BMRB Entry 52753

Name: NMR chemical shifts of [15N,13C] DynorphinA, 17 amino acid peptide, in Phosphate buffer pH 6.5
Published: 2024-12-19

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52753

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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 chemical shifts of [15N,13C] DynorphinA, 17 amino acid peptide, in Phosphate buffer pH 6.5

Deposition date:

2024-12-14

Original release date:

2024-12-19

Authors:

Ramelot, Theresa; Gaur, Amit; Wu, Kejia; Baker, David; Montelione, Gaetano

Citation:

Citation: Wu, Kejia. "Sequence-specific targeting of intrinsically disordered protein regions" BioRxiv ., .-. (2024).

Assembly members:

Assembly members:
entity_1, polymer, 17 residues, 2147.5 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3) Vector: pET15_SUMO_NESG

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: YGGFLRRIRPKLKWDNQ

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	71
15N chemical shifts	17
1H chemical shifts	118

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Dynorphin peptide	1

Entities:

Entity 1, Dynorphin peptide 17 residues - 2147.5 Da.

1

TYR

GLY

PHE

LEU

ARG

ILE

ARG

PRO

2

LYS

LEU

LYS

TRP

ASP

ASN

GLN

Samples:

sample_1: peptide, [U-13C; U-15N], 4 ± 1 mM; sodium phosphate 20 ± 2 mM; sodium chloride 150 ± 5 mM; sodium azide 0.02 ± .005 %

sample_conditions_1: ionic strength: 150 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HMQC	sample_1	isotropic	sample_conditions_1
2D HNCACB	sample_1	isotropic	sample_conditions_1
2D HN(CO)CA	sample_1	isotropic	sample_conditions_1
2D HNCO	sample_1	isotropic	sample_conditions_1
2D HNCA	sample_1	isotropic	sample_conditions_1
2D C(CO)NH	sample_1	isotropic	sample_conditions_1
2D TOCSY-NHSQC	sample_1	isotropic	sample_conditions_1
2D CCH-TOCSY aliph	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC ct	sample_1	isotropic	sample_conditions_1
2D H(CCO)NH	sample_1	isotropic	sample_conditions_1
2D HN(CO)CACB	sample_1	isotropic	sample_conditions_1

Software:

NMRFAM-SPARKY v1.37 - visualize data, peak picking, export bmrb file

NMRPipe vv10.9 - processing

TOPSPIN v4.0 - collection

NMR spectrometers:

Bruker AVANCE III 800 MHz
Bruker AVANCE III 600 MHz