BMRB Entry 6738
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6738
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Title: Solution structure of Sep15 from Drosophila melanogaster PubMed: 16319061
Deposition date: 2005-07-21 Original release date: 2005-12-28
Authors: Ferguson, A.; Labunskyy, V.; Fomenko, D.; Arac, D.; Chelliah, Y.; Amezcua, C.; Rizo, J.; Gladyshev, V.; Deisenhofer, J.
Citation: Ferguson, A.; Labunskyy, V.; Fomenko, D.; Arac, D.; Chelliah, Y.; Amezcua, C.; Rizo, J.; Gladyshev, V.; Deisenhofer, J.. "NMR structures of the selenoproteins Sep15 and SelM reveal redox activity of new thioredoxin-like family." J. Biol. Chem. ., .-. (2005).
Assembly members:
Selenoprotein Sep15, polymer, 126 residues, Formula weight is not available
Natural source: Common Name: Drosophila melanogaster Taxonomy ID: 7227 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Drosophila melanogaster
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
Selenoprotein Sep15: MASHHHHHHLDQQPAAQRTY
AKAILEVCTCKFRAYPQIQA
FIQSGRPAKFPNLQIKYVRG
LDPVVKLLDASGKVQETLSI
TKWNTDTVEEFFETHLAKDG
AGKNSYSVVEDADGDDDEDY
LRTNRI
- assigned_chemical_shifts
Data type | Count |
1H chemical shifts | 809 |
13C chemical shifts | 496 |
15N chemical shifts | 122 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Selenoprotein Sep15 | 1 |
Entities:
Entity 1, Selenoprotein Sep15 126 residues - Formula weight is not available
1 | MET | ALA | SER | HIS | HIS | HIS | HIS | HIS | HIS | LEU | ||||
2 | ASP | GLN | GLN | PRO | ALA | ALA | GLN | ARG | THR | TYR | ||||
3 | ALA | LYS | ALA | ILE | LEU | GLU | VAL | CYS | THR | CYS | ||||
4 | LYS | PHE | ARG | ALA | TYR | PRO | GLN | ILE | GLN | ALA | ||||
5 | PHE | ILE | GLN | SER | GLY | ARG | PRO | ALA | LYS | PHE | ||||
6 | PRO | ASN | LEU | GLN | ILE | LYS | TYR | VAL | ARG | GLY | ||||
7 | LEU | ASP | PRO | VAL | VAL | LYS | LEU | LEU | ASP | ALA | ||||
8 | SER | GLY | LYS | VAL | GLN | GLU | THR | LEU | SER | ILE | ||||
9 | THR | LYS | TRP | ASN | THR | ASP | THR | VAL | GLU | GLU | ||||
10 | PHE | PHE | GLU | THR | HIS | LEU | ALA | LYS | ASP | GLY | ||||
11 | ALA | GLY | LYS | ASN | SER | TYR | SER | VAL | VAL | GLU | ||||
12 | ASP | ALA | ASP | GLY | ASP | ASP | ASP | GLU | ASP | TYR | ||||
13 | LEU | ARG | THR | ASN | ARG | ILE |
Samples:
sample_1: Selenoprotein Sep15, [U-15N; U-13C], 1 mM; phosphate buffer 50 mM; H2O 90%; D2O 10%
sample_cond_1: pH: 6; temperature: 298 K; ionic strength: 50 mM; pressure: 1 atm
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D 15N-separated NOESY | sample_1 | not available | sample_cond_1 |
3D 13C-separated NOESY | sample_1 | not available | sample_cond_1 |
2D NOESY | sample_1 | not available | sample_cond_1 |
2D TOCSY | sample_1 | not available | sample_cond_1 |
Software:
VNMR v6.1C, Varian - collection
NMRPipe v1, Delaglio - processing
NMRView v5.2.2, Johnson - data analysis
ARIA v2.0, Nilges - refinement, structure solution
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
REF | XP_002094982 XP_002076553 XP_002030922 NP_649000 |
GenBank | EDX15740 EDW94694 EDW41908 AAM51078 AAF49314 |
EMBL | CAL26591 CAL26585 CAL26581 CAL26580 CAL26579 |
PDB |
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