BMRB Entry 30087
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30087
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Title: NMR solution structure of a thermophilic lysine methyl transferase from Sulfolobus islandicus
Deposition date: 2016-05-12 Original release date: 2017-05-19
Authors: de Lichtenberg, C.; Stiefler-Jensen, D.; Schwarz-Linnet, T.; She, Q.; Teilum, K.
Citation: de Lichtenberg, C.; Stiefler-Jensen, D.; Schwarz-Linnet, T.; She, Q.; Teilum, K.. "NMR solution structure of a thermophilic lysine methyl transferase from Sulfolobus islandicus" . ., .-..
Assembly members:
Protein-lysine N-methyltransferase, polymer, 172 residues, 19420.371 Da.
Natural source: Common Name: crenarchaeotes Taxonomy ID: 930945 Superkingdom: Archaea Kingdom: not available Genus/species: sulfolobus sulfolobus islandicus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)
Entity Sequences (FASTA):
Protein-lysine N-methyltransferase: MSYVPHVPYVPTPEKVVRRM
LEIAKVSQDDIVYALGCGDG
RIIITAAKDFNVKKAVGVEI
NDERIREALANIEKNGVTGR
ASIVKGNFFEVDISEATVVT
MFLLTNVNEMLKPKLEKELK
PGTRVVSHEFEIRGWNPKEV
IKVEDGNMNHTVYLYVIGEH
KAAALEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 631 |
| 15N chemical shifts | 154 |
| 1H chemical shifts | 1001 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 172 residues - 19420.371 Da.
| 1 | MET | SER | TYR | VAL | PRO | HIS | VAL | PRO | TYR | VAL | ||||
| 2 | PRO | THR | PRO | GLU | LYS | VAL | VAL | ARG | ARG | MET | ||||
| 3 | LEU | GLU | ILE | ALA | LYS | VAL | SER | GLN | ASP | ASP | ||||
| 4 | ILE | VAL | TYR | ALA | LEU | GLY | CYS | GLY | ASP | GLY | ||||
| 5 | ARG | ILE | ILE | ILE | THR | ALA | ALA | LYS | ASP | PHE | ||||
| 6 | ASN | VAL | LYS | LYS | ALA | VAL | GLY | VAL | GLU | ILE | ||||
| 7 | ASN | ASP | GLU | ARG | ILE | ARG | GLU | ALA | LEU | ALA | ||||
| 8 | ASN | ILE | GLU | LYS | ASN | GLY | VAL | THR | GLY | ARG | ||||
| 9 | ALA | SER | ILE | VAL | LYS | GLY | ASN | PHE | PHE | GLU | ||||
| 10 | VAL | ASP | ILE | SER | GLU | ALA | THR | VAL | VAL | THR | ||||
| 11 | MET | PHE | LEU | LEU | THR | ASN | VAL | ASN | GLU | MET | ||||
| 12 | LEU | LYS | PRO | LYS | LEU | GLU | LYS | GLU | LEU | LYS | ||||
| 13 | PRO | GLY | THR | ARG | VAL | VAL | SER | HIS | GLU | PHE | ||||
| 14 | GLU | ILE | ARG | GLY | TRP | ASN | PRO | LYS | GLU | VAL | ||||
| 15 | ILE | LYS | VAL | GLU | ASP | GLY | ASN | MET | ASN | HIS | ||||
| 16 | THR | VAL | TYR | LEU | TYR | VAL | ILE | GLY | GLU | HIS | ||||
| 17 | LYS | ALA | ALA | ALA | LEU | GLU | HIS | HIS | HIS | HIS | ||||
| 18 | HIS | HIS |
Samples:
sample_1: DSS 0.5 mM; Na-acetate 20 mM; aKMT_D34A, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O 10%
sample_2: DSS 0.5 mM; Na-acetate 20 mM; aKMT_D34A, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O 10%
sample_3: C12E5 0.123 M; DSS 0.5 mM; Na-acetate 20 mM; aKMT_D34A, [U-100% 13C; U-100% 15N], 1 mM; hexanol 0.111 M; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.02 M; pH: 5; pressure: 1 atm; temperature: 313 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | 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 HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D IPAP HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY aromatic | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 2D IPAP HSQC | sample_3 | anisotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_2 | isotropic | sample_conditions_1 |
Software:
Analysis, CCPN - chemical shift assignment
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement
NMR spectrometers:
- Agilent DD2 800 MHz
- Bruker AvanceIII 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts