BMRB Entry 25543
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25543
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Title: Solution structure of human Myosin VI isoform3 (998-1071) PubMed: 26971995
Deposition date: 2015-03-20 Original release date: 2016-03-07
Authors: He, Fahu; Walters, Kylie
Citation: He, Fahu; Wollscheid, Hans-Peter; Nowicka, Urszula; Biancospino, Matteo; Valentini, Eleonora; Ehlinger, Aaron; Acconcia, Filippo; Magistrati, Elisa; Polo, Simona; Walters, Kylie. "Myosin VI Contains a Compact Structural Motif that Binds to Ubiquitin Chains" Cell Rep. 14, 2683-2694 (2016).
Assembly members:
entity, polymer, 74 residues, 8399.430 Da.
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
Entity Sequences (FASTA):
entity: QQQAVLEQERRDRELALRIA
QSEAELISDEAQADLALRRS
LDSYPVSKNDGTRPKMTPEQ
MAKEMSEFLSRGPA
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 294 |
15N chemical shifts | 82 |
1H chemical shifts | 525 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | entity | 1 |
Entities:
Entity 1, entity 74 residues - 8399.430 Da.
1 | GLN | GLN | GLN | ALA | VAL | LEU | GLU | GLN | GLU | ARG | ||||
2 | ARG | ASP | ARG | GLU | LEU | ALA | LEU | ARG | ILE | ALA | ||||
3 | GLN | SER | GLU | ALA | GLU | LEU | ILE | SER | ASP | GLU | ||||
4 | ALA | GLN | ALA | ASP | LEU | ALA | LEU | ARG | ARG | SER | ||||
5 | LEU | ASP | SER | TYR | PRO | VAL | SER | LYS | ASN | ASP | ||||
6 | GLY | THR | ARG | PRO | LYS | MET | THR | PRO | GLU | GLN | ||||
7 | MET | ALA | LYS | GLU | MET | SER | GLU | PHE | LEU | SER | ||||
8 | ARG | GLY | PRO | ALA |
Samples:
sample_1: entity, [U-13C; U-15N], 0.7 mM; sodium phosphate buffer 20 mM; NaCl 50 mM; DTT 2 mM; NaN3 0.1%; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 283 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
Kujira, Naohiro Kobayashi - chemical shift assignment
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts