2RNM: Small s protein

Structure of The HET-s(218-289) prion in its amyloid form obtained by solid-state NMR. Determined by solution NMR. Released 1 Apr 2008.

Method: Solution NMR
Organism: Podospora anserina
Chains: 5
Atoms: 3,045
Mol. weight: 43.34 kDa
Released: 1 Apr 2008

Explore 2RNM in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2RNM contains 0 α-helices and 30 β-strands across 5 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 0 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	227-233	7	1
β-strand	238-241	4	2
β-strand	244-245	2	3
β-strand	261-269	9	1
β-strand	274-277	4	2
β-strand	280-281	2	3

Chain B: 0 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	225-233	9	1
β-strand	238-241	4	2
β-strand	244-245	2	3
β-strand	261-269	9	1
β-strand	274-277	4	2
β-strand	280-281	2	3

Chain C: 0 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	226-233	8	1
β-strand	238-241	4	2
β-strand	244-245	2	3
β-strand	262-269	8	1
β-strand	274-277	4	2
β-strand	280-281	2	3

Chain D: 0 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	226-233	8	1
β-strand	238-241	4	2
β-strand	244-245	2	3
β-strand	263-269	7	1
β-strand	274-277	4	2
β-strand	280-281	2	3

Chain E: 0 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	226-233	8	1
β-strand	238-241	4	2
β-strand	244-245	2	3
β-strand	262-268	7	1
β-strand	274-277	4	2
β-strand	280-281	2	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Small s protein	A, B, C, D, E	protein	79	Podospora anserina	Q03689 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E), FASTA

>2RNM_1 Small s protein (chains A, B, C, D, E)
MKIDAIVGRNSAKDIRTEERARVQLGNVVTAAALHGGIRISDQTTNSVETVVGKGESRVL
IGNEYGGKGFWDNHHHHHH

Primary citation

Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core. Wasmer, C., Lange, A., Van Melckebeke, H. et al. Science (2008) 319:1523-1526. DOI 10.1126/science.1151839 · PubMed

Other PDB entries of the same protein (UniProt Q03689 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2WVQ 2.0 Å, Structure of the HET-s N-terminal domain. Mutant D23A, P33H
2WVN 2.62 Å, Structure of the HET-s N-terminal domain
2KJ3 High-resolution structure of the HET-s(218-289) prion in its amyloid form obtained by…
2LBU HADDOCK calculated model of Congo red bound to the HET-s amyloid
2MUS HADDOCK calculated model of LIN5001 bound to the HET-s amyloid

Browse more

2RNM is part of these collections:

Protein folding, misfolding and amyloid

About this viewer

MolViewer shows 2RNM directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.