BMRB Entry 15797

Name: Solution structure of Tpx in the reduced state
Published: 2008-07-29

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PDB ID: 2jsz
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15797
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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:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Tpx monomer: MAEITFKGGPVTLVGQEVKV GDQAPDFTVLTNSLEEKSLA DMKGKVTIISVIPSIDTGVC DAQTRRFNEEAAKLGDVNVY TISADLPFAQARWCGANGID KVETLSDHRDMSFGEAFGVY IKELRLLARSVFVLDENGKV VYAEYVSEATNHPNYEKPIE AAKALVK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	654
15N chemical shifts	157
1H chemical shifts	1072

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Tpx monomer	1

Entities:

Entity 1, Tpx monomer 167 residues - 18241.838 Da.

1

MET

ALA

GLU

ILE

THR

PHE

LYS

GLY

PRO

2

VAL

THR

LEU

VAL

GLY

GLN

GLU

VAL

LYS

VAL

3

GLY

ASP

GLN

ALA

PRO

ASP

PHE

THR

VAL

LEU

4

THR

ASN

SER

LEU

GLU

LYS

SER

LEU

ALA

5

ASP

MET

LYS

GLY

LYS

VAL

THR

ILE

SER

6

VAL

ILE

PRO

SER

ILE

ASP

THR

GLY

VAL

CYS

7

ASP

ALA

GLN

THR

ARG

PHE

ASN

GLU

8

ALA

LYS

LEU

GLY

ASP

VAL

ASN

VAL

TYR

9

THR

ILE

SER

ALA

ASP

LEU

PRO

PHE

ALA

GLN

10

ALA

ARG

TRP

CYS

GLY

ALA

ASN

GLY

ILE

ASP

11

LYS

VAL

GLU

THR

LEU

SER

ASP

HIS

ARG

ASP

12

MET

SER

PHE

GLY

GLU

ALA

PHE

GLY

VAL

TYR

13

ILE

LYS

GLU

LEU

ARG

LEU

ALA

ARG

SER

14

VAL

PHE

VAL

LEU

ASP

GLU

ASN

GLY

LYS

VAL

15

VAL

TYR

ALA

GLU

TYR

VAL

SER

GLU

ALA

THR

16

ASN

HIS

PRO

ASN

TYR

GLU

LYS

PRO

ILE

GLU

17

ALA

LYS

ALA

LEU

VAL

LYS

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:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_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

BMRB	15798
PDB	2JSY 2JSZ
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