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 34074

Title: HYL-20   PubMed: 28830077

Authors: Hexnerova, R.

Citation: Nesuta, O.; Budesinsky, M.; Hadravova, R.; Monincova, L.; Humpolickova, J.; Cerovsky, V.. "How proteases from Enterococcus faecalis contribute to its resistance to short alpha-helical antimicrobial peptides."  Pathog. Dis. 75, .-. (2017).

Assembly members:
entity_1, polymer, 16 residues, 1831.356 Da.
entity_NH2, non-polymer, 16.023 Da.

Natural source:   Common Name: bees   Taxonomy ID: 1126410   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Hylaeus signatus

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
entity_1: GILSSLWKKLKKIIAK

Data sets:
Data typeCount
13C chemical shifts50
15N chemical shifts16
1H chemical shifts135

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 16 residues - 1831.356 Da.

1   GLYILELEUSERSERLEUTRPLYSLYSLEU
2   LYSLYSILEILEALALYS

Entity 2, entity_2 - H2 N - 16.023 Da.

1   NH2

Samples:

sample_1: entity_1 5 mM; trifluoroethanol, CF3CD2OH, 30%

sample_conditions_1: pH: 4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H COSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

SPARKY, Goddard - chemical shift assignment, peak picking

TOPSPIN, Bruker Biospin - collection, data analysis

NMR spectrometers:

  • Bruker AvanceIII 600 MHz

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