BMRB Entry 26962

Title:
Backbone resonance assignment of insect arylalkylamine N-acetyltransferase from bombyx mori reveals conformational heterogeneity
Deposition date:
2016-11-29
Original release date:
2017-03-02
Authors:
Aboalroub, Adam; Zhang, Ziming; Keramisanou, Dimitra; Gelis, Ioannis
Citation:

Citation: Aboalroub, Adam; Zhang, ziming; Keramisanou, Dimitra; Gelis, Ioannis. "Backbone resonance assignment of an insect arylalkylamine N-acetyltransferase from Bombyx mori reveals conformational heterogeneity"  J. Biomol. NMR 11, 105-109 (2017).
PubMed: 28236225

Assembly members:

Assembly members:
bmAANAT3, polymer, 216 residues, Formula weight is not available

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: pET28a

Data sets:
Data typeCount
13C chemical shifts601
15N chemical shifts197
1H chemical shifts197

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1bmAANAT31

Entities:

Entity 1, bmAANAT3 216 residues - Formula weight is not available

The three amino acids GSH remain after thrombin cleavage.

1   GLYSERHISMETALAASPPHEVALVALVAL
2   METPROSERMETLYSASPALAVALILEGLN
3   HISLEUARGASPSERPHEPHEALAASPGLU
4   PROLEUASNLYSALAVALGLYLEUCYSGLU
5   ARGGLYGLNPROHISALAALALEUGLUARG
6   LEUCYSLEUALATHRMETTHRASPGLYLEU
7   SERILEALAALAMETASPGLYASPLYSVAL
8   LEUGLYVALALALEUASNGLYILELEUARG
9   HISGLYASPILEGLUGLNSERILEGLULYS
10   ILELYSGLNSERTHRASPGLULYSPHEASN
11   LYSILEPHEASNILELEUTYRTHRVALSER
12   ARGASPLEUASNLEUPHEASNTHRPHEGLU
13   VALASPLEUILEMETGLUCYSARGILEILE
14   SERVALHISGLUASNALAARGGLYARGGLY
15   LEUALALYSGLULEUMETLYSARGSERILE
16   ASPLEUALAARGASPASNGLUPHELYSLEU
17   PHELYSVALASPALATHRGLYALAPHESER
18   GLNARGILECYSARGSERLEUSERLEUGLU
19   GLULEULYSSERVALARGTYRASPGLUTYR
20   CYSASPGLUSERGLYTHRPROILEPHEARG
21   VALPROPROPROASPHISALALEUCYSVAL
22   METILELEULYSLEUPRO

Samples:

sample_1: bmAANAT3, [U-100% 15N], 0.4 mM; D2O 7%; TRIS, [U-2H], 20 mM; potassium chloride 150 mM; EDTA 0.5 mM

sample_2: bmAANAT3, [U-100% 13C; U-100% 15N], 0.4 mM; D2O 7%; TRIS, [U-2H], 20 mM; potassium chloride 150 mM; EDTA 0.5 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 80; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMRJ, Varian - collection

NMR spectrometers:

  • Varian Uniform NMR System 800 MHz

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