BMRB Entry 18399
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18399
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Wang, Rui; Liao, Shanhui; Wang, Tao; Zhang, Jiahai; Tu, Xiaoming. "Solution structure of a ubiqutin-like protein from Trypanosoma bucei" .
Assembly members:
entity, polymer, 84 residues, 8680.189 Da.
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 Vector: pET28
Entity Sequences (FASTA):
entity: HHHHHHMLLKVKTVSNKVIQ
ITSLTDDNTIAELKGKLEES
EGIPGNMIRLVYQGKQLEDE
KRLKDYQMSAGATFHMVVAL
RAGC
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 224 |
| 15N chemical shifts | 77 |
| 1H chemical shifts | 447 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ubiqutin-like protein from Trypanosoma bucei | 1 |
Entities:
Entity 1, ubiqutin-like protein from Trypanosoma bucei 84 residues - 8680.189 Da.
| 1 | HIS | HIS | HIS | HIS | HIS | HIS | MET | LEU | LEU | LYS | ||||
| 2 | VAL | LYS | THR | VAL | SER | ASN | LYS | VAL | ILE | GLN | ||||
| 3 | ILE | THR | SER | LEU | THR | ASP | ASP | ASN | THR | ILE | ||||
| 4 | ALA | GLU | LEU | LYS | GLY | LYS | LEU | GLU | GLU | SER | ||||
| 5 | GLU | GLY | ILE | PRO | GLY | ASN | MET | ILE | ARG | LEU | ||||
| 6 | VAL | TYR | GLN | GLY | LYS | GLN | LEU | GLU | ASP | GLU | ||||
| 7 | LYS | ARG | LEU | LYS | ASP | TYR | GLN | MET | SER | ALA | ||||
| 8 | GLY | ALA | THR | PHE | HIS | MET | VAL | VAL | ALA | LEU | ||||
| 9 | ARG | ALA | GLY | CYS |
Samples:
sample_1: tbubl, [U-100% 13C; U-100% 15N], 0.5 mM; H2O 0.5 mM; D2O 0.5 mM
sample_conditions_1: ionic strength: 0.15 M; 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 |
| 2D 1H-13C 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 HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(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:
CYANA, Guntert, Mumenthaler and Wuthrich - chemical shift calculation
NMR spectrometers:
- Bruker DMX 500 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks