BMRB Entry 11513

Title:
NMR chemical shift of carbohydrate binding module, C1, derived from GH8 chitosanase/glucanase from Paenibacillus fukuinensis D2
Deposition date:
2012-10-03
Original release date:
2012-11-02
Authors:
Shinya, Shoko; Kimoto, Hisashi; Kusaoke, Hideo; Ohnuma, Takayuki
Citation:

Citation: Shinya, Shoko; Kimoto, Hisashi; Kusaoke, Hideo; Ohnuma, Takayuki; Fukamizo, Tamo. "Chitosan-binding modules derived from Paenibacillus fukuinensis D1 : binding mode and specificity evaluated from NMR spectroscopy"  J. Biol. Chem. ., .-..

Assembly members:

Assembly members:
C1_domain, polymer, 130 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Paenibacillus fukuinensis   Taxonomy ID: 170835   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Paenibacillus fukuinensis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET Blue-1

Data sets:
Data typeCount
13C chemical shifts344
15N chemical shifts112
1H chemical shifts112

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1C1 domain1

Entities:

Entity 1, C1 domain 130 residues - Formula weight is not available

1   ASNLEUALALEUASNLYSTHRALATHRALA
2   SERSERILEGLUGLYALAGLYPHEGLUALA
3   SERARGALAPHEASPGLYSERSERTHRTHR
4   ARGTRPALASERALAGLUGLYVALASPPRO
5   GLNTRPILETYRVALASNLEUGLYSERSER
6   GLNTHRVALASNARGVALLYSLEUASNTRP
7   GLUALAALATYRALASERSERTYRTHRILE
8   GLNVALSERASNASPSERGLYTHRPROTHR
9   ASNTRPTHRTHRVALTYRTHRTHRTHRTHR
10   GLYASPGLYGLYILEASPASPILETHRPHE
11   THRALAARGTHRALALYSTYRVALARGVAL
12   HISGLYTHRVALARGGLYTHRPROTYRGLY
13   TYRSERLEUTRPGLUPHEGLUVALTYRGLY

Samples:

C1: C1 domain, [U-99% 13C; U-99% 15N], 0.2 mM; sodium acetate 50 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 5.0; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCC1isotropicsample_conditions_1
3D CBCA(CO)NHC1isotropicsample_conditions_1
3D HNCACBC1isotropicsample_conditions_1
3D HNCOC1isotropicsample_conditions_1
3D HNCACOC1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 500 MHz

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