BMRB Entry 27096

Title:
apo-AFABP chemical shift assignments
Deposition date:
2017-05-04
Original release date:
2020-01-06
Authors:
Wang, Qian; Bernard, Cedric; Stark, Ruth
Citation:

Citation: Wang, Qian; Rizk, Samar; Bernard, Cedric; Lai, MayPoh; Kam, David; Storch, Judith; Stark, Ruth. "Protocols and pitfalls in obtaining fatty acid-binding proteins for biophysical studies of ligand-protein and protein-protein interactions"  Biochem. Biophys. Rep. 10, 318-324 (2017).
PubMed: 28955759

Assembly members:

Assembly members:
AFABP_mouse, polymer, 133 residues, 14706.9 Da.

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pDEST17

Data sets:
Data typeCount
15N chemical shifts123
1H chemical shifts390

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1apo_AFABP1

Entities:

Entity 1, apo_AFABP 133 residues - 14706.9 Da.

TEV cleavage left the glycine at the N-termus. Assignment table starts from 1,C.

1   GLYMETCYSASPALAPHEVALGLYTHRTRP
2   LYSLEUVALSERSERGLUASNPHEASPASP
3   TYRMETLYSGLUVALGLYVALGLYPHEALA
4   THRARGLYSVALALAGLYMETALALYSPRO
5   ASNMETILEILESERVALASNGLYASPLEU
6   VALTHRILEARGSERGLUSERTHRPHELYS
7   ASNTHRGLUILESERPHELYSLEUGLYVAL
8   GLUPHEASPGLUILETHRALAASPASPARG
9   LYSVALLYSSERILEILETHRLEUASPGLY
10   GLYALALEUVALGLNVALGLNLYSTRPASP
11   GLYLYSSERTHRTHRILELYSARGLYSARG
12   ASPGLYASPLYSLEUVALVALGLUCYSVAL
13   METLYSGLYVALTHRSERTHRARGVALTYR
14   GLUARGALA

Samples:

sample_1: AFABP mouse, [U-98% 15N], 710 uM; H2O 90 % v/v; potassium chloride 150 mM; potassium phosphate 10 mM; sodium azide 0.2 g/L; D2O, [U-99% 2H], 10 % v/v

sample_conditions_1: ionic strength: 0.17552 M; pH: 7.4; pressure: 1 atm; temperature: 293.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

NMRView vv9.1.0-b10, Johnson, One Moon Scientific - chemical shift assignment, chemical shift calculation, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 500 MHz

Related Database Links:

PIR P04117

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