BMRB Entry 26641

Title:
Backbone assignments for E. coli MurD
Deposition date:
2015-08-27
Original release date:
2015-12-17
Authors:
Ogura, Kenji; Kumeta, Hiroyuki; Yokochi, Masashi; Inagaki, Fuyuhiko
Citation:

Citation: Saio, Tomohide; Ogura, Kenji; Kumeta, Hiroyuki; Kobashigawa, Yoshihiro; Shimizu, Kazumi; Yokochi, Masashi; Kodama, Kota; Yamaguchi, Hiroto; Tsujishita, Hideki; Inagaki, Fuyuhiko. "Ligand-driven conformational changes of MurD visualized by paramagnetic NMR"  Sci. Rep. ., .-. (2015).
PubMed: 2015

Assembly members:

Assembly members:
MurD, polymer, 441 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: enterobacteria   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: pGBHPS

Data sets:
Data typeCount
15N chemical shifts371
1H chemical shifts371

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MurD monomer1

Entities:

Entity 1, MurD monomer 441 residues - Formula weight is not available

"HMGS" at the N-terminus is cloning artifact. Ala right after "HMGS" is the first residue.

1   HISMETGLYSERALAASPTYRGLNGLYLYS
2   ASNVALVALILEILEGLYLEUGLYLEUTHR
3   GLYLEUSERCYSVALASPPHEPHELEUALA
4   ARGGLYVALTHRPROARGVALMETASPTHR
5   ARGMETTHRPROPROGLYLEUASPLYSLEU
6   PROGLUALAVALGLUARGHISTHRGLYSER
7   LEUASNASPGLUTRPLEUMETALAALAASP
8   LEUILEVALALASERPROGLYILEALALEU
9   ALAHISPROSERLEUSERALAALAALAASP
10   ALAGLYILEGLUILEVALGLYASPILEGLU
11   LEUPHECYSARGGLUALAGLNALAPROILE
12   VALALAILETHRGLYSERASNGLYLYSSER
13   THRVALTHRTHRLEUVALGLYGLUMETALA
14   LYSALAALAGLYVALASNVALGLYVALGLY
15   GLYASNILEGLYLEUPROALALEUMETLEU
16   LEUASPASPGLUCYSGLULEUTYRVALLEU
17   GLULEUSERSERPHEGLNLEUGLUTHRTHR
18   SERSERLEUGLNALAVALALAALATHRILE
19   LEUASNVALTHRGLUASPHISMETASPARG
20   TYRPROPHEGLYLEUGLNGLNTYRARGALA
21   ALALYSLEUARGILETYRGLUASNALALYS
22   VALCYSVALVALASNALAASPASPALALEU
23   THRMETPROILEARGGLYALAASPGLUARG
24   CYSVALSERPHEGLYVALASNMETGLYASP
25   TYRHISLEUASNHISGLNGLNGLYGLUTHR
26   TRPLEUARGVALLYSGLYGLULYSVALLEU
27   ASNVALLYSGLUMETLYSLEUSERGLYGLN
28   HISASNTYRTHRASNALALEUALAALALEU
29   ALALEUALAASPALAALAGLYLEUPROARG
30   ALASERSERLEULYSALALEUTHRTHRPHE
31   THRGLYLEUPROHISARGPHEGLUVALVAL
32   LEUGLUHISASNGLYVALARGTRPILEASN
33   ASPSERLYSALATHRASNVALGLYSERTHR
34   GLUALAALALEUASNGLYLEUHISVALASP
35   GLYTHRLEUHISLEULEULEUGLYGLYASP
36   GLYLYSSERALAASPPHESERPROLEUALA
37   ARGTYRLEUASNGLYASPASNVALARGLEU
38   TYRCYSPHEGLYARGASPGLYALAGLNLEU
39   ALAALALEUARGPROGLUVALALAGLUGLN
40   THRGLUTHRMETGLUGLNALAMETARGLEU
41   LEUALAPROARGVALGLNPROGLYASPMET
42   VALLEULEUSERPROALACYSALASERLEU
43   ASPGLNPHELYSASNPHEGLUGLNARGGLY
44   ASNGLUPHEALAARGLEUALALYSGLULEU
45   GLY

Samples:

sample_1: MurD, [U-100% 13C; U-100% 15N; U-100% 2H], 0.5 mM; H2O 90%; D2O 10%; Tris-HCl 20 mM; NaCl 200 mM; DTT 10 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 7.2; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSY-HSQCsample_1isotropicsample_conditions_1
TROSY-HN(CO)CAsample_1isotropicsample_conditions_1
TROSY-HNCAsample_1isotropicsample_conditions_1
TROSY-HNCAsample_1isotropicsample_conditions_1
TROSY-HNCOsample_1isotropicsample_conditions_1
TROSY-HN(COCA)CBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
TROSY-HNCACBsample_1isotropicsample_conditions_1

Software:

OLIVIA, Masashi Yokochi - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Varian Unity Inova 800 MHz

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