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 17450

Title: Solution structure of AS1p-Tar in 10% negatively charged bicelles   PubMed: 21763270

Deposition date: 2011-02-09 Original release date: 2011-08-17

Authors: Unnerstale, Sofia; von Heijne, Gunnar; Draheim, Roger; Maler, Lena

Citation: Unnerstale, Sofia; Maler, Lena; Draheim, Roger. "Structural characterization of AS1-membrane interactions from a subset of HAMP domains."  Biochim. Biophys. Acta. 1808, 2403-2412 (2011).

Assembly members:
AS1p-TarEc, polymer, 19 residues, 2120.664 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: chemical synthesis   Host organism: Escherichia coli

Entity Sequences (FASTA):

Data sets:
Data typeCount
1H chemical shifts116

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Entity Assembly IDEntity NameEntity ID


Entity 1, AS1p-TarEc 19 residues - 2120.664 Da.



sample_1: sodium phosphate 50 mM; DHPC, [U-2H], 240 mM; DMPC, [U-2H], 54 mM; DMPG, [U-2H], 6 mM; H2O 90%; D2O 10%; AS1p-TarEc 2 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 7.2; pressure: 1 atm; temperature: 298 K


NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1


TOPSPIN v2.1, Bruker Biospin - collection

SPARKY v3.114, Goddard - chemical shift assignment, peak picking

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

DBJ BAA15702 BAB36019 BAG77645 BAI25977 BAI30940
EMBL CAP76374 CAQ32363 CAQ98826 CAR03245 CAR08345
GB AAA23566 AAC74956 AAG56876 AAN80760 AAZ87948
REF NP_310623 NP_416400 WP_000610393 WP_001178545 WP_001178547
SP P07017
AlphaFold P07017