Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR19165
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Citation: Garrison, McKinzie; Crowhurst, Karin. "NMR-monitored titration of acid-stress bacterial chaperone HdeA reveals that Asp and Glu charge neutralization produces a loosened dimer structure in preparation for protein unfolding and chaperone activation." Protein Sci. 23, 167-178 (2014).
PubMed: 24375557
Assembly members:
HdeA, polymer, 89 residues, 9741 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21a
Entity Sequences (FASTA):
HdeA: ADAQKAADNKKPVNSWTCED
FLAVDESFQPTAVGFAEALN
NKDKPEDAVLDVQGIATVTP
AIVQACTQDKQANFKDKVKG
EWDKIKKDM
Data type | Count |
13C chemical shifts | 358 |
15N chemical shifts | 91 |
1H chemical shifts | 493 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | HdeA homodimer, 1 | 1 |
2 | HdeA homodimer, 2 | 1 |
Entity 1, HdeA homodimer, 1 89 residues - 9741 Da.
1 | ALA | ASP | ALA | GLN | LYS | ALA | ALA | ASP | ASN | LYS | ||||
2 | LYS | PRO | VAL | ASN | SER | TRP | THR | CYS | GLU | ASP | ||||
3 | PHE | LEU | ALA | VAL | ASP | GLU | SER | PHE | GLN | PRO | ||||
4 | THR | ALA | VAL | GLY | PHE | ALA | GLU | ALA | LEU | ASN | ||||
5 | ASN | LYS | ASP | LYS | PRO | GLU | ASP | ALA | VAL | LEU | ||||
6 | ASP | VAL | GLN | GLY | ILE | ALA | THR | VAL | THR | PRO | ||||
7 | ALA | ILE | VAL | GLN | ALA | CYS | THR | GLN | ASP | LYS | ||||
8 | GLN | ALA | ASN | PHE | LYS | ASP | LYS | VAL | LYS | GLY | ||||
9 | GLU | TRP | ASP | LYS | ILE | LYS | LYS | ASP | MET |
PDB | 1BG8 1DJ8 |
DBJ | BAA01883 BAB37813 BAE77784 BAG79302 BAI27765 |
EMBL | CAP77965 CAQ33828 CAR00456 CAR05133 CAR10321 |
GB | AAB18486 AAC76535 AAG58651 AAN44999 AAN82757 |
PRF | 1912293A |
REF | NP_312417 NP_417967 NP_709292 WP_000756547 WP_000756548 |
SP | P0AES9 P0AET0 P0AET1 |
AlphaFold | P0AES9 P0AET0 P0AET1 |
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CSV: Backbone
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SPARKY: Backbone
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