BMRB Entry 15471
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PDB ID: 2jva
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:
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