BMRB Entry 30477

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30477
MolProbity Validation Chart

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Title:
NMR solution structure of wild type apo hFABP1 at 308 K
Deposition date:
2018-06-09
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.

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 BL21(DE3)   Vector: PET-45b(+)

Entity Sequences (FASTA):

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

Data sets:
Data typeCount
13C chemical shifts446
15N chemical shifts144
1H chemical shifts934

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

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

Samples:

sample_1: sodium phosphate 20 mM; sodium chloride 50 mM; Human liver fatty acid binding protein (hFABP1), [U-13C; U-15N], 1 mM

sample_conditions_1: ionic strength: 70 mM; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 13Cali-edited [1H,1H]-NOESYsample_1isotropicsample_conditions_1
3D 15N-edited [1H,1H]-NOESYsample_1isotropicsample_conditions_1
3D 13Caro-edited [1H,1H]-NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

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

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

UNIO10-ATNOS/CANID v2.0.2, Dr. Torsten Herrmann - structure calculation

OPALp, Koradi et al, 2000 - refinement

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

NMR spectrometers:

  • Bruker AvanceIII 600 MHz
  • Bruker AvanceIII 800 MHz

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