Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15589
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Citation: Kurt, Nese; Cavagnero, Silvia. "Nonnative helical motif in a chaperone-bound protein fragment" Biophys. J. 94, 48-50 (2008).
PubMed: 18192369
Assembly members:
Apomyoglobin_(1-77), polymer, 77 residues, Formula weight is not available
DnaK-beta, polymer, . residues, Formula weight is not available
Natural source: Common Name: Physeter catodon Taxonomy ID: 9755 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Physeter catodon
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET
Entity Sequences (FASTA):
Apomyoglobin_(1-77): VLSEGEWQLVLHVWAKVEAD
VAGHGQDILIRLFKSHPETL
EKFDRFKHLKTEAEMKASED
LKKHGVTVLTALGAILK
Data type | Count |
13C chemical shifts | 47 |
15N chemical shifts | 46 |
1H chemical shifts | 46 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Substrate | 1 |
2 | Chaperone | 2 |
Entity 1, Substrate 77 residues - Formula weight is not available
1 | VAL | LEU | SER | GLU | GLY | GLU | TRP | GLN | LEU | VAL | ||||
2 | LEU | HIS | VAL | TRP | ALA | LYS | VAL | GLU | ALA | ASP | ||||
3 | VAL | ALA | GLY | HIS | GLY | GLN | ASP | ILE | LEU | ILE | ||||
4 | ARG | LEU | PHE | LYS | SER | HIS | PRO | GLU | THR | LEU | ||||
5 | GLU | LYS | PHE | ASP | ARG | PHE | LYS | HIS | LEU | LYS | ||||
6 | THR | GLU | ALA | GLU | MET | LYS | ALA | SER | GLU | ASP | ||||
7 | LEU | LYS | LYS | HIS | GLY | VAL | THR | VAL | LEU | THR | ||||
8 | ALA | LEU | GLY | ALA | ILE | LEU | LYS |
Entity 2, Chaperone - Formula weight is not available
sample_1: Apomyoglobin (1-77), [U-99% 13C; U-99% 15N], 100 uM; DnaK-beta, [U-2H], 100 uM; sodium acetate 10 mM; D2O, [U-100% 2H], 5%; H2O 95%
sample_conditions_1: ionic strength: 10 mM; pH: 5.8; pressure: 1 atm; temperature: 277 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
NMRView, Johnson, One Moon Scientific - chemical shift assignment
BMRB | 1027 1029 1200 1413 1455 1457 1459 1461 1463 1465 1467 1469 1471 16217 16218 16499 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 |
AlphaFold | P02185 |
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