BMRB Entry 50336
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50336
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Title: yarp PubMed: 32722282
Deposition date: 2020-06-22 Original release date: 2020-08-25
Authors: Bucholc, Katarzyna; Skrajna, Aleksandra; Adamska, Kinga; Yang, Xiao-Cui; Krajewski, Krzysztof; Poznanski, Jaroslaw; Dadlez, Michal; Dominski, Zbigniew; Zhukov, Igor
Citation: Bucholc, Katarzyna; Skrajna, Aleksandra; Adamska, Kinga; Yang, Xiao-Cui; Krajewski, Krzysztof; Poznanski, Jaroslaw; Dadlez, Michal; Dominski, Zbigniew; Zhukov, Igor. "Structural Analysis of the SANT/Myb Domain of FLASH and YARP Proteins and Their Complex with the C-Terminal Fragment of NPAT by NMR Spectroscopy and Computer Simulations" Int. J. Mol. Sci. 21, 5268-5268 (2020).
Assembly members:
entity_1, polymer, 61 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a
Entity Sequences (FASTA):
entity_1: GEKVVLWTREADRVILTMCQ
EQGAQPQTFNIISQQLGNKT
PAEVSHRFRELMQLFHTACE
A
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 273 |
| 15N chemical shifts | 69 |
| 1H chemical shifts | 458 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | yarp | 1 |
Entities:
Entity 1, yarp 61 residues - Formula weight is not available
| 1 | GLY | GLU | LYS | VAL | VAL | LEU | TRP | THR | ARG | GLU | ||||
| 2 | ALA | ASP | ARG | VAL | ILE | LEU | THR | MET | CYS | GLN | ||||
| 3 | GLU | GLN | GLY | ALA | GLN | PRO | GLN | THR | PHE | ASN | ||||
| 4 | ILE | ILE | SER | GLN | GLN | LEU | GLY | ASN | LYS | THR | ||||
| 5 | PRO | ALA | GLU | VAL | SER | HIS | ARG | PHE | ARG | GLU | ||||
| 6 | LEU | MET | GLN | LEU | PHE | HIS | THR | ALA | CYS | GLU | ||||
| 7 | ALA |
Samples:
sample_1: YARP, [U-99% 13C; U-99% 15N], 0.3 ± 0.05 mM; YARP, [U-99% 15N], 0.3 ± 0.05 mM; TRIS-d11 25 mM; KCl 250 mM; Arg+Glu 50 mM; TCEP 40 mM
sample_conditions_1: ionic strength: 250 mM; pH: 6.2; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe - processing
NMRFAM-SPARKY - chemical shift assignment, peak picking
CYANA - structure solution
YASARA - refinement
NMR spectrometers:
- Agilent Uniform NMR System 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts