BMRB Entry 18789

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18789
MolProbity Validation Chart

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Title:
Solution structure of Kunitz-type neurotoxin LmKKT-1a from scorpion venom
Deposition date:
2012-10-15
Original release date:
2013-11-11
Authors:
Luo, Fan; Jiang, Ling; Liu, Maili; Chen, Zongyun; Wu, Yingliang
Citation:

Citation: Chen, Zongyun; Luo, Fan; Feng, Jing; Yang, Weishan; Zeng, Danyun; Zhao, Ruiming; Cao, Zhijian; Liu, Maili; Li, Wenxin; Jiang, Ling; Wu, Yingliang. "Genomic and structural characterization of Kunitz-type peptide LmKTT-1a highlights diversity and evolution of scorpion potassium channel toxins"  Plos One 8, e60201-e60201 (2013).
PubMed: 23573241

Assembly members:

Assembly members:
LmKKT-1a, polymer, 59 residues, 6510.300 Da.

Natural source:

Natural source:   Common Name: Chinese striped bark scorpion; Vietnamese brown scorpion   Taxonomy ID: 172552   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Lychas mucronatus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
LmKKT-1a: KKKCQLPSDVGKGKASFTRY YYNEESGKCETFIYGGVGGN SNNFLTKEDCCRECAQGSC

Data sets:
Data typeCount
13C chemical shifts157
15N chemical shifts58
1H chemical shifts334

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1LmKKT-1a1

Entities:

Entity 1, LmKKT-1a 59 residues - 6510.300 Da.

The recombinant protein contain 79 residues ,but residues 1-20 represent a tag, so we renumber the last 59 residues from 1.

1   LYSLYSLYSCYSGLNLEUPROSERASPVAL
2   GLYLYSGLYLYSALASERPHETHRARGTYR
3   TYRTYRASNGLUGLUSERGLYLYSCYSGLU
4   THRPHEILETYRGLYGLYVALGLYGLYASN
5   SERASNASNPHELEUTHRLYSGLUASPCYS
6   CYSARGGLUCYSALAGLNGLYSERCYS

Samples:

sample_1: potassium phosphate 20 mM; LmKKT-1a, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 20 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CARA, Keller and Wuthrich - chemical shift assignment

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

CSI, David Wishart, Brian Sykes, Leigh Willard, Tim Jellard - chemical shift calculation

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

TALOS, Cornilescu, Delaglio and Bax - data analysis

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

Molmol, Koradi, Billeter and Wuthrich - data analysis

ProcheckNMR, Laskowski and MacArthur - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz

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