BMRB Entry 51608

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:
Data typeCount
13C chemical shifts40
15N chemical shifts19
1H chemical shifts19

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1u(P3-7)21

Entities:

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

1   LYSLYSLEUALAALALEUGLNALALEUGLN
2   ALALEUGLNALAALAGLNALAALALYSLYS
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:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
2D CACOsample_1isotropicsample_conditions_1
2D CONsample_1isotropicsample_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