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 7102

Title: High-resolution structural and thermodynamic analysis of extreme stabilization of human procarboxypeptidase by computational protein design   PubMed: 17196978

Deposition date: 2006-05-05 Original release date: 2007-04-16

Authors: Reichow, S.

Citation: Dantas, G.; Corrent, C.; Reichow, S.; Havranek, J.; Eletr, Z.; Isern, N.; Kuhlman, B.; Varani, G.; Merritt, E.; Baker, D.. "High-resolution structural and thermodynamic analysis of extreme stabilization of human procarboxypeptidase by computational protein design"  J. Mol. Biol. 366, 1209-1221 (2007).

Assembly members:
Designed Protein AYE, polymer, 78 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 AYE: HHHHHHGSKTIFVIVPTNEE QVAFLEALAKQDELNFDWQN PPTEPGQPVVILIPSDMVEW FLEMLKAKGIPFTVYVEE

Data sets:
Data typeCount
13C chemical shifts234
15N chemical shifts73
1H chemical shifts542

Additional metadata:

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Related Database Links:

PDB 1VJQ 2GJF

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