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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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

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

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:

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).
PubMed: 18247350

Assembly members:

Assembly members:
Peptidyl-tRNA hydrolase domain protein, polymer, 108 residues, 12100.852 Da.

Natural source:

Natural source: Common Name: Pseudomonas Syringae pv.tomato Taxonomy ID: 317 Superkingdom: Bacteria Kingdom: not available Genus/species: Pseudomonas syringae

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pEt21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Peptidyl-tRNA hydrolase domain protein: MLVISNNVHLPDAEIELTAI RAQGAGGQNVNKVSSAMHLR FDINASSLPPFYKERLLALN DSRITSDGVIVLKAQQYRTQ EQNRADALLRLSELIVNAAK LEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	446
15N chemical shifts	116
1H chemical shifts	762

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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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

VAL

HIS

LEU

2

PRO

ASP

ALA

GLU

ILE

GLU

LEU

THR

ALA

ILE

3

ARG

ALA

GLN

GLY

ALA

GLY

GLN

ASN

VAL

4

ASN

LYS

VAL

SER

ALA

MET

HIS

LEU

ARG

5

PHE

ASP

ILE

ASN

ALA

SER

LEU

PRO

6

PHE

TYR

LYS

GLU

ARG

LEU

ALA

LEU

ASN

7

ASP

SER

ARG

ILE

THR

SER

ASP

GLY

VAL

ILE

8

VAL

LEU

LYS

ALA

GLN

TYR

ARG

THR

GLN

9

GLU

GLN

ASN

ARG

ALA

ASP

ALA

LEU

ARG

10

LEU

SER

GLU

LEU

ILE

VAL

ASN

ALA

LYS

11

LEU

GLU

HIS

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

PDB	2JVA
GB	EPN16620 KPW06216

BMRB Entry 15471

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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