BMRB Entry 25848

Name: Chemical shift assignments and structure calculation of spider toxin pi-hexatoxin-Hi1a
Published: 2016-10-13

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PDB ID: 2n8f
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25848
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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: Chemical shift assignments and structure calculation of spider toxin pi-hexatoxin-Hi1a

Deposition date: 2015-10-13 Original release date: 2016-10-13

Authors: Chin, Yanni; Pineda, Sandy; Mobli, Mehdi; King, Glenn

Citation: Pineda, Sandy; Chin, Yanni; Senff, Sebastian; Mobli, Mehdi; Escoubas, Pierre; Nicholson, Graham; Kass, Quentin; Fry, Bryan; Mattick, John; King, Glenn. "Single-gene recruitment underlies venom complexity in the Australian Funnel-web spider Hadronyche infensa" Nature Commun. ., .-..

Assembly members:
hi1a, polymer, 76 residues, 8750.226 Da.

Natural source: Common Name: spiders Taxonomy ID: 153481 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Hadronyche infensa

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):
hi1a: SNECIRKWLSCVDRKNDCCE GLECYKRRHSFEVCVPIPGF CLVKWKQCDGRERDCCAGLE CWKRSGNKSSVCAPIT

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	299
15N chemical shifts	75
1H chemical shifts	502

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hi1a	1

Entities:

Entity 1, hi1a 76 residues - 8750.226 Da.

1

SER

ASN

GLU

CYS

ILE

ARG

LYS

TRP

LEU

SER

2

CYS

VAL

ASP

ARG

LYS

ASN

ASP

CYS

GLU

3

GLY

LEU

GLU

CYS

TYR

LYS

ARG

HIS

SER

4

PHE

GLU

VAL

CYS

VAL

PRO

ILE

PRO

GLY

PHE

5

CYS

LEU

VAL

LYS

TRP

LYS

GLN

CYS

ASP

GLY

6

ARG

GLU

ARG

ASP

CYS

ALA

GLY

LEU

GLU

7

CYS

TRP

LYS

ARG

SER

GLY

ASN

LYS

SER

8

VAL

CYS

ALA

PRO

ILE

THR

Samples:

sample_1: hi1a, [U-99% 13C; U-99% 15N], 300 uM; D2O 5%; DSS 10 uM; sodium azide 0.02%; MES 20 mM; H2O 95%

sample_conditions_1: pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D HNCO	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 HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.2, Bruker Biospin - collection

TALOS, Cornilescu, Delaglio and Bax - Dihedral angle prediction

SPARKY, Goddard - chemical shift assignment, peak picking

XEASY, Bartels et al. - chemical shift assignment, peak picking

Rowland_NMR_Toolkit, Hoch JC - processing, processing NUS data

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

NMR spectrometers:

Bruker Avance II+ 900 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts