BMRB Entry 17250
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17250
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Title: GNA1946 PubMed: 21188561
Deposition date: 2010-10-12 Original release date: 2012-07-25
Authors: Bonvin, Alexandre; Neumoin, Alexey
Citation: Neumoin, Alexey; Leonchiks, Ainars; Petit, Pierre; Vuillard, Laurent; Pizza, M.; Soriani, Marco; Boelens, Rolf; Bonvin, Alexandre. "1H, 13C and 15N assignment of the GNA1946 outer membrane lipoprotein from Neisseria meningitidis" Biomol. NMR Assignments 5, 135-138 (2011).
Assembly members:
GNA1946, polymer, 287 residues, Formula weight is not available
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):
GNA1946: MKTFFKTLSAAALALILAAC
GGQKDSAPAASASAAADNGA
AKKEIVFGTTVGDFGDMVKE
QIQAELEKKGYTVKLVEFTD
YVRPNLALAEGELDINVFQH
KPYLDDFKKEHNLDITEVFQ
VPTAPLGLYPGKLKSLEEVK
DGSTVSAPNDPSNFARVLVM
LDELGWIKLKDGINPLTASK
ADIAENLKNIKIVELEAAQL
PRSRADVDFAVVNGNYAISS
GMKLTEALFQEPSFAYVNWS
AVKTADKDSQWLKDVTEAYN
SDAFKAYAHKRFEGYKSPAA
WNEGAAK
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 1186 |
15N chemical shifts | 282 |
1H chemical shifts | 1927 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | GNA1946 | 1 |
Entities:
Entity 1, GNA1946 287 residues - Formula weight is not available
1 | MET | LYS | THR | PHE | PHE | LYS | THR | LEU | SER | ALA | ||||
2 | ALA | ALA | LEU | ALA | LEU | ILE | LEU | ALA | ALA | CYS | ||||
3 | GLY | GLY | GLN | LYS | ASP | SER | ALA | PRO | ALA | ALA | ||||
4 | SER | ALA | SER | ALA | ALA | ALA | ASP | ASN | GLY | ALA | ||||
5 | ALA | LYS | LYS | GLU | ILE | VAL | PHE | GLY | THR | THR | ||||
6 | VAL | GLY | ASP | PHE | GLY | ASP | MET | VAL | LYS | GLU | ||||
7 | GLN | ILE | GLN | ALA | GLU | LEU | GLU | LYS | LYS | GLY | ||||
8 | TYR | THR | VAL | LYS | LEU | VAL | GLU | PHE | THR | ASP | ||||
9 | TYR | VAL | ARG | PRO | ASN | LEU | ALA | LEU | ALA | GLU | ||||
10 | GLY | GLU | LEU | ASP | ILE | ASN | VAL | PHE | GLN | HIS | ||||
11 | LYS | PRO | TYR | LEU | ASP | ASP | PHE | LYS | LYS | GLU | ||||
12 | HIS | ASN | LEU | ASP | ILE | THR | GLU | VAL | PHE | GLN | ||||
13 | VAL | PRO | THR | ALA | PRO | LEU | GLY | LEU | TYR | PRO | ||||
14 | GLY | LYS | LEU | LYS | SER | LEU | GLU | GLU | VAL | LYS | ||||
15 | ASP | GLY | SER | THR | VAL | SER | ALA | PRO | ASN | ASP | ||||
16 | PRO | SER | ASN | PHE | ALA | ARG | VAL | LEU | VAL | MET | ||||
17 | LEU | ASP | GLU | LEU | GLY | TRP | ILE | LYS | LEU | LYS | ||||
18 | ASP | GLY | ILE | ASN | PRO | LEU | THR | ALA | SER | LYS | ||||
19 | ALA | ASP | ILE | ALA | GLU | ASN | LEU | LYS | ASN | ILE | ||||
20 | LYS | ILE | VAL | GLU | LEU | GLU | ALA | ALA | GLN | LEU | ||||
21 | PRO | ARG | SER | ARG | ALA | ASP | VAL | ASP | PHE | ALA | ||||
22 | VAL | VAL | ASN | GLY | ASN | TYR | ALA | ILE | SER | SER | ||||
23 | GLY | MET | LYS | LEU | THR | GLU | ALA | LEU | PHE | GLN | ||||
24 | GLU | PRO | SER | PHE | ALA | TYR | VAL | ASN | TRP | SER | ||||
25 | ALA | VAL | LYS | THR | ALA | ASP | LYS | ASP | SER | GLN | ||||
26 | TRP | LEU | LYS | ASP | VAL | THR | GLU | ALA | TYR | ASN | ||||
27 | SER | ASP | ALA | PHE | LYS | ALA | TYR | ALA | HIS | LYS | ||||
28 | ARG | PHE | GLU | GLY | TYR | LYS | SER | PRO | ALA | ALA | ||||
29 | TRP | ASN | GLU | GLY | ALA | ALA | LYS |
Samples:
sample: GNA1946, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 20 mM; sodium chloride 200 mM; H2O 95%; D2O 5%
sample_conditions: pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample | isotropic | sample_conditions |
2D 1H-13C HSQC | sample | isotropic | sample_conditions |
3D HNCO | sample | isotropic | sample_conditions |
3D HNCA | sample | isotropic | sample_conditions |
3D HN(CO)CA | sample | isotropic | sample_conditions |
3D HN(CA)CO | sample | isotropic | sample_conditions |
3D HCCH-TOCSY | sample | isotropic | sample_conditions |
3D CBCA(CO)NH | sample | isotropic | sample_conditions |
3D 1H-15N NOESY | sample | isotropic | sample_conditions |
3D 1H-13C NOESY | sample | isotropic | sample_conditions |
Software:
TOPSPIN v2.1, Bruker Biospin - collection
NMR spectrometers:
- Bruker Avance 900 MHz
Related Database Links:
PDB | |
EMBL | CAM07784 CAM11078 CAX50901 CBA03352 CBA03733 |
GB | AAF42275 AAF42629 AAF42630 AAF42631 AAF42632 |
REF | NP_274940 WP_002214810 WP_002218060 WP_002221629 WP_002223094 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts