BMRB Entry 19727
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19727
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Title: HIFABP_Ketorolac_complex PubMed: 25144524
Deposition date: 2014-01-09 Original release date: 2014-10-27
Authors: Patil, Rahul; Laguerre, Aisha; Wielens, Jerome; Headey, Stephen; Williams, Martin; Mohanty, Biswaranjan; Porter, Christopher; Scanlon, Martin
Citation: Patil, Rahul; Scanlon, Martin. "Characterization of Two Distinct Modes of Drug Binding to Human Intestinal Fatty Acid Binding Protein" ACS Chem. Biol. ., .-. (2014).
Assembly members:
HIFABP, polymer, 131 residues, 15098.187 Da.
2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYLENE)-AMINO]-SUCCINIC ACID, non-polymer, 363.237 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
Entity Sequences (FASTA):
HIFABP: AFDSTWKVDRSENYDKFMEK
MGVNIVKRKLAAHDNLKLTI
TQEGNKFTVKESSAFRNIEV
VFELGVTFNYNLADGTELRG
TWSLEGNKLIGKFKRTDNGN
ELNTVREIIGDELVQTYVYE
GVEAKRIFKKD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 434 |
| 15N chemical shifts | 126 |
| 1H chemical shifts | 830 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | KET | 2 |
Entities:
Entity 1, entity_1 131 residues - 15098.187 Da.
| 1 | ALA | PHE | ASP | SER | THR | TRP | LYS | VAL | ASP | ARG | ||||
| 2 | SER | GLU | ASN | TYR | ASP | LYS | PHE | MET | GLU | LYS | ||||
| 3 | MET | GLY | VAL | ASN | ILE | VAL | LYS | ARG | LYS | LEU | ||||
| 4 | ALA | ALA | HIS | ASP | ASN | LEU | LYS | LEU | THR | ILE | ||||
| 5 | THR | GLN | GLU | GLY | ASN | LYS | PHE | THR | VAL | LYS | ||||
| 6 | GLU | SER | SER | ALA | PHE | ARG | ASN | ILE | GLU | VAL | ||||
| 7 | VAL | PHE | GLU | LEU | GLY | VAL | THR | PHE | ASN | TYR | ||||
| 8 | ASN | LEU | ALA | ASP | GLY | THR | GLU | LEU | ARG | GLY | ||||
| 9 | THR | TRP | SER | LEU | GLU | GLY | ASN | LYS | LEU | ILE | ||||
| 10 | GLY | LYS | PHE | LYS | ARG | THR | ASP | ASN | GLY | ASN | ||||
| 11 | GLU | LEU | ASN | THR | VAL | ARG | GLU | ILE | ILE | GLY | ||||
| 12 | ASP | GLU | LEU | VAL | GLN | THR | TYR | VAL | TYR | GLU | ||||
| 13 | GLY | VAL | GLU | ALA | LYS | ARG | ILE | PHE | LYS | LYS | ||||
| 14 | ASP |
Entity 2, KET - C12 H16 N2 O9 P - 363.237 Da.
| 1 | KET |
Samples:
sample_1: HIFABP, [U-13C; U-15N], 1 mM; 5-benzoyl-2,3-dihydro-1H-pyrrolizine-1-carboxylic acid 10 mM; NaCl 50 mM; MES 20 mM; H2O 90%; D2O 10%
Sample_3: HIFABP, [U-13C; U-15N], 0.5 mM; 5-benzoyl-2,3-dihydro-1H-pyrrolizine-1-carboxylic acid 5 mM; NaCl 50 mM; MES 20 mM; H2O 90%; D2O 10%
Sample_2: HIFABP, [U-13C; U-15N], 0.25 mM; 5-benzoyl-2,3-dihydro-1H-pyrrolizine-1-carboxylic acid 2.5 mM; NaCl 50 mM; MES 20 mM; H2O 90%; D2O 10%
sample_conditions_1: pH: 5.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | Sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | Sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | Sample_3 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | Sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | Sample_3 | isotropic | sample_conditions_1 |
| 3D HNCO | Sample_3 | isotropic | sample_conditions_1 |
| 3D HNCACB | Sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.2, Bruker Biospin - collection, data analysis, processing
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY v3.113, Goddard - chemical shift assignment, peak picking
VNMRJ, Varian - collection
CNS v3, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation
CARA v4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking
CYANA v3, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Bruker Avance 800 MHz
- Varian INOVA 600 MHz
Related Database Links:
| BMRB | 19921 |
| PDB | |
| GB | AAA52417 AAH69466 AAH69617 AAH69625 AAH69637 |
| REF | NP_000125 XP_001149448 XP_002815138 XP_003830103 XP_004040374 |
| SP | P12104 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts