BMRB Entry 36349

Name: Template lasso peptide C24 mutant V3A
Published: 2025-10-24

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36349

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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:

Template lasso peptide C24 mutant V3A

Deposition date:

2020-04-27

Original release date:

2025-10-24

Authors:

Liu, X.; Liu, T.; Ma, X.; Yu, J.; Yang, D.; Ma, M.

Citation:

Citation: Liu, Tan; Ma, Xiaojie; Yu, Jiahui; Yang, Wensheng; Wang, Guiyang; Wang, Zhengdong; Ge, Yuanjie; Song, Juan; Han, Hua; Zhang, Wen; Yang, Donghui; Liu, Xuehui; Ma, Ming. "Rational generation of lasso peptides based on biosynthetic gene mutations and site-selective chemical modifications." Chem. Sci. 12, 12353-12364 (2021).
PubMed: 34603665

Assembly members:

Assembly members:
lasso peptide, polymer, 15 residues, 1686.905 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: 1931 Superkingdom: Bacteria Kingdom: Bacillati Genus/species: Streptomyces sp.

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Streptomyces sp.

Entity Sequences (FASTA):

Entity Sequences (FASTA):
lasso peptide: LVAIVQADWNAPGWF

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	16
15N chemical shifts	12
1H chemical shifts	100

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 15 residues - 1686.905 Da.

1

LEU

VAL

ALA

ILE

VAL

GLN

ALA

ASP

TRP

ASN

2

ALA

PRO

GLY

TRP

PHE

Samples:

v3a: lasso peptide, [U-13C; U-15N], mM; NaCl 100 mM; DMSO 20 v/v; H2O 80 v/v

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	v3a	isotropic	sample_conditions_1
2D 1H-13C HSQC	v3a	isotropic	sample_conditions_1
2D 1H-1H TOCSY	v3a	isotropic	sample_conditions_1
2D 1H-1H NOESY	v3a	isotropic	sample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

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

CcpNmr Analysis, CCPN - chemical shift assignment

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

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

NMR spectrometers:

Agilent DD2 600 MHz

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