BMRB Entry 28058
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR28058
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
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Title: NMR assignment of self-processing module of FrpC protein of Neisseria meningitidis loaded with calcium ions PubMed: 32184239
Deposition date: 2020-01-02 Original release date: 2020-02-20
Authors: Kuban, Vojtech; Zidek, Lukas; Macek, Pavel; Hritz, Jozef; Bumba, Ladislav; M., Faldyna; K., Nedbalcova; K., Nechvatalova
Citation: Kuban, V.; Macek, P.; Hritz, J.; Nechvatalova, K.; Nedbalcova, K.; Faldyna, M.; Zidek, L.; Bumba, L.. "Structural basis of Ca 2+ -dependent self-processing activity of repeat-in-toxin proteins" mBio 11, e00226-20-e00226-20 (2020).
Assembly members:
SPM, polymer, 179 residues, Formula weight is not available
entity_CA, non-polymer, 40.078 Da.
Natural source: Common Name: Neisseria meningitidis Taxonomy ID: 487 Superkingdom: Bacteria Kingdom: not available Genus/species: Neisseria meningitidis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pSPM-His
Entity Sequences (FASTA):
SPM: PLALDLDGDGIETVATKGFS
GSLFDHNRDGIRTATGWVSA
DDGLLVRDLNGNGIIDNGAE
LFGDNTKLADGSFAKHGYAA
LAELDSNGDNIINAADAAFQ
SLRVWQDLNQDGISQANELR
TLEELGIQSLDLAYKDVNKN
LGNGNTLAQQGSYTKTNGTT
AKMGDLLLAADNLHSRFLE
- assigned_chemical_shifts
- heteronucl_NOEs
- heteronucl_T1_relaxation
- heteronucl_T2_relaxation
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 608 |
| 15N chemical shifts | 162 |
| 1H chemical shifts | 974 |
| T1 relaxation values | 124 |
| T2 relaxation values | 124 |
| heteronuclear NOE values | 124 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SPM | 1 |
| 2 | CA | 2 |
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 |
Entity 2, CA - Ca - 40.078 Da.
| 1 | CA |
Samples:
sample_1: SPM, [U-100% 13C; U-100% 15N], 0.4 mM; TRIS 5 mM; sodium chloride 50 mM; sodium azide 0.1%; Calcium chloride 10 mM
sample_conditions_1: ionic strength: 65 mM; pH: 7.4; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D R2 15N,1H correlation | sample_1 | isotropic | sample_conditions_1 |
| 2D R1 15N,1H correlation | sample_1 | isotropic | sample_conditions_1 |
| 2D NOE 15N,1H correlation | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY v3.115, Goddard - chemical shift assignment, peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TOPSPIN v3.2, Bruker Biospin - collection
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 700 MHz
- Bruker Avance 850 MHz
- Bruker Avance 950 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts