BMRB Entry 26303

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26303

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry

Title:
NMR chemical shift of Bryum coronatum chitinase W103A mutant
Deposition date:
2020-10-28
Original release date:
2026-06-19
Authors:
Nagata, Takuya; Shinya, Shoko; Ohnuma, Takayuki; Fukamizo, Tamo
Citation:

Citation: Nagata, Takuya; Shinya, Shoko; Ohnuma, Takayuki; Fukamizo, Tamo. "Multi-functionality of a tryptophan residue conserved in substrate-binding groove of GH19 chitinases. "  Sci. Rep. 11, 2494-2494 (2021).
PubMed: 33510258

Assembly members:

Assembly members:
Bryum coronatum chitinase W103A mutant, polymer, 205 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Gemmabryum coronatum   Taxonomy ID: 216087   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Gemmabryum coronatum

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET22b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Bryum coronatum chitinase W103A mutant: QSWTSFVTPAVFEGWFPNRN PFYTYDGLVSASNGYPEFGT TGSLDDQKRELAAFLGNINQ ESGGLQFIQEQNPQSDYCDT SSTQYPCAAGKQYYGRGPIQ LSANYNYGEAGADLGLDLLN NPDLVAQDSTVAWRTALWFW MKRDCHGAITASPPSFSGTI RIINGGLECNQPAGSIGNMQ MENRVTYYTQFCQTLGVDPG TDLRC

Data sets:
Data typeCount
13C chemical shifts576
15N chemical shifts188
1H chemical shifts188

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Bryum coronatum chitinase W103A mutant1

Entities:

Entity 1, Bryum coronatum chitinase W103A mutant 205 residues - Formula weight is not available

1   GLNSERTRPTHRSERPHEVALTHRPROALA
2   VALPHEGLUGLYTRPPHEPROASNARGASN
3   PROPHETYRTHRTYRASPGLYLEUVALSER
4   ALASERASNGLYTYRPROGLUPHEGLYTHR
5   THRGLYSERLEUASPASPGLNLYSARGGLU
6   LEUALAALAPHELEUGLYASNILEASNGLN
7   GLUSERGLYGLYLEUGLNPHEILEGLNGLU
8   GLNASNPROGLNSERASPTYRCYSASPTHR
9   SERSERTHRGLNTYRPROCYSALAALAGLY
10   LYSGLNTYRTYRGLYARGGLYPROILEGLN
11   LEUSERALAASNTYRASNTYRGLYGLUALA
12   GLYALAASPLEUGLYLEUASPLEULEUASN
13   ASNPROASPLEUVALALAGLNASPSERTHR
14   VALALATRPARGTHRALALEUTRPPHETRP
15   METLYSARGASPCYSHISGLYALAILETHR
16   ALASERPROPROSERPHESERGLYTHRILE
17   ARGILEILEASNGLYGLYLEUGLUCYSASN
18   GLNPROALAGLYSERILEGLYASNMETGLN
19   METGLUASNARGVALTHRTYRTYRTHRGLN
20   PHECYSGLNTHRLEUGLYVALASPPROGLY
21   THRASPLEUARGCYS

Samples:

sample_1: Bryum coronatum chitinase W103A mutant, [U-13C; U-15N], 0.4 mM; sodium acetate 50 mM; D2O, [U-2H], 10%; H2O 90%

sample_conditions_1: ionic strength: 50 mM; pH: 5.0; 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 CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

SPARKY - 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