BMRB Entry 30420

Name: Structure of a new ShKT peptide from the sea anemone Oulactis sp: OspTx2a-p2
Published: 2019-03-01

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PDB ID: 6ckf
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30420
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 a new ShKT peptide from the sea anemone Oulactis sp: OspTx2a-p2

Deposition date:

2018-02-28

Original release date:

2019-03-01

Authors:

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

Citation:

Citation: Sunanda, Punnepalli; Krishnarjuna, Bankala; Peigneur, Steve; Mitchell, Michela; Estrada, Rosendo; Villegas-Moreno, Jessica; Pennington, Michael; Tytgat, Jan; Norton, Raymond. "Identification, chemical synthesis, structure, and function of a new KV1 channel blocking peptide from Oulactis sp." Pept. Sci. 110, e24073-e24073 (2018).

Assembly members:

Assembly members:
entity_1, polymer, 36 residues, 3801.426 Da.

Natural source:

Natural source: Common Name: Oulactis Taxonomy ID: 308031 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Oulactis not available

Experimental source:

Experimental source: Production method: na

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: ACKDVFPAATCRHAKSVGNC SSEKYKRNCAITCGAC

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
15N chemical shifts	38
1H chemical shifts	224

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 36 residues - 3801.426 Da.

1

ALA

CYS

LYS

ASP

VAL

PHE

PRO

ALA

THR

2

CYS

ARG

HIS

ALA

LYS

SER

VAL

GLY

ASN

CYS

3

SER

GLU

LYS

TYR

LYS

ARG

ASN

CYS

ALA

4

ILE

THR

CYS

GLY

ALA

CYS

Samples:

sample_1: OspTx2a-p2 1 mM

sample_conditions_1: pH: 5; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
1D 1H	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D DQF-COSY	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:

TOPSPIN, Bruker Biospin - collection, processing

CcpNMR, CCPN - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMR spectrometers:

Bruker Avance 600 MHz

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