BMRB Entry 18471
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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/BMR18471
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Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for PWWP domain from Trypanosoma brucei PubMed: 22836947
Deposition date: 2012-05-17 Original release date: 2012-08-29
Authors: Dai, Kun; 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:
PWWP_domain, polymer, 118 residues, Formula weight is not available
Natural source: Common Name: Kinetoplastids 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):
PWWP_domain: MIPSFAPGTLVWLKQDRFPW
WPGFVMDPDEVRDITLPEGS
DVWVCCLPRDSLTLSAANSE
DEGQIRYFLPDRDEGMMEEG
KLDASCAVAIEEAIQLYEEQ
LKAQAGGTNELEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 298 |
| 15N chemical shifts | 101 |
| 1H chemical shifts | 645 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PWWP_domain | 1 |
Entities:
Entity 1, PWWP_domain 118 residues - Formula weight is not available
| 1 | MET | ILE | PRO | SER | PHE | ALA | PRO | GLY | THR | LEU | ||||
| 2 | VAL | TRP | LEU | LYS | GLN | ASP | ARG | PHE | PRO | TRP | ||||
| 3 | TRP | PRO | GLY | PHE | VAL | MET | ASP | PRO | ASP | GLU | ||||
| 4 | VAL | ARG | ASP | ILE | THR | LEU | PRO | GLU | GLY | SER | ||||
| 5 | ASP | VAL | TRP | VAL | CYS | CYS | LEU | PRO | ARG | ASP | ||||
| 6 | SER | LEU | THR | LEU | SER | ALA | ALA | ASN | SER | GLU | ||||
| 7 | ASP | GLU | GLY | GLN | ILE | ARG | TYR | PHE | LEU | PRO | ||||
| 8 | ASP | ARG | ASP | GLU | GLY | MET | MET | GLU | GLU | GLY | ||||
| 9 | LYS | LEU | ASP | ALA | SER | CYS | ALA | VAL | ALA | ILE | ||||
| 10 | GLU | GLU | ALA | ILE | GLN | LEU | TYR | GLU | GLU | GLN | ||||
| 11 | LEU | LYS | ALA | GLN | ALA | GLY | GLY | THR | ASN | GLU | ||||
| 12 | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: PWWP_domain, [U-99% 13C; U-99% 15N], 0.6 mM; sodium phosphate 25 mM; sodium chloride 100 mM; DTT 1 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 125 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 HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
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