BMRB Entry 15433
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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/BMR15433
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Title: Solution-State Structures of Oleate-Liganded LFABP, Protein Only PubMed: 17927211
Deposition date: 2007-08-15 Original release date: 2008-06-18
Authors: He, Yan; Yang, Xiaomin; Wang, Hsin; Estephan, Rima; Francis, Fouad; Kodukula, Sarala; Storch, Judith; Stark, Ruth
Citation: He, Yan; Yang, Xiaomin; Wang, Hsin; Estephan, Rima; Francis, Fouad; Kodukula, Sarala; Storch, Judith; Stark, Ruth. "Solution-state molecular structure of apo and oleate-liganded liver fatty acid-binding protein" Biochemistry 46, 12543-12556 (2007).
Assembly members:
LFABP, polymer, 127 residues, 14295.663 Da.
OLA, non-polymer, 282.461 Da.
Natural source: Common Name: Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
LFABP: MNFSGKYQVQSQENFEPFMK
AMGLPEDLIQKGKDIKGVSE
IVHEGKKVKLTITYGSKVIH
NEFTLGEECELETMTGEKVK
AVVKMEGDNKMVTTFKGIKS
VTEFNGDTITNTMTLGDIVY
KRVSKRI
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 608 |
| 15N chemical shifts | 135 |
| 1H chemical shifts | 862 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | LFABP | 1 |
| 2 | oleate | 2 |
| 3 | oleate | 2 |
Entities:
Entity 1, LFABP 127 residues - 14295.663 Da.
| 1 | MET | ASN | PHE | SER | GLY | LYS | TYR | GLN | VAL | GLN | ||||
| 2 | SER | GLN | GLU | ASN | PHE | GLU | PRO | PHE | MET | LYS | ||||
| 3 | ALA | MET | GLY | LEU | PRO | GLU | ASP | LEU | ILE | GLN | ||||
| 4 | LYS | GLY | LYS | ASP | ILE | LYS | GLY | VAL | SER | GLU | ||||
| 5 | ILE | VAL | HIS | GLU | GLY | LYS | LYS | VAL | LYS | LEU | ||||
| 6 | THR | ILE | THR | TYR | GLY | SER | LYS | VAL | ILE | HIS | ||||
| 7 | ASN | GLU | PHE | THR | LEU | GLY | GLU | GLU | CYS | GLU | ||||
| 8 | LEU | GLU | THR | MET | THR | GLY | GLU | LYS | VAL | LYS | ||||
| 9 | ALA | VAL | VAL | LYS | MET | GLU | GLY | ASP | ASN | LYS | ||||
| 10 | MET | VAL | THR | THR | PHE | LYS | GLY | ILE | LYS | SER | ||||
| 11 | VAL | THR | GLU | PHE | ASN | GLY | ASP | THR | ILE | THR | ||||
| 12 | ASN | THR | MET | THR | LEU | GLY | ASP | ILE | VAL | TYR | ||||
| 13 | LYS | ARG | VAL | SER | LYS | ARG | ILE |
Entity 2, oleate - C18 H34 O2 - 282.461 Da.
| 1 | OLA |
Samples:
sample_1: LFABP, [U-99% 13C; U-99% 15N], 0.7 – 1.0 mM; sodium phosphate 50 mM; sodium azide 0.02%; EDTA 5 uM; D2O 5%; oleate 3 eq; sodium chloride 100 mM
sample_2: LFABP, [U-99% 13C; U-99% 15N], 0.7 – 1.0 mM; sodium phosphate 50 mM; sodium azide 0.02%; EDTA 5 uM; D2O 98%; oleate 3 eq; sodium chloride 100 mM
sample_3: LFABP, [U-99% 15N], 0.5 – 1.3 mM; sodium phosphate 50 mM; sodium azide 0.02%; EDTA 5 uM; D2O 5%; oleate, [U-99% 13C], 3 eq; sodium chloride 100 mM
sample_4: LFABP, [U-99% 15N], 0.3 mM; sodium phosphate 50 mM; sodium azide 0.02%; EDTA 5 uM; D2O 5%; C12E5 5%; oleate, [U-99% 13C], 3 eq; sodium chloride 100 mM
sample_conditions_1: ionic strength: 0.15 M; pH: 7; pressure: 1 atm; temperature: 303 K
sample_conditions_2: ionic strength: 0.15 M; pD: 7; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_3 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_2 |
| 4D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_2 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 4D 1H-13C-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_3 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCACOHA | sample_1 | isotropic | sample_conditions_1 |
| 2D (HB)CB(CD)HD | sample_1 | isotropic | sample_conditions_1 |
| 2D (HB)CB(CDCE)HE | sample_1 | isotropic | sample_conditions_1 |
| 2D CG(CB)HB | sample_1 | isotropic | sample_conditions_1 |
| 2D CG(CD)HD | sample_1 | isotropic | sample_conditions_1 |
| 2D CG(CDCE)HE | sample_1 | isotropic | sample_conditions_1 |
| 3D CT-HMQC-COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D hisHCN | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
ARIA v2.0, Linge, O'Donoghue and Nilges - structure solution
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView v5, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking
VNMR v6.1C, Varian - collection
Molmol, Koradi, Billeter and Wuthrich - data analysis, graphic display
Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Th - structure analysis
CSI, Wishart, Sykes - data analysis
NMR spectrometers:
- Varian INOVA 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts