BMRB Entry 15426

Title:
Solution NMR structure of OmpG
Deposition date:
2007-08-09
Original release date:
2008-03-14
Authors:
Liang, Binyong; Tamm, Lukas
Citation:

Citation: Liang, Binyong; Tamm, Lukas. "Structure of outer membrane protein G by solution NMR spectroscopy."  Proc. Natl. Acad. Sci. U.S.A. 104, 16140-16145 (2007).
PubMed: 17911261

Assembly members:

Assembly members:
OmpG, polymer, 280 residues, 32813.707 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pT7

Data sets:
Data typeCount
13C chemical shifts697
15N chemical shifts226
1H chemical shifts226

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1OmpG1

Entities:

Entity 1, OmpG 280 residues - 32813.707 Da.

1   GLUGLUARGASNASPTRPHISPHEASNILE
2   GLYALAMETTYRGLUILEGLUASNVALGLU
3   GLYTYRGLYGLUASPMETASPGLYLEUALA
4   GLUPROSERVALTYRPHEASNALAALAASN
5   GLYPROTRPARGILEALALEUALATYRTYR
6   GLNGLUGLYPROVALASPTYRSERALAGLY
7   LYSARGGLYTHRTRPPHEASPARGPROGLU
8   LEUGLUVALHISTYRGLNPHELEUGLUASN
9   ASPASPPHESERPHEGLYLEUTHRGLYGLY
10   PHEARGASNTYRGLYTYRHISTYRVALASP
11   GLUPROGLYLYSASPTHRALAASNMETGLN
12   ARGTRPLYSILEALAPROASPTRPASPVAL
13   LYSLEUTHRASPASPLEUARGPHEASNGLY
14   TRPLEUSERMETTYRLYSPHEALAASNASP
15   LEUASNTHRTHRGLYTYRALAASPTHRARG
16   VALGLUTHRGLUTHRGLYLEUGLNTYRTHR
17   PHEASNGLUTHRVALALALEUARGVALASN
18   TYRTYRLEUGLUARGGLYPHEASNMETASP
19   ASPSERARGASNASNGLYGLUPHESERTHR
20   GLNGLUILEARGALATYRLEUPROLEUTHR
21   LEUGLYASNHISSERVALTHRPROTYRTHR
22   ARGILEGLYLEUASPARGTRPSERASNTRP
23   ASPTRPGLNASPASPILEGLUARGGLUGLY
24   HISASPPHEASNARGVALGLYLEUPHETYR
25   GLYTYRASPPHEGLNASNGLYLEUSERVAL
26   SERLEUGLUTYRALAPHEGLUTRPGLNASP
27   HISASPGLUGLYASPSERASPLYSPHEHIS
28   TYRALAGLYVALGLYVALASNTYRSERPHE

Samples:

sample_1: OmpG, [U-13C; U-15N; U-2H], 1 mM; DPC15 – 300 mM; Bis-Tris 25 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.3; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)CBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D TROSYNOESYsample_1isotropicsample_conditions_1
3D TROSYNOESYTROSYsample_1isotropicsample_conditions_1
2D heteronuclear 1H-15N NOEsample_1isotropicsample_conditions_1

Software:

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

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 500 MHz

Related Database Links:

PDB
DBJ BAB35321 BAE76401 BAG76895 BAI25168 BAI35617
EMBL CAP75863 CAQ31824 CAQ98203 CAR02781 CAR07725
GB AAC34720 AAC74401 AAG56483 AAN80257 ABE07068
REF NP_309925 NP_415835 WP_000735233 WP_000735234 WP_000735235
SP P76045
AlphaFold P76045

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