BMRB Entry 18474
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18474
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Title: the pwwp domain of TFIIS2-1 from Trypanosoma brucei PubMed: 22836947
Deposition date: 2012-05-18 Original release date: 2012-08-29
Authors: Wang, Rui; Fan, Kai; Liao, Shanhui; Zhang, Jiahai; Tu, Xiaoming
Citation: Zhang, Jiahai; Dai, Kun; Liao, Shanhui; Tu, Xiaoming. "H, C and N resonance assignments of TbTFIIS2-2 PWWP domain from Trypanosoma brucei." Biomol. NMR Assignments 7, 207-209 (2013).
Assembly members:
entity, polymer, 118 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):
entity: MLQERVFHINDRVWLKTGAN
TWWPAKVTSVTGVEGVDGRS
SETGTSTVTVLTYPGTQNKA
TYKNVDSHSSAITFFEPSSE
KAVTANEDLLQAIRNAEEDK
ESNALRFEPTLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 294 |
| 15N chemical shifts | 107 |
| 1H chemical shifts | 614 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | pwwp domain of TFIIS2-1 | 1 |
Entities:
Entity 1, pwwp domain of TFIIS2-1 118 residues - Formula weight is not available
| 1 | MET | LEU | GLN | GLU | ARG | VAL | PHE | HIS | ILE | ASN | ||||
| 2 | ASP | ARG | VAL | TRP | LEU | LYS | THR | GLY | ALA | ASN | ||||
| 3 | THR | TRP | TRP | PRO | ALA | LYS | VAL | THR | SER | VAL | ||||
| 4 | THR | GLY | VAL | GLU | GLY | VAL | ASP | GLY | ARG | SER | ||||
| 5 | SER | GLU | THR | GLY | THR | SER | THR | VAL | THR | VAL | ||||
| 6 | LEU | THR | TYR | PRO | GLY | THR | GLN | ASN | LYS | ALA | ||||
| 7 | THR | TYR | LYS | ASN | VAL | ASP | SER | HIS | SER | SER | ||||
| 8 | ALA | ILE | THR | PHE | PHE | GLU | PRO | SER | SER | GLU | ||||
| 9 | LYS | ALA | VAL | THR | ALA | ASN | GLU | ASP | LEU | LEU | ||||
| 10 | GLN | ALA | ILE | ARG | ASN | ALA | GLU | GLU | ASP | LYS | ||||
| 11 | GLU | SER | ASN | ALA | LEU | ARG | PHE | GLU | PRO | THR | ||||
| 12 | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: Tbpwwp, [U-100% 13C; U-100% 15N], 0.5 mM; H2O 90%; D2O 10%; Na2HPO4 25 mM; NaCl 150 mM; EDTA 2 mM
sample_conditions_1: ionic strength: 0.15 M; pH: 6.7; 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 HNCACB | 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 C(CO)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 |
Software:
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker DMX 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts