BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 34026

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

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

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 103 residues - 11858.316 Da.

1   METGLNPROVALARGGLUPROSERALAPRO
2   LYSLEUGLUGLYGLNMETGLYGLUASPGLY
3   ASNSERILELYSVALASNLEUILELYSGLN
4   ASPASPGLYGLYSERPROILEARGHISTYR
5   LEUVALARGTYRARGALALEUSERSERGLU
6   TRPLYSPROGLUILEARGLEUPROSERGLY
7   SERASPHISVALMETLEULYSSERLEUASP
8   TRPASNALAGLUTYRGLUVALTYRVALVAL
9   ALAGLUASNGLNGLNGLYLYSSERLYSALA
10   ALAHISPHEVALPHEARGTHRHISHISHIS
11   HISHISHIS

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D CC(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_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