BMRB Entry 36014

Title:
Solution structure of the Pin1-PPIase (S138A) mutant
Deposition date:
2016-08-02
Original release date:
2017-08-07
Authors:
Tochio, N.; Wang, J.; Tate, S.
Citation:

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).
PubMed: 28617332

Assembly members:

Assembly members:
entity_1, polymer, 117 residues, 13105.732 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

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

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 117 residues - 13105.732 Da.

1   GLYSERHISMETGLUPROALAARGVALARG
2   CYSSERHISLEULEUVALLYSHISSERGLN
3   SERARGARGPROSERSERTRPARGGLNGLU
4   LYSILETHRARGTHRLYSGLUGLUALALEU
5   GLULEUILEASNGLYTYRILEGLNLYSILE
6   LYSSERGLYGLUGLUASPPHEGLUSERLEU
7   ALASERGLNPHESERASPCYSSERSERALA
8   LYSALAARGGLYASPLEUGLYALAPHESER
9   ARGGLYGLNMETGLNLYSPROPHEGLUASP
10   ALAALAPHEALALEUARGTHRGLYGLUMET
11   SERGLYPROVALPHETHRASPSERGLYILE
12   HISILEILELEUARGTHRGLU

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