BMRB Entry 19168

Title:
Solution structure of the a C-terminal domain of translation initiation factor IF-3 from Campylobacter jejuni
Deposition date:
2013-04-16
Original release date:
2013-05-13
Authors:
Harris, R.; Ahmed, M.; Attonito, J.; Bonanno, J.; Chamala, S.; Chowdhury, S.; Evans, B.; Fiser, A.; Glenn, A.; Hammonds, J.; Hillerich, B.; Khafizov, K.; Lafleur, J.; Love, J.; Seidel, R.; Stead, M.; Girvin, M.; Almo, S.
Citation:

Citation: Harris, R.; Ahmed, M.; Attonito, J.; Bonanno, J.; Chamala, S.; Chowdhury, S.; Evans, B.; Fiser, A.; Glenn, A.; Hammonds, J.; Hillerich, B.; Khafizov, K.; Lafleur, J.; Love, J.; Seidel, R.; Stead, M.; Girvin, M.; Almo, S.. "Solution structure of the a C-terminal domain of translation initiation factor IF-3 from Campylobacter jejuni"  To be published ., .-..

Assembly members:

Assembly members:
IF-3, polymer, 101 residues, 11502.454 Da.

Natural source:

Natural source:   Common Name: e-proteobacteria   Taxonomy ID: 197   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Campylobacter jejuni

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: modified pET26

Data sets:
Data typeCount
13C chemical shifts433
15N chemical shifts95
1H chemical shifts703

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1IF-31

Entities:

Entity 1, IF-3 101 residues - 11502.454 Da.

expressed sequence start-stop 83-172 N-term cloning artifact: MSL C-term cloning artifact: EGHHHHHH

1   METSERLEULYSVALILEASPILELYSGLU
2   ILELYSLEUSERVALLYSILEALAGLNASN
3   ASPILEASNTYRLYSVALLYSHISALALEU
4   GLUPHELEUGLUGLNGLYLYSHISVALARG
5   PHEARGVALPHELEULYSGLYARGGLUMET
6   ALATHRPROGLUALAGLYVALALALEULEU
7   GLULYSILETRPTHRMETILEGLUASNGLU
8   ALAASNARGASPLYSGLUPROASNPHEGLU
9   GLYARGTYRVALASNMETLEUVALTHRPRO
10   LYSLYSALAGLUGLYHISHISHISHISHIS
11   HIS

Samples:

sample_1: IF-3, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O 10%; Na phosphate buffer 20 mM; NaCl 50 mM; EDTA 0.1 mM

sample_2: IF-3, [U-100% 13C; U-100% 15N], 1 mM; D2O 100%; Na phosphate buffer 20 mM; NaCl 50 mM; EDTA 0.1 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.8; pressure: 1 ATM; temperature: 298 K

sample_conditions_2: ionic strength: 50 mM; pH: 6.8; pressure: 1 ATM; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
15N HSQCsample_1isotropicsample_conditions_1
15N NOESY-HSQCsample_1isotropicsample_conditions_1
13C HSQCsample_2isotropicsample_conditions_2
aromatic 13C HSQCsample_2isotropicsample_conditions_2
13C NOESY-HSQCsample_2isotropicsample_conditions_2
13C aromatic NOESY-HSQCsample_2isotropicsample_conditions_2
HNCOsample_1isotropicsample_conditions_1
HNCACOsample_1isotropicsample_conditions_1
HNCAsample_1isotropicsample_conditions_1
HNCOCAsample_1isotropicsample_conditions_1
HNCACBsample_1isotropicsample_conditions_1
CBCACONHsample_1isotropicsample_conditions_1

Software:

CNS v1.21, Brunger A. T. et.al. - structure calcuation

X-PLOR NIH v2.32, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

ARIA v2.3, Linge, O'Donoghue and Nilges - structure solution

CCPN_Analysis v2.2, CCPN - chemical shift assignment, data analysis, peak picking

MDDNMR v2.2, (MDDNMR) Orekhov, Jaravine, Kazimierczuk - collection, processing

MDDGUI v1.0, (MDDGUI) Lemak, Gutmanas, Chitayat, Karra, Fares, Sunnerhagen, Arrowsmith - collection, processing

NMRPipe v7.5, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMRJ v2.2D, Varian - collection

TOPSPIN v2.1, Bruker Biospin - collection

MolProbity v4.01a, Richardson - data analysis

NMR spectrometers:

  • Varian Inova 600 MHz
  • Bruker Avance 700 MHz

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