BMRB Entry 31024

Name: NMR structure of a Stapled Lanthipeptide Natural Product
Published: 2022-10-05

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PDB ID: 8cwx
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31024
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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 structure of a Stapled Lanthipeptide Natural Product

Deposition date:

2022-05-19

Original release date:

2022-10-05

Authors:

Pei, Z.; Zhu, L.; Nair, S.

Citation:

Citation: Pei, Zeng-Fei; Zhu, Lingyang; Sarksian, Raymond; van der Donk, Wilfred; Nair, Satish. "Class V Lanthipeptide Cyclase Directs the Biosynthesis of a Stapled Peptide Natural Product" J. Am. Chem. Soc. 144, 17549-17557 (2022).
PubMed: 36107785

Assembly members:

Assembly members:
entity_1, polymer, 28 residues, 2783.145 Da.

Natural source:

Natural source: Common Name: Streptomyces morookaense Taxonomy ID: 1970 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptomyces morookaense

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: FAADAWAAQDMAXGNPLXXX FCCXVQCG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
1H chemical shifts	158

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 28 residues - 2783.145 Da.

1

PHE

ALA

ASP

ALA

TRP

ALA

GLN

ASP

2

MET

ALA

DAL

GLY

ASN

PRO

LEU

DBU

DBB

3

PHE

CYS

DAL

VAL

GLN

CYS

GLY

Samples:

sample_1: mSmoAc 1.5 ± 0.2 mM

sample_conditions_1: ionic strength: 0 mM; pH: 6.0; pressure: 1 atm; temperature: 298 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

Software:

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

PROCHECK / PROCHECK-NMR, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Thornton - data analysis

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

Sparky, Goddard - chemical shift assignment

NMR spectrometers:

Agilent VNMRS 750 MHz