BMRB Entry 15471
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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/BMR15471
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Title: NMR Structure of Peptidyl-tRNA hydrolase domain protein from Pseudomonas syringae pv. tomato:Northeast Structural Genomics Consortium Target PsR211 PubMed: 18247350
Deposition date: 2007-09-14 Original release date: 2007-10-12
Authors: SINGARAPU, KIRAN KUMAR; SUKUMARAN, DINESH; PARISH, DAVID; ELETSKY, ALEX; ZHANG, QI; ZHAO, LI; JIANG, MEI; MAGLAQUI, MELISSA; XIAO, RONG; LIU, JINFENG; BARAN, MICHAEL; SWAPNA, G.V.T; HUANG, YUANPENG; ACTON, THOMAS; ROST, BURKHARD; MONTELIONE, GAETANO; SZYPERSKI, THOMAS
Citation: SINGARAPU, KIRAN KUMAR; XIAO, RONG; ACTON, THOMAS; ROST, BURKHARD; MONTELIONE, GAETANO; SZYPERSKI, THOMAS. "NMR structure of the peptidyl-tRNA hydrolase domain from Pseudomonas syringae expands the structural coverage of the hydrolysis domains of class 1 peptide chain release factors" Proteins 71, 1027-1031 (2008).
Assembly members:
Peptidyl-tRNA hydrolase domain protein, polymer, 108 residues, 12100.852 Da.
Natural source: Common Name: Pseudomonas Syringae pv.tomato Taxonomy ID: 317 Superkingdom: Bacteria Kingdom: not available Genus/species: Pseudomonas syringae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Peptidyl-tRNA hydrolase domain protein: MLVISNNVHLPDAEIELTAI
RAQGAGGQNVNKVSSAMHLR
FDINASSLPPFYKERLLALN
DSRITSDGVIVLKAQQYRTQ
EQNRADALLRLSELIVNAAK
LEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 446 |
| 15N chemical shifts | 116 |
| 1H chemical shifts | 762 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Peptidyl-tRNA hydrolase domain protein | 1 |
Entities:
Entity 1, Peptidyl-tRNA hydrolase domain protein 108 residues - 12100.852 Da.
| 1 | MET | LEU | VAL | ILE | SER | ASN | ASN | VAL | HIS | LEU | ||||
| 2 | PRO | ASP | ALA | GLU | ILE | GLU | LEU | THR | ALA | ILE | ||||
| 3 | ARG | ALA | GLN | GLY | ALA | GLY | GLY | GLN | ASN | VAL | ||||
| 4 | ASN | LYS | VAL | SER | SER | ALA | MET | HIS | LEU | ARG | ||||
| 5 | PHE | ASP | ILE | ASN | ALA | SER | SER | LEU | PRO | PRO | ||||
| 6 | PHE | TYR | LYS | GLU | ARG | LEU | LEU | ALA | LEU | ASN | ||||
| 7 | ASP | SER | ARG | ILE | THR | SER | ASP | GLY | VAL | ILE | ||||
| 8 | VAL | LEU | LYS | ALA | GLN | GLN | TYR | ARG | THR | GLN | ||||
| 9 | GLU | GLN | ASN | ARG | ALA | ASP | ALA | LEU | LEU | ARG | ||||
| 10 | LEU | SER | GLU | LEU | ILE | VAL | ASN | ALA | ALA | LYS | ||||
| 11 | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: Peptidyl-tRNA hydrolase domain protein, [U-100% 13C; U-100% 15N], 1.28 mM; CaCl2 5 mM; NaCl 100 mM; NH4OAc 20 mM; DTT 10 mM; NaN3 0.02%; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 100 mM; pH: 5.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 4,3D GFT CABCACONHN | sample_1 | isotropic | sample_conditions_1 |
| 4,3D GFT HNNCABCA | sample_1 | isotropic | sample_conditions_1 |
| 4,3D GFT HCCH COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH COSY | sample_1 | isotropic | sample_conditions_1 |
| 4,3D GFT HABCABCONHN | sample_1 | isotropic | sample_conditions_1 |
| 3D sim NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
VNMRJ, Varian - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
XEASY, Bartels et al. - data analysis
TALOS, Cornilescu, Delaglio and Bax - data analysis
DYANA, Guntert, Mumenthaler and Wuthrich - data analysis
CYANA, Guntert, Mumenthaler and Wuthrich - chemical shift assignment
AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
AutoStruct, Huang, Tejero, Powers and Montelione - chemical shift assignment
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
Molmol, Koradi, Billeter and Wuthrich - data analysis
NMR spectrometers:
- Varian INOVA 750 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts