BMRB Entry 34088

Title:
Solid-state NMR Structure of outer membrane protein G in lipid bilayers
Deposition date:
2017-01-20
Original release date:
2018-01-19
Authors:
Retel, J.; Nieuwkoop, A.; Hiller, M.; Higman, V.; Barbet-Massin, E.; Stanek, J.; Andreas, L.; Franks, W.; van Rossum, B.-J., .; Vinothkumar, K.; Handel, L.; de Palma, G.; Bardiaux, B.; Pintacuda, G.; Emsley, L.; Kuelbrandt, W.; Oschkinat, H.
Citation:

Citation: Retel, J.; Nieuwkoop, A.; Hiller, M.; Higman, V.; Barbet-Massin, E.; Stanek, J.; Andreas, L.; Franks, W.; van Rossum, B.; Vinothkumar, K.; Handel, L.; de Palma, G.; Bardiaux, B.; Pintacuda, G.; Emsley, L.; Kuhlbrandt, W.; Oschkinat, H.. "Structure of outer membrane protein G in lipid bilayers."  Nat. Commun. 8, 2073-2073 (2017).
PubMed: 29233991

Assembly members:

Assembly members:
entity_1, polymer, 281 residues, 32936.527 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 83333   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

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

Data typeCount
13C chemical shifts1195
15N chemical shifts433
1H chemical shifts307

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 281 residues - 32936.527 Da.

1   METGLUGLUARGASNASPTRPHISPHEASN
2   ILEGLYALAMETTYRGLUILEGLUASNVAL
3   GLUGLYTYRGLYGLUASPMETASPGLYLEU
4   ALAGLUPROSERVALTYRPHEASNALAALA
5   ASNGLYPROTRPARGILEALALEUALATYR
6   TYRGLNGLUGLYPROVALASPTYRSERALA
7   GLYLYSARGGLYTHRTRPPHEASPARGPRO
8   GLULEUGLUVALHISTYRGLNPHELEUGLU
9   ASNASPASPPHESERPHEGLYLEUTHRGLY
10   GLYPHEARGASNTYRGLYTYRHISTYRVAL
11   ASPGLUPROGLYLYSASPTHRALAASNMET
12   GLNARGTRPLYSILEALAPROASPTRPASP
13   VALLYSLEUTHRASPASPLEUARGPHEASN
14   GLYTRPLEUSERMETTYRLYSPHEALAASN
15   ASPLEUASNTHRTHRGLYTYRALAASPTHR
16   ARGVALGLUTHRGLUTHRGLYLEUGLNTYR
17   THRPHEASNGLUTHRVALALALEUARGVAL
18   ASNTYRTYRLEUGLUARGGLYPHEASNMET
19   ASPASPSERARGASNASNGLYGLUPHESER
20   THRGLNGLUILEARGALATYRLEUPROLEU
21   THRLEUGLYASNHISSERVALTHRPROTYR
22   THRARGILEGLYLEUASPARGTRPSERASN
23   TRPASPTRPGLNASPASPILEGLUARGGLU
24   GLYHISASPPHEASNARGVALGLYLEUPHE
25   TYRGLYTYRASPPHEGLNASNGLYLEUSER
26   VALSERLEUGLUTYRALAPHEGLUTRPGLN
27   ASPHISASPGLUGLYASPSERASPLYSPHE
28   HISTYRALAGLYVALGLYVALASNTYRSER
29   PHE

Samples:

sample_4: Outer Membrane Protein G, [U-15N; U-1H], 0.66 w/w; lipids 0.33 w/w; NaCl 50 mM

sample_5: Outer Membrane Protein G, [U-15N; U-1H], 0.66 w/w; lipids 0.33 w/w; NaCl 50 mM

sample_6: Outer Membrane Protein G, [U-15N; U-1H], 0.66 w/w; lipids, na, 0.33 w/w; NaCl 50 mM

sample_7: Outer Membrane Protein G, [U-15N; U-1H], 0.66 w/w; lipids 0.33 w/w; NaCl 50 mM

sample_8: Outer Membrane Protein G, [U-13C; U-15N; U-2H] backexchanged 1H, 0.66 w/w; NaCl 50 mM

sample_1: Outer Membrane Protein G, [U-13C; U-15N; U-2H] backexchanged 1H, 0.66 w/w; lipids 0.33 w/w; NaCl 50 mM

sample_2: Outer Membrane Protein G, [U-15N; U-1H], 0.66 w/w; lipids 0.33 w/w; NaCl 50 mM

sample_3: Outer Membrane Protein G, [U-15N; U-1H], 0.66 w/w; lipids 0.33 w/w; NaCl 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.3; pressure: 1 atm; temperature: 280 K

sample_conditions_2: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 280 K

sample_conditions_3: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 280 K

Experiments:

NameSampleSample stateSample conditions
3D (H)N(HH)NH RFDR 2mssample_1isotropicsample_conditions_1
3D (H)NHH RFDR 2mssample_1isotropicsample_conditions_1
2D 13C-13C DARR 200mssample_2isotropicsample_conditions_2
2D 13C-13C DARR 400mssample_2isotropicsample_conditions_2
2D 13C-13C DARR 200mssample_3isotropicsample_conditions_2
2D 13C-13C DARR 400mssample_3isotropicsample_conditions_2
2D 13C-13C DARR 400mssample_4isotropicsample_conditions_2
2D 13C-13C DARR 150mssample_4isotropicsample_conditions_2
2D 13C-13C DARR 150mssample_5isotropicsample_conditions_2
2D 13C-13C DARR 400mssample_5isotropicsample_conditions_2
2D 13C-13C DARR 150mssample_6isotropicsample_conditions_2
2D 13C-13C DARR 400mssample_6isotropicsample_conditions_2
2D 13C-13C DARR 500mssample_7isotropicsample_conditions_2
3D (H)CANHsample_1isotropicsample_conditions_1
3D (H)CANHsample_8isotropicsample_conditions_3
3D (HCO)CA(CO)NHsample_8isotropicsample_conditions_3
3D (HCA)CB(CA)NHsample_8isotropicsample_conditions_3
3D (HCA)CBCA(CO)NHsample_8isotropicsample_conditions_3
3D (H)CONHsample_8isotropicsample_conditions_3
3D (H)CO(CA)NHsample_8isotropicsample_conditions_3

Software:

CNS, Brunger A. T. et.al. - refinement

ARIA v1.21, Linge, O'Donoghue and Nilges - structure calculation

Analysis v2.4, CCPN - chemical shift assignment, peak picking

TALOS vTALOS+, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 1000 MHz
  • Bruker Avance 800 MHz

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