BMRB Entry 15933
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15933
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Citation: Vasudevan, Sheeja; Schulz, Jessica; Zhou, Chunyi; Cocco, Melanie. "Protein folding at the membrane interface, the structure of Nogo-66 requires interactions with a phosphocholine surface." Proc. Natl. Acad. Sci. U.S.A. 107, 6847-6851 (2010).
PubMed: 20351248
Assembly members:
NOGO, polymer, 79 residues, Formula weight is not available
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 Vector: pET28b
Entity Sequences (FASTA):
NOGO: MHHHHHHLVPRGMRIYKGVI
QAIQKSDEGHPFRAYLESEV
AISEELVQKYSNSALGHVNS
TIKELRRLFLVDDLVDSLK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 200 |
| 15N chemical shifts | 67 |
| 1H chemical shifts | 432 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NOGO | 1 |
Entities:
Entity 1, NOGO 79 residues - Formula weight is not available
| 1 | MET | HIS | HIS | HIS | HIS | HIS | HIS | LEU | VAL | PRO | ||||
| 2 | ARG | GLY | MET | ARG | ILE | TYR | LYS | GLY | VAL | ILE | ||||
| 3 | GLN | ALA | ILE | GLN | LYS | SER | ASP | GLU | GLY | HIS | ||||
| 4 | PRO | PHE | ARG | ALA | TYR | LEU | GLU | SER | GLU | VAL | ||||
| 5 | ALA | ILE | SER | GLU | GLU | LEU | VAL | GLN | LYS | TYR | ||||
| 6 | SER | ASN | SER | ALA | LEU | GLY | HIS | VAL | ASN | SER | ||||
| 7 | THR | ILE | LYS | GLU | LEU | ARG | ARG | LEU | PHE | LEU | ||||
| 8 | VAL | ASP | ASP | LEU | VAL | ASP | SER | LEU | LYS |
Samples:
sample_1: NOGO 0.5-1.0 mM; NOGO, [U-100% 15N], 0.5-1.0 mM; NOGO, [U-100% 13C], 0.5 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.0 M; pH: 4.0; pressure: 1 atm; temperature: 308.15 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | 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 HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | 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 HNHA | sample_1 | isotropic | sample_conditions_1 |
Software:
X-PLOR NIH v2.20, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution
ANALYSIS v1.0.15, CCPN - chemical shift assignment, data analysis, peak picking
NMRDraw v2.2, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Varian INOVA 800 MHz
Related Database Links:
| BMRB | 16257 |
| PDB | |
| DBJ | BAA74909 BAA83712 BAB18927 BAB18928 BAC75974 |
| EMBL | CAB71027 CAB71028 CAB99248 CAB99249 CAH93187 |
| GB | AAD31019 AAD31020 AAD31021 AAG12176 AAG12177 |
| REF | NP_001106692 NP_001126875 NP_001192056 NP_065393 NP_114019 |
| SP | Q99P72 Q9JK11 Q9NQC3 |
| TPG | DAA24679 |
| AlphaFold | Q99P72 Q9JK11 Q9NQC3 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks