2LN3: Solution NMR Structure of DE NOVO DESIGNED PROTEIN, IF3-like fold, Northeast Structural Genomics Consortium Target OR135 (CASD target)

Unlike random heteropolymers, natural proteins fold into unique ordered structures. Understanding how these are encoded in amino-acid sequences is complicated by energetically unfavourable non-ideal features--for example kinked alpha-helices, bulged beta-strands, strained loops and buried polar groups--that arise in proteins from evolutionary selection for biological function or from neutral drift. Here we describe an approach to designing ideal protein structures stabilized by completely consistent local and non-local interactions. The approach is based on a set of rules relating secondary structure patterns to protein tertiary motifs, which make possible the design of funnel-shaped protein folding energy landscapes leading into the target folded state. Guided by these rules, we designed sequences predicted to fold into ideal protein structures consisting of alpha-helices, beta-strands and minimal loops. Designs for five different topologies were found to be monomeric and very stable and to adopt structures in solution nearly identical to the computational models. These results illuminate how the folding funnels of natural proteins arise and provide the foundation for engineering a new generation of functional proteins free from natural evolution.
PDB ID: 2LN3Download
MMDB ID: 97195
PDB Deposition Date: 2011/12/15
Updated in MMDB: 2012/11
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 2LN3: monomeric; determined by author
Molecular Components in 2LN3
Label Count Molecule
Protein (1 molecule)
DE Novo Designed Protein Or135
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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