BMRB Entry 15797

Title:
Solution structure of Tpx in the reduced state
Deposition date:
2008-06-07
Original release date:
2008-07-29
Authors:
Jin, Changwen; Lu, Jie; Yang, Fan
Citation:

Citation: Lu, Jie; Yang, Fan; Li, You; Xia, Bin; Jin, Changwen. "Reversible conformational switch revealed by the redox structures of Bacillus subtilis thiol peroxidase"  Biomol. NMR Assignments 2, 183-186 (2008).
PubMed: 19636900

Assembly members:

Assembly members:
Tpx monomer, polymer, 167 residues, 18241.838 Da.

Natural source:

Natural source:   Common Name: Bacillus subtilis   Taxonomy ID: 1423   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus subtilis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21a

Data sets:
Data typeCount
13C chemical shifts654
15N chemical shifts157
1H chemical shifts1072

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Tpx monomer1

Entities:

Entity 1, Tpx monomer 167 residues - 18241.838 Da.

1   METALAGLUILETHRPHELYSGLYGLYPRO
2   VALTHRLEUVALGLYGLNGLUVALLYSVAL
3   GLYASPGLNALAPROASPPHETHRVALLEU
4   THRASNSERLEUGLUGLULYSSERLEUALA
5   ASPMETLYSGLYLYSVALTHRILEILESER
6   VALILEPROSERILEASPTHRGLYVALCYS
7   ASPALAGLNTHRARGARGPHEASNGLUGLU
8   ALAALALYSLEUGLYASPVALASNVALTYR
9   THRILESERALAASPLEUPROPHEALAGLN
10   ALAARGTRPCYSGLYALAASNGLYILEASP
11   LYSVALGLUTHRLEUSERASPHISARGASP
12   METSERPHEGLYGLUALAPHEGLYVALTYR
13   ILELYSGLULEUARGLEULEUALAARGSER
14   VALPHEVALLEUASPGLUASNGLYLYSVAL
15   VALTYRALAGLUTYRVALSERGLUALATHR
16   ASNHISPROASNTYRGLULYSPROILEGLU
17   ALAALALYSALALEUVALLYS

Samples:

sample_1: Tpx 1 mM; sodium phosphate 20 mM; DTT 20 mM

sample_conditions_1: ionic strength: 20 mM; pH: 7.0; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Koll - refinement

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 500 MHz

Related Database Links:

BMRB 15798
PDB
DBJ BAI86453 BAM54200 BAM59029 GAK82014
EMBL CAB14927 CCU59457 CEI58181 CEJ78603 CJR44398
GB AAC00316 ADM38894 ADV93745 AEP87796 AEP91943
REF NP_390827 WP_003223506 WP_010335298 WP_015714515 WP_019259177
SP P80864
AlphaFold P80864

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks