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 30976

Title: The peptide Lt-MAP4 is an analog derived from the Ltc-3a. The primary sequence of the parental peptide was used as template for rational design, using the amino acid residues for modification of charge and hydrophobicity.

Deposition date: 2021-12-15 Original release date: 2023-01-18

Authors: Freitas, C.; Moraes, L.; Migliolo, L.; Liao, L.

Citation: Freitas, C.; Liao, L.; Migliolo, L.; Moraes, L.. "Two-dimensional NMR structural study of latarasin analogue Lt-MAP4 multifunctional synthetic peptide."  .

Assembly members:
entity_1, polymer, 11 residues, 1477.943 Da.

Natural source:   Common Name: Lachesana tarabaevi   Taxonomy ID: 379576   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Lachesana tarabaevi

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
entity_1: LKKLWRFLKKL

Data sets:
Data typeCount
13C chemical shifts38
1H chemical shifts93

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 11 residues - 1477.943 Da.

1   LEULYSLYSLEUTRPARGPHELEULYSLYS
2   LEU

Samples:

sample_1: Latarasin-L4 1 mM; SDS-d25, [U-98% 2H], 100 mM; DSS-d6, [U-98% 2H], 0.035%

sample_conditions_1: pH: 4.46; pressure: 1 atm; temperature: 313 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

Software:

CcpNmr Analysis, CCPN - chemical shift assignment, peak picking

ARIA, Linge, O'Donoghue and Nilges - structure calculation

TopSpin, Bruker Biospin - processing

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Bruker AVANCE III 500 MHz