BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15471

Title: NMR Structure of Peptidyl-tRNA hydrolase domain protein from Pseudomonas syringae pv. tomato:Northeast Structural Genomics Consortium Target PsR211   PubMed: 18247350

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

Data sets:
Data typeCount
13C chemical shifts446
15N chemical shifts116
1H chemical shifts762

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Peptidyl-tRNA hydrolase domain protein1

Entities:

Entity 1, Peptidyl-tRNA hydrolase domain protein 108 residues - 12100.852 Da.

1   METLEUVALILESERASNASNVALHISLEU
2   PROASPALAGLUILEGLULEUTHRALAILE
3   ARGALAGLNGLYALAGLYGLYGLNASNVAL
4   ASNLYSVALSERSERALAMETHISLEUARG
5   PHEASPILEASNALASERSERLEUPROPRO
6   PHETYRLYSGLUARGLEULEUALALEUASN
7   ASPSERARGILETHRSERASPGLYVALILE
8   VALLEULYSALAGLNGLNTYRARGTHRGLN
9   GLUGLNASNARGALAASPALALEULEUARG
10   LEUSERGLULEUILEVALASNALAALALYS
11   LEUGLUHISHISHISHISHISHIS

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
4,3D GFT CABCACONHNsample_1isotropicsample_conditions_1
4,3D GFT HNNCABCAsample_1isotropicsample_conditions_1
4,3D GFT HCCH COSYsample_1isotropicsample_conditions_1
3D HCCH COSYsample_1isotropicsample_conditions_1
4,3D GFT HABCABCONHNsample_1isotropicsample_conditions_1
3D sim NOESYsample_1isotropicsample_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

Related Database Links:

PDB
GB EPN16620 KPW06216