BMRB Entry 30976

Name: 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.
Published: 2023-01-18

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PDB ID: 7t7w
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30976
MolProbity Validation Chart

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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:

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

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: LKKLWRFLKKL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
13C chemical shifts	38
1H chemical shifts	93

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 11 residues - 1477.943 Da.

1

LEU

LYS

LEU

TRP

ARG

PHE

LEU

LYS

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:

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_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