BMRB Entry 19028
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19028
MolProbity Validation Chart
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: Flexible anchoring of archaeal MBF1 on ribosomes suggests role as recruitment factor
Deposition date: 2013-02-12 Original release date: 2014-06-05
Authors: Launay, Helene; Blombarch, Fabian; van des Oost, John; Christodoulou, John
Citation: Launay, Helene; Blombarch, Fabian; van des Oost, John; Christodoulou, John. "Flexible anchoring of archeal MBF1 on ribosomes suggests role as recruitment factor." Nucleic Acids Res. ., .-..
Assembly members:
MBF1-C, polymer, 106 residues, Formula weight is not available
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):
MBF1-C: ENAELEIVTDYYKIIKTARE
QLGISQQQLAQKLKVSENIV
KRFESGKLKPTISQARQLEK
ILGIKLVTPLENNEESEKEF
DDTGLTLGDVVNIKEGKKLE
HHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 238 |
| 15N chemical shifts | 77 |
| 1H chemical shifts | 77 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | MBF1-C | 1 |
Entities:
Entity 1, MBF1-C 106 residues - Formula weight is not available
| 1 | GLU | ASN | ALA | GLU | LEU | GLU | ILE | VAL | THR | ASP | ||||
| 2 | TYR | TYR | LYS | ILE | ILE | LYS | THR | ALA | ARG | GLU | ||||
| 3 | GLN | LEU | GLY | ILE | SER | GLN | GLN | GLN | LEU | ALA | ||||
| 4 | GLN | LYS | LEU | LYS | VAL | SER | GLU | ASN | ILE | VAL | ||||
| 5 | LYS | ARG | PHE | GLU | SER | GLY | LYS | LEU | LYS | PRO | ||||
| 6 | THR | ILE | SER | GLN | ALA | ARG | GLN | LEU | GLU | LYS | ||||
| 7 | ILE | LEU | GLY | ILE | LYS | LEU | VAL | THR | PRO | LEU | ||||
| 8 | GLU | ASN | ASN | GLU | GLU | SER | GLU | LYS | GLU | PHE | ||||
| 9 | ASP | ASP | THR | GLY | LEU | THR | LEU | GLY | ASP | VAL | ||||
| 10 | VAL | ASN | ILE | LYS | GLU | GLY | LYS | LYS | LEU | GLU | ||||
| 11 | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: MBF1-C, [U-100% 13C; U-100% 15N], 1 mM; sodium chloride 50 mM; D2O 10%; H2O 90%
sample_conditions_1: ionic strength: 0.05 M; pH: 7.4; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Zhengrong and Bax - processing
NMR spectrometers:
- Bruker AMX 700 MHz
- Varian INOVA 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts