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BMRB: 15471

2JVA

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

Authors

SINGARAPU, K., SUKUMARAN, D., PARISH, D., ELETSKY, A., ZHANG, Q., ZHAO, L., JIANG, M., MAGLAQUI, M., XIAO, R., LIU, J., BARAN, M.C., SWAPNA, G., HUANG, Y.J., ACTON, T.B., ROST, B., MONTELIONE, G.T., SZYPERSKI, T.

Assembly

Peptidyl-tRNA hydrolase domain protein

Entity

1. Peptidyl-tRNA hydrolase domain protein (polymer, Thiol state: all free), 108 monomers, 12078.56 Da Detail

MLVISNNVHL PDAEIELTAI RAQGAGGQNV NKVSSAMHLR FDINASSLPP FYKERLLALN DSRITSDGVI VLKAQQYRTQ EQNRADALLR LSELIVNAAK LEHHHHHH

Formula weight

12078.56 Da

Source organism

Pseudomonas syringae

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 97.2 %, Completeness: 94.1 %, Completeness (bb): 95.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	94.1 % (1173 of 1247)	94.9 % (613 of 646)	92.9 % (448 of 482)	94.1 % (112 of 119)
Backbone	95.5 % (613 of 642)	95.4 % (207 of 217)	95.6 % (306 of 320)	95.2 % (100 of 105)
Sidechain	93.1 % (660 of 709)	94.6 % (406 of 429)	91.0 % (242 of 266)	85.7 % (12 of 14)
Aromatic	52.9 % (36 of 68)	64.7 % (22 of 34)	41.2 % (14 of 34)
Methyl	100.0 % (142 of 142)	100.0 % (71 of 71)	100.0 % (71 of 71)

1. Peptidyl-tRNA hydrolase domain protein

MLVISNNVHL PDAEIELTAI RAQGAGGQNV NKVSSAMHLR FDINASSLPP FYKERLLALN DSRITSDGVI VLKAQQYRTQ EQNRADALLR LSELIVNAAK LEHHHHHH

Show sample condition

Sample

Pressure 1 atm, Temperature 298 K, pH 5.5

#	Name	Isotope labeling	Concentration
1	Peptidyl-tRNA hydrolase domain protein	[U-100% 13C; U-100% 15N]	1.28 mM
2	CaCl2	natural abundance	5 mM
3	NaCl	natural abundance	100 mM
4	NH4OAc	natural abundance	20 mM
5	DTT	natural abundance	10 mM
6	NaN3	natural abundance	0.02 %
7	H2O	natural abundance	95 %
8	D2O		5 %

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: -0.87 ppm, Outliers: 3 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: -0.87 ppm, Outliers: 3 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: -0.02 ppm, Outliers: 2 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.3 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2JVA, Strand ID: A Detail

Release date

2007-10-11

Citation

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
SINGARAPU, K., XIAO, R., ACTON, T.B., ROST, B., MONTELIONE, G., SZYPERSKI, T.
Proteins (2008), 71, 1027-1031, PubMed 18247350 , DOI 10.1002/prot.21947 , Abstract

Related entities 1. Peptidyl-tRNA hydrolase domain protein, : 1 : 82 entities Detail

Experiments performed 8 experiments Detail

1 2D 1H-15N HSQC