BMRB Entry 16035

Title:
Sequence-specific 1H, 13C and 15N backbone resonance assignments of BamC, a component of the outer membrane protein assembly machinery in Escherichia coli
Deposition date:
2008-11-18
Original release date:
2009-07-22
Authors:
Knowles, Timothy; McClelland, Darren; Rajesh, Sandya; Henderson, Ian; Overduin, Michael
Citation:

Citation: Knowles, Timothy; McClelland, Darren; Rajesh, Sandya; Henderson, Ian; Overduin, Michael. "Secondary structure and (1)H, (13)C and (15)N backbone resonance assignments of BamC, a component of the outer membrane protein assembly machinery in Escherichia coli."  Biomol. NMR Assignments 3, 203-206 (2009).
PubMed: 19888691

Assembly members:

Assembly members:
BamC, polymer, 322 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: chemical synthesis

Data sets:
Data typeCount
13C chemical shifts929
15N chemical shifts302
1H chemical shifts302

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BamC1

Entities:

Entity 1, BamC 322 residues - Formula weight is not available

This sequence represents the final processed E. coli BamC sequence lacking its N-terminal signal peptide and mutated (C26S) to remove its lipoprotein acylation site. The first three residues (HMG) are derived from the vector.

1   HISMETGLYSERSERASPSERARGTYRLYS
2   ARGGLNVALSERGLYASPGLUALATYRLEU
3   GLUALAALAPROLEUALAGLULEUHISALA
4   PROALAGLYMETILELEUPROVALTHRSER
5   GLYASPTYRALAILEPROVALTHRASNGLY
6   SERGLYALAVALGLYLYSALALEUASPILE
7   ARGPROPROALAGLNPROLEUALALEUVAL
8   SERGLYALAARGTHRGLNPHETHRGLYASP
9   THRALASERLEULEUVALGLUASNGLYARG
10   GLYASNTHRLEUTRPPROGLNVALVALSER
11   VALLEUGLNALALYSASNTYRTHRILETHR
12   GLNARGASPASPALAGLYGLNTHRLEUTHR
13   THRASPTRPVALGLNTRPASNARGLEUASP
14   GLUASPGLUGLNTYRARGGLYARGTYRGLN
15   ILESERVALLYSPROGLNGLYTYRGLNGLN
16   ALAVALTHRVALLYSLEULEUASNLEUGLU
17   GLNALAGLYLYSPROVALALAASPALAALA
18   SERMETGLNARGTYRSERTHRGLUMETMET
19   ASNVALILESERALAGLYLEUASPLYSSER
20   ALATHRASPALAALAASNALAALAGLNASN
21   ARGALASERTHRTHRMETASPVALGLNSER
22   ALAALAASPASPTHRGLYLEUPROMETLEU
23   VALVALARGGLYPROPHEASNVALVALTRP
24   GLNARGLEUPROALAALALEUGLULYSVAL
25   GLYMETLYSVALTHRASPSERTHRARGSER
26   GLNGLYASNMETALAVALTHRTYRLYSPRO
27   LEUSERASPSERASPTRPGLNGLULEUGLY
28   ALASERASPPROGLYLEUALASERGLYASP
29   TYRLYSLEUGLNVALGLYASPLEUASPASN
30   ARGSERSERLEUGLNPHEILEASPPROLYS
31   GLYHISTHRLEUTHRGLNSERGLNASNASP
32   ALALEUVALALAVALPHEGLNALAALAPHE
33   SERLYS

Samples:

sample_1: BamC, [U-13C; U-15N; U-2H], 1 mM; sodium phosphate 50 mM; potassium chloride 50 mM; sodium azide 0.02%

sample_conditions_1: pH: 6; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSY HSQCsample_1isotropicsample_conditions_1
3D TROSY HNCAsample_1isotropicsample_conditions_1
3D TROSY HN(CO)CAsample_1isotropicsample_conditions_1
3D TROSY HNCACBsample_1isotropicsample_conditions_1
3D TROSY HN(CO)CACBsample_1isotropicsample_conditions_1
3D TROSY HNCOsample_1isotropicsample_conditions_1
3D TROSY HN(CA)COsample_1isotropicsample_conditions_1

Software:

SPARKY v3.110, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Varian INOVA 800 MHz

Related Database Links:

BMRB 17521
PDB
DBJ BAA16354 BAB36762 BAG78285 BAI26723 BAI31755
EMBL CAA40661 CAP76938 CAQ32848 CAQ99368 CAR03928
GB AAC75530 AAG57587 AAN44023 AAN81455 AAP17837
REF NP_311366 NP_416972 NP_708316 WP_000968412 WP_001295468
SP P0A903 P0A904
AlphaFold P0A903 P0A904

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