spectroscopy" J. Phys. Chem. B 126, 5219-5230 (2022).
Assembly members:
entity_1, polymer, 151 residues, Formula weight is not available
Natural source: Common Name: Bacillus subtilis Taxonomy ID: 1423 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus subtilis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-21a
Entity Sequences (FASTA):
entity_1: MSMKNKLKNFFSMEDEEYEY
EYIETERESHEEHEQKEKPA
YNGNKPAGKQNVVSLQSVQK
SSKVVLSEPRVYAEAQEIAD
HLKNRRAVVVNLQRIQHDQA
KRIVDFLSGTVYAIGGDIQR
IGSDIFLCTPDNVDVSGTIS
ELISEDEHQRW
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 310 |
| 15N chemical shifts | 79 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SepF monomer | 1 |
Entities:
Entity 1, SepF monomer 151 residues - Formula weight is not available
| 1 | MET | SER | MET | LYS | ASN | LYS | LEU | LYS | ASN | PHE | ||||
| 2 | PHE | SER | MET | GLU | ASP | GLU | GLU | TYR | GLU | TYR | ||||
| 3 | GLU | TYR | ILE | GLU | THR | GLU | ARG | GLU | SER | HIS | ||||
| 4 | GLU | GLU | HIS | GLU | GLN | LYS | GLU | LYS | PRO | ALA | ||||
| 5 | TYR | ASN | GLY | ASN | LYS | PRO | ALA | GLY | LYS | GLN | ||||
| 6 | ASN | VAL | VAL | SER | LEU | GLN | SER | VAL | GLN | LYS | ||||
| 7 | SER | SER | LYS | VAL | VAL | LEU | SER | GLU | PRO | ARG | ||||
| 8 | VAL | TYR | ALA | GLU | ALA | GLN | GLU | ILE | ALA | ASP | ||||
| 9 | HIS | LEU | LYS | ASN | ARG | ARG | ALA | VAL | VAL | VAL | ||||
| 10 | ASN | LEU | GLN | ARG | ILE | GLN | HIS | ASP | GLN | ALA | ||||
| 11 | LYS | ARG | ILE | VAL | ASP | PHE | LEU | SER | GLY | THR | ||||
| 12 | VAL | TYR | ALA | ILE | GLY | GLY | ASP | ILE | GLN | ARG | ||||
| 13 | ILE | GLY | SER | ASP | ILE | PHE | LEU | CYS | THR | PRO | ||||
| 14 | ASP | ASN | VAL | ASP | VAL | SER | GLY | THR | ILE | SER | ||||
| 15 | GLU | LEU | ILE | SER | GLU | ASP | GLU | HIS | GLN | ARG | ||||
| 16 | TRP |
Samples:
sample_1: SepF 57-151, [U-100% 13C; U-100% 15N], 38.9 % w/w
sample_conditions_1: pH: 8.5; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 13C-detected NCA | sample_1 | isotropic | sample_conditions_1 |
| 2D 13C-13C DARR | sample_1 | isotropic | sample_conditions_1 |
| NCACX | sample_1 | isotropic | sample_conditions_1 |
| NCOCX | sample_1 | isotropic | sample_conditions_1 |
| CONCA | sample_1 | isotropic | sample_conditions_1 |
| 2D NcaCX | sample_1 | isotropic | sample_conditions_1 |
Software:
VNMR - collection
NMRPipe - data analysis
SPARKY - chemical shift assignment
NMR spectrometers:
- Varian Uniform NMR System 600 MHz