BMRB Entry 30005
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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/BMR30005
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Title: Solution structure of coiled coil domain of myosin binding subunit of myosin light chain phosphatase PubMed: 24693955
Deposition date: 2016-01-27 Original release date: 2016-03-14
Authors: Sharma, A.; Birrane, G.; Anklin, C.; Rigby, A.; Pollak, M.; Alper, S.
Citation: Sharma, A.; Rigby, A.; Sharma, A.; Rigby, A.. "NMR assignment and secondary structure of coiled coil domain of C-terminal myosin binding subunit of myosin phosphatase." Protein Pept. Lett. 21, 639-645 (2014).
Assembly members:
entity_1, polymer, 47 residues, 5358.105 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_1: DFKKLYEQILAENEKLKAQL
HDTNMELTDLKLQLEKATQR
QERFARS
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 206 |
15N chemical shifts | 50 |
1H chemical shifts | 346 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | entity_1 | 1 |
2 | entity_2 | 1 |
Entities:
Entity 1, entity_1 47 residues - 5358.105 Da.
1 | ASP | PHE | LYS | LYS | LEU | TYR | GLU | GLN | ILE | LEU | ||||
2 | ALA | GLU | ASN | GLU | LYS | LEU | LYS | ALA | GLN | LEU | ||||
3 | HIS | ASP | THR | ASN | MET | GLU | LEU | THR | ASP | LEU | ||||
4 | LYS | LEU | GLN | LEU | GLU | LYS | ALA | THR | GLN | ARG | ||||
5 | GLN | GLU | ARG | PHE | ALA | ARG | SER |
Samples:
sample_1: coiled coil mbs-1, [U-99% 13C; U-99% 15N], 1.0 mM; coiled coil mbs-2, [U-99% 15N], 1.0 mM; coiled coil mbs-3 1.0 mM
sample_conditions_1: ionic strength: 10 mM; pH: 7.0; pressure: 1 atm; temperature: 303 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC NH2 ONLY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO) NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D H(CCO)NH | 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 |
2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
isotope filtered 3D 1H-13C NOESY | sample_1 | anisotropic | sample_conditions_1 |
isotope filtered 3D 1H-15N NOESY | sample_1 | anisotropic | sample_conditions_1 |
isotope filtered 2D NOESY | sample_1 | anisotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
ANSIG, Kraulis - chemical shift assignment
Analysis v2.4.0, CCPN - chemical shift assignment
CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 700 MHz
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts