BMRB Entry 15084
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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/BMR15084
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Title: NMR structure of cl-BABP complexed to chenodeoxycholic acid PubMed: 17929837
Deposition date: 2006-12-22 Original release date: 2008-02-11
Authors: Eliseo, Tommaso; Ragona, Laura; Catalano, Maddalena; Assfalf, Michael; Paci, Maurizio; Zetta, Lucia; Molinari, Henriette; Cicero, Daniel
Citation: Eliseo, Tommaso; Ragona, Laura; Catalano, Maddalena; Assfalf, Michael; Paci, Maurizio; Zetta, Lucia; Molinari, Henriette; Cicero, Daniel. "Structural and dynamic determinants of ligand binding in the ternary complex of chicken liver bile acid binding protein with two bile salts revealed by NMR." Biochemistry 46, 12557-12567 (2007).
Assembly members:
cl-BABP, polymer, 125 residues, 392.572 Da.
JN3, non-polymer, 392.572 Da.
Natural source: Common Name: chicken Taxonomy ID: 9031 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Gallus gallus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
cl-BABP: AFSGTWQVYAQENYEEFLKA
LALPEDLIKMARDIKPIVEI
QQKGDDFVVTSKTPRQTVTN
SFTLGKEADITTMDGKKLKC
TVHLANGKLVTKSEKFSHEQ
EVKGNEMVETITFGGVTLIR
RSKRV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 596 |
| 15N chemical shifts | 123 |
| 1H chemical shifts | 898 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | cl-BABP | 1 |
| 2 | CDA-1 | 2 |
| 3 | CDA-2 | 2 |
Entities:
Entity 1, cl-BABP 125 residues - 392.572 Da.
| 1 | ALA | PHE | SER | GLY | THR | TRP | GLN | VAL | TYR | ALA | ||||
| 2 | GLN | GLU | ASN | TYR | GLU | GLU | PHE | LEU | LYS | ALA | ||||
| 3 | LEU | ALA | LEU | PRO | GLU | ASP | LEU | ILE | LYS | MET | ||||
| 4 | ALA | ARG | ASP | ILE | LYS | PRO | ILE | VAL | GLU | ILE | ||||
| 5 | GLN | GLN | LYS | GLY | ASP | ASP | PHE | VAL | VAL | THR | ||||
| 6 | SER | LYS | THR | PRO | ARG | GLN | THR | VAL | THR | ASN | ||||
| 7 | SER | PHE | THR | LEU | GLY | LYS | GLU | ALA | ASP | ILE | ||||
| 8 | THR | THR | MET | ASP | GLY | LYS | LYS | LEU | LYS | CYS | ||||
| 9 | THR | VAL | HIS | LEU | ALA | ASN | GLY | LYS | LEU | VAL | ||||
| 10 | THR | LYS | SER | GLU | LYS | PHE | SER | HIS | GLU | GLN | ||||
| 11 | GLU | VAL | LYS | GLY | ASN | GLU | MET | VAL | GLU | THR | ||||
| 12 | ILE | THR | PHE | GLY | GLY | VAL | THR | LEU | ILE | ARG | ||||
| 13 | ARG | SER | LYS | ARG | VAL |
Entity 2, CDA-1 - C24 H40 O4 - 392.572 Da.
| 1 | JN3 |
Samples:
sample_1: cl-BABP, [U-100% 13C; U-100% 15N], 1.2 mM; CDA 3 mM; H2O 90%; D2O 10%
sample_2: cl-BABP, [U-100% 13C; U-100% 15N], 1.2 mM; CDA 3 mM; H2O 100%
sample_3: cl-BABP, [U-100% 13C; U-100% 15N], 1.2 mM; CDA 3 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.15 M; pH: 7.0; pressure: 1 atm; temperature: 298 K
sample_conditions_2: ionic strength: 0.15 M; pH: 7.0; pressure: 1 atm; temperature: 298 K
sample_conditions_3: ionic strength: 0.45 M; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY | sample_2 | isotropic | sample_conditions_2 |
| 3D H(C)CH-TOCSY | sample_2 | isotropic | sample_conditions_2 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 13C-edited 13C-filtered NOESY | sample_2 | isotropic | sample_conditions_2 |
Software:
xwinnmr, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution
NMRView, Johnson, One Moon Scientific - data analysis
NMR spectrometers:
- Bruker Avance 700 MHz
- Bruker Avance 400 MHz
- Bruker Avance 500 MHz
Related Database Links:
| BMRB | 15854 16309 16310 16458 17767 |
| PDB | |
| GB | AAK58094 ADE59142 ADE59143 ADE59144 ADE59145 |
| PRF | 2106165A |
| REF | NP_989965 |
| SP | P80226 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts