BMRB Entry 51043

Title:
WT Pin1 with 5x FFpSPR ligand   PubMed: 35927276
Deposition date:
2021-07-29
Original release date:
2022-08-11
Authors:
Born, Alexandra; Henen, Morkos; Vogeli, Beat
Citation:

Citation: Born, Alexandra; Soetbeer, Janne; Henen, Morkos; Breitgoff, Frauke; Nichols, Parker; Jeschke, Gunnar; Vogeli, Beat. "Ligand-specific conformational change drives interdomain allostery in Pin1"  Nat. Commun. 13, 4546-4546 (2022).

Assembly members:

Assembly members:
entity_1, polymer, 163 residues, 18243 Da.
entity_2, polymer, 5 residues, 774 Da.

Natural source:

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   Vector: pet28a

Experimental source:

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   Vector: pet28a

Data sets:
Data typeCount
13C chemical shifts475
15N chemical shifts168
1H chemical shifts1068

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Pin11
2FFpSPR2

Entities:

Entity 1, Pin1 163 residues - 18243 Da.

Starting at 1, should be 163 amino acids long

1   METALAASPGLUGLULYSLEUPROPROGLY
2   TRPGLULYSARGMETSERARGSERSERGLY
3   ARGVALTYRTYRPHEASNHISILETHRASN
4   ALASERGLNTRPGLUARGPROSERGLYASN
5   SERSERSERGLYGLYLYSASNGLYGLNGLY
6   GLUPROALAARGVALARGCYSSERHISLEU
7   LEUVALLYSHISSERGLNSERARGARGPRO
8   SERSERTRPARGGLNGLULYSILETHRARG
9   THRLYSGLUGLUALALEUGLULEUILEASN
10   GLYTYRILEGLNLYSILELYSSERGLYGLU
11   GLUASPPHEGLUSERLEUALASERGLNPHE
12   SERASPCYSSERSERALALYSALAARGGLY
13   ASPLEUGLYALAPHESERARGGLYGLNMET
14   GLNLYSPROPHEGLUASPALASERPHEALA
15   LEUARGTHRGLYGLUMETSERGLYPROVAL
16   PHETHRASPSERGLYILEHISILEILELEU
17   ARGTHRGLU

Entity 2, FFpSPR 5 residues - 774 Da.

phosphorylated serine (pS) at position X

1   PHEPHESEPPROARG

Samples:

sample_1: Pin1, [U-99% 13C; U-99% 15N], 600 uM; FFpSPR 3.6 mM; DTT 5 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 0.03%

sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 15N-separated NOESYsample_1isotropicsample_conditions_1
3D 13C-separated NOESYsample_1isotropicsample_conditions_1

Software:

CcpNMR v2.4.2 - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 900 MHz

Related Database Links:

BMRB 27579

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks