BMRB Entry 25899
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25899
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Title: Solution NMR Structure of Antiparallel Myosin-10:GCN4 Tandem Coiled-Coil
Deposition date: 2015-11-12 Original release date: 2016-06-08
Authors: Vavra, K.; Xia, Youlin; Rock, Ronald
Citation: Vavra, K.; Xia, Youlin; Rock, Ronald. "Competition between Coiled-Coil Structures and the Impact on Myosin-10 Bundle Selection" Biophys. J. 110, 2517-2527 (2016).
Assembly members:
entity, polymer, 69 residues, 8200.371 Da.
Natural source: Common Name: cow Taxonomy ID: 9913 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Bos taurus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: GSHENKQVEEILRLEKEIED
LQRMKERQELSLTEASLQKL
QLEDKVEELLSKNYHLENEV
ARLKKLVGE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 620 |
| 15N chemical shifts | 148 |
| 1H chemical shifts | 946 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 1 |
Entities:
Entity 1, entity_1 69 residues - 8200.371 Da.
| 1 | GLY | SER | HIS | GLU | ASN | LYS | GLN | VAL | GLU | GLU | ||||
| 2 | ILE | LEU | ARG | LEU | GLU | LYS | GLU | ILE | GLU | ASP | ||||
| 3 | LEU | GLN | ARG | MET | LYS | GLU | ARG | GLN | GLU | LEU | ||||
| 4 | SER | LEU | THR | GLU | ALA | SER | LEU | GLN | LYS | LEU | ||||
| 5 | GLN | LEU | GLU | ASP | LYS | VAL | GLU | GLU | LEU | LEU | ||||
| 6 | SER | LYS | ASN | TYR | HIS | LEU | GLU | ASN | GLU | VAL | ||||
| 7 | ALA | ARG | LEU | LYS | LYS | LEU | VAL | GLY | GLU |
Samples:
sample_1: entity, [U-100% 13C; U-100% 15N], 1.1 mM; potassium phosphate 100 mM; EDTA 1 mM; sodium azide 0.03%
sample_conditions_1: ionic strength: 0.6 M; pH: 6.5; pressure: 1 atm; temperature: 35 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | 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 CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCANH | sample_1 | isotropic | sample_conditions_1 |
| 2D HBCBCGCDHD | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC NH2 only | 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:
Xplor-NIH v2.38, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution
CCPN v2.4.1, CCPN - chemical shift assignment, data analysis, peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker Avance 850 MHz
- Varian INOVA 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts