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 6822

Title: The Structure of the Hamp Domain Implies a Rotational Mechanism in Transmembrane Signalling   PubMed: 16959572

Deposition date: 2005-09-09 Original release date: 2006-10-19

Authors: Coles, M.; Truffault, V.; Hulko, M.; Martin, J.; Lupas, A.

Citation: Hulko, M.; Berndt, F.; Gruber, M.; Linder, J.; Truffault, V.; Schultz, A.; Martin, J.; Schultz, J.; Lupas, A.; Coles, M.. "The HAMP domain structure implies helix rotation in transmembrane signaling"  Cell 126, 929-940 (2006).

Assembly members:
hypothetical protein AF1503, polymer, 56 residues, Formula weight is not available

Natural source:   Common Name: Archaeoglobus fulgidus   Taxonomy ID: 2234   Superkingdom: Archaea   Kingdom: not available   Genus/species: Archaeoglobus fulgidus

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
hypothetical protein AF1503: GSSTITRPIIELSNTADKIA EGNLEAEVPHQNRADEIGIL AKSIERLRRSLKVAME

Data sets:
Data typeCount
13C chemical shifts229
15N chemical shifts55
1H chemical shifts397

Additional metadata:

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Related Database Links:

BMRB 17775 17776
PDB 2ASW 2ASX 2L7H 2L7I 2LFR 2Y0Q 2Y0T 2Y20 2Y21 3ZCC 3ZRV 3ZRW 3ZRX 3ZX6 4CQ4 4CTI 4GN0
GB AAB89755 AIG98513
REF NP_070332 WP_010879000

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