BMRB Entry 30378

Name: Structure of a new ShKT peptide from the sea anemone Oulactis sp.
Published: 2018-05-24

Click here to enlarge.

PDB ID: 6buc
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30378
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Structure of a new ShKT peptide from the sea anemone Oulactis sp.

Deposition date:

2017-12-10

Original release date:

2018-05-24

Authors:

Krishnarjuna, B.; Norton, R.

Citation:

Citation: Krishnarjuna, Bankala; Villegas-Moreno, Jessica; Mitchell, Michela; Csoti, Agota; Peigneur, Steve; Amero, Carlos; Pennington, Michael; Tytgat, Jan; Panyi, Gyorgy; Norton, Raymond. "Synthesis, folding, structure and activity of a predicted peptide from the sea anemone Oulactis sp. with an ShKT fold" Toxicon 150, 50-59 (2018).
PubMed: 29772211

Assembly members:

Assembly members:
entity_1, polymer, 36 residues, 3790.266 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: ACKDNLPAATCSNVKANNNC SSEKYKTNCAKTCGEC

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	39
1H chemical shifts	218

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 36 residues - 3790.266 Da.

1

ALA

CYS

LYS

ASP

ASN

LEU

PRO

ALA

THR

2

CYS

SER

ASN

VAL

LYS

ALA

ASN

CYS

3

SER

GLU

LYS

TYR

LYS

THR

ASN

CYS

ALA

4

LYS

THR

CYS

GLY

GLU

CYS

Samples:

sample_1: peptide 1 mM

sample_conditions_1: pH: 3.8; pressure: 1 atm; temperature: 293 K

Experiments:

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-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

Analysis, CCPN - chemical shift assignment, peak picking

TOPSPIN, Bruker Biospin - processing

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