BMRB Entry 11572
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11572
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Title: Chemical shift assignments of the human Smoothelin CH domain PubMed: 26293126
Deposition date: 2014-07-31 Original release date: 2018-12-11
Authors: Kasai, Takuma; Koshiba, Seizo; Yokoyama, Jun; Kigawa, Takanori
Citation: Kasai, Takuma; Koshiba, Seizo; Yokoyama, Jun; Kigawa, Takanori. "Stable isotope labeling strategy based on coding theory." J. Biomol. NMR 63, 213-221 (2015).
Assembly members:
Smoothelin_CH_domain, polymer, 116 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: cell free synthesis Host organism: E. coli - cell free Vector: P120404-01
Entity Sequences (FASTA):
Smoothelin_CH_domain: GIKQMLLDWCRAKTRGYEHV
DIQNFSSSWSDGMAFCALVH
NFFPEAFDYGQLSPQNRRQN
FEVAFSSAETHADCPQLLDT
EDMVRLREPDWKCVYTYIQE
FYRCLVQKGLVKTKKS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 352 |
| 15N chemical shifts | 125 |
| 1H chemical shifts | 74 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Smoothelin CH domain | 1 |
Entities:
Entity 1, Smoothelin CH domain 116 residues - Formula weight is not available
Residue 1 represents a non-native cloning artifact. This is the CH domain of human Smoothelin protein.
| 1 | GLY | ILE | LYS | GLN | MET | LEU | LEU | ASP | TRP | CYS | ||||
| 2 | ARG | ALA | LYS | THR | ARG | GLY | TYR | GLU | HIS | VAL | ||||
| 3 | ASP | ILE | GLN | ASN | PHE | SER | SER | SER | TRP | SER | ||||
| 4 | ASP | GLY | MET | ALA | PHE | CYS | ALA | LEU | VAL | HIS | ||||
| 5 | ASN | PHE | PHE | PRO | GLU | ALA | PHE | ASP | TYR | GLY | ||||
| 6 | GLN | LEU | SER | PRO | GLN | ASN | ARG | ARG | GLN | ASN | ||||
| 7 | PHE | GLU | VAL | ALA | PHE | SER | SER | ALA | GLU | THR | ||||
| 8 | HIS | ALA | ASP | CYS | PRO | GLN | LEU | LEU | ASP | THR | ||||
| 9 | GLU | ASP | MET | VAL | ARG | LEU | ARG | GLU | PRO | ASP | ||||
| 10 | TRP | LYS | CYS | VAL | TYR | THR | TYR | ILE | GLN | GLU | ||||
| 11 | PHE | TYR | ARG | CYS | LEU | VAL | GLN | LYS | GLY | LEU | ||||
| 12 | VAL | LYS | THR | LYS | LYS | SER |
Samples:
sample_1: Smoothelin CH domain, [U-13C; U-15N], 0.9 mM; Tris-Cl, [U-2H], 20 mM; sodium chloride 100 mM; DTT, [U-2H], 1 mM; sodium azide 0.02 % (w/v); H2O 90%; D2O, [U-2H], 10%
sample_conditions_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 295 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 HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | 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 HCCH-COSY aromatic | 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:
TOPSPIN v2.1, Bruker Biospin - collection
NMRPipe v20130801, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView v5.0.4, Johnson, One Moon Scientific - data analysis
Kujira v0.9843, Naohiro Kobayashi - chemical shift assignment, data analysis
NMR spectrometers:
- Bruker Avance 700 MHz