BMRB Entry 17052

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17052

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Title:
Nuclear Magnetic Resonane Structural and Ligand Binding Studies of BLBC, a Two-Domain Fragment of Barley Lectin
Deposition date:
2010-07-13
Original release date:
2010-09-08
Authors:
Weaver, Jeanne; Prestegard, J.
Citation:

Citation: Weaver, Jeanne; Prestegard, J.. "Nuclear Magnetic Resonance Structural and Ligand Binding Studies of BLBC, a Two-Domain Fragment of Barley Lectin"  Biochemistry 37, 116-128 (1998).
PubMed: 9425031

Assembly members:

Assembly members:
BLBC, polymer, 89 residues, Formula weight is not available
CTO, non-polymer, 627.593 Da.

Natural source:

Natural source:   Common Name: barley   Taxonomy ID: 4513   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Hordeum vulgare

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pMAL-p2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BLBC: TSKRCGTQAGGKTCPNNHCC SQWGYCGFGAEYCGAGCQGG PCRADIKCGSQAGGKLCPNN LCCSQWGYCGLGSEFCGEGC QGGACSTDK

Data sets:
  • binding constants
Data typeCount
binding constants2

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1BLBC1
2CTO2

Entities:

Entity 1, BLBC 89 residues - Formula weight is not available

1   THRSERLYSARGCYSGLYTHRGLNALAGLY
2   GLYLYSTHRCYSPROASNASNHISCYSCYS
3   SERGLNTRPGLYTYRCYSGLYPHEGLYALA
4   GLUTYRCYSGLYALAGLYCYSGLNGLYGLY
5   PROCYSARGALAASPILELYSCYSGLYSER
6   GLNALAGLYGLYLYSLEUCYSPROASNASN
7   LEUCYSCYSSERGLNTRPGLYTYRCYSGLY
8   LEUGLYSERGLUPHECYSGLYGLUGLYCYS
9   GLNGLYGLYALACYSSERTHRASPLYS

Entity 2, CTO - C24 H41 N3 O16 - 627.593 Da.

1   CTO