BMRB Entry 51608

Name: Single alpha helix peptide u(P3-7)2
Published: 2022-11-04

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51608

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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:

Single alpha helix peptide u(P3-7)2

Deposition date:

2022-08-31

Original release date:

2022-11-04

Authors:

Escobedo, Albert; Piccirillo, Jonathan; Aranda, Juan; Diercks, Tammo; Mateos, Borja; Garcia-Cabau, Carla; Sanchez-Navarro, Macarena; Topal, Busra; Biesaga, Mateusz; Staby, Lasse; Kragelund, Birthe; Garcia, Jesus; Millet, Oscar; Orozco, Modesto; Coles, Murray; Crehuet, Ramon; Salvatella, Xavier

Citation:

Citation: Escobedo, Albert; Piccirillo, Jonathan; Aranda, Juan; Diercks, Tammo; Mateos, Borja; Garcia-Cabau, Carla; Sanchez-Navarro, Macarena; Topal, Busra; Biesaga, Mateusz; Staby, Lasse; Kragelund, Birthe; Garcia, Jesus; Millet, Oscar; Orozco, Modesto; Coles, Murray; Crehuet, Ramon; Salvatella, Xavier. "A glutamine-based single alpha-helix scaffold to target globular proteins" Nat. Commun. 13, 7073-7073 (2022).
PubMed: 36400768

Assembly members:

Assembly members:
entity_1, polymer, 21 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 Host organism: Escherichia coli Vector: pDEST17

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: KKLAALQALQALQAAQAAKK Y

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	40
15N chemical shifts	19
1H chemical shifts	19

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	u(P3-7)2	1

Entities:

Entity 1, u(P3-7)2 21 residues - Formula weight is not available

1

LYS

LEU

ALA

LEU

GLN

ALA

LEU

GLN

2

ALA

LEU

GLN

ALA

GLN

ALA

LYS

3

TYR

Samples:

sample_1: u(P3-7)2, [U-100% 13C; U-100% 15N], 100 uM; DSS 10 uM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 120 mM; pH: 7.4; pressure: 1 atm; temperature: 278 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
2D CACO	sample_1	isotropic	sample_conditions_1
2D CON	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR - chemical shift assignment

TOPSPIN - collection, processing

NMRPipe - processing

qMDD - processing

NMR spectrometers:

Bruker AVANCE NEO 800 MHz
Bruker AVANCE III 600 MHz

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