BMRB Entry 27353
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27353
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Li, Tao; Li, Shuangli; Liang, Chunjie; Zhu, Jiang; Liu, Maili; Yang, Yunhuang. "Chemical shift assignments of RHE_RS02845, a NTF2-like domain-containing protein from Rhizobium etli" Biomol. NMR Assign. 12, 249-252 (2018).
PubMed: 29572784
Assembly members:
NTF2_containing-domain, polymer, 163 residues, Formula weight is not available
Natural source: Common Name: Rhizobium etli Taxonomy ID: 29449 Superkingdom: Bacteria Kingdom: not available Genus/species: Rhizobium etli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET32M
Entity Sequences (FASTA):
NTF2_containing-domain: MHHHHHHSSGLVPRGSVKDE
AIARHEEEAVIAMLMMRAKA
LGEKNAEEALSYEAEDSVEF
SLAPPLVINGKDKAGLQAWF
DTWEGPIGGEVRDAKLTVGE
GVAFWCGLTRMTGTKTDGTK
VDLWFRQTLGLVKQDGRWLV
THQHASVPFAMDGSGRALLD
LQP
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 301 |
| 15N chemical shifts | 85 |
| 1H chemical shifts | 466 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | RHE_CH00563 | 1 |
Entities:
Entity 1, RHE_CH00563 163 residues - Formula weight is not available
| 1 | MET | HIS | HIS | HIS | HIS | HIS | HIS | SER | SER | GLY | ||||
| 2 | LEU | VAL | PRO | ARG | GLY | SER | VAL | LYS | ASP | GLU | ||||
| 3 | ALA | ILE | ALA | ARG | HIS | GLU | GLU | GLU | ALA | VAL | ||||
| 4 | ILE | ALA | MET | LEU | MET | MET | ARG | ALA | LYS | ALA | ||||
| 5 | LEU | GLY | GLU | LYS | ASN | ALA | GLU | GLU | ALA | LEU | ||||
| 6 | SER | TYR | GLU | ALA | GLU | ASP | SER | VAL | GLU | PHE | ||||
| 7 | SER | LEU | ALA | PRO | PRO | LEU | VAL | ILE | ASN | GLY | ||||
| 8 | LYS | ASP | LYS | ALA | GLY | LEU | GLN | ALA | TRP | PHE | ||||
| 9 | ASP | THR | TRP | GLU | GLY | PRO | ILE | GLY | GLY | GLU | ||||
| 10 | VAL | ARG | ASP | ALA | LYS | LEU | THR | VAL | GLY | GLU | ||||
| 11 | GLY | VAL | ALA | PHE | TRP | CYS | GLY | LEU | THR | ARG | ||||
| 12 | MET | THR | GLY | THR | LYS | THR | ASP | GLY | THR | LYS | ||||
| 13 | VAL | ASP | LEU | TRP | PHE | ARG | GLN | THR | LEU | GLY | ||||
| 14 | LEU | VAL | LYS | GLN | ASP | GLY | ARG | TRP | LEU | VAL | ||||
| 15 | THR | HIS | GLN | HIS | ALA | SER | VAL | PRO | PHE | ALA | ||||
| 16 | MET | ASP | GLY | SER | GLY | ARG | ALA | LEU | LEU | ASP | ||||
| 17 | LEU | GLN | PRO |
Samples:
sample_1: RHE_RS02845, [U-100% 13C; U-100% 15N], 0.5 mM; Tris-HCl 10 mM; DTT 5 mM; NaCl 100 mM; NaN3 0.02%
sample_conditions_1: ionic strength: 0.2 M; pH: 7.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.1, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment
TALOS, Cornilescu, Delaglio and Bax - chemical shift calculation
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 850 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks