BMRB Entry 16589
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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/BMR16589
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Title: peptide_ptha PubMed: 20848643
Deposition date: 2009-10-28 Original release date: 2011-05-19
Authors: Neves, Jorge Luiz; Sforca, Mauricio Luis; Murakami, Mario Tyago; Zeri, Ana Carolina de Mattos; Benedetti, Celso Eduardo
Citation: Murakami, Mario Tyago; Sforca, Mauricio Luis; Neves, Jorge Luiz; Paiva, Joice Helena; Domingues, Mariane Noronha; Pereira, Andre Luiz Araujo; Zeri, Ana Carolina de Mattos; Benedetti, Celso Eduardo. "The repeat domain of the type III effector protein PthA shows a TPR-like structure and undergoes conformational changes upon DNA interaction." Proteins 78, 3386-3395 (2010).
Assembly members:
pthA, polymer, 51 residues, Formula weight is not available
Natural source: Common Name: Xanthomonas axonopodis pv citri Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Xanthomonas citri
Experimental source: Production method: obtained from a vendor Host organism: Xanthomonas axonopodis pv citri
Entity Sequences (FASTA):
pthA: EQVVAIASNIGGKQALETVQ
RLLPVLCQAHGLTPEQVVAI
ASHDGGKQALE
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 295 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PthA | 1 |
Entities:
Entity 1, PthA 51 residues - Formula weight is not available
| 1 | GLU | GLN | VAL | VAL | ALA | ILE | ALA | SER | ASN | ILE | ||||
| 2 | GLY | GLY | LYS | GLN | ALA | LEU | GLU | THR | VAL | GLN | ||||
| 3 | ARG | LEU | LEU | PRO | VAL | LEU | CYS | GLN | ALA | HIS | ||||
| 4 | GLY | LEU | THR | PRO | GLU | GLN | VAL | VAL | ALA | ILE | ||||
| 5 | ALA | SER | HIS | ASP | GLY | GLY | LYS | GLN | ALA | LEU | ||||
| 6 | GLU |
Samples:
sample_1: entity 1.0 mM; sodium phosphate 20 mM; SDS 70 mM; DTT 1 mM; H2O 95%; D2O 5%
sample_conditions_1: pH: 5; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Varian INOVA 600 MHz