BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 7101

Title: Mistranslation of a computationally designed protein yields an exceptionally stable homodimer: Implications for protein evolution and engineering.   PubMed: 16949611

Deposition date: 2006-05-05 Original release date: 2006-11-17

Authors: Dantas, G.

Citation: Dantas, G.; Watters, A.; Lunde, B.; Eletr, Z.; Isern, N.; Roseman, T.; Lipfert, J.; Doniach, S.; Tompa, M.; Kuhlman, B.; Stoddard, B.; Varani, G.; Baker, D.. "Mis-translation of a computationally designed protein yields an exceptionally stable homodimer: Implications for protein evolution and engineering."  J. Mol. Biol. 362, 1004-1024 (2006).

Assembly members:
Designed protein TOP7, polymer, 62 residues, Formula weight is not available

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
Designed protein TOP7: MERVRISITARTKKEAEKFA AILIKVFAELGYNDINVTWD GDTVTVEGQLEGGSLEHHHH HH

Data sets:
Data typeCount
13C chemical shifts223
15N chemical shifts59
1H chemical shifts390

Additional metadata:

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Related Database Links:

PDB 2GJH

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