BMRB Entry 34026
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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/BMR34026
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Title: NMR solution structure of human FNIII domain 2 of NCAM PubMed: 27535221
Deposition date: 2016-07-22 Original release date: 2016-09-09
Authors: Slapsak, U.; Salzano, G.; Amin, L.; Abskharon, R.; Ilc, G.; Zupancic, B.; Biljan, I.; Plavec, J.; Giachin, G.; Legname, G.
Citation: Slapsak, U.; Salzano, G.; Amin, L.; Abskharon, R.; Ilc, G.; Zupancic, B.; Biljan, I.; Plavec, J.; Giachin, G.; Legname, G.. "The N Terminus of the Prion Protein Mediates Functional Interactions with the Neuronal Cell Adhesion Molecule (NCAM) Fibronectin Domain" J. Biol. Chem. 291, 21857-21868 (2016).
Assembly members:
Neural cell adhesion molecule 1, polymer, 103 residues, 11858.316 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):
Neural cell adhesion molecule 1: MQPVREPSAPKLEGQMGEDG
NSIKVNLIKQDDGGSPIRHY
LVRYRALSSEWKPEIRLPSG
SDHVMLKSLDWNAEYEVYVV
AENQQGKSKAAHFVFRTHHH
HHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 331 |
| 15N chemical shifts | 101 |
| 1H chemical shifts | 674 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 103 residues - 11858.316 Da.
| 1 | MET | GLN | PRO | VAL | ARG | GLU | PRO | SER | ALA | PRO | ||||
| 2 | LYS | LEU | GLU | GLY | GLN | MET | GLY | GLU | ASP | GLY | ||||
| 3 | ASN | SER | ILE | LYS | VAL | ASN | LEU | ILE | LYS | GLN | ||||
| 4 | ASP | ASP | GLY | GLY | SER | PRO | ILE | ARG | HIS | TYR | ||||
| 5 | LEU | VAL | ARG | TYR | ARG | ALA | LEU | SER | SER | GLU | ||||
| 6 | TRP | LYS | PRO | GLU | ILE | ARG | LEU | PRO | SER | GLY | ||||
| 7 | SER | ASP | HIS | VAL | MET | LEU | LYS | SER | LEU | ASP | ||||
| 8 | TRP | ASN | ALA | GLU | TYR | GLU | VAL | TYR | VAL | VAL | ||||
| 9 | ALA | GLU | ASN | GLN | GLN | GLY | LYS | SER | LYS | ALA | ||||
| 10 | ALA | HIS | PHE | VAL | PHE | ARG | THR | HIS | HIS | HIS | ||||
| 11 | HIS | HIS | HIS |
Samples:
sample_1: fibronectin type III domain 2, [U-99% 13C; U-99% 15N], 0.9 mM; D2O, [U-2H], 10%; H2O 90%; TBS 20 mM; sodium chloride 150 mM
sample_conditions_1: ionic strength: 150 mM; pH: 7.45; 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 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CC(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
Software:
CARA vv1.8.42, Keller and Wuthrich - chemical shift assignment
CING, Doreleijers JF - data analysis
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
PSVS, Bhattacharya and Montelione - data analysis
Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Thornton - data analysis
SPARKY, Goddard - peak picking
TALOS, Cornilescu, Delaglio and Bax - data analysis
VNMR, Varian - collection
YASARA, Elmar Krieger and Gert Vriend - refinement
NMR spectrometers:
- Varian VNMRS 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts