BMRB Entry 34043

Name: Salt-inducible protein splicing by inteins from extremely halophilic archaea and application to scarless segmental labeling of TonB protein
Published: 2016-10-14

Click here to enlarge.

PDB ID: 5lw8
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34043
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Salt-inducible protein splicing by inteins from extremely halophilic archaea and application to scarless segmental labeling of TonB protein

Deposition date:

2016-09-15

Original release date:

2016-10-14

Authors:

Iwai, H.; Ciragan, A.; Tascon, I.; Aranko, S.

Citation:

Citation: Ciragan, Annika; Aranko, A Sesilja; Tascon, Igor; Iwai, Hideo. "Salt-inducible Protein Splicing in cis and trans by Inteins from Extremely Halophilic Archaea as a Novel Protein-Engineering Tool" J. Mol. Biol. 428, 4573-4588 (2016).
PubMed: 27720988

Assembly members:

Assembly members:
Protein TonB, polymer, 92 residues, 10151.667 Da.

Natural source:

Natural source: Common Name: e-proteobacteria Taxonomy ID: 85962 Superkingdom: Bacteria Kingdom: not available Genus/species: Helicobacter Helicobacter pylori

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Protein TonB: SNEFLMKIQTAISSKNRYPK MAQIRGIEGEVLVSFTINAD GSVTDIKVVKSNTTDILNHA ALEAIKSAAHLFPKPEETVH LKIPIAYSLKED

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	384
15N chemical shifts	92
1H chemical shifts	656

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 92 residues - 10151.667 Da.

1

SER

ASN

GLU

PHE

LEU

MET

LYS

ILE

GLN

THR

2

ALA

ILE

SER

LYS

ASN

ARG

TYR

PRO

LYS

3

MET

ALA

GLN

ILE

ARG

GLY

ILE

GLU

GLY

GLU

4

VAL

LEU

VAL

SER

PHE

THR

ILE

ASN

ALA

ASP

5

GLY

SER

VAL

THR

ASP

ILE

LYS

VAL

LYS

6

SER

ASN

THR

ASP

ILE

LEU

ASN

HIS

ALA

7

ALA

LEU

GLU

ALA

ILE

LYS

SER

ALA

HIS

8

LEU

PHE

PRO

LYS

PRO

GLU

THR

VAL

HIS

9

LEU

LYS

ILE

PRO

ILE

ALA

TYR

SER

LEU

LYS

10

GLU

ASP

Samples:

sample_1: TonB CTD, [U-100% 13C; U-100% 15N], 0.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 20 mM; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCA	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

CcpNMR, CCPN - chemical shift assignment

PSVS, Bhattacharya and Montelione - data analysis

NMR spectrometers:

Bruker AvanceIII 850 MHz

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