BMRB Entry 19088
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR19088
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Title: Backbone chemical shift assignment of Rv2140c, a phosphatidylethanolamine binding protein from Mycobacterium tuberculosis PubMed: 23907008
Deposition date: 2013-03-13 Original release date: 2013-08-14
Authors: Eulenberg, Georg; Higman, Victoria; Diehl, Anne; Wilmanns, Matthias; Holton, Simon
Citation: Eulenburg, Georg; Higman, Victoria; Diehl, Anne; Wilmanns, Matthias; Holton, Simon. "Structural and biochemical characterization of Rv2140c, a phosphatidylethanolamine-binding protein from Mycobacterium tuberculosis." FEBS Lett. 587, 2936-2942 (2013).
Assembly members:
Rv2140c, polymer, 176 residues, 18603.878 Da.
Natural source: Common Name: Mycobacterium tuberculosis Taxonomy ID: 1773 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycobacterium tuberculosis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pETM-11
Entity Sequences (FASTA):
Rv2140c: MATSPDPYAALPKLPSFSLT
STSITDGQPLATPQVSGIMG
AGGADASPQLRWSGFPSETR
SFAVTVYDPDAPTLSGFWHW
AVANLPANVTELPEGVGDGR
ELPGGALTLVNDAGMRRYVG
AAPPPGHGVHRYYVAVHAVK
VEKLDLPEDASPAYLGFNLF
QHAIARAVIFGTYEQR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 308 |
| 15N chemical shifts | 155 |
| 1H chemical shifts | 155 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Rv2140c | 1 |
Entities:
Entity 1, Rv2140c 176 residues - 18603.878 Da.
| 1 | MET | ALA | THR | SER | PRO | ASP | PRO | TYR | ALA | ALA | ||||
| 2 | LEU | PRO | LYS | LEU | PRO | SER | PHE | SER | LEU | THR | ||||
| 3 | SER | THR | SER | ILE | THR | ASP | GLY | GLN | PRO | LEU | ||||
| 4 | ALA | THR | PRO | GLN | VAL | SER | GLY | ILE | MET | GLY | ||||
| 5 | ALA | GLY | GLY | ALA | ASP | ALA | SER | PRO | GLN | LEU | ||||
| 6 | ARG | TRP | SER | GLY | PHE | PRO | SER | GLU | THR | ARG | ||||
| 7 | SER | PHE | ALA | VAL | THR | VAL | TYR | ASP | PRO | ASP | ||||
| 8 | ALA | PRO | THR | LEU | SER | GLY | PHE | TRP | HIS | TRP | ||||
| 9 | ALA | VAL | ALA | ASN | LEU | PRO | ALA | ASN | VAL | THR | ||||
| 10 | GLU | LEU | PRO | GLU | GLY | VAL | GLY | ASP | GLY | ARG | ||||
| 11 | GLU | LEU | PRO | GLY | GLY | ALA | LEU | THR | LEU | VAL | ||||
| 12 | ASN | ASP | ALA | GLY | MET | ARG | ARG | TYR | VAL | GLY | ||||
| 13 | ALA | ALA | PRO | PRO | PRO | GLY | HIS | GLY | VAL | HIS | ||||
| 14 | ARG | TYR | TYR | VAL | ALA | VAL | HIS | ALA | VAL | LYS | ||||
| 15 | VAL | GLU | LYS | LEU | ASP | LEU | PRO | GLU | ASP | ALA | ||||
| 16 | SER | PRO | ALA | TYR | LEU | GLY | PHE | ASN | LEU | PHE | ||||
| 17 | GLN | HIS | ALA | ILE | ALA | ARG | ALA | VAL | ILE | PHE | ||||
| 18 | GLY | THR | TYR | GLU | GLN | ARG |
Samples:
Rv2140c_1: Rv2140c, [[U-95% 13C; U-95% 15N]], 0.36 mM; Sodium Chloride 50.00 mM; Phophate buffer 20.00 mM
CondSet1: pH: 7.000; temperature: 300 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | Rv2140c_1 | isotropic | CondSet1 |
| 3D HNCA | Rv2140c_1 | isotropic | CondSet1 |
| 3D HN(CO)CA | Rv2140c_1 | isotropic | CondSet1 |
| 3D HNCO | Rv2140c_1 | isotropic | CondSet1 |
| 3D HN(CA)CO | Rv2140c_1 | isotropic | CondSet1 |
Software:
ANALYSIS v2.1, CCPN - resonance assignment
XWIN-NMR v3.5, Bruker Biospin - data acquisition, data processing
NMR spectrometers:
- Bruker DMX 750 MHz
Related Database Links:
| PDB | |
| DBJ | BAH26435 BAL66151 BAQ06208 GAA45837 |
| EMBL | CAL72145 CCC27222 CCC44496 CCC64734 CCE37614 |
| GB | AAK46482 ABQ73916 ABR06501 ACT24902 AEB03982 |
| REF | NP_216656 NP_855813 WP_003411119 WP_003903767 WP_003904790 |
| SP | P67227 P9WFN0 P9WFN1 |
| AlphaFold | P67227 P9WFN1 P9WFN0 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts