BMRB Entry 19181
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR19181
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: 1H, and 15N Chemical Shift Assignments for mycoloylated PorH in DMSO solution PubMed: 24100136
Deposition date: 2013-04-19 Original release date: 2013-09-25
Authors: Saurel, Olivier; Demange, Pascal; Rath, Parth; Tropis, Maryelle; Daffe, Mamadou; MILON, Alain
Citation: Rath, Parthasarathi; Saurel, Olivier; Tropis, Maryelle; Daffe, Mamadou; Demange, Pascal; Milon, Alain. "NMR localization of the O-mycoloylation on PorH, a channel forming peptide from Corynebacterium glutamicum." FEBS Lett. 587, 3687-3691 (2013).
Assembly members:
PorH, polymer, 74 residues, Formula weight is not available
Natural source: Common Name: High GC Gram+ Taxonomy ID: 1718 Superkingdom: Bacteria Kingdom: not available Genus/species: corynebacterium glutamicum
Experimental source: Production method: recombinant technology Host organism: C. glutamicum PorA PorH
Entity Sequences (FASTA):
PorH: MDLSLLKETLGNYETFGGNI
GTALQSIPTLLDSILNFFDN
FGDLADTTGENLDNFSSIEG
RASRGSHHHHHHHH
- assigned_chemical_shifts
Data type | Count |
15N chemical shifts | 66 |
1H chemical shifts | 351 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | PorH | 1 |
Entities:
Entity 1, PorH 74 residues - Formula weight is not available
1 | MET | ASP | LEU | SER | LEU | LEU | LYS | GLU | THR | LEU | ||||
2 | GLY | ASN | TYR | GLU | THR | PHE | GLY | GLY | ASN | ILE | ||||
3 | GLY | THR | ALA | LEU | GLN | SER | ILE | PRO | THR | LEU | ||||
4 | LEU | ASP | SER | ILE | LEU | ASN | PHE | PHE | ASP | ASN | ||||
5 | PHE | GLY | ASP | LEU | ALA | ASP | THR | THR | GLY | GLU | ||||
6 | ASN | LEU | ASP | ASN | PHE | SER | SER | ILE | GLU | GLY | ||||
7 | ARG | ALA | SER | ARG | GLY | SER | HIS | HIS | HIS | HIS | ||||
8 | HIS | HIS | HIS | HIS |
Samples:
sample_1: PorH, [U-99% 15N], 1 mM; mycolic acid 1 mM; DMSO 100%
sample_conditions_1: temperature: 313 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Keller and Wuthrich - chemical shift assignment
NMR spectrometers:
- 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