BMRB Entry 34043

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):

Data sets:
Data typeCount
13C chemical shifts384
15N chemical shifts92
1H chemical shifts656

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 92 residues - 10151.667 Da.

1   SERASNGLUPHELEUMETLYSILEGLNTHR
2   ALAILESERSERLYSASNARGTYRPROLYS
3   METALAGLNILEARGGLYILEGLUGLYGLU
4   VALLEUVALSERPHETHRILEASNALAASP
5   GLYSERVALTHRASPILELYSVALVALLYS
6   SERASNTHRTHRASPILELEUASNHISALA
7   ALALEUGLUALAILELYSSERALAALAHIS
8   LEUPHEPROLYSPROGLUGLUTHRVALHIS
9   LEULYSILEPROILEALATYRSERLEULYS
10   GLUASP

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:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_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