BMRB Entry 52543

Name: Structure and functional studies of Avt1, a novel peptide from the sea anemone Aulactinia veratra
Published: 2024-10-07

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52543

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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:

Structure and functional studies of Avt1, a novel peptide from the sea anemone Aulactinia veratra

Deposition date:

2024-07-10

Original release date:

2024-10-07

Authors:

Albar, Renad; Sanches, Karoline; Wai, Dorothy; Norton, Raymond

Citation:

Citation: Albar, Renad; Smith, Hayden; Sanches, Karoline; Wai, Dorothy; Naseem, Muhammad Umair; Szanto, Tibor; Panyi, Gyorgy; Prentis, Peter; Norton, Raymond. "Structure and functional studies of Avt1, a novel peptide from the sea anemone Aulactinia veratra" Biochim. Biophys. Acta Proteins Proteom. 1873, 141050-141050 (2024).
PubMed: 39357665

Assembly members:

Assembly members:
entity_1, polymer, 28 residues, Formula weight is not available

Natural source:

Natural source: Common Name: sea anemones Taxonomy ID: 1730095 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Aulactinia veratra

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SCARGCGGDSDCPCPGWHCP SPGGRCEP

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	64
15N chemical shifts	25
1H chemical shifts	140

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	U-AITx-Avt1	1

Entities:

Entity 1, U-AITx-Avt1 28 residues - Formula weight is not available

1

SER

CYS

ALA

ARG

GLY

CYS

GLY

ASP

SER

2

ASP

CYS

PRO

CYS

PRO

GLY

TRP

HIS

CYS

PRO

3

SER

PRO

GLY

ARG

CYS

GLU

PRO

Samples:

sample_1: U-AITx-Avt1 1.5 mM

sample_conditions_1: ionic strength: 0 M; pH: 5; pressure: 1 atm; temperature: 293 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
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1

Software:

ARIA2 vVersion 2.3 - structure solution

TOPSPIN v3.2 - collection

CcpNMR v2.4.2 - chemical shift assignment

NMRPipe - processing

NMR spectrometers:

Bruker AVANCE III 600 MHz MHz

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