BMRB Entry 17675
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17675
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Title: Backbone 1H,15N,13C and 13CB chemical shifts of folded state and denatured state for the N-terminal domain of ribosomal protein L9 (NTL9) V3AI4A double mutant PubMed: 21915914
Deposition date: 2011-05-30 Original release date: 2011-10-12
Authors: Meng, Wenli; Raleigh, Daniel
Citation: Meng, Wenli; Raleigh, Daniel. "Analysis of electrostatic interactions in the denatured state ensemble of the N-terminal domain of L9 under native conditions." Proteins 79, 3500-3510 (2011).
Assembly members:
NTL9_V3AI4A, polymer, 56 residues, Formula weight is not available
Natural source: Common Name: Geobacillus stearothermophilus Taxonomy ID: 1422 Superkingdom: Bacteria Kingdom: not available Genus/species: Geobacillus stearothermophilus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
NTL9_V3AI4A: MKAAFLKDVKGKGKKGEIKN
VADGYANNFLFKQGLAIEAT
PANLKALEAQKQKEQR
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 317 |
15N chemical shifts | 105 |
1H chemical shifts | 210 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | folded state | 1 |
2 | denatured state | 1 |
Entities:
Entity 1, folded state 56 residues - Formula weight is not available
1 | MET | LYS | ALA | ALA | PHE | LEU | LYS | ASP | VAL | LYS | ||||
2 | GLY | LYS | GLY | LYS | LYS | GLY | GLU | ILE | LYS | ASN | ||||
3 | VAL | ALA | ASP | GLY | TYR | ALA | ASN | ASN | PHE | LEU | ||||
4 | PHE | LYS | GLN | GLY | LEU | ALA | ILE | GLU | ALA | THR | ||||
5 | PRO | ALA | ASN | LEU | LYS | ALA | LEU | GLU | ALA | GLN | ||||
6 | LYS | GLN | LYS | GLU | GLN | ARG |
Samples:
15N_sample: NTL9_V3AI4A, [U-99% 15N], 0.5 mM; DSS 0.4 mM; sodium chloride 100 mM; sodium acetate, [U-99% 2H], 20 mM; H2O 90%; D2O 10%
13C15N_sample: NTL9_V3AI4A, [U-99% 13C; U-99% 15N], 0.5 mM; DSS 0.4 mM; sodium chloride 100 mM; sodium acetate, [U-99% 2H], 20 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.12 M; pH: 5.5; pressure: 1 atm; temperature: 285 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | 15N_sample | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | 15N_sample | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | 13C15N_sample | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | 13C15N_sample | isotropic | sample_conditions_1 |
3D HNCACB | 13C15N_sample | isotropic | sample_conditions_1 |
3D HNCACB | 13C15N_sample | isotropic | sample_conditions_1 |
3D HNCO | 13C15N_sample | isotropic | sample_conditions_1 |
3D 1H-15N TOCSY | 15N_sample | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - chemical shift assignment
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts