BMRB Entry 50555
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50555
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Title: Backbone assignment of B-domain of bacterial Fatty acid kinase bound to palmitic acid PubMed: 35122790
Deposition date: 2020-11-10 Original release date: 2022-02-17
Authors: Royappa, Grace; White, Stephen
Citation: Gullett, Jessica; Cuypers, Maxime; Grace, Christy; Pant, Shashank; Subramanian, Chitra; Tajkhorshid, Emad; Rock, Charles; White, Stephen. "Identification of Structural transitions in bacterial fatty acid binding proteins that permit ligand entry and exit at membranes" J. Biol. Chem. 298, 101676-101676 (2022).
Assembly members:
entity_1, polymer, 308 residues, Formula weight is not available
entity_PLM, non-polymer, 256.424 Da.
Natural source: Common Name: Staphylococcus aureus Taxonomy ID: 1280 Superkingdom: Bacteria Kingdom: not available Genus/species: Staphylococcus aureus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pCS106
Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH
MKIAVMTDSTSYLSQDLIDK
YNIQIAPLSVTFDDGKNFTE
SNEIAIEEFYNKMASSQTIP
TTSQPAIGEWITKYEMLRDQ
GYTDIIVICLSSGISGSYQS
SYQAGEMVEGVNVHAFDSKL
AAMIEGCYVLRAIEMVEEGY
EPQQIIDDLTNMREHTGAYL
IVDDLKNLQKSGRITGAQAW
VGTLLKMKPVLKFEDGKIIP
EEKVRTKKRAIQTLEKKVLD
IVKDFEEVTLFVINGDHFED
GQALYKKLQDDCPSAYQVAY
SEFGPVVAAHLGSGGLGLGY
VGRKIRLT
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 732 |
| 15N chemical shifts | 282 |
| 1H chemical shifts | 282 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | FakB1 chain | 1 |
| 2 | Palmitic Acid | 2 |
Entities:
Entity 1, FakB1 chain 308 residues - Formula weight is not available
Assignment of His tag at the N-terminus is marked by negative number. Actual sequence starts from 21st aminoacid (20 amino acids are from His-tag).
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | ||||
| 3 | MET | LYS | ILE | ALA | VAL | MET | THR | ASP | SER | THR | ||||
| 4 | SER | TYR | LEU | SER | GLN | ASP | LEU | ILE | ASP | LYS | ||||
| 5 | TYR | ASN | ILE | GLN | ILE | ALA | PRO | LEU | SER | VAL | ||||
| 6 | THR | PHE | ASP | ASP | GLY | LYS | ASN | PHE | THR | GLU | ||||
| 7 | SER | ASN | GLU | ILE | ALA | ILE | GLU | GLU | PHE | TYR | ||||
| 8 | ASN | LYS | MET | ALA | SER | SER | GLN | THR | ILE | PRO | ||||
| 9 | THR | THR | SER | GLN | PRO | ALA | ILE | GLY | GLU | TRP | ||||
| 10 | ILE | THR | LYS | TYR | GLU | MET | LEU | ARG | ASP | GLN | ||||
| 11 | GLY | TYR | THR | ASP | ILE | ILE | VAL | ILE | CYS | LEU | ||||
| 12 | SER | SER | GLY | ILE | SER | GLY | SER | TYR | GLN | SER | ||||
| 13 | SER | TYR | GLN | ALA | GLY | GLU | MET | VAL | GLU | GLY | ||||
| 14 | VAL | ASN | VAL | HIS | ALA | PHE | ASP | SER | LYS | LEU | ||||
| 15 | ALA | ALA | MET | ILE | GLU | GLY | CYS | TYR | VAL | LEU | ||||
| 16 | ARG | ALA | ILE | GLU | MET | VAL | GLU | GLU | GLY | TYR | ||||
| 17 | GLU | PRO | GLN | GLN | ILE | ILE | ASP | ASP | LEU | THR | ||||
| 18 | ASN | MET | ARG | GLU | HIS | THR | GLY | ALA | TYR | LEU | ||||
| 19 | ILE | VAL | ASP | ASP | LEU | LYS | ASN | LEU | GLN | LYS | ||||
| 20 | SER | GLY | ARG | ILE | THR | GLY | ALA | GLN | ALA | TRP | ||||
| 21 | VAL | GLY | THR | LEU | LEU | LYS | MET | LYS | PRO | VAL | ||||
| 22 | LEU | LYS | PHE | GLU | ASP | GLY | LYS | ILE | ILE | PRO | ||||
| 23 | GLU | GLU | LYS | VAL | ARG | THR | LYS | LYS | ARG | ALA | ||||
| 24 | ILE | GLN | THR | LEU | GLU | LYS | LYS | VAL | LEU | ASP | ||||
| 25 | ILE | VAL | LYS | ASP | PHE | GLU | GLU | VAL | THR | LEU | ||||
| 26 | PHE | VAL | ILE | ASN | GLY | ASP | HIS | PHE | GLU | ASP | ||||
| 27 | GLY | GLN | ALA | LEU | TYR | LYS | LYS | LEU | GLN | ASP | ||||
| 28 | ASP | CYS | PRO | SER | ALA | TYR | GLN | VAL | ALA | TYR | ||||
| 29 | SER | GLU | PHE | GLY | PRO | VAL | VAL | ALA | ALA | HIS | ||||
| 30 | LEU | GLY | SER | GLY | GLY | LEU | GLY | LEU | GLY | TYR | ||||
| 31 | VAL | GLY | ARG | LYS | ILE | ARG | LEU | THR |
Entity 2, Palmitic Acid - C16 H32 O2 - 256.424 Da.
| 1 | PLM |
Samples:
sample_1: FakB1 bound to Palmitic acid, [U-100% 13C; U-100% 15N], 1 mM; NaCl 200 mM
sample_2: FakB1 bound to Palmitic acid, [U-100% 13C; U-100% 15N; U-80% 2H], 1 mM; NaCl 200 mM
sample_conditions_1: ionic strength: 200 mM; pH: 7.5; pressure: 1 atm; temperature: 313 K
sample_conditions_2: ionic strength: 200 mM; pH: 7.5; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N TROSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D 15N-separated NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N TROSY | sample_2 | isotropic | sample_conditions_2 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_2 |
| 3D 15N-separated NOESY | sample_2 | isotropic | sample_conditions_2 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_2 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_2 |
Software:
CARA - chemical shift assignment, peak picking
TOPSPIN - processing, data collection
NMR spectrometers:
- Bruker AVANCE III 600 MHz
- Bruker AVANCE NEO 700 MHz
- Bruker AVANCE NEO 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts