BMRB Entry 25308
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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/BMR25308
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Title: Chemical shift assignments of human obscurin Ig58
Deposition date: 2014-11-03 Original release date: 2015-12-07
Authors: Wright, Nathan; Meyer, Logan
Citation: Wright, Nathan; Meyer, Logan; Kontrogianni-Konstantopoulos, Katia; Ackermann, Maegen; Hu, Rebecca. "Obscurin Ig58 disrupts myocyte development" Not known ., .-..
Assembly members:
Ig58, polymer, 102 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
Entity Sequences (FASTA):
Ig58: TAKNTVVRGLENVEALEGGE
ALFECQLSQPEVAAHTWLLD
DEPVRTSENAEVVFFENGLR
HLLLLKNLRPQDSCRVTFLA
GDMVTSAFLTVRGGLEHHHH
HH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 376 |
| 15N chemical shifts | 91 |
| 1H chemical shifts | 625 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Ig58 | 1 |
Entities:
Entity 1, Ig58 102 residues - Formula weight is not available
| 1 | THR | ALA | LYS | ASN | THR | VAL | VAL | ARG | GLY | LEU | ||||
| 2 | GLU | ASN | VAL | GLU | ALA | LEU | GLU | GLY | GLY | GLU | ||||
| 3 | ALA | LEU | PHE | GLU | CYS | GLN | LEU | SER | GLN | PRO | ||||
| 4 | GLU | VAL | ALA | ALA | HIS | THR | TRP | LEU | LEU | ASP | ||||
| 5 | ASP | GLU | PRO | VAL | ARG | THR | SER | GLU | ASN | ALA | ||||
| 6 | GLU | VAL | VAL | PHE | PHE | GLU | ASN | GLY | LEU | ARG | ||||
| 7 | HIS | LEU | LEU | LEU | LEU | LYS | ASN | LEU | ARG | PRO | ||||
| 8 | GLN | ASP | SER | CYS | ARG | VAL | THR | PHE | LEU | ALA | ||||
| 9 | GLY | ASP | MET | VAL | THR | SER | ALA | PHE | LEU | THR | ||||
| 10 | VAL | ARG | GLY | GLY | LEU | GLU | HIS | HIS | HIS | HIS | ||||
| 11 | HIS | HIS |
Samples:
sample_1: Ig58, [U-99% 13C; U-99% 15N], 0.5 – 1.5 mM; Tris 20 mM; NaCl 50 mM; NaN3 0.3 mM; H20 90%; D20 10%
sample_conditions_1: ionic strength: 0.05 M; pH: 7.5; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | 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-15N TOCSY | 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
NMR spectrometers:
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts