BMRB Entry 11434

Title:
NMR Chemical Shift Assignments for Ostrich egg white Lysozyme
Deposition date:
2011-03-14
Original release date:
2012-02-08
Authors:
Fukamizo, Tamo
Citation:

Citation: Shinya, Shoko; Ohnuma, Takayuki; Kawamura, Shunsuke; Torikata, Takao; Nishimura, Shigenori; Katoh, Etsuko; Fukamizo, Tamo. "Interaction of a goose-type lysozyme with chitin oligosaccharides as determined by NMR spectroscopy"  J. Biochem. 150, 569-577 (2011).
PubMed: 21859795

Assembly members:

Assembly members:
OEL, polymer, 187 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Ostrich   Taxonomy ID: 8801   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Struthio Linnaeus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Pichia pastoris   Vector: pPIC9K

Data sets:
Data typeCount
13C chemical shifts484
15N chemical shifts173
1H chemical shifts173

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Ostrich egg white lysozyme1

Entities:

Entity 1, Ostrich egg white lysozyme 187 residues - Formula weight is not available

1   SERARGTHRGLYCYSTYRGLYASPVALASN
2   ARGVALASPTHRTHRGLYALASERCYSLYS
3   SERALALYSPROGLULYSLEUASNTYRCYS
4   GLYVALALAALASERARGLYSILEALAGLU
5   ARGASPLEUGLNSERMETASPARGTYRLYS
6   ALALEUILELYSLYSVALGLYGLNLYSLEU
7   CYSVALASPPROALAVALILEALAGLYILE
8   ILESERARGGLUSERHISALAGLYLYSALA
9   LEUARGASNGLYTRPGLYASPASNGLYASN
10   GLYPHEGLYLEUMETGLNVALASPARGARG
11   SERHISLYSPROVALGLYGLUTRPASNGLY
12   GLUARGHISLEUMETGLNGLYTHRGLUILE
13   LEUILESERMETILELYSALAILEGLNLYS
14   LYSPHEPROARGTRPTHRLYSGLUGLNGLN
15   LEULYSGLYGLYILESERALATYRASNALA
16   GLYPROGLYASNVALARGSERTYRGLUARG
17   METASPILEGLYTHRTHRHISASPASPTYR
18   ALAASNASPVALVALALAARGALAGLNTYR
19   TYRLYSGLNHISGLYTYR205

Samples:

sample_1: OEL, [U-99% 13C; U-99% 15N], 0.4 mM; sodium acetate 50 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 5.0; 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 HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 500 MHz

Related Database Links:

BMRB 11436
PDB
DBJ BAL03620
GB KFV76629
REF XP_009664638
SP P00719
AlphaFold P00719

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