BMRB Entry 6822

Title:
The Structure of the Hamp Domain Implies a Rotational Mechanism in Transmembrane Signalling
Deposition date:
2005-09-09
Original release date:
2006-10-19
Authors:
Coles, M.; Truffault, V.; Hulko, M.; Martin, J.; Lupas, A.
Citation:

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).
PubMed: 16959572

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

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

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

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1hypothetical protein AF1503 chain A1
2hypothetical protein AF1503 chain B1

Entities:

Entity 1, hypothetical protein AF1503 chain A 56 residues - Formula weight is not available

1   GLYSERSERTHRILETHRARGPROILEILE
2   GLULEUSERASNTHRALAASPLYSILEALA
3   GLUGLYASNLEUGLUALAGLUVALPROHIS
4   GLNASNARGALAASPGLUILEGLYILELEU
5   ALALYSSERILEGLUARGLEUARGARGSER
6   LEULYSVALALAMETGLU

Samples:

sample_1: hypothetical protein AF1503 1.0 mM; phosphate buffer 20 mM; NACL 150 mM; H2O 90%; D2O 10%

sample_2: hypothetical protein AF1503, [U-15N], 1.0 mM; phosphate buffer 20 mM; NACL 150 mM; H2O 90%; D2O 10%

sample_3: hypothetical protein AF1503, [U-13C; U-15N], 1.0 mM; phosphate buffer 20 mM; NACL 150 mM; H2O 90%; D2O 10%

sample_cond_1: ionic strength: 150 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYnot availablenot availablenot available
2D NOESYnot availablenot availablenot available
HNHAnot availablenot availablenot available
2D 12C-FILTERED/13C-EDITED NOESYnot availablenot availablenot available
3D-NNH-NOESYnot availablenot availablenot available
3D-CNH-NOESYnot availablenot availablenot available

Software:

X-PLOR vNIH-2.9.7 - refinement, structure solution

xwinnmr v3.5 - processing

SPARKY v3.110 - data analysis

NMR spectrometers:

  • Bruker DMX 900 MHz

Related Database Links:

BMRB 17775 17776
PDB
GB AAB89755 AIG98513
REF NP_070332 WP_010879000

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks