1QYS

Crystal structure of Top7: A computationally designed protein with a novel fold

Summary for 1QYS

Entry DOI	10.2210/pdb1qys/pdb
Descriptor	TOP7 (2 entities in total)
Functional Keywords	alpha-beta, computationally designed, novel fold, de novo protein
Biological source	Computationally Designed Sequence
Total number of polymer chains	1
Total formula weight	12130.25
Authors	Kuhlman, B.,Dantas, G.,Ireton, G.C.,Varani, G.,Stoddard, B.L.,Baker, D. (deposition date: 2003-09-11, release date: 2003-11-25, Last modification date: 2024-10-30)
Primary citation	Kuhlman, B.,Dantas, G.,Ireton, G.C.,Varani, G.,Stoddard, B.L.,Baker, D. Design of a Novel Globular Protein Fold with Atomic-Level Accuracy Science, 302:1364-1368, 2003 Cited by PubMed Abstract: A major challenge of computational protein design is the creation of novel proteins with arbitrarily chosen three-dimensional structures. Here, we used a general computational strategy that iterates between sequence design and structure prediction to design a 93-residue alpha/beta protein called Top7 with a novel sequence and topology. Top7 was found experimentally to be folded and extremely stable, and the x-ray crystal structure of Top7 is similar (root mean square deviation equals 1.2 angstroms) to the design model. The ability to design a new protein fold makes possible the exploration of the large regions of the protein universe not yet observed in nature. PubMed: 14631033 DOI: 10.1126/science.1089427 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.5 Å)

Structure validation