BMRB Entry 30478

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30478
MolProbity Validation Chart

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Title:
NMR solution structure of wild type hFABP1 in the presence of GW7647
Deposition date:
2018-06-11
Original release date:
2019-01-02
Authors:
Scanlon, M.; Mohanty, B.; Doak, B.; Patil, R.
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:
entity_1, polymer, 135 residues, 15225.457 Da.
entity_2VN, non-polymer, 502.752 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: pET-45b (+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: HHHHHHVAMSFSGKYQLQSQ ENFEAFMKAIGLPEELIQKG KDIKGVSEIVQNGKHFKFTI TAGSKVIQNEFTVGEECELE TMTGEKVKTVVQLEGDNKLV TTFKNIKSVTELNGDIITNT MTLGDIVFKRISKRI

Data sets:
Data typeCount
13C chemical shifts449
15N chemical shifts145
1H chemical shifts932

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 135 residues - 15225.457 Da.

1   HISHISHISHISHISHISVALALAMETSER
2   PHESERGLYLYSTYRGLNLEUGLNSERGLN
3   GLUASNPHEGLUALAPHEMETLYSALAILE
4   GLYLEUPROGLUGLULEUILEGLNLYSGLY
5   LYSASPILELYSGLYVALSERGLUILEVAL
6   GLNASNGLYLYSHISPHELYSPHETHRILE
7   THRALAGLYSERLYSVALILEGLNASNGLU
8   PHETHRVALGLYGLUGLUCYSGLULEUGLU
9   THRMETTHRGLYGLULYSVALLYSTHRVAL
10   VALGLNLEUGLUGLYASPASNLYSLEUVAL
11   THRTHRPHELYSASNILELYSSERVALTHR
12   GLULEUASNGLYASPILEILETHRASNTHR
13   METTHRLEUGLYASPILEVALPHELYSARG
14   ILESERLYSARGILE

Entity 2, entity_2 - C29 H46 N2 O3 S - 502.752 Da.

1   2VN

Samples:

sample_1: hFABP1 wild type, [U-15N13C], 0.5 mM; GW7647 0.5 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DMSO, D6, 1%

sample_2: hFABP1 wild type, [U-2H,15N13C], 1 mM; GW7647 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DMSO, D6, 1%

sample_conditions_1: ionic strength: 70 mM; pH: 5.5; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 15N-resolved [1H,1H]-NOESYsample_1isotropicsample_conditions_1
3D 13Cali resolved [1H,1H]-NOESYsample_1isotropicsample_conditions_1
3D 13Caro resolved [1H,1H]-NOESYsample_1isotropicsample_conditions_1
2D F1-edited, F2-13C,15N-filtered [1H,1H] NOESYsample_1isotropicsample_conditions_1
3D F1-13C,15N-filtered, F2-13Cali edited [1H,1H] NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D F1, F2-13C,15N-filtered [1H,1H] NOESYsample_2isotropicsample_conditions_1
2D F1-edited, F2-13C,15N-filtered [1H,1H] NOESYsample_2isotropicsample_conditions_1
3D F1-13C,15N-filtered, F2-15N edited [1H,1H] NOESYsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

Prime, Prime, Schrodinger, LLC, New York, NY, 2018 - refinement

OPALp, Koradi et al, 2000 - refinement

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE III 800 MHz

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