BMRB Entry 36347

Name: The solution NMR structure of VV14 peptide in the presence of Deuterated SDS micelle.
Published: 2025-10-24

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PDB ID: 7bx2
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36347
MolProbity Validation Chart

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NMR-STAR v3 text file.
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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 solution NMR structure of VV14 peptide in the presence of Deuterated SDS micelle.

Deposition date:

2020-04-16

Original release date:

2025-10-24

Authors:

Bhunia, A.; Mohid, S.; Chowdhury, N.

Citation:

Citation: Pandit, Gopal; Chowdhury, Nabarupa; Abdul Mohid, Sk; Bidkar, Anil; Bhunia, Anirban; Chatterjee, Sunanda. "Effect of Secondary Structure and Side Chain Length of Hydrophobic Amino Acid Residues on the Antimicrobial Activity and Toxicity of 14-Residue-Long de novo AMPs." ChemMedChem 16, 355-367 (2021).
PubMed: 33026188

Assembly members:

Assembly members:
VAL-LYS-TRP-VAL-LYS-LYS-VAL-VAL-LYS-TRP-VAL-LYS-LYS-VAL, polymer, 14 residues, 1760.298 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 Host organism: unidentified

Entity Sequences (FASTA):

Entity Sequences (FASTA):
VAL-LYS-TRP-VAL-LYS-LYS-VAL-VAL-LYS-TRP-VAL-LYS-LYS-VAL: VKWVKKVVKWVKKV

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
1H chemical shifts	106

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 14 residues - 1760.298 Da.

1

VAL

LYS

TRP

VAL

LYS

VAL

LYS

TRP

2

VAL

LYS

VAL

Samples:

1mM_VV14_peptide: VAL-LYS-TRP-VAL-LYS-LYS-VAL-VAL-LYS-TRP-VAL-LYS-LYS-VAL, 1H, 1 ± 0.2 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 0 Not defined; pH: 4.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	1mM_VV14_peptide	isotropic	sample_conditions_1
2D 1H-1H NOESY	1mM_VV14_peptide	isotropic	sample_conditions_1

Software:

TopSpin v3.5, Bruker Biospin - collection

TopSpin v3.5, Bruker Biospin - processing

Sparky v3.114, Goddard - chemical shift assignment

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement

NMR spectrometers:

Bruker AVANCE III 700 MHz
Bruker AVANCE III 500 MHz