BMRB Entry 34026
Click here to enlarge.
PDB ID: 5lkn
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
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
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:
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts