BMRB Entry 4393
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR4393
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Title: 1H, 15N, and 13C NMR Backbone Assignments of the N Terminal Region of Human Erythrocyte Alpha Spectrin Including One Repeating Unit. PubMed: 10685345
Deposition date: 1999-09-08 Original release date: 2003-06-05
Authors: Park, Sunghyouk; Liao, Xiubei; Johnson, Michael; Fung, Leslie
Citation: Park, Sunghyouk; Liao, Xiubei; Johnson, Michael; Fung, Leslie. "1H, 15N, and 13C NMR Backbone Assignments of the N-terminal Region of Human Erythrocyte alpha Spectrin Including one Structural Domain" J. Biomol. NMR 15, 345-346 (1999).
Assembly members:
spectrin, polymer, 156 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
Entity Sequences (FASTA):
spectrin: MEQFPKETVVESSGPKVLET
AEEIQERRQEVLTRYQSFKE
RVAERGQKLEDSYHLQVFKR
DADDLGKWIMEKVNILTDKS
YEDPTNIQGKYQKHQSLEAE
VQTKSRLMSELEKTREERFT
MGHSAHEETKAHIEELRHLW
DLLLELTLEKGDQLLR
- assigned_chemical_shifts
- coupling_constants
| Data type | Count |
| 13C chemical shifts | 301 |
| 15N chemical shifts | 149 |
| 1H chemical shifts | 298 |
| coupling constants | 96 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | spectrin | 1 |
Entities:
Entity 1, spectrin 156 residues - Formula weight is not available
| 1 | MET | GLU | GLN | PHE | PRO | LYS | GLU | THR | VAL | VAL | ||||
| 2 | GLU | SER | SER | GLY | PRO | LYS | VAL | LEU | GLU | THR | ||||
| 3 | ALA | GLU | GLU | ILE | GLN | GLU | ARG | ARG | GLN | GLU | ||||
| 4 | VAL | LEU | THR | ARG | TYR | GLN | SER | PHE | LYS | GLU | ||||
| 5 | ARG | VAL | ALA | GLU | ARG | GLY | GLN | LYS | LEU | GLU | ||||
| 6 | ASP | SER | TYR | HIS | LEU | GLN | VAL | PHE | LYS | ARG | ||||
| 7 | ASP | ALA | ASP | ASP | LEU | GLY | LYS | TRP | ILE | MET | ||||
| 8 | GLU | LYS | VAL | ASN | ILE | LEU | THR | ASP | LYS | SER | ||||
| 9 | TYR | GLU | ASP | PRO | THR | ASN | ILE | GLN | GLY | LYS | ||||
| 10 | TYR | GLN | LYS | HIS | GLN | SER | LEU | GLU | ALA | GLU | ||||
| 11 | VAL | GLN | THR | LYS | SER | ARG | LEU | MET | SER | GLU | ||||
| 12 | LEU | GLU | LYS | THR | ARG | GLU | GLU | ARG | PHE | THR | ||||
| 13 | MET | GLY | HIS | SER | ALA | HIS | GLU | GLU | THR | LYS | ||||
| 14 | ALA | HIS | ILE | GLU | GLU | LEU | ARG | HIS | LEU | TRP | ||||
| 15 | ASP | LEU | LEU | LEU | GLU | LEU | THR | LEU | GLU | LYS | ||||
| 16 | GLY | ASP | GLN | LEU | LEU | ARG |
Samples:
sample_one: spectrin, [U-2H; U-15N; U-13C], 0.9 – 1.1 mM; Phosphate Buffer 5 mM; Sodium Chloride 150 mM
sample_conditions: ionic strength: 0.18 M; pH: 6.5 na; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|
Software:
No software information available
NMR spectrometers:
- Bruker DRX 600.13 MHz
Related Database Links:
| PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
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SPARKY: Backbone
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