BMRB Entry 30073

Name: LP2006, a handcuff-topology lasso peptide antibiotic
Published: 2017-02-23

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PDB ID: 5jpl
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30073
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:

LP2006, a handcuff-topology lasso peptide antibiotic

Deposition date:

2016-05-03

Original release date:

2017-02-23

Authors:

Tietz, Jonathan; Schwalen, Christopher; Blair, Patricia; Zakai, Uzma; Mitchell, Douglas

Citation:

Citation: Tietz, Jonathan; Schwalen, Christopher; Patel, Parth; Maxson, Tucker; Blair, Patricia; Tai, C.; Zakai, Uzma; Mitchell, Douglas. "A new genome mining tool redefines the lasso peptide biosynthetic landscape" Nat. Chem. Biol. 13, 470-478 (2017).
PubMed: 28244986

Assembly members:

Assembly members:
Uncharacterized protein, polymer, 17 residues, 2027.247 Da.

Natural source:

Natural source: Common Name: high GC Gram+ Taxonomy ID: 1205910 Superkingdom: Bacteria Kingdom: not available Genus/species: Nocardiopsis not available

Experimental source:

Experimental source: Production method: na

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Uncharacterized protein: GRPNWGFENDWSCVRVC

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	17
1H chemical shifts	108

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 - 2027.247 Da.

1

GLY

ARG

PRO

ASN

TRP

GLY

PHE

GLU

ASN

ASP

2

TRP

SER

CYS

VAL

ARG

VAL

CYS

Samples:

sample_1: LP2006 5 ± 1 mM

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
1H	sample_1	anisotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	anisotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	anisotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	anisotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	anisotropic	sample_conditions_1

Software:

MestReNova v8.1.1, Mestrelab Research - chemical shift assignment

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

SPARKY, Goddard - peak picking

TOPSPIN v1.3, Bruker Biospin - collection

XPLOR-NIH v2.36, Charles Schwieters, Marius Clore (NIH) - structure calculation

NMR spectrometers:

Bruker AVANCE 900 MHz