BMRB Entry 52088
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52088
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: Stadler, Karina; Ortiz-Joya, Lesly; Singh Sahrawat, Amit; Buhlheller, Christoph; Gruber, Karl; Pavkov-Keller, Tea; O'Hagan, Treasa; Guarne, Alba; Pulido, Sergio; Marin-Villa, Marcel; Zangger, Klaus; Gubensak, Nina. "Structural investigation of Trypanosoma cruzi Akt-like kinase as drug target against Chagas disease" Sci. Rep. 14, 10039-10039 (2024).
PubMed: 38693166
Assembly members:
entity_1, polymer, 114 residues, Formula weight is not available
Natural source: Common Name: Trypanosoma cruzi Taxonomy ID: 5693 Superkingdom: Eukaryota Kingdom: not available Genus/species: Trypanosoma cruzi
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-28a(+)
Entity Sequences (FASTA):
entity_1: MGSVEYSGYLQKTGGKFYKK
NQTRYFELRGPMLCYWKRRP
SGPHVSPTGTIDLTNARFVE
NPKDPRSWTIEGDHLSKTFT
LTADTEEQREAWVREMSKVK
PENREQLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 364 |
| 15N chemical shifts | 86 |
| 1H chemical shifts | 402 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PH domain of Akt-like kinase | 1 |
Entities:
Entity 1, PH domain of Akt-like kinase 114 residues - Formula weight is not available
| 1 | MET | GLY | SER | VAL | GLU | TYR | SER | GLY | TYR | LEU | ||||
| 2 | GLN | LYS | THR | GLY | GLY | LYS | PHE | TYR | LYS | LYS | ||||
| 3 | ASN | GLN | THR | ARG | TYR | PHE | GLU | LEU | ARG | GLY | ||||
| 4 | PRO | MET | LEU | CYS | TYR | TRP | LYS | ARG | ARG | PRO | ||||
| 5 | SER | GLY | PRO | HIS | VAL | SER | PRO | THR | GLY | THR | ||||
| 6 | ILE | ASP | LEU | THR | ASN | ALA | ARG | PHE | VAL | GLU | ||||
| 7 | ASN | PRO | LYS | ASP | PRO | ARG | SER | TRP | THR | ILE | ||||
| 8 | GLU | GLY | ASP | HIS | LEU | SER | LYS | THR | PHE | THR | ||||
| 9 | LEU | THR | ALA | ASP | THR | GLU | GLU | GLN | ARG | GLU | ||||
| 10 | ALA | TRP | VAL | ARG | GLU | MET | SER | LYS | VAL | LYS | ||||
| 11 | PRO | GLU | ASN | ARG | GLU | GLN | LEU | GLU | HIS | HIS | ||||
| 12 | HIS | HIS | HIS | HIS |
Samples:
sample_1: TcAkt-PH protein, [U-13C; U-15N], 0.46 mM; KPi pH 6.5 50 mM; NaCl 100 mM
sample_2: TcAkt-PH protein, [U-13C; U-15N], 0.5 mM; NaCl 100 mM; KPi pH 6.5 50 mM
sample_conditions_1: ionic strength: 100.08 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(COCA)CB | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
Software:
CcpNMR v2.4.2. - chemical shift assignment, data analysis, peak picking
CS-Rosetta - refinement, structure solution
NMRPipe - processing
TOPSPIN v3.5. - collection
NMR spectrometers:
- Bruker AVANCE III 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks