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 36077

Title: Solution structure for human HSP70 substrate binding domain   PubMed: 29495458

Deposition date: 2017-04-26 Original release date: 2018-05-14

Authors: Hoshikawa, M.; Tochio, N.; Tate, S.

Citation: Umehara, Kohei; Hoshikawa, Miho; Tochio, Naoya; Tate, Shin-Ichi. "Substrate Binding Switches the Conformation at the Lynchpin Site in the Substrate-Binding Domain of Human Hsp70 to Enable Allosteric Interdomain Communication"  Molecules 23, E528-E528 (2018).

Assembly members:
Heat shock 70 kDa protein 1A, polymer, 185 residues, 20323.885 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):
Heat shock 70 kDa protein 1A: HMGDKSENVQDLLLLDVAPL SLGLETAGGVMTALIKRNST IPTKQTQIFTTYSDNQPGVL IQVYEGERAMTKDNNLLGRF ELSGIPPAPRGVPQIEVTFD IDANGILNVTATDKSTGKAN KITITNDKGRLSKEEIERMV QEAEKYKAEDEVQRERVSAK NALESYAFNMKSAVEDEGLK GKISE

Data sets:
Data typeCount
13C chemical shifts781
15N chemical shifts197
1H chemical shifts1136

Additional metadata:

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