BMRB Entry 30322
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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/BMR30322
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
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Title: NMR solution structure of a-lytic protease 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:
Alpha-lytic protease, polymer, 198 residues, 19875.131 Da.
Natural source: Common Name: Lysobacter enzymogenes Taxonomy ID: 69 Superkingdom: Bacteria Kingdom: not available Genus/species: Lysobacter enzymogenes
Experimental source: Production method: .
Entity Sequences (FASTA):
Alpha-lytic protease: ANIVGGIEYSINNASLCSVG
FSVTRGATKGFVTAGHCGTV
NATARIGGAVVGTFAARVFP
GNDRAWVSLTSAQTLLPRVA
NGSSFVTVRGSTEAAVGAAV
CRSGRTTGYQCGTITAKNVT
ANYAEGAVRGLTQGNACMGR
GDSGGSWITSAGQAQGVMSG
GNVQSNGNNCGIPASQRSSL
FERLQPILSQYGLSLVTG
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 540 |
| 15N chemical shifts | 222 |
| 1H chemical shifts | 1201 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 198 residues - 19875.131 Da.
| 1 | ALA | ASN | ILE | VAL | GLY | GLY | ILE | GLU | TYR | SER | ||||
| 2 | ILE | ASN | ASN | ALA | SER | LEU | CYS | SER | VAL | GLY | ||||
| 3 | PHE | SER | VAL | THR | ARG | GLY | ALA | THR | LYS | GLY | ||||
| 4 | PHE | VAL | THR | ALA | GLY | HIS | CYS | GLY | THR | VAL | ||||
| 5 | ASN | ALA | THR | ALA | ARG | ILE | GLY | GLY | ALA | VAL | ||||
| 6 | VAL | GLY | THR | PHE | ALA | ALA | ARG | VAL | PHE | PRO | ||||
| 7 | GLY | ASN | ASP | ARG | ALA | TRP | VAL | SER | LEU | THR | ||||
| 8 | SER | ALA | GLN | THR | LEU | LEU | PRO | ARG | VAL | ALA | ||||
| 9 | ASN | GLY | SER | SER | PHE | VAL | THR | VAL | ARG | GLY | ||||
| 10 | SER | THR | GLU | ALA | ALA | VAL | GLY | ALA | ALA | VAL | ||||
| 11 | CYS | ARG | SER | GLY | ARG | THR | THR | GLY | TYR | GLN | ||||
| 12 | CYS | GLY | THR | ILE | THR | ALA | LYS | ASN | VAL | THR | ||||
| 13 | ALA | ASN | TYR | ALA | GLU | GLY | ALA | VAL | ARG | GLY | ||||
| 14 | LEU | THR | GLN | GLY | ASN | ALA | CYS | MET | GLY | ARG | ||||
| 15 | GLY | ASP | SER | GLY | GLY | SER | TRP | ILE | THR | SER | ||||
| 16 | ALA | GLY | GLN | ALA | GLN | GLY | VAL | MET | SER | GLY | ||||
| 17 | GLY | ASN | VAL | GLN | SER | ASN | GLY | ASN | ASN | CYS | ||||
| 18 | GLY | ILE | PRO | ALA | SER | GLN | ARG | SER | SER | LEU | ||||
| 19 | PHE | GLU | ARG | LEU | GLN | PRO | ILE | LEU | SER | GLN | ||||
| 20 | TYR | GLY | LEU | SER | LEU | VAL | THR | GLY |
Samples:
sample_1: alpha-lytic protease protein, [U-13C; U-15N], 2.0 mM; sodium acetate 10 mM; NaCl 50 mM
sample_conditions_1: ionic strength: 50 mM; pH: 4.0; 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:
4D-CHAINS, Evangelidis and Tripsianes - chemical shift assignment
CS-Rosetta, Shen, Vernon, Baker and Bax - data analysis, refinement, structure calculation
SPARKY, Goddard - peak picking
NMR spectrometers:
- Bruker AvanceIII 950 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts