BMRB Entry 17626
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR17626
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Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for Act2-EF34 in complex with palladin peptide PubMed: 21925511
Deposition date: 2011-05-05 Original release date: 2011-10-12
Authors: Beck, Moriah; Campbell, Sharon
Citation: Beck, Moriah; Otey, Carol; Campbell, Sharon. "Structural characterization of the interactions between palladin and -actinin." J. Mol. Biol. 413, 712-725 (2011).
Assembly members:
Act2-EF34, polymer, 75 residues, 8071.05 Da.
palladin, polymer, 17 residues, 1777 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):
Act2-EF34: GAMADTDTAEQVIASFRILA
SDKPYILAEELRRELPPDQA
QYCIKRMPAYSGPGSVPGAL
DYAAFSSALYGESDL
palladin: HGQTPAAFLSALLPSQP
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 103 |
15N chemical shifts | 54 |
1H chemical shifts | 54 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | protein | 1 |
2 | ligand | 2 |
Entities:
Entity 1, protein 75 residues - 8071.05 Da.
1 | GLY | ALA | MET | ALA | ASP | THR | ASP | THR | ALA | GLU | ||||
2 | GLN | VAL | ILE | ALA | SER | PHE | ARG | ILE | LEU | ALA | ||||
3 | SER | ASP | LYS | PRO | TYR | ILE | LEU | ALA | GLU | GLU | ||||
4 | LEU | ARG | ARG | GLU | LEU | PRO | PRO | ASP | GLN | ALA | ||||
5 | GLN | TYR | CYS | ILE | LYS | ARG | MET | PRO | ALA | TYR | ||||
6 | SER | GLY | PRO | GLY | SER | VAL | PRO | GLY | ALA | LEU | ||||
7 | ASP | TYR | ALA | ALA | PHE | SER | SER | ALA | LEU | TYR | ||||
8 | GLY | GLU | SER | ASP | LEU |
Entity 2, ligand 17 residues - 1777 Da.
Residues 235-252 of 90kDa (isoform #4) of palladin
1 | HIS | GLY | GLN | THR | PRO | ALA | ALA | PHE | LEU | SER | ||||
2 | ALA | LEU | LEU | PRO | SER | GLN | PRO |
Samples:
sample_1: Act2-EF34, [U-100% 15N], 0.2 0.5 mM; palladin0.5 2 mM; D2O 10%; sodium azide 0.05 mM; TCEP2 5 mM; MOPS 20 mM; sodium chloride 10 mM; H2O 90%
sample_2: Act2-EF34, [U-100% 13C; U-100% 15N], 0.2 0.5 mM; palladin0.5 2 mM; D2O 10%; sodium azide 0.05 mM; TCEP2 5 mM; MOPS 20 mM; sodium chloride 10 mM; H2O 90%
sample_conditions_1: ionic strength: 0.01 M; pH: 6.6; pressure: 1 atm; temperature: 300 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
3D HNCO | sample_2 | isotropic | sample_conditions_1 |
3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
Software:
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRViewJ v8.1, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking
NMR spectrometers:
- Varian INOVA 600 MHz
- Varian INOVA 700 MHz
- Varian INOVA 700 MHz
Related Database Links:
BMRB | 17627 4453 4454 |
PDB | |
DBJ | BAB22865 BAD92758 BAG37672 BAH11921 BAH12587 BAA76836 BAG09933 |
EMBL | CAB61269 |
GB | AAA51583 AAF76325 AAH47901 AAH51770 AAH89579 AAG00079 EDL87206 |
REF | NP_001029807 NP_001094 NP_001163796 NP_001230595 NP_001265272 XP_004852973 XP_004852974 XP_005003446 XP_005369855 XP_005369857 |
SP | P35609 Q3ZC55 Q9JI91 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts