BMRB Entry 30651

Name: Lasso peptide pandonodin
Published: 2019-12-02

Click here to enlarge.

PDB ID: 6q1x
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30651
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Lasso peptide pandonodin

Deposition date:

2019-08-06

Original release date:

2019-12-02

Authors:

Link, A.; Cheung-Lee, W.

Citation:

Citation: Cheung-Lee, W.; Cao, L.; Link, A.. "Pandonodin: a proteobacterial lasso peptide with an exceptionally long C-terminal tail." Acs Chem. Biol. 14, 2783-2792 (2019).
PubMed: 31742991

Assembly members:

Assembly members:
entity_1, polymer, 33 residues, 3330.956 Da.

Natural source:

Natural source: Common Name: Pandoraea norimbergensis Taxonomy ID: 93219 Superkingdom: Bacteria Kingdom: not available Genus/species: Pandoraea norimbergensis

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GVLGNDAEGITLLPLCFKPI CIPTLPPLTGGHA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
1H chemical shifts	235

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 33 residues - 3330.956 Da.

1

GLY

VAL

LEU

GLY

ASN

ASP

ALA

GLU

GLY

ILE

2

THR

LEU

PRO

LEU

CYS

PHE

LYS

PRO

ILE

3

CYS

ILE

PRO

THR

LEU

PRO

LEU

THR

GLY

4

GLY

HIS

ALA

Samples:

sample_1: pandonodin 6 mg/mL

sample_conditions_1: ionic strength: 0 Not defined; pH: 6.9; pressure: 1 atm; temperature: 295 K

Experiments:

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

Software:

MestreLab (Mnova / MestReNova / MestReC) v11.0, Mestrelab Research - chemical shift assignment, peak picking, processing

CYANA v2.0, Guntert, Mumenthaler and Wuthrich - structure calculation

NMR spectrometers:

Bruker AVANCE III 800 MHz