BMRB Entry 30682

Name: Structure of acrorhagin I from the sea anemone Actinia equina
Published: 2020-11-13

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PDB ID: 6ux5
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30682
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:

Structure of acrorhagin I from the sea anemone Actinia equina

Deposition date:

2019-11-06

Original release date:

2020-11-13

Authors:

Krishnarjuna, B.; Sunanda, P.; Norton, R.

Citation:

Citation: Krishnarjuna, Bankala; Sunanda, Punnepalli; Villegas-Moreno, Jessica; Csoti, Agota; A V Morales, Rodrigo; Wai, Dorothy; Panyi, Gyorgy; Prentis, Peter; Norton, Raymond. "A disulfide-stabilised helical hairpin fold in acrorhagin I: An emerging structural motif in peptide toxins" J. Struct. Biol. 213, 107692-107692 (2021).
PubMed: 33387653

Assembly members:

Assembly members:
entity_1, polymer, 50 residues, 5672.312 Da.

Natural source:

Natural source: Common Name: Beadlet anemone Taxonomy ID: 6106 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Actinia equina

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SSTPDGTWVKCRHDCFTKYK SCQMSDSCHDEQSCHQCHVK HTDCVNTGCP

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	188
15N chemical shifts	52
1H chemical shifts	296

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 50 residues - 5672.312 Da.

1	SER	SER	THR	PRO	ASP	GLY	THR	TRP	VAL	LYS
2	CYS	ARG	HIS	ASP	CYS	PHE	THR	LYS	TYR	LYS
3	SER	CYS	GLN	MET	SER	ASP	SER	CYS	HIS	ASP
4	GLU	GLN	SER	CYS	HIS	GLN	CYS	HIS	VAL	LYS
5	HIS	THR	ASP	CYS	VAL	ASN	THR	GLY	CYS	PRO

Name	Sample	Sample state	Sample conditions
2D DQF-COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1

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

BMRB Entry 30682

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

1	SER	SER	THR	PRO	ASP	GLY	THR	TRP	VAL	LYS
2	CYS	ARG	HIS	ASP	CYS	PHE	THR	LYS	TYR	LYS
3	SER	CYS	GLN	MET	SER	ASP	SER	CYS	HIS	ASP
4	GLU	GLN	SER	CYS	HIS	GLN	CYS	HIS	VAL	LYS
5	HIS	THR	ASP	CYS	VAL	ASN	THR	GLY	CYS	PRO

1	SER	SER	THR	PRO	ASP	GLY	THR	TRP	VAL	LYS
2	CYS	ARG	HIS	ASP	CYS	PHE	THR	LYS	TYR	LYS
3	SER	CYS	GLN	MET	SER	ASP	SER	CYS	HIS	ASP
4	GLU	GLN	SER	CYS	HIS	GLN	CYS	HIS	VAL	LYS
5	HIS	THR	ASP	CYS	VAL	ASN	THR	GLY	CYS	PRO

1	SER	SER	THR	PRO	ASP	GLY	THR	TRP	VAL	LYS
2	CYS	ARG	HIS	ASP	CYS	PHE	THR	LYS	TYR	LYS
3	SER	CYS	GLN	MET	SER	ASP	SER	CYS	HIS	ASP
4	GLU	GLN	SER	CYS	HIS	GLN	CYS	HIS	VAL	LYS
5	HIS	THR	ASP	CYS	VAL	ASN	THR	GLY	CYS	PRO