BMRB Entry 18428
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18428
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Title: N0N1 domains of Neisseria meningitidis Pilus assembly protein PilQ PubMed: 23028322
Deposition date: 2012-04-27 Original release date: 2013-01-03
Authors: Phelan, Marie; Berry, Jamie-Lee; Derrick, jeremy; Lian, Lu-Yun
Citation: Berry, Jamie-Lee; Phelan, Marie; Collins, Richard; Adomavicius, Tomas; Tnjum, Tone; Frye, Stefan; Bird, Louise; Owens, Ray; Ford, Robert; Lian, Lu-Yun; Derrick, Jeremy. "Structure and assembly of a trans-periplasmic channel for type IV pili in Neisseria meningitidis." PLoS Pathog. 8, .-. (2012).
Assembly members:
PilQ_N0N1, polymer, 237 residues, 26149.8016 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
Entity Sequences (FASTA):
PilQ_N0N1: MGSSHHHHHHSSGLVPRGSH
MASMTGGQQMGRGSFTGRKI
SLDFQDVEIRTILQILAKES
GMNIVASDSVNGKMTLSLKD
VPWDQALDLVMQARNLDMRQ
QGNIVNIAPRDELLAKDKAF
LQAEKDIADLGALYSQNFQL
KYKNVEEFRSILRLDNADTT
GNRNTLVSGRGSVLIDPATN
TLIVTDTRSVIEKFRKLIDE
LDVPAQQVMIEARIVEAADG
FSRDLGVKFGATGKKKL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 721 |
| 15N chemical shifts | 209 |
| 1H chemical shifts | 965 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PilQ_N0N1 | 1 |
Entities:
Entity 1, PilQ_N0N1 237 residues - 26149.8016 Da.
M309-S342 = non-native purification tag F343-L545 PilQ N0N1 domains
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | ||||
| 3 | MET | ALA | SER | MET | THR | GLY | GLY | GLN | GLN | MET | ||||
| 4 | GLY | ARG | GLY | SER | PHE | THR | GLY | ARG | LYS | ILE | ||||
| 5 | SER | LEU | ASP | PHE | GLN | ASP | VAL | GLU | ILE | ARG | ||||
| 6 | THR | ILE | LEU | GLN | ILE | LEU | ALA | LYS | GLU | SER | ||||
| 7 | GLY | MET | ASN | ILE | VAL | ALA | SER | ASP | SER | VAL | ||||
| 8 | ASN | GLY | LYS | MET | THR | LEU | SER | LEU | LYS | ASP | ||||
| 9 | VAL | PRO | TRP | ASP | GLN | ALA | LEU | ASP | LEU | VAL | ||||
| 10 | MET | GLN | ALA | ARG | ASN | LEU | ASP | MET | ARG | GLN | ||||
| 11 | GLN | GLY | ASN | ILE | VAL | ASN | ILE | ALA | PRO | ARG | ||||
| 12 | ASP | GLU | LEU | LEU | ALA | LYS | ASP | LYS | ALA | PHE | ||||
| 13 | LEU | GLN | ALA | GLU | LYS | ASP | ILE | ALA | ASP | LEU | ||||
| 14 | GLY | ALA | LEU | TYR | SER | GLN | ASN | PHE | GLN | LEU | ||||
| 15 | LYS | TYR | LYS | ASN | VAL | GLU | GLU | PHE | ARG | SER | ||||
| 16 | ILE | LEU | ARG | LEU | ASP | ASN | ALA | ASP | THR | THR | ||||
| 17 | GLY | ASN | ARG | ASN | THR | LEU | VAL | SER | GLY | ARG | ||||
| 18 | GLY | SER | VAL | LEU | ILE | ASP | PRO | ALA | THR | ASN | ||||
| 19 | THR | LEU | ILE | VAL | THR | ASP | THR | ARG | SER | VAL | ||||
| 20 | ILE | GLU | LYS | PHE | ARG | LYS | LEU | ILE | ASP | GLU | ||||
| 21 | LEU | ASP | VAL | PRO | ALA | GLN | GLN | VAL | MET | ILE | ||||
| 22 | GLU | ALA | ARG | ILE | VAL | GLU | ALA | ALA | ASP | GLY | ||||
| 23 | PHE | SER | ARG | ASP | LEU | GLY | VAL | LYS | PHE | GLY | ||||
| 24 | ALA | THR | GLY | LYS | LYS | LYS | LEU |
Samples:
sample_1: PilQ_N0N1, [U-98% 13C; U-98% 15N], 600 ± 100 uM; sodium chloride 50 ± 1 mM; potassium phosphate 50 ± 1 mM; sodium azide 0.2 ± 0.02 %; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| CBCACONH (H[N[co[{CA|ca[C]}]]]) | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| HNCACO (H[N[ca[CO]]]) | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC/HMQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC/HMQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC/HMQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| hbhaconh (H[N[co[{ca[H]|ca[c[H]]}]]]) | sample_1 | isotropic | sample_conditions_1 |
| hbhanh (H[N[{ca[H]|ca[c[H]}]]) | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC/HMQC | sample_1 | isotropic | sample_conditions_1 |
| Cb_Hd (hbCBcgcdHD) | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
ANALYSIS v2.1, CCPN - chemical shift assignment, data analysis, peak picking
TOPSPIN v2.1, Bruker - Processing and acquisition
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts