BMRB Entry 17525
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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/BMR17525
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Title: ATR13 Chemical Shifts PubMed: 22194684
Deposition date: 2011-03-15 Original release date: 2012-01-18
Authors: Leonelli, Lauriebeth; Pelton, Jeffrey; Wemmer, David; Staskawicz, Brian
Citation: Leonelli, Lauriebeth; Pelton, Jeffery; Schoeffler, Allyn; Dahlbeck, Douglas; Berger, James; Wemmer, David; Staskawicz, Brian. "Structural Elucidation and Functional Characterization of the Hyaloperonospora arabidopsidis Effector Protein ATR13" Plos Pathog. 7, e1002428-e1002428 (2011).
Assembly members:
ATR13, polymer, 202 residues, 22593.979 Da.
Natural source: Common Name: Hyaloperonospora parasitica Taxonomy ID: 123356 Superkingdom: Eukaryota Kingdom: not available Genus/species: Hyaloperonospora parasitica
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
ATR13: SFGLGKAQDPLDKFFSKIIF
SGKPIETSYSAKGIHEKIIE
AHDLHVSKSKNAPIQYASVM
EYLKKTYPGPDIERIVSTLE
RHDEVGAKDLGAKLRDALDR
QSFGLGKAQDPLDKFFSKII
FSGKPIETSYSAKGIHEKII
EAHDLHVSKSKNAPIQYASV
MEYLKKTYPGPDIERIVSTL
ERHDEVGAKDLGAKLRDALD
RQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 320 |
| 15N chemical shifts | 77 |
| 1H chemical shifts | 479 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ATR13 | 1 |
Entities:
Entity 1, ATR13 202 residues - 22593.979 Da.
| 1 | SER | PHE | GLY | LEU | GLY | LYS | ALA | GLN | ASP | PRO | ||||
| 2 | LEU | ASP | LYS | PHE | PHE | SER | LYS | ILE | ILE | PHE | ||||
| 3 | SER | GLY | LYS | PRO | ILE | GLU | THR | SER | TYR | SER | ||||
| 4 | ALA | LYS | GLY | ILE | HIS | GLU | LYS | ILE | ILE | GLU | ||||
| 5 | ALA | HIS | ASP | LEU | HIS | VAL | SER | LYS | SER | LYS | ||||
| 6 | ASN | ALA | PRO | ILE | GLN | TYR | ALA | SER | VAL | MET | ||||
| 7 | GLU | TYR | LEU | LYS | LYS | THR | TYR | PRO | GLY | PRO | ||||
| 8 | ASP | ILE | GLU | ARG | ILE | VAL | SER | THR | LEU | GLU | ||||
| 9 | ARG | HIS | ASP | GLU | VAL | GLY | ALA | LYS | ASP | LEU | ||||
| 10 | GLY | ALA | LYS | LEU | ARG | ASP | ALA | LEU | ASP | ARG | ||||
| 11 | GLN | SER | PHE | GLY | LEU | GLY | LYS | ALA | GLN | ASP | ||||
| 12 | PRO | LEU | ASP | LYS | PHE | PHE | SER | LYS | ILE | ILE | ||||
| 13 | PHE | SER | GLY | LYS | PRO | ILE | GLU | THR | SER | TYR | ||||
| 14 | SER | ALA | LYS | GLY | ILE | HIS | GLU | LYS | ILE | ILE | ||||
| 15 | GLU | ALA | HIS | ASP | LEU | HIS | VAL | SER | LYS | SER | ||||
| 16 | LYS | ASN | ALA | PRO | ILE | GLN | TYR | ALA | SER | VAL | ||||
| 17 | MET | GLU | TYR | LEU | LYS | LYS | THR | TYR | PRO | GLY | ||||
| 18 | PRO | ASP | ILE | GLU | ARG | ILE | VAL | SER | THR | LEU | ||||
| 19 | GLU | ARG | HIS | ASP | GLU | VAL | GLY | ALA | LYS | ASP | ||||
| 20 | LEU | GLY | ALA | LYS | LEU | ARG | ASP | ALA | LEU | ASP | ||||
| 21 | ARG | GLN |
Samples:
sample_1: ATR13, [U-100% 13C; U-100% 15N], 1 ± 0.1 mM; potassium phosphate 20 ± 1 mM; sodium chloride 150 ± 5 mM; D2O, [U-99% 2H], 10 ± 0.5 %; H2O 90%
sample_2: ATR13, [U-98% 15N], 1 ± 0.1 mM; potassium phosphate 20 ± 1 mM; sodium chloride 150 ± 5 mM; D2O, [U-99% 2H], 10 ± 1 %; H2O 90%
sample_3: ATR13, [U-10% 13C; U-99% 15N], 1 ± 0.1 mM; potassium phosphate 20 ± 1 mM; sodium chloride 150 ± 5 mM; D2O, [U-99% 2H], 10 ± 1 %; H2O 90%
sample_4: ATR13, [U-98% 15N], 1 ± 0.1 mM; potassium phosphate 20 ± 1 mM; sodium chloride 150 ± 5 mM; D2O, [U-99% 2H], 10 ± 1 %; Pf1 phage 12 ± 1 mg/ml; H2O 90%
sample_conditions_1: ionic strength: 210 mM; pH: 7.1; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_1 |
| 2D IPAP | sample_4 | anisotropic | sample_conditions_1 |
| 2D 15N Heteronuclear NOE | sample_2 | isotropic | sample_conditions_1 |
Software:
NMRPipe v3.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CARA v1.8.4.2, Keller and Wuthrich - chemical shift assignment
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 800 MHz
- Bruker Avance II 900 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts