Allosteric network of dynamic coupling within BAP1-UCH revealed by methyl NMR

Yong-Sheng Wang.

SASDXD6 – Ubiquitin C-terminal hydrolase (UCH) domain of BAP1

Ubiquitin C-terminal hydrolase (UCH) domain of BAP1 wild type
MWexperimental 28 kDa
MWexpected 27 kDa
VPorod 35 nm3
log I(s) 9.99×10-2 9.99×10-3 9.99×10-4 9.99×10-5
Ubiquitin C-terminal hydrolase (UCH) domain of BAP1 wild type small angle scattering data  s, nm-1
ln I(s)
Ubiquitin C-terminal hydrolase (UCH) domain of BAP1 wild type Guinier plot ln 10.00×10-2 Rg: 2.1 nm 0 (2.1 nm)-2 s2
(sRg)2I(s)/I(0)
Ubiquitin C-terminal hydrolase (UCH) domain of BAP1 wild type Kratky plot 1.104 0 3 sRg
p(r)
Ubiquitin C-terminal hydrolase (UCH) domain of BAP1 wild type pair distance distribution function Rg: 2.1 nm 0 Dmax: 8 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Ubiquitin C-terminal hydrolase (UCH) domain of BAP1 in 20 mM HEPES, 150 mM NaCl, 3 mM CaCl2, 0.02% NaN3, pH 7.5 were collected on the 13A beam line at the Taiwan Photon Source, NSRRC storage ring (Hsinchu, Taiwan) using a Eiger X 1M and Eiger X 9M detector at a sample-detector distance of 9 m and at a wavelength of λ = 0.0826 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 90.00 μl sample at 12 mg/ml was injected at a 0.10 ml/min flow rate onto a Agilent Bio SEC-3, 300 Å column at 10°C. 16 successive 2 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Ubiquitin C-terminal hydrolase (UCH) domain of BAP1 wild type
Mol. type   Protein
Olig. state   Monomer
Mon. MW   27.2 kDa
 
UniProt   Q92560 (1-238)
Sequence   FASTA