BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 30604

Title: Solution NMR structure of a quiet outer membrane protein G Nanopore (OmpG mutant: Delta-L6-D215)   PubMed: 30990011

Deposition date: 2019-04-26 Original release date: 2019-05-31

Authors: Sanganna Gari, R.; Seelheim, P.; Liang, B.; Tamm, L.

Citation: Sanganna Gari, R.; Seelheim, P.; Liang, B.; Tamm, L.. "Quiet Outer Membrane Protein G (OmpG) Nanopore for Biosensing."  ACS Sens. 4, 1230-1235 (2019).

Assembly members:
entity_1, polymer, 271 residues, 31502.029 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli K-12

Entity Sequences (FASTA):
entity_1: EERNDWHFNIGAMYEIENVE GYGEDMDGLAEPSVYFNAAN GPWRIALAYYQEGPVDYSAG KRGTWFDRPELEVHYQFLEN DDFSFGLTGGFRNYGYHYVD EPGKDTANMQRWKIAPDWDV KLTDDLRFNGWLSMYKFAND LNTTGYADTRVETETGLQYT FNETVALRVNYYLERGFNMD DSRNNGEFSTQEIRAYLPLT LGNHSVTPYTRIGLRWSNGE GHDFNRVGLFYGYDFQNGLS VSLEYAFEWQDHDEGDSDKF HYAGVGVNYSF

Data sets:
Data typeCount
13C chemical shifts725
15N chemical shifts237
1H chemical shifts237

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 271 residues - 31502.029 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   ARGILEGLYLEUARGTRPSERASNGLYGLU
23   GLYHISASPPHEASNARGVALGLYLEUPHE
24   TYRGLYTYRASPPHEGLNASNGLYLEUSER
25   VALSERLEUGLUTYRALAPHEGLUTRPGLN
26   ASPHISASPGLUGLYASPSERASPLYSPHE
27   HISTYRALAGLYVALGLYVALASNTYRSER
28   PHE

Samples:

sample_1: OmpG delta-L6-D215 mutant, [U-13C; U-15N; U-2H], 1 mM; DPC 200 mM; Bis-Tris 25 mM; sodium chloride 50 mM; sodium azide 0.05 % w/v

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

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D 15N-1H-1H NOESY-TROSYsample_1isotropicsample_conditions_1
3D 15N-1H-15N HSQC-NOESY-HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

Sparky v3, Goddard and Kneller - chemical shift assignment

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts