BMRB Entry 34026

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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

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Title:
NMR solution structure of human FNIII domain 2 of NCAM
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:

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).
PubMed: 27535221

Assembly members:

Assembly members:
Neural cell adhesion molecule 1, polymer, 103 residues, 11858.316 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Neural cell adhesion molecule 1: MQPVREPSAPKLEGQMGEDG NSIKVNLIKQDDGGSPIRHY LVRYRALSSEWKPEIRLPSG SDHVMLKSLDWNAEYEVYVV AENQQGKSKAAHFVFRTHHH HHH

Data sets:
Data typeCount
13C chemical shifts331
15N chemical shifts101
1H chemical shifts674

Additional metadata:

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