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 26661

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26661

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Title: 1H, 13C, and 15N Chemical Shift Assignments for SRC in the 6'-sialyllactose-bound state   PubMed: 27172906

Deposition date: 2015-09-16 Original release date: 2017-03-03

Authors: Hemmi, Hikaru

Citation: Hemmi, Hikaru; Kuno, Atsushi; Unno, Sachiko; Hirabayashi, Jun. "NMR analysis on the sialic acid-binding mechanism of an R-type lectin mutant by natural evolution-mimicry"  FEBS Lett. 590, 1720-1728 (2016).

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

Natural source:   Common Name: earthworm   Taxonomy ID: 6398   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Lumbricus terrestris

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-27b

Entity Sequences (FASTA):
src: PKFFYIKSELNGKVLDIGGQ NPAPGSKIITWDQKKGPTAV NQLWYTDQQGVIRSKLNDFA IDASHEQIETQPFDPNNPKR AWIVSGNTIAQLSDRDNVLG VIKSDKGASAHICAWKQHGG PNQKFIIESE

Data sets:
Data typeCount
13C chemical shifts566
15N chemical shifts140
1H chemical shifts959

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1src1

Entities:

Entity 1, src 130 residues - Formula weight is not available

1   PROLYSPHEPHETYRILELYSSERGLULEU
2   ASNGLYLYSVALLEUASPILEGLYGLYGLN
3   ASNPROALAPROGLYSERLYSILEILETHR
4   TRPASPGLNLYSLYSGLYPROTHRALAVAL
5   ASNGLNLEUTRPTYRTHRASPGLNGLNGLY
6   VALILEARGSERLYSLEUASNASPPHEALA
7   ILEASPALASERHISGLUGLNILEGLUTHR
8   GLNPROPHEASPPROASNASNPROLYSARG
9   ALATRPILEVALSERGLYASNTHRILEALA
10   GLNLEUSERASPARGASPASNVALLEUGLY
11   VALILELYSSERASPLYSGLYALASERALA
12   HISILECYSALATRPLYSGLNHISGLYGLY
13   PROASNGLNLYSPHEILEILEGLUSERGLU

Samples:

sample_1: src, [U-95% 13C; U-95% 15N], 0.9 mM; 6'-sialyllactose 72 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1

Software:

Felix, Accelrys Software Inc. - processing

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker Avance 800 MHz

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