BMRB Entry 19860
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19860
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Title: Solution structure of a ribosomal protein PubMed: 24875358
Deposition date: 2014-03-17 Original release date: 2014-06-09
Authors: Feng, Yingang
Citation: Feng, Yingang; Song, Xiaxia; Lin, Jinzhong; Xuan, Jinsong; Cui, Qiu; Wang, Jinfeng. "Structure determination of archaea-specific ribosomal protein L46a reveals a novel protein fold." Biochem. Biophys. Res. Commun. 450, 67-72 (2014).
Assembly members:
rib_prot, polymer, 77 residues, 9223.893 Da.
Natural source: Common Name: crenarchaeotes Taxonomy ID: 2287 Superkingdom: Archaea Kingdom: not available Genus/species: Sulfolobus solfataricus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
rib_prot: MLKHGKYVYIDLNNGKYVKV
RILKSRDDNSVEKYVLTSHV
SKNRPKNAIVIKMDNLPIEV
KDKLTRFFLLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 360 |
| 15N chemical shifts | 83 |
| 1H chemical shifts | 579 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | rib_prot | 1 |
Entities:
Entity 1, rib_prot 77 residues - 9223.893 Da.
| 1 | MET | LEU | LYS | HIS | GLY | LYS | TYR | VAL | TYR | ILE | ||||
| 2 | ASP | LEU | ASN | ASN | GLY | LYS | TYR | VAL | LYS | VAL | ||||
| 3 | ARG | ILE | LEU | LYS | SER | ARG | ASP | ASP | ASN | SER | ||||
| 4 | VAL | GLU | LYS | TYR | VAL | LEU | THR | SER | HIS | VAL | ||||
| 5 | SER | LYS | ASN | ARG | PRO | LYS | ASN | ALA | ILE | VAL | ||||
| 6 | ILE | LYS | MET | ASP | ASN | LEU | PRO | ILE | GLU | VAL | ||||
| 7 | LYS | ASP | LYS | LEU | THR | ARG | PHE | PHE | LEU | LEU | ||||
| 8 | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: rib_prot, [U-13C; U-15N], 0.5 – 1.0 mM; potassium phosphate 50 mM; potassium chloride 50 mM; EDTA 2 mM; DSS 0.02%; H2O 90%; D2O, [U-100% 2H], 10%
sample_conditions_1: ionic strength: 100 mM; pH: 6.0; 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 | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHANH | sample_1 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
xwinnmr, Bruker Biospin - collection
Felix, Accelrys Software Inc. - processing
NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
SANE, Duggan, Legge, Dyson & Wright - refinement
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Bruker DMX 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts