BMRB Entry 50569

Name: 1H and 15N assignments for 14-residue peptide after cleavage by MPro
Published: 2021-04-12

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50569

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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:

1H and 15N assignments for 14-residue peptide after cleavage by MPro

Deposition date:

2020-11-11

Original release date:

2021-04-12

Authors:

Bafna, Khushboo; Ramelot, Theresa; Montelione, Gaetano

Citation:

Citation: Bafna, Khushboo; White, Kris; Harish, Balasubramanian; Rosales, Romel; Ramelot, Theresa; Acton, Thomas; Moreno, Elena; Kehrer, Thomas; Miorin, Lisa; Royer, Catherine; Garcia-Sastre, Adolfo; Krug, Robert; Montelione, Gaetano. "Hepatitis C virus drugs that inhibit SARS-CoV-2 papain-like protease synergize with remdesivir to suppress viral replication in cell culture" Cell Reports 35, 109133-109133 (2021).
PubMed: 33984267

Assembly members:

Assembly members:
entity_1, polymer, 14 residues, Formula weight is not available

Natural source:

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: KTSAVLQSGFRKME

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	11
1H chemical shifts	12

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	14-residue peptide	1

Entities:

Entity 1, 14-residue peptide 14 residues - Formula weight is not available

1

LYS

THR

SER

ALA

VAL

LEU

GLN

SER

GLY

PHE

2

ARG

LYS

MET

GLU

Samples:

sample_1: peptide-uncleaved 1 ± 0.1 mM; HEPES 20 ± 2 mM; sodium chloride 100 ± 5 mM

sample_2: peptide-uncleaved 0.2 ± 0.02 mM; HEPES 20 ± 2 mM; sodium chloride 100 ± 5 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
1D 1H	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-1H COSY	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN v3.6.2 - collection, data analysis, integration, peak picking, processing

NMRFAM-SPARKY v1.470 - chemical shift assignment, data analysis, peak picking

NMRPipe v9.9 - processing

NMR spectrometers:

Bruker Avance II 600 MHz

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