BMRB Entry 16499
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16499
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Title: (1-77)Apomyoglobin PubMed: 20816043
Deposition date: 2009-09-15 Original release date: 2010-11-01
Authors: Fedyukina, Daria; Cavagnero, Silvia
Citation: Fedyukina, Daria; Rajagopalan, Senapathy; Sekhar, Ashok; Fulmer, Eric; Eun, Ye-Jin; Cavagnero, Silvia. "Contribution of long-range interactions to the secondary structure of an unfolded globin." Biophys. J. 99, L37-L39 (2010).
Assembly members:
1-77_Apomyoglobin, polymer, 78 residues, Formula weight is not available
Natural source: Common Name: Sperm Whale Taxonomy ID: 9755 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Physeter catodon
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
1-77_Apomyoglobin: MVLSEGEWQLVLHVWAKVEA
DVAGHGQDILIRLFKSHPET
LEKFDRFKHLKTEAEMKASE
DLKKHGVTVLTALGAILK
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 227 |
15N chemical shifts | 76 |
1H chemical shifts | 76 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | (1-77)Apomyoglobin | 1 |
Entities:
Entity 1, (1-77)Apomyoglobin 78 residues - Formula weight is not available
1 | MET | VAL | LEU | SER | GLU | GLY | GLU | TRP | GLN | LEU | ||||
2 | VAL | LEU | HIS | VAL | TRP | ALA | LYS | VAL | GLU | ALA | ||||
3 | ASP | VAL | ALA | GLY | HIS | GLY | GLN | ASP | ILE | LEU | ||||
4 | ILE | ARG | LEU | PHE | LYS | SER | HIS | PRO | GLU | THR | ||||
5 | LEU | GLU | LYS | PHE | ASP | ARG | PHE | LYS | HIS | LEU | ||||
6 | LYS | THR | GLU | ALA | GLU | MET | LYS | ALA | SER | GLU | ||||
7 | ASP | LEU | LYS | LYS | HIS | GLY | VAL | THR | VAL | LEU | ||||
8 | THR | ALA | LEU | GLY | ALA | ILE | LEU | LYS |
Samples:
sample_1: (1-77)Apomyoglobin, [U-99% 13C; U-99% 15N], 313 uM; CD3COOH 5 mM; H2O 95%; D2O 5%
sample_conditions_1: pH: 2.40; pressure: 1 atm; temperature: 298.15 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
BMRB | 1027 1029 1200 1413 1455 1457 1459 1461 1463 1465 1467 1469 1471 15589 16217 16218 16500 16501 1752 2345 2346 2347 2348 2431 2432 2433 2434 291 292 293 40 4061 4062 426 4568 4676 4695 |
PDB | |
DBJ | BAF03579 |
GB | AAA72199 |
PRF | 742482A |
REF | NP_001277651 |
SP | P02185 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts