BMRB Entry 30471
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30471
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Title: Human Titin ZIg10
Deposition date: 2018-05-31 Original release date: 2019-08-16
Authors: Wright, N.
Citation: Letourneau, A.; Wright, N.. "Solution structure and function of human titin ZIg10" . ., .-..
Assembly members:
Titin, polymer, 119 residues, 13965.898 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapienss
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Titin: RMAHEGALTGVTTDQKEKQK
PDIVLYPEPVRVLEGETARF
RCRVTGYPQPKVNWYLNGQL
IRKSKRFRVRYDGIHYLDIV
DCKSYDTGEVKVTAENPEGV
IEHKVKLEIQQLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 299 |
| 15N chemical shifts | 94 |
| 1H chemical shifts | 623 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 119 residues - 13965.898 Da.
| 1 | ARG | MET | ALA | HIS | GLU | GLY | ALA | LEU | THR | GLY | ||||
| 2 | VAL | THR | THR | ASP | GLN | LYS | GLU | LYS | GLN | LYS | ||||
| 3 | PRO | ASP | ILE | VAL | LEU | TYR | PRO | GLU | PRO | VAL | ||||
| 4 | ARG | VAL | LEU | GLU | GLY | GLU | THR | ALA | ARG | PHE | ||||
| 5 | ARG | CYS | ARG | VAL | THR | GLY | TYR | PRO | GLN | PRO | ||||
| 6 | LYS | VAL | ASN | TRP | TYR | LEU | ASN | GLY | GLN | LEU | ||||
| 7 | ILE | ARG | LYS | SER | LYS | ARG | PHE | ARG | VAL | ARG | ||||
| 8 | TYR | ASP | GLY | ILE | HIS | TYR | LEU | ASP | ILE | VAL | ||||
| 9 | ASP | CYS | LYS | SER | TYR | ASP | THR | GLY | GLU | VAL | ||||
| 10 | LYS | VAL | THR | ALA | GLU | ASN | PRO | GLU | GLY | VAL | ||||
| 11 | ILE | GLU | HIS | LYS | VAL | LYS | LEU | GLU | ILE | GLN | ||||
| 12 | GLN | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: TRIS 20 mM; sodium chloride 50 mM; Human Titin ZIg10, [U-99% 13C; U-99% 15N], 1 mM
sample_conditions_1: ionic strength: 50 mM; pH: 7.5; pressure: 1 atm; temperature: 298 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 C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | 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:
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment, peak picking
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