BMRB Entry 34298
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34298
MolProbity Validation Chart
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NMR-STAR v3 text file.
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Title: Solution structure of Melampsora larici-populina MlpP4.1 PubMed: 31792250
Deposition date: 2018-07-09 Original release date: 2018-08-16
Authors: Tsan, P.
Citation: de Guillen, K.; Lorrain, C.; Tsan, P.; Barthe, P.; Petre, B.; Saveleva, N.; Rouhier, N.; Duplessis, S.; Padilla, A.; Hecker, A.. "Structural genomics applied to the rust fungus Melampsora larici-populina reveals two candidate effector proteins adopting cystine knot and NTF2-like protein folds." Sci. Rep. 9, 18084-18084 (2019).
Assembly members:
entity_1, polymer, 75 residues, 7978.616 Da.
Natural source: Common Name: Melampsora larici-populina Taxonomy ID: 747676 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Melampsora larici-populina
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: MCEFIEDSEDIQGLKSLRKS
HTSLEDDDDGSRGGDCEGCS
GTACSSDAQCRARGCDGCST
SGVCVLSSLHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 115 |
| 15N chemical shifts | 67 |
| 1H chemical shifts | 318 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 75 residues - 7978.616 Da.
| 1 | MET | CYS | GLU | PHE | ILE | GLU | ASP | SER | GLU | ASP | ||||
| 2 | ILE | GLN | GLY | LEU | LYS | SER | LEU | ARG | LYS | SER | ||||
| 3 | HIS | THR | SER | LEU | GLU | ASP | ASP | ASP | ASP | GLY | ||||
| 4 | SER | ARG | GLY | GLY | ASP | CYS | GLU | GLY | CYS | SER | ||||
| 5 | GLY | THR | ALA | CYS | SER | SER | ASP | ALA | GLN | CYS | ||||
| 6 | ARG | ALA | ARG | GLY | CYS | ASP | GLY | CYS | SER | THR | ||||
| 7 | SER | GLY | VAL | CYS | VAL | LEU | SER | SER | LEU | HIS | ||||
| 8 | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: entity_1, [U-15N], 1.8 mM; potassium phosphate 50 mM; sodium azide 0.02%
sample_conditions_1: ionic strength: 50 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHB | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRView, Johnson, One Moon Scientific - data analysis
ARIA, Linge, O'Donoghue and Nilges - structure calculation
TOPSPIN, Bruker Biospin - processing
NMR spectrometers:
- Bruker AvanceIII 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts