BMRB Entry 17374
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17374
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Title: 1H, 13C and 15N resonance assignments for ADF/Cofilin from Trypanosoma brucei PubMed: 21523437
Deposition date: 2010-12-22 Original release date: 2011-01-06
Authors: Dai, Kun; Yuan, Guangfa; Liao, Shanhui; Zhang, Jiahai; Tu, Xiaoming
Citation: Dai, Kun; Yuan, Guangfa; Liao, Shanhui; Zhang, Jiahai; Tu, Xiaoming. "(1)H, (13)C and (15)N resonance assignments for a putative ADF/Cofilin from Trypanosoma brucei." Biomol. NMR Assignments 5, 249-251 (2011).
Assembly members:
ADF_Cofilin, polymer, 144 residues, Formula weight is not available
Natural source: Common Name: Trypanosoma brucei Taxonomy ID: 5691 Superkingdom: Eukaryota Kingdom: not available Genus/species: Trypanosoma brucei
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
ADF_Cofilin: MGHHHHHHMAMSGVSVADEC
VTALNDLRHKKSRYVIMHIV
DQKSIAVKTIGERGANFDQF
IEAIDKNVPCYAAFDFEYTT
NDGPRDKLILISWNPDSGAP
RTKMLYSSSRDALVPLTQGF
QGIQANDASGLDFEEISRKV
KSNR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 527 |
| 15N chemical shifts | 130 |
| 1H chemical shifts | 812 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ADF/Cofilin from Trypanosoma brucei | 1 |
Entities:
Entity 1, ADF/Cofilin from Trypanosoma brucei 144 residues - Formula weight is not available
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | MET | ALA | ||||
| 2 | MET | SER | GLY | VAL | SER | VAL | ALA | ASP | GLU | CYS | ||||
| 3 | VAL | THR | ALA | LEU | ASN | ASP | LEU | ARG | HIS | LYS | ||||
| 4 | LYS | SER | ARG | TYR | VAL | ILE | MET | HIS | ILE | VAL | ||||
| 5 | ASP | GLN | LYS | SER | ILE | ALA | VAL | LYS | THR | ILE | ||||
| 6 | GLY | GLU | ARG | GLY | ALA | ASN | PHE | ASP | GLN | PHE | ||||
| 7 | ILE | GLU | ALA | ILE | ASP | LYS | ASN | VAL | PRO | CYS | ||||
| 8 | TYR | ALA | ALA | PHE | ASP | PHE | GLU | TYR | THR | THR | ||||
| 9 | ASN | ASP | GLY | PRO | ARG | ASP | LYS | LEU | ILE | LEU | ||||
| 10 | ILE | SER | TRP | ASN | PRO | ASP | SER | GLY | ALA | PRO | ||||
| 11 | ARG | THR | LYS | MET | LEU | TYR | SER | SER | SER | ARG | ||||
| 12 | ASP | ALA | LEU | VAL | PRO | LEU | THR | GLN | GLY | PHE | ||||
| 13 | GLN | GLY | ILE | GLN | ALA | ASN | ASP | ALA | SER | GLY | ||||
| 14 | LEU | ASP | PHE | GLU | GLU | ILE | SER | ARG | LYS | VAL | ||||
| 15 | LYS | SER | ASN | ARG |
Samples:
sample_1: ADF/Cofilin, [U-99% 13C; U-99% 15N], 0.6 mM; sodium chloride 100 mM; sodium phosphate 20 mM; EDTA 2 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - data analysis
NMR spectrometers:
- Bruker DMX 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts