BMRB Entry 27510

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27510

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Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for hFABP1 triple-mutant (K57A,E77A,K96A)in complex with GW7647
Deposition date:
2018-06-06
Original release date:
2018-12-19
Authors:
Chandrashekaran, Indu; Mohanty, Biswaranjan; Scanlon, Martin
Citation:

Citation: Patil, Rahul; Mohanty, Biswaranjan; Liu, Bonan; Chandrashekaran, Indu; Headey, Stephen; Williams, Martin; Clements, Craig; Ilyichova, Olga; Doak, Bradley; Genissel, Patrick; Weaver, Richard; Vuillard, Laurent; Halls, Michelle; Porter, Christopher; Scanlon, Martin. "A ligand-induced structural change in fatty acid-binding protein 1 is associated with potentiation of peroxisome proliferator-activated receptor alpha agonists"  J. Biol. Chem. 294, 3720-3734 (2019).
PubMed: 30598509

Assembly members:

Assembly members:
Human_liver_fatty_acid_binding_protein_(hFABP1)_K57A_E77A_K96A_mutant, polymer, 129 residues, 14180.3 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Human_liver_fatty_acid_binding_protein_(hFABP1)_K57A_E77A_K96A_mutant: GSMSFSGKYQLQSQENFEAF MKAIGLPEELIQKGKDIKGV SEIVQNGKHFKFTITAGSAV IQNEFTVGEECELETMTGAK VKTVVQLEGDNKLVTTFANI KSVTELNGDIITNTMTLGDI VFKRISKRI

Data sets:
Data typeCount
13C chemical shifts241
15N chemical shifts122
1H chemical shifts122

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1holo hFABP1 K567A, E77A, K96A mutant1

Entities:

Entity 1, holo hFABP1 K567A, E77A, K96A mutant 129 residues - 14180.3 Da.

Residues 1 and 2 represent a non-native affinity tag

1   GLYSERMETSERPHESERGLYLYSTYRGLN
2   LEUGLNSERGLNGLUASNPHEGLUALAPHE
3   METLYSALAILEGLYLEUPROGLUGLULEU
4   ILEGLNLYSGLYLYSASPILELYSGLYVAL
5   SERGLUILEVALGLNASNGLYLYSHISPHE
6   LYSPHETHRILETHRALAGLYSERALAVAL
7   ILEGLNASNGLUPHETHRVALGLYGLUGLU
8   CYSGLULEUGLUTHRMETTHRGLYALALYS
9   VALLYSTHRVALVALGLNLEUGLUGLYASP
10   ASNLYSLEUVALTHRTHRPHEALAASNILE
11   LYSSERVALTHRGLULEUASNGLYASPILE
12   ILETHRASNTHRMETTHRLEUGLYASPILE
13   VALPHELYSARGILESERLYSARGILE

Samples:

sample_1: GW7647 0.3 mM; Human liver fatty acid binding protein (hFABP1) mutant K57A, E77A, K96A, [U-99% 13C; U-99% 15N], 0.25 mM; D2O, [U-100% 2H], 10%; sodium chloride 50 mM; MES 20 mM; sodium azide 0.02%; H2O 90%

sample_conditions_1: ionic strength: 20 mM; pH: 5.5; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.5, Bruker Biospin - collection, processing

CARA_1.2 v4, Keller and Wuthrich - chemical shift assignment, chemical shift calculation, data analysis, peak picking

MddNMR v2, Orekhov, Jaravine, Mayzel and Kazimierczuk,Swedish NMR Center, University of Gothenburg - processing

NMR spectrometers:

  • Bruker Avance 600 MHz

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