BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17052

Title: Nuclear Magnetic Resonane Structural and Ligand Binding Studies of BLBC, a Two-Domain Fragment of Barley Lectin   PubMed: 9425031

Deposition date: 2010-07-13 Original release date: 2010-09-08

Authors: Weaver, Jeanne; Prestegard, J.

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).

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

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

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

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
  • Hide all

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

Samples:

sample_1: potassium phosphate 0.1 M; sodium chloride 0.15 mM; sodium azide 0.1%; BLBC, [U-98% 15N], 1.24 mM; CTO 32 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

FELIX v95, Accelrys Software Inc. - processing

HYDRO, (Gacia de la Torre, J., Navarro, S., Lopez Martinez, M., Diaz, F., & Lopez Cascales, J, 1994) - calculation execution

X-PLOR v3.840, Brunger - structure solution

Molmol, Koradi, Billeter and Wuthrich - visualization

Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Tho - angle comparison

NMR spectrometers:

  • Omega n/a 500 MHz
  • Varian Unity 500 MHz
  • Varian UnityPlus 600 MHz