2N8W
Solution NMR Structure of Designed Protein DA05R1, Northeast Structural Genomics Consortium (NESG) Target OR690
Summary for 2N8W
| Entry DOI | 10.2210/pdb2n8w/pdb |
| Related | 2N8I |
| NMR Information | BMRB: 25868 |
| Descriptor | Designed Protein DA05R1 (1 entity in total) |
| Functional Keywords | designed protein, de novo protein, psi-biology, structural genomics, northeast structural genomics consortium, nesg |
| Biological source | synthetic construct (artificial gene) |
| Total number of polymer chains | 1 |
| Total formula weight | 11932.48 |
| Authors | Eletsky, A.,Federizon, J.F.,Xu, X.,Pulavarti, S.,Jacobs, T.M.,Kuhlman, B.,Szyperski, T.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2015-10-27, release date: 2015-11-25, Last modification date: 2024-05-15) |
| Primary citation | Jacobs, T.M.,Williams, B.,Williams, T.,Xu, X.,Eletsky, A.,Federizon, J.F.,Szyperski, T.,Kuhlman, B. Design of structurally distinct proteins using strategies inspired by evolution. Science, 352:687-690, 2016 Cited by PubMed Abstract: Natural recombination combines pieces of preexisting proteins to create new tertiary structures and functions. We describe a computational protocol, called SEWING, which is inspired by this process and builds new proteins from connected or disconnected pieces of existing structures. Helical proteins designed with SEWING contain structural features absent from other de novo designed proteins and, in some cases, remain folded at more than 100°C. High-resolution structures of the designed proteins CA01 and DA05R1 were solved by x-ray crystallography (2.2 angstrom resolution) and nuclear magnetic resonance, respectively, and there was excellent agreement with the design models. This method provides a new strategy to rapidly create large numbers of diverse and designable protein scaffolds. PubMed: 27151863DOI: 10.1126/science.aad8036 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
