BMRB Entry 30516

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30516
MolProbity Validation Chart

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Title:
The peptide PaAMP1B3 is an analog derived from the PaAMP1. The sequence of the ribosomal protein of Pyrobaculum aerophylum was used as template for rational design, using the Joker algorithm.
Deposition date:
2018-09-19
Original release date:
2019-09-17
Authors:
Mundim, H.; Alves, E.; Rodrigues, L.; Liao, L.
Citation:

Citation: Mundim, H.; Alves, E.; Liao, L.. "NMR SOLUTION STRUCTURE OF THE ANTIMICROBIAL PEPTIDE PAAMP1B3."  .

Assembly members:

Assembly members:
entity_1, polymer, 20 residues, 2172.791 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: 32630   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: PMARNKILGKILRKIAAFKX

Data typeCount
13C chemical shifts38
15N chemical shifts19
1H chemical shifts112

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 20 residues - 2172.791 Da.

1   PROMETALAARGASNLYSILELEUGLYLYS
2   ILELEUARGLYSILEALAALAPHELYSNH2

Samples:

sample_1: PaAMP1B3 1 mM; SDS-D25, [U-98% 2H], 100 mM; TMSP-d4, [U-98% 2H], 5 % v/v; H2O 90 % v/v; D2O, [U-99% 2H], 10 % v/v

sample_conditions_1: pH: 4.3; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HMQCsample_1isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

  • Bruker AvanceIII 500 MHz

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