BMRB Entry 26530
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26530
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: NMR assignment of intrinsically disordered self-processing module of FrpC protein of Neisseria meningitidis PubMed: 26138689
Deposition date: 2015-03-06 Original release date: 2015-12-04
Authors: Kuban, Vojtech; Zidek, Lukas; Novacek, Jiri; Bumba, Ladislav
Citation: Kuban, Vojtech; Novacek, Jiri; Bumba, Ladislav; Zidek, Lukas. "NMR assignment of intrinsically disordered self-processing module of the FrpC protein of Neisseria meningitidis" Biomol NMR Assign. 9, 435-440 (2015).
Assembly members:
Self-processing_module_of_FrpC, polymer, 179 residues, Formula weight is not available
Natural source: Common Name: b-proteobacteria Taxonomy ID: 487 Superkingdom: Bacteria Kingdom: not available Genus/species: Neisseria meningitidis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Self-processing_module_of_FrpC: PLALDLDGDGIETVATKGFS
GSLFDHNRDGIRTATGWVSA
DDGLLVRDLNGNGIIDNGAE
LFGDNTKLADGSFAKHGYAA
LAELDSNGDNIINAADAAFQ
SLRVWQDLNQDGISQANELR
TLEELGIQSLDLAYKDVNKN
LGNGNTLAQQGSYTKTNGTT
AKMGDLLLAADNLHSRFLE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 460 |
| 15N chemical shifts | 154 |
| 1H chemical shifts | 608 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SPM | 1 |
Entities:
Entity 1, SPM 179 residues - Formula weight is not available
| 1 | PRO | LEU | ALA | LEU | ASP | LEU | ASP | GLY | ASP | GLY | ||||
| 2 | ILE | GLU | THR | VAL | ALA | THR | LYS | GLY | PHE | SER | ||||
| 3 | GLY | SER | LEU | PHE | ASP | HIS | ASN | ARG | ASP | GLY | ||||
| 4 | ILE | ARG | THR | ALA | THR | GLY | TRP | VAL | SER | ALA | ||||
| 5 | ASP | ASP | GLY | LEU | LEU | VAL | ARG | ASP | LEU | ASN | ||||
| 6 | GLY | ASN | GLY | ILE | ILE | ASP | ASN | GLY | ALA | GLU | ||||
| 7 | LEU | PHE | GLY | ASP | ASN | THR | LYS | LEU | ALA | ASP | ||||
| 8 | GLY | SER | PHE | ALA | LYS | HIS | GLY | TYR | ALA | ALA | ||||
| 9 | LEU | ALA | GLU | LEU | ASP | SER | ASN | GLY | ASP | ASN | ||||
| 10 | ILE | ILE | ASN | ALA | ALA | ASP | ALA | ALA | PHE | GLN | ||||
| 11 | SER | LEU | ARG | VAL | TRP | GLN | ASP | LEU | ASN | GLN | ||||
| 12 | ASP | GLY | ILE | SER | GLN | ALA | ASN | GLU | LEU | ARG | ||||
| 13 | THR | LEU | GLU | GLU | LEU | GLY | ILE | GLN | SER | LEU | ||||
| 14 | ASP | LEU | ALA | TYR | LYS | ASP | VAL | ASN | LYS | ASN | ||||
| 15 | LEU | GLY | ASN | GLY | ASN | THR | LEU | ALA | GLN | GLN | ||||
| 16 | GLY | SER | TYR | THR | LYS | THR | ASN | GLY | THR | THR | ||||
| 17 | ALA | LYS | MET | GLY | ASP | LEU | LEU | LEU | ALA | ALA | ||||
| 18 | ASP | ASN | LEU | HIS | SER | ARG | PHE | LEU | GLU |
Samples:
sample_1: Self-processing module of FrpC, [U-100% 13C; U-100% 15N], 0.35 mM; sodium chloride 50 mM; sodium azide 0.1 % v/v; TRIS 5 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 55 mM; pH: 7.4; pressure: 1 atm; temperature: 303.2 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D CON | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 4D HCBCACON | sample_1 | isotropic | sample_conditions_1 |
| 4D HCBCANCO | sample_1 | isotropic | sample_conditions_1 |
| 5D HN(CA)CONH | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - data analysis
TOPSPIN, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
MFT, W. Kozminski - processing
NMR spectrometers:
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts