BMRB Entry 5044
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5044
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Title: 1H, 13C, and 15N Chemical shift assignments for the third Immunoglobulin domain from the neural cell adhesion molecule, N-CAM PubMed: 11469865
Deposition date: 2001-06-05 Original release date: 2001-11-14
Authors: Atkins, A.; Chung, J.; Deechongkit, S.; Little, E.; Edelman, G.; Wright, P.; Cunningham, B.; Dyson, H.
Citation: Atkins, A.; Chung, J.; Deechongkit, S.; Little, E.; Edelman, G.; Wright, P.; Cunningham, B.; Dyson, H.. "Solution Structure of the Third Immunoglobulin Domain of the Neural Cell Adhesion Molecule N-CAM: Can Solution Studies Define the Mechanism of Homophilic Binding?" J. Mol. Biol. 311, 161-172 (2001).
Assembly members:
Third Immunoglobulin domain of the Neural cell adhesion molecule, polymer, 107 residues, 11839 Da.
Natural source: Common Name: chicken Taxonomy ID: 9031 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: gallus gallus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Third Immunoglobulin domain of the Neural cell adhesion molecule: GKDIQVIVNVPPSVRARQST
MNATANLSQSVTLACDADGF
PEPTMTWTKDGEPIEQEDNE
EKYSFNYDGSELIIKKVDKS
DEAEYICIAENKAGEQDATI
HLKVFAK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 324 |
| 15N chemical shifts | 111 |
| 1H chemical shifts | 721 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | IgIII | 1 |
Entities:
Entity 1, IgIII 107 residues - 11839 Da.
| 1 | GLY | LYS | ASP | ILE | GLN | VAL | ILE | VAL | ASN | VAL | ||||
| 2 | PRO | PRO | SER | VAL | ARG | ALA | ARG | GLN | SER | THR | ||||
| 3 | MET | ASN | ALA | THR | ALA | ASN | LEU | SER | GLN | SER | ||||
| 4 | VAL | THR | LEU | ALA | CYS | ASP | ALA | ASP | GLY | PHE | ||||
| 5 | PRO | GLU | PRO | THR | MET | THR | TRP | THR | LYS | ASP | ||||
| 6 | GLY | GLU | PRO | ILE | GLU | GLN | GLU | ASP | ASN | GLU | ||||
| 7 | GLU | LYS | TYR | SER | PHE | ASN | TYR | ASP | GLY | SER | ||||
| 8 | GLU | LEU | ILE | ILE | LYS | LYS | VAL | ASP | LYS | SER | ||||
| 9 | ASP | GLU | ALA | GLU | TYR | ILE | CYS | ILE | ALA | GLU | ||||
| 10 | ASN | LYS | ALA | GLY | GLU | GLN | ASP | ALA | THR | ILE | ||||
| 11 | HIS | LEU | LYS | VAL | PHE | ALA | LYS |
Samples:
sample_1: Third Immunoglobulin domain of the Neural cell adhesion molecule, [U-15N; U-13C], 1.0 mM
sample_cond_1: ionic strength: 0 mM; pH*: 6.8; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D_13C-separated NOESY | sample_1 | not available | sample_cond_1 |
| 3D_15N-separated NOESY | sample_1 | not available | sample_cond_1 |
| HNHB | sample_1 | not available | sample_cond_1 |
| CGCN | sample_1 | not available | sample_cond_1 |
| CGCO | sample_1 | not available | sample_cond_1 |
Software:
NMRPipe v1.8 - processing
DYANA v1.5 - structure calculations
AMBER v7 - structure refinement
NMRView v3 - data analysis
SANE v1 - noe assignments
NMR spectrometers:
- Bruker AMX 500 MHz
Download simulated HSQC data in one of the following formats:
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