BMRB Entry 18459
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18459
MolProbity Validation Chart
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: N0 domain of Neisseria meningitidis Pilus assembly protein PilQ PubMed: 23028322
Deposition date: 2012-05-11 Original release date: 2013-01-03
Authors: Phelan, Marie; Berry, J.; Derrick, J.; Lian, L.
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:
TYPE_IV_PILUS_BIOGENESIS_AND_COMPETENCE_PROTEIN_P, polymer, 128 residues, 14465.3886 Da.
Natural source: Common Name: b-proteobacteria Taxonomy ID: 487 Superkingdom: Bacteria Kingdom: Neisseria Genus/species: Neisseria meningitidis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
TYPE_IV_PILUS_BIOGENESIS_AND_COMPETENCE_PROTEIN_P: MKHHHHHHPMSDYDIPTTEN
LYFEGAMGFTGRKISLDFQD
VEIRTILQILAKESGMNIVA
SDSVNGKMTLSLKDVPWDQA
LDLVMQARNLDMRQQGNIVN
IAPRDELLAKDKAFLQAEKD
IADLGALY
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 518 |
| 15N chemical shifts | 133 |
| 1H chemical shifts | 869 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | TYPE IV PILUS BIOGENESIS AND COMPETENCE PROTEIN P | 1 |
Entities:
Entity 1, TYPE IV PILUS BIOGENESIS AND COMPETENCE PROTEIN P 128 residues - 14465.3886 Da.
| 1 | MET | LYS | HIS | HIS | HIS | HIS | HIS | HIS | PRO | MET | ||||
| 2 | SER | ASP | TYR | ASP | ILE | PRO | THR | THR | GLU | ASN | ||||
| 3 | LEU | TYR | PHE | GLU | GLY | ALA | MET | GLY | PHE | THR | ||||
| 4 | GLY | ARG | LYS | ILE | SER | LEU | ASP | PHE | GLN | ASP | ||||
| 5 | VAL | GLU | ILE | ARG | THR | ILE | LEU | GLN | ILE | LEU | ||||
| 6 | ALA | LYS | GLU | SER | GLY | MET | ASN | ILE | VAL | ALA | ||||
| 7 | SER | ASP | SER | VAL | ASN | GLY | LYS | MET | THR | LEU | ||||
| 8 | SER | LEU | LYS | ASP | VAL | PRO | TRP | ASP | GLN | ALA | ||||
| 9 | LEU | ASP | LEU | VAL | MET | GLN | ALA | ARG | ASN | LEU | ||||
| 10 | ASP | MET | ARG | GLN | GLN | GLY | ASN | ILE | VAL | ASN | ||||
| 11 | ILE | ALA | PRO | ARG | ASP | GLU | LEU | LEU | ALA | LYS | ||||
| 12 | ASP | LYS | ALA | PHE | LEU | GLN | ALA | GLU | LYS | ASP | ||||
| 13 | ILE | ALA | ASP | LEU | GLY | ALA | LEU | TYR |
Samples:
sample_1: TYPE IV PILUS BIOGENESIS AND COMPETENCE PROTEIN P, [U-13C; U-15N], 0.5 mM; H2O 10%; D2O 90%
sample_conditions_1: ionic strength: 100.000 mM; pH: 6.800; pressure: 1.000 atm; temperature: 298.000 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D CBCA(CO)NH | sample_1 | solution | sample_conditions_1 |
| 3D HNCACB | sample_1 | solution | sample_conditions_1 |
| 3D HN(CA)CO 3D HNCO | sample_1 | solution | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | solution | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | solution | sample_conditions_1 |
| 3D HBHANH | sample_1 | solution | sample_conditions_1 |
| 2D hbCBcgcdHD | sample_1 | solution | sample_conditions_1 |
| 2D ali 1H-13C HSQC | sample_1 | solution | sample_conditions_1 |
| 2D aro 1H-13C HSQC | sample_1 | solution | sample_conditions_1 |
| 3D ali HC-NOESY | sample_1 | solution | sample_conditions_1 |
| 3D aro HC-NOESY | sample_1 | solution | sample_conditions_1 |
| 3D HN-NOESY | sample_1 | solution | sample_conditions_1 |
| 3D ali HCcH-TOCSY | sample_1 | solution | sample_conditions_1 |
| 3D aro HCcH-TOCSY | sample_1 | solution | sample_conditions_1 |
| 3D HNCACB | sample_1 | solution | sample_conditions_1 |
Software:
AutoDep v4.3, PDBe - collection
CCPN_analysis vany, CCPN - chemical shift assignment
CNS1.2 vany, Brunger, Adams, Clore, Gros, Nilges and Read - chemical shift assignment
CYANA2.1 vany, Guntert, Mumenthaler and Wuthrich - chemical shift assignment
TALOSPLUS vany, Cornilescu, Delaglio and Bax - chemical shift assignment
Topspin2.1 vany, Bruker Biospin - chemical shift assignment
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
- 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