BMRB Entry 11494

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11494

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Title:
NMR chemical shift of E22A mutant of Streptomyces sp. N174 chitosanase
Deposition date:
2012-04-09
Original release date:
2012-05-02
Authors:
Shinya, Shoko; Brzezinski, Ryszard; Fukamizo, Tamo
Citation:

Citation: Shinya, Shoko; Brzezinski, Ryszard; Fukamizo, Tamo. "Chitosan oligosaccharide binding to GH-46 chitosanase from Streptomyces sp. N174 as determined by NMR spectroscopy"  FEBS J. ., .-..

Assembly members:

Assembly members:
CsnN174_E22A, polymer, 238 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Streptomyces sp.   Taxonomy ID: 1931   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptomyces sp.

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Streptomyces lividans   Vector: pFD666

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CsnN174_E22A: AGAGLDDPHKKEIAMELVSS AANSSLDWKAQYKYIEDIGD GRGYTGGIIGFCSGTGDMLE LVQHYTDLEPGNILAKYLPA LKKVNGSASHSGLGTPFTKD WATAAKDTVFQQAQNDERDR VYFDPAVSQAKADGLRALGQ FAYYDAIVMHGPGNDPTSFG GIRKTAMKKARTPAQGGDET TYLNGFLDARKAAMLTEAAH DDTSRVDTEQRVFLKAGNLD LNPPLKWKTYGDPYVINS

Data sets:
Data typeCount
13C chemical shifts506
15N chemical shifts172
1H chemical shifts172

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CsnN174 E22A1

Entities:

Entity 1, CsnN174 E22A 238 residues - Formula weight is not available

1   ALAGLYALAGLYLEUASPASPPROHISLYS
2   LYSGLUILEALAMETGLULEUVALSERSER
3   ALAALAASNSERSERLEUASPTRPLYSALA
4   GLNTYRLYSTYRILEGLUASPILEGLYASP
5   GLYARGGLYTYRTHRGLYGLYILEILEGLY
6   PHECYSSERGLYTHRGLYASPMETLEUGLU
7   LEUVALGLNHISTYRTHRASPLEUGLUPRO
8   GLYASNILELEUALALYSTYRLEUPROALA
9   LEULYSLYSVALASNGLYSERALASERHIS
10   SERGLYLEUGLYTHRPROPHETHRLYSASP
11   TRPALATHRALAALALYSASPTHRVALPHE
12   GLNGLNALAGLNASNASPGLUARGASPARG
13   VALTYRPHEASPPROALAVALSERGLNALA
14   LYSALAASPGLYLEUARGALALEUGLYGLN
15   PHEALATYRTYRASPALAILEVALMETHIS
16   GLYPROGLYASNASPPROTHRSERPHEGLY
17   GLYILEARGLYSTHRALAMETLYSLYSALA
18   ARGTHRPROALAGLNGLYGLYASPGLUTHR
19   THRTYRLEUASNGLYPHELEUASPALAARG
20   LYSALAALAMETLEUTHRGLUALAALAHIS
21   ASPASPTHRSERARGVALASPTHRGLUGLN
22   ARGVALPHELEULYSALAGLYASNLEUASP
23   LEUASNPROPROLEULYSTRPLYSTHRTYR
24   GLYASPPROTYRVALILEASNSER

Samples:

sample_1: CsnN174 E22A, [U-13C; U-15N], 0.1 mM; sodium acetate 50 mM; D2O, [U-99% 2H], 5%; H2O 95%

sample_conditions_1: pH: 5.5; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 500 MHz

Related Database Links:

BMRB 11493
PDB
GB AAA19865
SP P33665
AlphaFold P33665

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