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
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Title: Solution structure of Kunitz-type neurotoxin LmKKT-1a from scorpion venom PubMed: 23573241
Deposition date: 2012-10-15 Original release date: 2013-11-11
Authors: Luo, Fan; Jiang, Ling; Liu, Maili; Chen, Zongyun; Wu, Yingliang
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).
Assembly members:
LmKKT-1a, polymer, 59 residues, 6510.300 Da.
Natural source: Common Name: Chinese striped bark scorpion; Vietnamese brown scorpion Taxonomy ID: 172552 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Lychas mucronatus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
LmKKT-1a: KKKCQLPSDVGKGKASFTRY
YYNEESGKCETFIYGGVGGN
SNNFLTKEDCCRECAQGSC
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 157 |
| 15N chemical shifts | 58 |
| 1H chemical shifts | 334 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | LmKKT-1a | 1 |
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 | LYS | LYS | LYS | CYS | GLN | LEU | PRO | SER | ASP | VAL | ||||
| 2 | GLY | LYS | GLY | LYS | ALA | SER | PHE | THR | ARG | TYR | ||||
| 3 | TYR | TYR | ASN | GLU | GLU | SER | GLY | LYS | CYS | GLU | ||||
| 4 | THR | PHE | ILE | TYR | GLY | GLY | VAL | GLY | GLY | ASN | ||||
| 5 | SER | ASN | ASN | PHE | LEU | THR | LYS | GLU | ASP | CYS | ||||
| 6 | CYS | ARG | GLU | CYS | ALA | GLN | GLY | SER | CYS |
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:
| 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-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_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 simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts