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
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Title: NMR solution structure of wild type apo hFABP1 at 308 K PubMed: 30598509
Deposition date: 2018-06-09 Original release date: 2019-01-02
Authors: Scanlon, M.; Mohanty, B.; Doak, B.; Patil, R.
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).
Assembly members:
entity_1, polymer, 135 residues, 15225.457 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)
Entity Sequences (FASTA):
entity_1: HHHHHHVAMSFSGKYQLQSQ
ENFEAFMKAIGLPEELIQKG
KDIKGVSEIVQNGKHFKFTI
TAGSKVIQNEFTVGEECELE
TMTGEKVKTVVQLEGDNKLV
TTFKNIKSVTELNGDIITNT
MTLGDIVFKRISKRI
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 446 |
| 15N chemical shifts | 144 |
| 1H chemical shifts | 934 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 135 residues - 15225.457 Da.
| 1 | HIS | HIS | HIS | HIS | HIS | HIS | VAL | ALA | MET | SER | ||||
| 2 | PHE | SER | GLY | LYS | TYR | GLN | LEU | GLN | SER | GLN | ||||
| 3 | GLU | ASN | PHE | GLU | ALA | PHE | MET | LYS | ALA | ILE | ||||
| 4 | GLY | LEU | PRO | GLU | GLU | LEU | ILE | GLN | LYS | GLY | ||||
| 5 | LYS | ASP | ILE | LYS | GLY | VAL | SER | GLU | ILE | VAL | ||||
| 6 | GLN | ASN | GLY | LYS | HIS | PHE | LYS | PHE | THR | ILE | ||||
| 7 | THR | ALA | GLY | SER | LYS | VAL | ILE | GLN | ASN | GLU | ||||
| 8 | PHE | THR | VAL | GLY | GLU | GLU | CYS | GLU | LEU | GLU | ||||
| 9 | THR | MET | THR | GLY | GLU | LYS | VAL | LYS | THR | VAL | ||||
| 10 | VAL | GLN | LEU | GLU | GLY | ASP | ASN | LYS | LEU | VAL | ||||
| 11 | THR | THR | PHE | LYS | ASN | ILE | LYS | SER | VAL | THR | ||||
| 12 | GLU | LEU | ASN | GLY | ASP | ILE | ILE | THR | ASN | THR | ||||
| 13 | MET | THR | LEU | GLY | ASP | ILE | VAL | PHE | LYS | ARG | ||||
| 14 | ILE | SER | LYS | ARG | ILE |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 13Cali-edited [1H,1H]-NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 15N-edited [1H,1H]-NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 13Caro-edited [1H,1H]-NOESY | sample_1 | isotropic | sample_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 simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts