BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 25527

Title: Chemical shift assignments and structure of the alpha-crystallin domain from human, HSPB5   PubMed: 25962097

Deposition date: 2015-06-01 Original release date: 2015-06-01

Authors: Rajagopal, Ponni; Klevit, Rachel; Shi, Lei; Baker, David

Citation: Rajagopal, Ponni; Tse, Eric; Borst, Andrew; Delbecq, Scott; Shi, Lei; Dove, Katja; Baker, David; Southworth, Daniel; Klevit, Rachel. "A conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress-related acidosis"  eLife ., .-. (2015).

Assembly members:
HSPB5-ACD, polymer, 89 residues, 10200.596 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
HSPB5-ACD: GLSEMRLEKDRFSVNLDVKH FSPEELKVKVLGDVIEVHGK HEERQDEHGFISREFHRKYR IPADVDPLTITSSLSSDGVL TVDGPRKQV

Data sets:
Data typeCount
13C chemical shifts359
15N chemical shifts95
1H chemical shifts622

Additional metadata:

  • Assembly
  • Samples and Experiments
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  • Spectrometers
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Related Database Links:

BMRB 16391 26640
PDB 2KLR 2N0K 2Y1Y 2YGD 3L1G 4M5S 4M5T
DBJ BAD51947 BAE27257 BAE40798 BAE87237 BAG36739
EMBL CAA64669 CAH91560 CAJ18549 CAL37427 CAL37905
GB AAA37472 AAA52104 AAA60267 AAA67045 AAB23453
REF NP_001075876 NP_001125917 NP_001166547 NP_001247830 NP_001271991
SP P02511 P23927 P41316 Q5R9K0 Q60HG8

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