BMRB Entry 5541

Title:
1H and 15N Chemical Shift Assignments of Lm-FABP
Deposition date:
2002-09-26
Original release date:
2006-01-04
Authors:
Luecke, Christian; Kizilbash, Nadeem; van Moerkerk, Herman; Veerkamp, Jacques; Hamilton, James
Citation:

Citation: Luecke, Christian; Kizilbash, Nadeem; van Moerkerk, Herman; Veerkamp, Jacques; Hamilton, James. "Letter to the Editor: NMR assignment and structural characterization of the fatty acid binding protein from the flight muscle of Locusta migratoria"  J. Biomol. NMR 25, 355-356 (2003).

Assembly members:

Assembly members:
fatty acid binding protein, polymer, 134 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Locust   Taxonomy ID: 7004   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Locusta migratoria

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-3d

Data sets:
Data typeCount
1H chemical shifts962
15N chemical shifts126

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Lm-FABP1

Entities:

Entity 1, Lm-FABP 134 residues - Formula weight is not available

1   METVALLYSGLUPHEALAGLYILELYSTYR
2   LYSLEUASPSERGLNTHRASNPHEGLUGLU
3   TYRMETLYSALAILEGLYVALGLYALAILE
4   GLUARGLYSALAGLYLEUALALEUSERPRO
5   VALILEGLULEUGLUVALLEUASPGLYASP
6   LYSPHELYSLEUTHRSERLYSTHRALAILE
7   LYSASNTHRGLUPHETHRPHELYSLEUGLY
8   GLUGLUPHEASPGLUASPTHRLEUASPGLY
9   ARGLYSVALLYSSERILEILETHRGLNASP
10   GLYPROASNLYSLEUVALHISGLUGLNLYS
11   GLYASPHISPROTHRILEILEILEARGGLU
12   PHESERLYSGLUGLNCYSVALILETHRILE
13   LYSLEUGLYASPLEUVALALATHRARGILE
14   TYRLYSALAGLN

Samples:

sample_1: fatty acid binding protein 5 mM

sample_2: fatty acid binding protein, [U-15N], 1 mM

cond_1: pH: 5.5; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
NOESY mixing times were set to 150ms (3D) and 200ms (2D);not availablenot availablecond_1
TOCSY spinlock times of either 80ms or 6ms were used.not availablenot availablecond_1

Software:

XWINNMR v1.3 - processing

AURELIA v2.5.9 - analysis

NMR spectrometers:

  • Bruker DMX 500 MHz

Related Database Links:

BMRB 6931
PDB
GB AAB30739 AAK20174
SP P41496 P41509
AlphaFold P41496 P41509

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