The plant nucleoplasmin AtFKBP43 needs its extended arms for histone interaction.

Singh AK, Saharan K, Baral S, Vasudevan D, Biochim Biophys Acta Gene Regul Mech 1865(7):194872 (2022) Europe PMC

SASDNN3 – Peptidyl-prolyl cis-trans isomerase FKBP43, nucleoplasmin domain (amino acids 1-96)

Peptidyl-prolyl cis-trans isomerase FKBP43

MW^experimental	83	kDa
MW^expected	58	kDa
V^Porod	141	nm³

log I(s) 8.35×10⁴ 8.35×10³ 8.35×10² 8.35×10¹

Peptidyl-prolyl cis-trans isomerase FKBP43 small angle scattering data

s, nm^-1

Log plot Log-Log plot

ln I(s)

Peptidyl-prolyl cis-trans isomerase FKBP43 Guinier plot

ln 8.36×10⁴ R_g: 2.5 nm 0 (2.5 nm)^-2 s²

(sR_g)²I(s)/I(0)

Peptidyl-prolyl cis-trans isomerase FKBP43 Kratky plot

1.104 0 √3 sR_g

p(r)	R_g: 2.6 nm 0 D_max: 7.3 nm

Data validation

Experimental data range

p(r) fit to data

Metric

Value

s_min D_max / π

0.4

N_Shannon

Worse

Better

Metric

Value

p_cormap

χ²

0.000
0.413

Worse

Better

Fits and models

log I(s)	s, nm^-1
+3 Δ/σ -3	s, nm^-1

Peptidyl-prolyl cis-trans isomerase FKBP43 ALPHAFOLD model

Synchrotron SAXS data from solutions of the peptidyl-prolyl cis-trans isomerase FKBP43 nucleoplasmin domain in 20 mM Tris, 300 mM NaCl, 1 mM β-mercaptoethanol, pH 7.5 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.0998 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.50 mg/ml was measured at 20°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

X-ray Exposure time = UNKNOWN. Number of frames = UNKNOWN

Peptidyl-prolyl cis-trans isomerase FKBP43 (FKBP43)
Mol. type		Protein
Organism		Arabidopsis thaliana
Olig. state		Pentamer
Mon. MW		11.6 kDa

UniProt		F4J9Q6 (1-96)
Sequence		FASTA

ALPHAFOLD ID		F4J9Q6