BMRB Entry 52035
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52035
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Title: FapA PubMed: 37798606
Deposition date: 2023-07-13 Original release date: 2023-07-18
Authors: Byeon, Chang-Hyeock; Akbey, Umit
Citation: Byeon, Chang-Hyeock; Akbey, Umit. "Solution-state NMR assignment and secondary structure analysis of the monomeric Pseudomonas biofilm-forming functional amyloid accessory protein FapA" Biomol. NMR Assign. 17, 275-280 (2023).
Assembly members:
entity_1, polymer, 128 residues, Formula weight is not available
Natural source: Common Name: Pseudomonas aeruginosa Taxonomy ID: 287 Superkingdom: Bacteria Kingdom: not available Genus/species: Pseudomonas aeruginosa
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET32
Entity Sequences (FASTA):
entity_1: SGTEDGIIVTGRNVQGFMVG
RPSFGKDPYPSTANANPSQQ
ILRATGGELSDNDFAGVSSG
STITRAILPNGDLPGLSNTL
GNNSAGLGAGAAAGHASGNS
LGGQISGSIERGLAPLNNIG
AMMGVQPW
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 231 |
15N chemical shifts | 120 |
1H chemical shifts | 120 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | FapA | 1 |
Entities:
Entity 1, FapA 128 residues - Formula weight is not available
FapA is a 152 amino acid containing protein. The first 28 amino acid is from the signal peptide that is cleaved in the functional form. In the construct we prepared for NMR analysis, there are four non-native - additional amino acids in this sequence: The first three amino acids 'SGT' and the last 'W' are not natively present in FapA protein. The first three are cleave artifacts, and the last W is added for quantification. The first amino acid of the functional FapA is E(29) and the last amino acid is P(152)
1 | SER | GLY | THR | GLU | ASP | GLY | ILE | ILE | VAL | THR | ||||
2 | GLY | ARG | ASN | VAL | GLN | GLY | PHE | MET | VAL | GLY | ||||
3 | ARG | PRO | SER | PHE | GLY | LYS | ASP | PRO | TYR | PRO | ||||
4 | SER | THR | ALA | ASN | ALA | ASN | PRO | SER | GLN | GLN | ||||
5 | ILE | LEU | ARG | ALA | THR | GLY | GLY | GLU | LEU | SER | ||||
6 | ASP | ASN | ASP | PHE | ALA | GLY | VAL | SER | SER | GLY | ||||
7 | SER | THR | ILE | THR | ARG | ALA | ILE | LEU | PRO | ASN | ||||
8 | GLY | ASP | LEU | PRO | GLY | LEU | SER | ASN | THR | LEU | ||||
9 | GLY | ASN | ASN | SER | ALA | GLY | LEU | GLY | ALA | GLY | ||||
10 | ALA | ALA | ALA | GLY | HIS | ALA | SER | GLY | ASN | SER | ||||
11 | LEU | GLY | GLY | GLN | ILE | SER | GLY | SER | ILE | GLU | ||||
12 | ARG | GLY | LEU | ALA | PRO | LEU | ASN | ASN | ILE | GLY | ||||
13 | ALA | MET | MET | GLY | VAL | GLN | PRO | TRP |
Samples:
sample_1: FapA, [U-13C; U-15N], 200 uM; DSS 1 mM; D2O, [U-99% 2H], 10%; sodium phosphate 20 mM
sample_conditions_1: pH: 7.8; pressure: 1 atm; temperature: 274 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 |
3D HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
Software:
CcpNMR v3.1 - chemical shift assignment
TOPSPIN v3.1 - collection, processing
NMR spectrometers:
- Bruker AVANCE III 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts