BMRB Entry 15884
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15884
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: Backbone 1H, 13C, and 15N Chemical Shift Assignments for CTL9 native state at pH 3.8 PubMed: 18707127
Deposition date: 2008-07-24 Original release date: 2008-09-19
Authors: Shan, Bing; Raleigh, Daniel
Citation: Shan, Bing; Raleigh, Daniel. "The Low pH Unfolded State of the C-terminal Domain of the Ribosomal Protein L9 Contains Significant Secondary Structure in the Absence of Denaturant but is No More Compact than the Low pH Urea Unfolded State" Biochemistry 47, 9565-9573 (2008).
Assembly members:
CTL9, polymer, 92 residues, Formula weight is not available
Natural source: Common Name: Bacillus stearothermophilus Taxonomy ID: 1422 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus stearothermophilus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
CTL9: AAEELANAKKLKEQLEKLTV
TIPAKAGEGGRLFGSITSKQ
IAESLQAQHGLKLDKRKIEL
ADAIRALGYTNVPVKLHPEV
TATLKVHVTEQK
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 257 |
15N chemical shifts | 82 |
1H chemical shifts | 270 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | CTL9 | 1 |
Entities:
Entity 1, CTL9 92 residues - Formula weight is not available
CTL9 is the c terminal domain of protein L9, consisting of residues 58-149
1 | ALA | ALA | GLU | GLU | LEU | ALA | ASN | ALA | LYS | LYS | ||||
2 | LEU | LYS | GLU | GLN | LEU | GLU | LYS | LEU | THR | VAL | ||||
3 | THR | ILE | PRO | ALA | LYS | ALA | GLY | GLU | GLY | GLY | ||||
4 | ARG | LEU | PHE | GLY | SER | ILE | THR | SER | LYS | GLN | ||||
5 | ILE | ALA | GLU | SER | LEU | GLN | ALA | GLN | HIS | GLY | ||||
6 | LEU | LYS | LEU | ASP | LYS | ARG | LYS | ILE | GLU | LEU | ||||
7 | ALA | ASP | ALA | ILE | ARG | ALA | LEU | GLY | TYR | THR | ||||
8 | ASN | VAL | PRO | VAL | LYS | LEU | HIS | PRO | GLU | VAL | ||||
9 | THR | ALA | THR | LEU | LYS | VAL | HIS | VAL | THR | GLU | ||||
10 | GLN | LYS |
Samples:
sample_1: CTL9, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O, [U-100% 2H], 10%; sodium acetate 20 mM; sodium chloride 100 mM
sample_conditions_1: ionic strength: 120 mM; pH: 3.8; pressure: 1 atm; temperature: 298.2 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 CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
HNCACO | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Zhengrong and Bax - processing
NMR spectrometers:
- Bruker Avance 800 MHz
Related Database Links:
BMRB | 15883 17460 |
PDB | |
EMBL | CAA43972 |
GB | AAA22701 AKM20686 AKU26730 KFL16938 KFX34457 |
PRF | 0701226A 1714237A |
REF | WP_033008865 WP_050368025 |
SP | P02417 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts