BMRB Entry 15236
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15236
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Title: 1H, 15N backbone chemical shift assignemnt of the G26K,D27S,D31A triple mutant of the protein CyaY PubMed: 18537827
Deposition date: 2007-05-04 Original release date: 2007-05-18
Authors: Pastore, Chiara; Pastore, Annalisa; Correia, Ana; Gomes, Claudio
Citation: Correia, Ana; Pastore, Chiara; Adinolfi, Salvatore; Pastore, Annalisa; Gomes, Claudio. "Dynamics, stability and iron-binding activity of frataxin clinical mutants." FEBS J. 275, 3680-3690 (2008).
Assembly members:
CyaYG26KD27SD31K, polymer, 108 residues, Formula weight is not available
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET
Entity Sequences (FASTA):
CyaYG26KD27SD31K: GAMNDSEFHRLADQLWLTIE
ERLDDWDKSSDIACEINGGV
LTITFENGSKIIINRQEPLH
QVWLATKQGGYHFDLKGDEW
ICDRSGETFWDLLEQAATQQ
AGETVSFR
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 104 |
| 1H chemical shifts | 104 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CyaYG26KD27SD31K | 1 |
Entities:
Entity 1, CyaYG26KD27SD31K 108 residues - Formula weight is not available
| 1 | GLY | ALA | MET | ASN | ASP | SER | GLU | PHE | HIS | ARG | ||||
| 2 | LEU | ALA | ASP | GLN | LEU | TRP | LEU | THR | ILE | GLU | ||||
| 3 | GLU | ARG | LEU | ASP | ASP | TRP | ASP | LYS | SER | SER | ||||
| 4 | ASP | ILE | ALA | CYS | GLU | ILE | ASN | GLY | GLY | VAL | ||||
| 5 | LEU | THR | ILE | THR | PHE | GLU | ASN | GLY | SER | LYS | ||||
| 6 | ILE | ILE | ILE | ASN | ARG | GLN | GLU | PRO | LEU | HIS | ||||
| 7 | GLN | VAL | TRP | LEU | ALA | THR | LYS | GLN | GLY | GLY | ||||
| 8 | TYR | HIS | PHE | ASP | LEU | LYS | GLY | ASP | GLU | TRP | ||||
| 9 | ILE | CYS | ASP | ARG | SER | GLY | GLU | THR | PHE | TRP | ||||
| 10 | ASP | LEU | LEU | GLU | GLN | ALA | ALA | THR | GLN | GLN | ||||
| 11 | ALA | GLY | GLU | THR | VAL | SER | PHE | ARG |
Samples:
sample_1: CyaYG26KD27SD31K, [U-98% 15N], 0.4 mM; NaP 20 mM; NaCl 50 mM; DTT 2 mM
sample_conditions_1: pH: 7.0; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
XEASY, Bartels et al. - chemical shift assignment
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Varian INOVA 800 MHz
Related Database Links:
| BMRB | 15237 |
| PDB | |
| DBJ | BAE77494 BAG79612 BAI27941 BAI33064 BAI38380 |
| EMBL | CAA47281 CAR00776 CAR15464 CAV00925 CBJ03590 |
| GB | AAA67603 AAC76810 AAZ90503 ABB63872 ABV17629 |
| REF | NP_418251 WP_000999947 WP_032267531 WP_042109681 WP_042113898 |
| SP | A7ZU09 B1IW97 B1XAH3 B6I4E2 B7L963 |
| AlphaFold | B1XAH3 B6I4E2 B7L963 B1IW97 A7ZU09 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts