BMRB Entry 34479

Name: NMR solution structure of class IV lasso peptide felipeptin A2 from Amycolatopsis sp. YIM10
Published: 2020-11-19

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PDB ID: 6xti
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34479
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:

NMR solution structure of class IV lasso peptide felipeptin A2 from Amycolatopsis sp. YIM10

Deposition date:

2020-01-16

Original release date:

2020-11-19

Authors:

Madland, E.; Guerrero-Garzon, J.; Zotchev, S.; Aachmann, F.; Courtade, G.

Citation:

Citation: Guerrero-Garzon, Jaime Felipe; Madland, Eva; Zehl, Martin; Singh, Madhurendra; Rezaei, Shiva; Aachmann, Finn; Courtade, Gaston; Urban, Ernst; Ruckert, Christian; Busche, Tobias; Kalinowski, Jorn; Cao, Yan-Ru; Jiang, Yi; Jiang, Cheng-Lin; Selivanova, Galina; Zotchev, Sergey. "Class IV Lasso Peptides Synergistically Induce Proliferation of Cancer Cells and Sensitize Them to Doxorubicin" iScience 23, 101785-101785 (2020).
PubMed: 33294793

Assembly members:

Assembly members:
entity_1, polymer, 17 residues, 1867.116 Da.

Natural source:

Natural source: Common Name: Amycolatopsis sp. Taxonomy ID: 37632 Superkingdom: Bacteria Kingdom: not available Genus/species: Amycolatopsis sp.

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Streptomyces coelicolor

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GGGGRGYEYNKQCLIFC

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	45
15N chemical shifts	12
1H chemical shifts	87

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 17 residues - 1867.116 Da.

1

GLY

ARG

GLY

TYR

GLU

TYR

ASN

2

LYS

GLN

CYS

LEU

ILE

PHE

CYS

Samples:

sample_1: Felipeptin A2 0.5 mM

sample_conditions_1: ionic strength: 0.5 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D DQF-COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1

Software:

TopSpin, Bruker Biospin - collection

CARA, Keller and Wuthrich - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMR spectrometers:

Bruker AVANCE III 800 MHz

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