BMRB Entry 34008

Name: NMR structure of the sea anemone peptide tau-AnmTx Ueq 12-1 with an uncommon fold
Published: 2017-05-04

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PDB ID: 5lah
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34008
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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 structure of the sea anemone peptide tau-AnmTx Ueq 12-1 with an uncommon fold

Deposition date:

2016-06-14

Original release date:

2017-05-04

Authors:

Mineev, K.; Arseniev, A.; Andreev, A.; Kozlov, S.; Logashina, Yu.

Citation:

Citation: Logashina, Yulia; Solstad, Runar Gjerp; Mineev, Konstantin; Korolkova, Yuliya; Mosharova, Irina; Dyachenko, Igor; Palikov, Victor; Palikova, Yulia; Murashev, Arkadii; Arseniev, Alexander; Kozlov, Sergey; Stensvag, Klara; Haug, Tor; Andreev, Yaroslav. "New Disulfide-Stabilized Fold Provides Sea Anemone Peptide to Exhibit Both Antimicrobial and TRPA1 Potentiating Properties" Toxins (Basel) 9, 154-154 (2017).
PubMed: 28468269

Assembly members:

Assembly members:
tau-AnmTx Ueq 12-1, polymer, 45 residues, 4808.258 Da.

Natural source:

Natural source: Common Name: sea anemones Taxonomy ID: 417072 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Urticina eques

Experimental source:

Experimental source: Production method: purified from the natural source

Entity Sequences (FASTA):

Entity Sequences (FASTA):
tau-AnmTx Ueq 12-1: CYPGQPGCGHCSRPNYCEGA RCESGFHDCGSDHWCDASGD RCCCA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	99
15N chemical shifts	45
1H chemical shifts	233

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 45 residues - 4808.258 Da.

1

CYS

TYR

PRO

GLY

GLN

PRO

GLY

CYS

GLY

HIS

2

CYS

SER

ARG

PRO

ASN

TYR

CYS

GLU

GLY

ALA

3

ARG

CYS

GLU

SER

GLY

PHE

HIS

ASP

CYS

GLY

4

SER

ASP

HIS

TRP

CYS

ASP

ALA

SER

GLY

ASP

5

ARG

CYS

ALA

Samples:

sample_1: sodium azide 1 mM; tau-AnmTx Ueq 12-1 0.5 ± 0.1 mM; H2O 95%; D2O 5%

sample_2: sodium azide 1 mM; tau-AnmTx Ueq 12-1 0.5 ± 0.1 mM; D2O 100%

sample_conditions_1: ionic strength: 10 mM; pH: 3.2; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_1
2D DQF-COSY	sample_2	isotropic	sample_conditions_1

Software:

CARA v1.9.4, Keller and Wuthrich - chemical shift assignment

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure calculation

TOPSPIN, Bruker Biospin - processing

NMR spectrometers:

Bruker Avance 700 MHz

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