BMRB Entry 18966
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18966
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Title: Global folded of the type IV pilin ComP from Neisseria meningitidis PubMed: 23386723
Deposition date: 2013-01-21 Original release date: 2013-02-11
Authors: Simpson, Peter
Citation: Cehovin, Ana; Simpson, Peter; McDowell, Melanie; Brown, Daniel; Noschese, Rossella; Pallett, Mitchell; Brady, Jacob; Baldwin, Geoffrey; Lea, Susan; Matthews, Stephen; Pelicic, Vladimir. "Specific DNA recognition mediated by a type IV pilin." Proc. Natl. Acad. Sci. U.S.A. 110, 3065-3070 (2013).
Assembly members:
ComP, polymer, 119 residues, 13512.874 Da.
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):
ComP: ISEFEKAKINAVRAALLENA
HFMEKFYLQNGRFKQTSTKW
PSLPIKEAEGFCIRLNGIAR
GALDSKFMLKAVAIDKDKNP
FIIKMNENLVTFICKKSASS
CSDGLDYFKGNDKDCKLFK
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 466 |
15N chemical shifts | 93 |
1H chemical shifts | 709 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | ComP | 1 |
Entities:
Entity 1, ComP 119 residues - 13512.874 Da.
1 | ILE | SER | GLU | PHE | GLU | LYS | ALA | LYS | ILE | ASN | ||||
2 | ALA | VAL | ARG | ALA | ALA | LEU | LEU | GLU | ASN | ALA | ||||
3 | HIS | PHE | MET | GLU | LYS | PHE | TYR | LEU | GLN | ASN | ||||
4 | GLY | ARG | PHE | LYS | GLN | THR | SER | THR | LYS | TRP | ||||
5 | PRO | SER | LEU | PRO | ILE | LYS | GLU | ALA | GLU | GLY | ||||
6 | PHE | CYS | ILE | ARG | LEU | ASN | GLY | ILE | ALA | ARG | ||||
7 | GLY | ALA | LEU | ASP | SER | LYS | PHE | MET | LEU | LYS | ||||
8 | ALA | VAL | ALA | ILE | ASP | LYS | ASP | LYS | ASN | PRO | ||||
9 | PHE | ILE | ILE | LYS | MET | ASN | GLU | ASN | LEU | VAL | ||||
10 | THR | PHE | ILE | CYS | LYS | LYS | SER | ALA | SER | SER | ||||
11 | CYS | SER | ASP | GLY | LEU | ASP | TYR | PHE | LYS | GLY | ||||
12 | ASN | ASP | LYS | ASP | CYS | LYS | LEU | PHE | LYS |
Samples:
sample_1: ComP, [U-100% 13C; U-100% 15N], 0.1 0.5 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.05 M; pH: 6.7; pressure: 1 atm; temperature: 310 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
ARIA, Linge, O, . - structure solution
NMR spectrometers:
- Bruker DRX 800 MHz
- Bruker DRX 600 MHz
Related Database Links:
PDB | |
EMBL | CAM07712 CAM11151 CAX50978 CBA03591 CBN88156 |
GB | AAF62338 AAW89839 ABX72399 ADO32435 ADY94460 |
REF | NP_275008 WP_002214937 WP_002218144 WP_002221685 WP_002233205 |
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