BMRB Entry 16344
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16344
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Title: Solution structure and backbone dynamics of the ribosomal protein S6wt. PubMed: 19966220
Deposition date: 2009-06-10 Original release date: 2009-12-16
Authors: Ohman, Anders; Oliveberg, Mikael; Oman, Tommy
Citation: Haglund, Ellinor; Lind, Jesper; Oman, Tommy; Ohman, Anders; Maler, Lena; Oliveberg, Mikael. "The HD-exchange motions of ribosomal protein S6 are insensitive to reversal of the protein-folding pathway." Proc. Natl. Acad. Sci. U.S.A. 106, 21619-21624 (2009).
Assembly members:
S6wt, polymer, 101 residues, 11972.7 Da.
Natural source: Common Name: Thermus thermophilus Taxonomy ID: 274 Superkingdom: Bacteria Kingdom: not available Genus/species: Thermus thermophilus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
S6wt: MRRYEVNIVLNPNLDQSQLA
LEKEIIQRALENYGARVEKV
EELGLRRLAYPIAKDPQGYF
LWYQVEMPEDRVNDLARELR
IRDNVRRVMVVKSQEPFLAN
A
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 106 |
| 1H chemical shifts | 659 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | S6wt | 1 |
Entities:
Entity 1, S6wt 101 residues - 11972.7 Da.
| 1 | MET | ARG | ARG | TYR | GLU | VAL | ASN | ILE | VAL | LEU | ||||
| 2 | ASN | PRO | ASN | LEU | ASP | GLN | SER | GLN | LEU | ALA | ||||
| 3 | LEU | GLU | LYS | GLU | ILE | ILE | GLN | ARG | ALA | LEU | ||||
| 4 | GLU | ASN | TYR | GLY | ALA | ARG | VAL | GLU | LYS | VAL | ||||
| 5 | GLU | GLU | LEU | GLY | LEU | ARG | ARG | LEU | ALA | TYR | ||||
| 6 | PRO | ILE | ALA | LYS | ASP | PRO | GLN | GLY | TYR | PHE | ||||
| 7 | LEU | TRP | TYR | GLN | VAL | GLU | MET | PRO | GLU | ASP | ||||
| 8 | ARG | VAL | ASN | ASP | LEU | ALA | ARG | GLU | LEU | ARG | ||||
| 9 | ILE | ARG | ASP | ASN | VAL | ARG | ARG | VAL | MET | VAL | ||||
| 10 | VAL | LYS | SER | GLN | GLU | PRO | PHE | LEU | ALA | ASN | ||||
| 11 | ALA |
Samples:
sample_1: entity, [U-15N], 0.8 – 1.2 mM; MES 20 mM; sodium chloride 50 mM; H2O 95%; D2O 5%
sample_2: entity0.8 – 1.2 mM; sodium chloride 50 mM; D2O 100%
sample_conditions_1: ionic strength: 0.06 M; pH: 6.3; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | 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 HNHA | sample_1 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
xwinnmr/TOPSPIN, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
ANSIG, Kraulis - chemical shift assignment, data analysis, peak picking
X-PLOR, Brunger - geometry optimization, refinement, structure solution
AQUA, Rullmann, Doreleijers and Kaptein - data analysis
ProcheckNMR, Laskowski and MacArthur - structure solution
TALOS, Cornilescu, Delaglio and Bax - data analysis
Molmol, Koradi, Billeter and Wuthrich - structure solution
Mulder, P. Padrta & V. Sklenar - data analysis
NMR spectrometers:
- Bruker DRX 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAD70068 |
| GB | AAF27295 AAS82082 AEG32576 AFH38067 EIA40156 |
| PIR | S43389 |
| REF | WP_011174099 WP_038034932 YP_143511 |
| SP | P23370 P62666 Q5SLP8 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts