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 36014

Title: Solution structure of the Pin1-PPIase (S138A) mutant   PubMed: 28617332

Deposition date: 2016-08-02 Original release date: 2017-08-07

Authors: Tochio, N.; Wang, J.; Tate, S.

Citation: Wang, Jing; Kawasaki, Ryosuke; Uewaki, Jun-Ichi; Rashid, Arif; Tochio, Naoya; Tate, Shin-Ichi. "Dynamic Allostery Modulates Catalytic Activity by Modifying the Hydrogen Bonding Network in the Catalytic Site of Human Pin1."  Molecules 22, E992-E992 (2017).

Assembly members:
entity_1, polymer, 117 residues, 13105.732 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 BL21(DE3)

Entity Sequences (FASTA):
entity_1: GSHMEPARVRCSHLLVKHSQ SRRPSSWRQEKITRTKEEAL ELINGYIQKIKSGEEDFESL ASQFSDCSSAKARGDLGAFS RGQMQKPFEDAAFALRTGEM SGPVFTDSGIHIILRTE

Data sets:
Data typeCount
13C chemical shifts510
15N chemical shifts127
1H chemical shifts804

Additional metadata:

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