BMRB Entry 16462
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16462
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Title: Ligand-induced changes in dynamics in the RT loop of the C-terminal SH3 domain of Sem-5 indicate cooperative conformational coupling PubMed: 12717021
Deposition date: 2009-08-19 Original release date: 2010-03-08
Authors: Ferreon, Josephine; Hilser, Vincent
Citation: Ferreon, Josephine; Hilser, Vincent. "Ligand-induced changes in dynamics in the RT loop of the C-terminal SH3 domain of Sem-5 indicate cooperative conformational coupling" Protein Sci. 12, 982-996 (2003).
Assembly members:
Sem-5, polymer, 58 residues, Formula weight is not available
Sos_peptide, polymer, 10 residues, Formula weight is not available
Natural source: Common Name: Caenorhabditis elegans Taxonomy ID: 6239 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Caenorhabditis elegans
Experimental source: Production method: purified from the natural source Host organism: Escherichia coli
Entity Sequences (FASTA):
Sem-5: ETKFVQALFDFNPQESGELA
FKRGDVITLINKDDPNWWEG
QLNNRRGIFPSNYVAPYN
Sos_peptide: XPPPVPPRRR
- binding_constants
| Data type | Count |
| binding constants | 1 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Sem-5 | 1 |
| 2 | Sos peptide | 2 |
Entities:
Entity 1, Sem-5 58 residues - Formula weight is not available
| 1 | GLU | THR | LYS | PHE | VAL | GLN | ALA | LEU | PHE | ASP | ||||
| 2 | PHE | ASN | PRO | GLN | GLU | SER | GLY | GLU | LEU | ALA | ||||
| 3 | PHE | LYS | ARG | GLY | ASP | VAL | ILE | THR | LEU | ILE | ||||
| 4 | ASN | LYS | ASP | ASP | PRO | ASN | TRP | TRP | GLU | GLY | ||||
| 5 | GLN | LEU | ASN | ASN | ARG | ARG | GLY | ILE | PHE | PRO | ||||
| 6 | SER | ASN | TYR | VAL | ALA | PRO | TYR | ASN |
Entity 2, Sos peptide 10 residues - Formula weight is not available
| 1 | ACE | PRO | PRO | PRO | VAL | PRO | PRO | ARG | ARG | ARG |
Samples:
sample_1: Sem-5, [U-15N], 0.66 mM; NaOAc 50 mM; sodium chloride 100 mM; calcium chloride 10 mM; Sos peptide0 – 1.32 mM; D2O 10%; H2O 90%
sample_2: Sem-5, [U-15N], 0.66 mM; NaOAc 50 mM; sodium chloride 100 mM; calcium chloride 10 mM; Sos peptide 1.32 mM; D2O 10%; H2O 90%
sample_3: Sem-5, [U-15N], 0.66 mM; NaOAc 50 mM; sodium chloride 100 mM; calcium chloride 10 mM; D2O 10%; H2O 90%
sample_conditions_1: pH: 4.8; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_3 | isotropic | sample_conditions_1 |
Software:
FELIX v98, Accelrys Software Inc. - processing
Modelfree_4.01, (Columbia University. http://cpmcnet.columbia.edu/dept/gsas/biochem/labs/palmer) - statistical tests
Molmol v2K.1, Koradi, Billeter and Wuthrich - visualization
NMR spectrometers:
- Varian UnityPlus 400 MHz
Related Database Links:
| PDB |