BMRB Entry 19485
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19485
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Title: Chemical Shift Assignments for SVIP (small VCP/p97-interacting protein) PubMed: 24055875
Deposition date: 2013-09-10 Original release date: 2013-10-09
Authors: Wu, Jiawen; Peng, Dungeng; Voehler, Markus; Sanders, Charles; Li, Jun
Citation: Wu, Jiawen; Peng, Dungeng; Voehler, Markus; Sanders, Charles; Li, Jun. "Structure and expression of a novel compact myelin protein - small VCP-interacting protein (SVIP)." Biochem. Biophys. Res. Commun. 440, 173-178 (2013).
Assembly members:
SVIPM, polymer, 85 residues, 9475.68 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 Vector: pET22b(+)
Entity Sequences (FASTA):
SVIPM: MGLSFPSPGESAPPTPDLEE
KRAKLAEAAERRQKEAASRG
ILDVQSVQEKRKKKEKIEKQ
IATSGPPPEGGLRWTVSLEH
HHHHH
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 280 |
15N chemical shifts | 67 |
1H chemical shifts | 477 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | SVIP mutation | 1 |
Entities:
Entity 1, SVIP mutation 85 residues - 9475.68 Da.
Residues 78-85 represent a non-native affinity His-tag
1 | MET | GLY | LEU | SER | PHE | PRO | SER | PRO | GLY | GLU | ||||
2 | SER | ALA | PRO | PRO | THR | PRO | ASP | LEU | GLU | GLU | ||||
3 | LYS | ARG | ALA | LYS | LEU | ALA | GLU | ALA | ALA | GLU | ||||
4 | ARG | ARG | GLN | LYS | GLU | ALA | ALA | SER | ARG | GLY | ||||
5 | ILE | LEU | ASP | VAL | GLN | SER | VAL | GLN | GLU | LYS | ||||
6 | ARG | LYS | LYS | LYS | GLU | LYS | ILE | GLU | LYS | GLN | ||||
7 | ILE | ALA | THR | SER | GLY | PRO | PRO | PRO | GLU | GLY | ||||
8 | GLY | LEU | ARG | TRP | THR | VAL | SER | LEU | GLU | HIS | ||||
9 | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: SVIPM, [U-99% 13C; U-99% 15N], 0.4 0.6 mM; potassium phosphate 25 mM; EDTA 0.1 mM; sodium chloride 25 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 50 mM; pH: 5.0; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | 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 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Avance 600 MHz
Related Database Links:
GB | NM_148893 AAM88869 EAW68312 EAW68313 EAW68314 EAW68315 |
EMBL | CAH92580 |
REF | NP_001126513 NP_001248626 NP_683691 XP_001173949 XP_003254381 |
SP | Q5R6N0 Q8NHG7 |
AlphaFold | Q5R6N0 Q8NHG7 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts