BMRB Entry 30538

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30538
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

Title:
Solution structure of alpha-KTx-6.21 (UroTx) from Urodacus yaschenkoi
Deposition date:
2018-11-05
Original release date:
2020-03-05
Authors:
Chin, Y.; Luna-Ramirez, K.; Anangi, R.; King, G.
Citation:

Citation: Luna-Ramirez, Karen; Csoti, Agota; McArthur, Jeffrey; Chin, Yanni; Anangi, Raveendra; Najera, Rosby Del Carmen; Possani, Lourival; King, Glenn; Panyi, Gyorgy; Yu, Haibo; Adams, David; Finol-Urdaneta, Rocio. "Structural basis of the potency and selectivity of Urotoxin, a potent Kv1 blocker from scorpion venom"  Biochem. Pharmacol. 174, 113782-113782 (2020).
PubMed: 31881193

Assembly members:

Assembly members:
entity_1, polymer, 37 residues, 4028.794 Da.

Natural source:

Natural source:   Common Name: Inland robust scorpion   Taxonomy ID: 1273102   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Urodacus yaschenkoi

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GDIKCSGTRQCWGPCKKQTT CTNSKCMNGKCKCYGCV

Data typeCount
13C chemical shifts140
15N chemical shifts40
1H chemical shifts217

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 37 residues - 4028.794 Da.

1   GLYASPILELYSCYSSERGLYTHRARGGLN
2   CYSTRPGLYPROCYSLYSLYSGLNTHRTHR
3   CYSTHRASNSERLYSCYSMETASNGLYLYS
4   CYSLYSCYSTYRGLYCYSVAL

Samples:

sample_1: UroTx, [U-13C; U-15N], 200 uM; sodium acetate 20 mM; D2O 5%

sample_conditions_1: pH: 5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, refinement, structure calculation

Analysis, CCPN - chemical shift assignment, data analysis, peak picking

TOPSPIN, Bruker Biospin - collection

TALOS-N, Cornilescu, Delaglio and Bax - geometry optimization

Rowland NMR Toolkit, http://www.rowland.org/rnmrtk/toolkit.html - processing

NMR spectrometers:

  • Bruker AvanceIII 900 MHz

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