BMRB Entry 20090

Name: KAAAD, single alpha helix turn
Published: 2010-10-13

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR20090

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

KAAAD, single alpha helix turn

Deposition date:

2009-08-12

Original release date:

2010-10-13

Authors:

Hoang, Huy

Citation:

Citation: Harrisona, Rosemary; Shepherda, Nicholas; Hoanga, Huy; Ruiz-Gomeza, Gloria; Hilla, Timothy; Drivera, Russell; Desaib, Vishal; Youngb, Paul; Abbenantea, Giovanni; Fairliea, David. "Downsizing human, bacterial, and viral proteins to short water-stable alpha helices that maintain biological potency" Proc. Natl. Acad. Sci. U. S. A. 107, 11686-11691 (2010).
PubMed: 20543141

Assembly members:

Assembly members:
single_turn_helix, polymer, 5 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
single_turn_helix: KAAAD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
coupling_constants
- coupling_constant_list_1

Data type	Count
1H chemical shifts	29
coupling constants	5

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Amino Acid	1

Entities:

Entity 1, Amino Acid 5 residues - Formula weight is not available

1

LYS

ALA

ASP

Samples:

sample_1: single turn helix 10 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 4.5; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - geometry optimization

NMR spectrometers:

Bruker AMX 900 MHz