BMRB Entry 34423
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34423
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Title: NMR structure of MLP124017 PubMed: 31792250
Deposition date: 2019-08-05 Original release date: 2019-12-13
Authors: Barthe, P.; de Guillen, K.; Padilla, A.; Hecker, A.
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, 157 residues, 18200.594 Da.
Natural source: Common Name: Poplar leaf rust fungus Taxonomy ID: 203908 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Melampsora larici-populina
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: MELPESFEFILTEDMVTDLD
VKGLGYDFIDLVTKSPDSVN
SEHELAHFLGPHDPEIYVNG
KIQTTTAFLQFFRQGLFKKL
KDAEFAINVSGKVKEGEGYK
LVWKSAAQRSHDQKIRWDEA
EAYIWRRKDGSCWLHSVKFI
MSKAAPYVAIDHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 344 |
| 15N chemical shifts | 127 |
| 1H chemical shifts | 852 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 157 residues - 18200.594 Da.
| 1 | MET | GLU | LEU | PRO | GLU | SER | PHE | GLU | PHE | ILE | ||||
| 2 | LEU | THR | GLU | ASP | MET | VAL | THR | ASP | LEU | ASP | ||||
| 3 | VAL | LYS | GLY | LEU | GLY | TYR | ASP | PHE | ILE | ASP | ||||
| 4 | LEU | VAL | THR | LYS | SER | PRO | ASP | SER | VAL | ASN | ||||
| 5 | SER | GLU | HIS | GLU | LEU | ALA | HIS | PHE | LEU | GLY | ||||
| 6 | PRO | HIS | ASP | PRO | GLU | ILE | TYR | VAL | ASN | GLY | ||||
| 7 | LYS | ILE | GLN | THR | THR | THR | ALA | PHE | LEU | GLN | ||||
| 8 | PHE | PHE | ARG | GLN | GLY | LEU | PHE | LYS | LYS | LEU | ||||
| 9 | LYS | ASP | ALA | GLU | PHE | ALA | ILE | ASN | VAL | SER | ||||
| 10 | GLY | LYS | VAL | LYS | GLU | GLY | GLU | GLY | TYR | LYS | ||||
| 11 | LEU | VAL | TRP | LYS | SER | ALA | ALA | GLN | ARG | SER | ||||
| 12 | HIS | ASP | GLN | LYS | ILE | ARG | TRP | ASP | GLU | ALA | ||||
| 13 | GLU | ALA | TYR | ILE | TRP | ARG | ARG | LYS | ASP | GLY | ||||
| 14 | SER | CYS | TRP | LEU | HIS | SER | VAL | LYS | PHE | ILE | ||||
| 15 | MET | SER | LYS | ALA | ALA | PRO | TYR | VAL | ALA | ILE | ||||
| 16 | ASP | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: MLP124017, [U-15N], 1 mM
sample_2: MLP124017, [U-13C; U-15N], 0.6 mM
sample_conditions_1: ionic strength: 200 mM; pH: 6.8; 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_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
CINDY, Padilla - chemical shift assignment
Gifa, Delsuc - peak picking
NMR spectrometers:
- Bruker AVANCE III 800 MHz
- Bruker AVANCE III 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts