BMRB Entry 25853

Name: Chemical Shift Assignments and Structure Determination for spider toxin, U33-theraphotoxin-Cg1c
Published: 2016-08-25

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PDB ID: 2n8k
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25853
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:

Chemical Shift Assignments and Structure Determination for spider toxin, U33-theraphotoxin-Cg1c

Deposition date:

2015-10-20

Original release date:

2016-08-25

Authors:

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

Citation:

Citation: Pineda, Sandy; Chin, Yanni K-Y; Undheim, Eivind; Senff, Sebastian; Mobli, Mehdi; Dauly, Claire; Escoubas, Pierre; Nicholson, Graham; Kaas, Quentin; Guo, Shaodong; Herzig, Volker; Mattick, John; King, Glenn. "Structural venomics reveals evolution of a complex venom by duplication and diversification of an ancient peptide-encoding gene" Proc. Natl. Acad. Sci. U. S. A. 117, 11399-11408 (2020).
PubMed: 32398368

Assembly members:

Assembly members:
entity, polymer, 76 residues, 8143.186 Da.

Natural source:

Natural source: Common Name: Chilobrachys guangxiensis Taxonomy ID: 278060 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Chilobrachys guangxiensis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pLICC vector

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: SVTCGGKQCKPNSCCVQNSH GKGKDSPRCHPLGKLNNPCE VEPNENGIYSQHCPCGEGLS CTKVGEPNKLRCQEES

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	290
15N chemical shifts	79
1H chemical shifts	476

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 76 residues - 8143.186 Da.

1

SER

VAL

THR

CYS

GLY

LYS

GLN

CYS

LYS

2

PRO

ASN

SER

CYS

VAL

GLN

ASN

SER

HIS

3

GLY

LYS

GLY

LYS

ASP

SER

PRO

ARG

CYS

HIS

4

PRO

LEU

GLY

LYS

LEU

ASN

PRO

CYS

GLU

5

VAL

GLU

PRO

ASN

GLU

ASN

GLY

ILE

TYR

SER

6

GLN

HIS

CYS

PRO

CYS

GLY

GLU

GLY

LEU

SER

7

CYS

THR

LYS

VAL

GLY

GLU

PRO

ASN

LYS

LEU

8

ARG

CYS

GLN

GLU

SER

Samples:

Cg1c: Cg1c, [U-99% 13C; U-99% 15N], 300 uM; D2O 5%; DSS 10 uM; H2O 95%; sodium azide 5%; MES 20 mM

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

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	Cg1c	isotropic	sample_conditions_1
3D CBCA(CO)NH	Cg1c	isotropic	sample_conditions_1
3D HNCACB	Cg1c	isotropic	sample_conditions_1
3D HNCO	Cg1c	isotropic	sample_conditions_1
3D 1H-15N NOESY	Cg1c	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	Cg1c	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	Cg1c	isotropic	sample_conditions_1
3D HBHA(CO)NH	Cg1c	isotropic	sample_conditions_1
4D HCC(CO)NH-TOCSY	Cg1c	isotropic	sample_conditions_1

Software:

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

TALOS, Cornilescu, Delaglio and Bax - Dihedral angle prediction

TOPSPIN v3.2, Bruker Biospin - collection

SPARKY, Goddard - chemical shift assignment

Rowland_NMR_Toolkit, Hoch JC - processing NUS data

NMR spectrometers:

Bruker Avance II+ 900 MHz

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