BMRB Entry 19915
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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/BMR19915
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Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for cold shock protein, TaCsp PubMed: 25101648
Deposition date: 2014-04-17 Original release date: 2014-08-25
Authors: Jeong, Ki-woong; Kim, Yangmee
Citation: Jin, Bonghwan; Jeong, Ki-Woong; Kim, Yangmee. "Structure and flexibility of the thermophilic cold-shock protein of Thermus aquaticus." Biochem. Biophys. Res. Commun. 451, 402-407 (2014).
Assembly members:
entity, polymer, 68 residues, 7692.736 Da.
Natural source: Common Name: thermophilic bacteria Taxonomy ID: 271 Superkingdom: Bacteria Kingdom: not available Genus/species: thermus aquaticus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: MKKGTVKWFNAEKGYGFIQQ
EEGPDVFVHFTAIEADGFRT
LNEGEHVEFEVEPGRGGKGP
QAKKVRRI
- assigned_chemical_shifts
Data type | Count |
1H chemical shifts | 380 |
13C chemical shifts | 155 |
15N chemical shifts | 66 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | entity | 1 |
Entities:
Entity 1, entity 68 residues - 7692.736 Da.
1 | MET | LYS | LYS | GLY | THR | VAL | LYS | TRP | PHE | ASN | ||||
2 | ALA | GLU | LYS | GLY | TYR | GLY | PHE | ILE | GLN | GLN | ||||
3 | GLU | GLU | GLY | PRO | ASP | VAL | PHE | VAL | HIS | PHE | ||||
4 | THR | ALA | ILE | GLU | ALA | ASP | GLY | PHE | ARG | THR | ||||
5 | LEU | ASN | GLU | GLY | GLU | HIS | VAL | GLU | PHE | GLU | ||||
6 | VAL | GLU | PRO | GLY | ARG | GLY | GLY | LYS | GLY | PRO | ||||
7 | GLN | ALA | LYS | LYS | VAL | ARG | ARG | ILE |
Samples:
sample_1: potassium phosphate 50 mM; KCl 100 mM; EDTA 0.1 mM; Thermus aquaticus cold shock protein, [U-99% 13C; U-99% 15N], 0.8 mM; H2O 90%; D2O 10%
Tacsp_free_condition1: pH: 6; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D HNCO | sample_1 | isotropic | Tacsp_free_condition1 |
3D HN(CA)CO | sample_1 | isotropic | Tacsp_free_condition1 |
3D CBCA(CO)NH | sample_1 | isotropic | Tacsp_free_condition1 |
3D HN(CO)CA | sample_1 | isotropic | Tacsp_free_condition1 |
3D HBHA(CO)NH | sample_1 | isotropic | Tacsp_free_condition1 |
3D HNHA | sample_1 | isotropic | Tacsp_free_condition1 |
3D HCCH-TOCSY | sample_1 | isotropic | Tacsp_free_condition1 |
3D 1H-15N NOESY | sample_1 | isotropic | Tacsp_free_condition1 |
3D 1H-13C NOESY | sample_1 | isotropic | Tacsp_free_condition1 |
2D 1H-15N HSQC | sample_1 | isotropic | Tacsp_free_condition1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - chemical shift calculation
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 500 MHz
Related Database Links:
BMRB | 19916 |
PDB | |
GB | ALJ89896 EED09135 KOX89549 |
REF | WP_003049060 WP_018110812 WP_022797725 WP_053768577 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts