BMRB Entry 18019

Name: High-resolution solution structure of the orally active insecticidal spider venom peptide U1-TRTX-Sp1a
Published: 2012-10-22

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PDB ID: 2ll1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18019
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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:

High-resolution solution structure of the orally active insecticidal spider venom peptide U1-TRTX-Sp1a

Deposition date:

2011-10-24

Original release date:

2012-10-22

Authors:

Hardy, Margaret; Daly, Norelle; Mobli, Mehdi

Citation:

Citation: Hardy, Margaret; Daly, Norelle; Mobli, Mehdi; King, Glenn. "High-resolution solution structure of the orally active insecticidal spider venom peptide U1-TRTX-Sp1a" .

Assembly members:

Assembly members:
U1-TRTX-Sp1a, polymer, 33 residues, 3732.358 Da.

Natural source:

Natural source: Common Name: Australian Featherleg Taxonomy ID: not available Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Selenotypus plumipes

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
U1-TRTX-Sp1a: DCGHLHDPCPNDRPGHRTCC IGLQCRYGKCLVR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	56
15N chemical shifts	26
1H chemical shifts	208

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	U1-TRTX-Sp1a	1

Entities:

Entity 1, U1-TRTX-Sp1a 33 residues - 3732.358 Da.

1

ASP

CYS

GLY

HIS

LEU

HIS

ASP

PRO

CYS

PRO

2

ASN

ASP

ARG

PRO

GLY

HIS

ARG

THR

CYS

3

ILE

GLY

LEU

GLN

CYS

ARG

TYR

GLY

LYS

CYS

4

LEU

VAL

ARG

Samples:

sample_1: U1-TRTX-Sp1a 700 uM; potassium phosphate 10 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 5.85; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	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

Software:

TOPSPIN, Bruker Biospin - collection

CcpNMR, CCPN - chemical shift assignment, data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

Bruker Avance 900 MHz

PDB	2LL1
SP	K7N5K9
AlphaFold	K7N5K9