BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 12000

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR12000

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Title: Backbone chemical shifts assignments of a two-domain family GH19 chitinase allergen from Japanese cedar (Cryptomeria japonica) pollen,CJP-4.   PubMed: 28032262

Deposition date: 2016-07-28 Original release date: 2017-03-07

Authors: Takashima, Tomoya; Ohnuma, Takayuki; Fukamizo, Tamo

Citation: Takashima, Tomoya; Ohnuma, Takayuki; Fukamizo, Tamo. "NMR assignments and ligand-binding studies on a two-domain family GH19 chitinase allergen from Japanese cedar (Cryptomeria japonica) pollen"  Biomol. NMR Assign. 11, 85-90 (2017).

Assembly members:
CJP-4, polymer, 254 residues, Formula weight is not available

Natural source:   Common Name: Cryptomeria japonica   Taxonomy ID: 3369   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Cryptomeria japonica

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-Blue1

Entity Sequences (FASTA):
CJP-4: MHHHHHHQNCGCNGLCCSQY GYCGSGEAYCGAGCKEGPCS SSSPPSTGTGVGSIVSSDVF NSIVGGAASGCAGNGFYTYD SFISAANAFNGFGTSGSSDV NKREIAAFFANAAHQTGGFC YIEEQNPTSIYCDASNTQYP CASGKTYHGRGPLQLSWNYN YGAAGSYIQFDGLNNPEIVG TDSTISFKTAVWFWMVNSNC HTAITSGQGFGATIRAINSM ECDGGNAATVASRVNYYQKF CQQLNVDTGSNLQC

Data sets:
Data typeCount
13C chemical shifts649
15N chemical shifts215
1H chemical shifts216

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CJP-41

Entities:

Entity 1, CJP-4 254 residues - Formula weight is not available

1   METHISHISHISHISHISHISGLNASNCYS
2   GLYCYSASNGLYLEUCYSCYSSERGLNTYR
3   GLYTYRCYSGLYSERGLYGLUALATYRCYS
4   GLYALAGLYCYSLYSGLUGLYPROCYSSER
5   SERSERSERPROPROSERTHRGLYTHRGLY
6   VALGLYSERILEVALSERSERASPVALPHE
7   ASNSERILEVALGLYGLYALAALASERGLY
8   CYSALAGLYASNGLYPHETYRTHRTYRASP
9   SERPHEILESERALAALAASNALAPHEASN
10   GLYPHEGLYTHRSERGLYSERSERASPVAL
11   ASNLYSARGGLUILEALAALAPHEPHEALA
12   ASNALAALAHISGLNTHRGLYGLYPHECYS
13   TYRILEGLUGLUGLNASNPROTHRSERILE
14   TYRCYSASPALASERASNTHRGLNTYRPRO
15   CYSALASERGLYLYSTHRTYRHISGLYARG
16   GLYPROLEUGLNLEUSERTRPASNTYRASN
17   TYRGLYALAALAGLYSERTYRILEGLNPHE
18   ASPGLYLEUASNASNPROGLUILEVALGLY
19   THRASPSERTHRILESERPHELYSTHRALA
20   VALTRPPHETRPMETVALASNSERASNCYS
21   HISTHRALAILETHRSERGLYGLNGLYPHE
22   GLYALATHRILEARGALAILEASNSERMET
23   GLUCYSASPGLYGLYASNALAALATHRVAL
24   ALASERARGVALASNTYRTYRGLNLYSPHE
25   CYSGLNGLNLEUASNVALASPTHRGLYSER
26   ASNLEUGLNCYS

Samples:

sample_1: CJP-4, [U-95% 13C; U-95% 15N], 0.3 mM; sodium acetate 50 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 0 M; pH: 5; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_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 shifts
SPARKY: Backbone or all simulated shifts