BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 51596

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51596

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: Switchable single alpha helix peptide E(P3-7)3   PubMed: 36400768

Deposition date: 2022-08-22 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: 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).

Assembly members:
entity_1, polymer, 31 residues, Formula weight is not available

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pDEST17

Entity Sequences (FASTA):
entity_1: KKPGASLAALEALEALEALE ALEAAEAAKKY

Data typeCount
13C chemical shifts265
15N chemical shifts87
1H chemical shifts86

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1E(P3-7)31

Entities:

Entity 1, E(P3-7)3 31 residues - Formula weight is not available

1   LYSLYSPROGLYALASERLEUALAALALEU
2   GLUALALEUGLUALALEUGLUALALEUGLU
3   ALALEUGLUALAALAGLUALAALALYSLYS
4   TYR

Samples:

sample_1: (P3-7)3, [U-100% 13C; U-100% 15N], 100 uM; DSS 10 uM; sodium phosphate 20 mM

sample_2: (P3-7)3, [U-100% 13C; U-100% 15N], 100 uM; DSS 10 uM; phosphoric acid 20 mM

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

sample_conditions_2: ionic strength: 90 mM; pH: 2.8; pressure: 1 atm; temperature: 278 K

sample_conditions_3: ionic strength: 90 mM; pH: 2.8; pressure: 1 atm; temperature: 310 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
3D HNCOsample_2isotropicsample_conditions_2
3D HN(CA)COsample_2isotropicsample_conditions_2
3D HN(CO)CAsample_2isotropicsample_conditions_2
3D HNCAsample_2isotropicsample_conditions_2
3D HN(CO)CACBsample_2isotropicsample_conditions_2
2D CONsample_2isotropicsample_conditions_2
2D CACOsample_2isotropicsample_conditions_2
3D HNCOsample_2isotropicsample_conditions_3
3D HN(CA)COsample_2isotropicsample_conditions_3
3D HN(CO)CAsample_2isotropicsample_conditions_3
3D HNCAsample_2isotropicsample_conditions_3
3D HN(CO)CACBsample_2isotropicsample_conditions_3
2D CONsample_2isotropicsample_conditions_3
2D CACOsample_2isotropicsample_conditions_3

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 shifts
SPARKY: Backbone or all simulated shifts