BMRB Entry 36489
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36489
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
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Title: Solution structure of T. brucei RAP1 PubMed: 36949076
Deposition date: 2022-05-12 Original release date: 2023-07-28
Authors: Yang, X.; Pan, X.; Ji, Z.; Wong, K.; Zhang, M.; Zhao, Y.
Citation: Gaurav, A.; Afrin, M.; Yang, X.; Saha, A.; Pan, X.; Ji, Z.; Zhang, M.; Zhao, Y.; Li, B.. "The RRM-mediated RNA binding activity in T. brucei RAP1 is essential for VSG monoallelic expression." Nat. Commun. 14, 1576-1576 (2023).
Assembly members:
Repressor activator protein 1, polymer, 127 residues, 14207.05 Da.
Natural source: Common Name: not available 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):
Repressor activator protein 1: GPGSEATEEIAALDQPFEKC
FIPTEALGSDREGLDRTQLE
RQLPFRNYPIKLNVSKSGIF
CQFPTVSDAKRFYEEGTVEI
LNRSLPIKPVFEKRNETVAP
AERKRRRSVSPGGVHPQTAA
VSALSRR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 381 |
| 15N chemical shifts | 111 |
| 1H chemical shifts | 720 |
| torsion angle constraints | 48 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 127 residues - 14207.05 Da.
| 1 | GLY | PRO | GLY | SER | GLU | ALA | THR | GLU | GLU | ILE | ||||
| 2 | ALA | ALA | LEU | ASP | GLN | PRO | PHE | GLU | LYS | CYS | ||||
| 3 | PHE | ILE | PRO | THR | GLU | ALA | LEU | GLY | SER | ASP | ||||
| 4 | ARG | GLU | GLY | LEU | ASP | ARG | THR | GLN | LEU | GLU | ||||
| 5 | ARG | GLN | LEU | PRO | PHE | ARG | ASN | TYR | PRO | ILE | ||||
| 6 | LYS | LEU | ASN | VAL | SER | LYS | SER | GLY | ILE | PHE | ||||
| 7 | CYS | GLN | PHE | PRO | THR | VAL | SER | ASP | ALA | LYS | ||||
| 8 | ARG | PHE | TYR | GLU | GLU | GLY | THR | VAL | GLU | ILE | ||||
| 9 | LEU | ASN | ARG | SER | LEU | PRO | ILE | LYS | PRO | VAL | ||||
| 10 | PHE | GLU | LYS | ARG | ASN | GLU | THR | VAL | ALA | PRO | ||||
| 11 | ALA | GLU | ARG | LYS | ARG | ARG | ARG | SER | VAL | SER | ||||
| 12 | PRO | GLY | GLY | VAL | HIS | PRO | GLN | THR | ALA | ALA | ||||
| 13 | VAL | SER | ALA | LEU | SER | ARG | ARG |
Samples:
sample_1: TbRAP1, [U-100% 15N], 0.1 mM; sodium phosphate 100 mM; H2O 90%; D2O, [U-2H], 10%
sample_2: TbRAP1, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 100 mM; H2O 90%; D2O, [U-2H], 10%
sample_3: TbRAP1 0.6 mM; sodium phosphate 100 mM; D2O, [U-2H], 100%
sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H NOESY | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation
CcpNmr Analysis, CCPN - chemical shift assignment
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement
NMR spectrometers:
- Varian INOVA 500 MHz
- Varian INOVA 750 MHz
- Varian INOVA 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts