BMRB Entry 16638
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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/BMR16638
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Title: Solution Structure of human sodium/ hydrogen exchange regulatory factor 1(150-358). PubMed: 20042604
Deposition date: 2009-12-18 Original release date: 2010-02-01
Authors: Bhattacharya, Shibani; Dai, Zhongping; Li, Jianquan; Baxter, Sabine; Callaway, David; Cowburn, David; Bu, Zimei
Citation: Bhattacharya, Shibani; Dai, Zhongping; Li, Jianquan; Baxter, Sabine; Callaway, David; Cowburn, David; Bu, Zimei. "A conformational switch in the scaffolding protein NHERF1 controls autoinhibition and complex formation." J. Biol. Chem. 285, 9981-9994 (2010).
Assembly members:
NHERF1_(150-358), polymer, 216 residues, 23669.648 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):
NHERF1_(150-358): GIDPFTMLRPRLCTMKKGPS
GYGFNLHSDKSKPGQFIRSV
DPDSPAEASGLRAQDRIVEV
NGVCMEGKQHGDVVSAIRAG
GDETKLLVVDRETDEFFKKC
RVIPSQEHLNGPLPVPFTNG
EIQKENSREALAEAALESPR
PALVRSASSDTSEELNSQDS
PPKQDSTAPSSTSSSDPILD
FNISLAMAKERAHQKRSSKR
APQMDWSKKNELFSNL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 758 |
| 15N chemical shifts | 174 |
| 1H chemical shifts | 1241 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NHERF1_(150-358) | 1 |
Entities:
Entity 1, NHERF1_(150-358) 216 residues - 23669.648 Da.
Residues 1-7 represent a non-native affinity tag
| 1 | GLY | ILE | ASP | PRO | PHE | THR | MET | LEU | ARG | PRO | ||||
| 2 | ARG | LEU | CYS | THR | MET | LYS | LYS | GLY | PRO | SER | ||||
| 3 | GLY | TYR | GLY | PHE | ASN | LEU | HIS | SER | ASP | LYS | ||||
| 4 | SER | LYS | PRO | GLY | GLN | PHE | ILE | ARG | SER | VAL | ||||
| 5 | ASP | PRO | ASP | SER | PRO | ALA | GLU | ALA | SER | GLY | ||||
| 6 | LEU | ARG | ALA | GLN | ASP | ARG | ILE | VAL | GLU | VAL | ||||
| 7 | ASN | GLY | VAL | CYS | MET | GLU | GLY | LYS | GLN | HIS | ||||
| 8 | GLY | ASP | VAL | VAL | SER | ALA | ILE | ARG | ALA | GLY | ||||
| 9 | GLY | ASP | GLU | THR | LYS | LEU | LEU | VAL | VAL | ASP | ||||
| 10 | ARG | GLU | THR | ASP | GLU | PHE | PHE | LYS | LYS | CYS | ||||
| 11 | ARG | VAL | ILE | PRO | SER | GLN | GLU | HIS | LEU | ASN | ||||
| 12 | GLY | PRO | LEU | PRO | VAL | PRO | PHE | THR | ASN | GLY | ||||
| 13 | GLU | ILE | GLN | LYS | GLU | ASN | SER | ARG | GLU | ALA | ||||
| 14 | LEU | ALA | GLU | ALA | ALA | LEU | GLU | SER | PRO | ARG | ||||
| 15 | PRO | ALA | LEU | VAL | ARG | SER | ALA | SER | SER | ASP | ||||
| 16 | THR | SER | GLU | GLU | LEU | ASN | SER | GLN | ASP | SER | ||||
| 17 | PRO | PRO | LYS | GLN | ASP | SER | THR | ALA | PRO | SER | ||||
| 18 | SER | THR | SER | SER | SER | ASP | PRO | ILE | LEU | ASP | ||||
| 19 | PHE | ASN | ILE | SER | LEU | ALA | MET | ALA | LYS | GLU | ||||
| 20 | ARG | ALA | HIS | GLN | LYS | ARG | SER | SER | LYS | ARG | ||||
| 21 | ALA | PRO | GLN | MET | ASP | TRP | SER | LYS | LYS | ASN | ||||
| 22 | GLU | LEU | PHE | SER | ASN | LEU |
Samples:
sample_1: NHERF1 (150-358), [U-100% 13C; U-100% 15N], 557 uM; HEPES 20 mM; sodium chloride 150 mM; DTT 0.5 mM; PMSF 0.1 mM; D2O 10%
sample_2: NHERF1 (150-358), [U-100% 13C; U-100% 15N; U-80% 2H], 389 uM; HEPES 20 mM; sodium chloride 150 mM; DTT 0.5 mM; PMSF 0.1 mM; D2O 10%
sample_3: NHERF1 (150-358), [U-100% 13C; U-100% 15N]-Leu,Val,Phe, 413 uM; HEPES 20 mM; sodium chloride 150 mM; DTT 0.5 mM; PMSF 0.1 mM; D2O 10%
sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | 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 HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_3 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1.3, Bruker Biospin - collection, processing
CARA v1.5, Keller and Wuthrich - chemical shift assignment, data analysis
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
X-PLOR NIH v2.24, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution
NMR spectrometers:
- Bruker Avance 900 MHz
- Bruker Avance 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts