BMRB Entry 50489

Title:
1H and 13C chemical shifts for [DPro2]-Orn analogue of hECP30 in aqueous solution
Deposition date:
2020-09-30
Original release date:
2021-08-11
Authors:
Chaves-Arquero, Belen; Jimenez, M. Angeles
Citation:

Citation: Sandin, Daniel; Valle, Javier; Chaves-Arquero, Belen; Prats-Ejarque, Guillem; Larrosa, Maria-Nieves; Gonzalez, Juan; Jimenez, M. Angeles; Boix, Ester; Andreu, David; Torrent, Marc. "Rationally Modified Antimicrobial Peptides from the N-Terminal Domain of Human RNase 3 Show Exceptional Serum Stability"  J. Med. Chem. 64, 11472-11482 (2021).
PubMed: 34342438

Assembly members:

Assembly members:
entity_1, polymer, 31 residues, 3505.15 Da.

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: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: XXFTXAQWFAIQHISPXTIA MXAINNYXWXX

Data sets:
Data typeCount
13C chemical shifts235
1H chemical shifts478

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1[D-Pro2]-Orn-hECP301

Entities:

Entity 1, [D-Pro2]-Orn-hECP30 31 residues - 3505.15 Da.

P2 is a D-aminoacid P2 is D-Pro2

1   ORNDPRPHETHRORNALAGLNTRPPHEALA
2   ILEGLNHISILESERPROORNTHRILEALA
3   METORNALAILEASNASNTYRORNTRPORN
4   NH2