BMRB Entry 15512
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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/BMR15512
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Title: 1H, 13C, and 15N NMR chemical shift assignments of the palladin Ig3 domain PubMed: 19636923
Deposition date: 2007-10-08 Original release date: 2008-03-31
Authors: Dixon, Richard; Rachlin, Andrew; Otey, Carol; Campbell, Sharon
Citation: Dixon, Richard; Campbell, Sharon. "1H, 15N, and 13C NMR chemical shift assignments for the Ig3 domain of palladin" Biomol. NMR Assignments 2, 51-53 (2008).
Assembly members:
Palladin_Ig3_domain, polymer, 108 residues, 11975 Da.
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Palladin_Ig3_domain: GGSNATAPFFEMKLKHYKIF
EGMPVTFTCRVAGNPKPKIY
WFKDGKQISPKSDHYTIQRD
LDGTCSLHTTASTLDDDGNY
TIMAANPQGRVSCTGRLMVQ
AVNQRGRS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 455 |
| 15N chemical shifts | 112 |
| 1H chemical shifts | 701 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | molecule 1 | 1 |
Entities:
Entity 1, molecule 1 108 residues - 11975 Da.
Residues 1-3 are non-native amino acids resulting from the cloning and purification strategy
| 1 | GLY | GLY | SER | ASN | ALA | THR | ALA | PRO | PHE | PHE | ||||
| 2 | GLU | MET | LYS | LEU | LYS | HIS | TYR | LYS | ILE | PHE | ||||
| 3 | GLU | GLY | MET | PRO | VAL | THR | PHE | THR | CYS | ARG | ||||
| 4 | VAL | ALA | GLY | ASN | PRO | LYS | PRO | LYS | ILE | TYR | ||||
| 5 | TRP | PHE | LYS | ASP | GLY | LYS | GLN | ILE | SER | PRO | ||||
| 6 | LYS | SER | ASP | HIS | TYR | THR | ILE | GLN | ARG | ASP | ||||
| 7 | LEU | ASP | GLY | THR | CYS | SER | LEU | HIS | THR | THR | ||||
| 8 | ALA | SER | THR | LEU | ASP | ASP | ASP | GLY | ASN | TYR | ||||
| 9 | THR | ILE | MET | ALA | ALA | ASN | PRO | GLN | GLY | ARG | ||||
| 10 | VAL | SER | CYS | THR | GLY | ARG | LEU | MET | VAL | GLN | ||||
| 11 | ALA | VAL | ASN | GLN | ARG | GLY | ARG | SER |
Samples:
sample_1: Palladin Ig3 domain, [U-98% 13C; U-98% 15N], 0.3-1.8 mM; D2O 10%; H2O 90%; TRIS 50 mM; sodium chloride 150 mM; DTT 2 mM
sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC (aliphatic) | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HC(CO)NH TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY (aliphatic) | sample_1 | isotropic | sample_conditions_1 |
| HBCBCGCDHD | sample_1 | isotropic | sample_conditions_1 |
| HBCBCGCDCEHE | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC (aromatic) | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY (aromatic) | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRView v5.2.2.01, Johnson, One Moon Scientific - chemical shift assignment
NMR spectrometers:
- Varian INOVA 700 MHz
- 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