BMRB Entry 30325
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30325
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Title: NMR solution structure of KanY protein (ms6282) using two 4D-spectra PubMed: 29374165
Deposition date: 2017-08-03 Original release date: 2018-01-29
Authors: Evangelidis, T.; Nerli, S.; Sgourakis, N.; Tripsianes, K.
Citation: Evangelidis, T.; Nerli, S.; Novacek, J.; Brereton, A.; Karplus, P.; Dotas, R.; Venditti, V.; Sgourakis, N.; Tripsianes, K.. "Automated NMR resonance assignments and structure determination using a minimal set of 4D spectra" Nat. Commun. 9, 384-384 (2018).
Assembly members:
Uncharacterized protein, polymer, 145 residues, 15285.261 Da.
Natural source: Common Name: Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155) Taxonomy ID: 246196 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycobacterium smegmatis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Uncharacterized protein: MGQVSAVSTVLINAEPAAVL
AAISDYQTVRPKILSSHYSG
YQVLEGGQGAGTVATWKLQA
TKSRVRDVKATVDVAGHTVI
EKDANSSLVSNWTVAPAGTG
SSVNLKTTWTGAGGVKGFFE
KTFAPLGLRRIQDEVLENLK
KHVEG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 445 |
| 15N chemical shifts | 152 |
| 1H chemical shifts | 959 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 145 residues - 15285.261 Da.
| 1 | MET | GLY | GLN | VAL | SER | ALA | VAL | SER | THR | VAL | ||||
| 2 | LEU | ILE | ASN | ALA | GLU | PRO | ALA | ALA | VAL | LEU | ||||
| 3 | ALA | ALA | ILE | SER | ASP | TYR | GLN | THR | VAL | ARG | ||||
| 4 | PRO | LYS | ILE | LEU | SER | SER | HIS | TYR | SER | GLY | ||||
| 5 | TYR | GLN | VAL | LEU | GLU | GLY | GLY | GLN | GLY | ALA | ||||
| 6 | GLY | THR | VAL | ALA | THR | TRP | LYS | LEU | GLN | ALA | ||||
| 7 | THR | LYS | SER | ARG | VAL | ARG | ASP | VAL | LYS | ALA | ||||
| 8 | THR | VAL | ASP | VAL | ALA | GLY | HIS | THR | VAL | ILE | ||||
| 9 | GLU | LYS | ASP | ALA | ASN | SER | SER | LEU | VAL | SER | ||||
| 10 | ASN | TRP | THR | VAL | ALA | PRO | ALA | GLY | THR | GLY | ||||
| 11 | SER | SER | VAL | ASN | LEU | LYS | THR | THR | TRP | THR | ||||
| 12 | GLY | ALA | GLY | GLY | VAL | LYS | GLY | PHE | PHE | GLU | ||||
| 13 | LYS | THR | PHE | ALA | PRO | LEU | GLY | LEU | ARG | ARG | ||||
| 14 | ILE | GLN | ASP | GLU | VAL | LEU | GLU | ASN | LEU | LYS | ||||
| 15 | LYS | HIS | VAL | GLU | GLY |
Samples:
sample_1: KanY protein ms6282, [U-13C; U-15N], 1.2 mM; sodium phosphate 50 mM; NaCl 150 mM
sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 4D HC(CC TOCSY(CO))NH | sample_1 | isotropic | sample_conditions_1 |
| 4D 13C,15N edited HMQC-NOESY-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 4D 13C,13C edited HMQC-NOESY-HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
CS-Rosetta, Shen, Vernon, Baker and Bax - data analysis, refinement, structure calculation
SPARKY, Goddard - peak picking
4D-CHAINS, Evangelidis and Tripsianes - chemical shift assignment
NMR spectrometers:
- Bruker AvanceIII 850 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts