BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 6575

Title: Backbone and side-chain chemical shift assignments for Human Nck2 SH2 domain   PubMed: 15764601

Deposition date: 2005-04-01 Original release date: 2005-06-02

Authors: Ran, Xiaoyuan; Song, Jianxing

Citation: Ran, Xiaoyuan; Song, Jianxing. "Structural Insight into the Binding Diversity between the Tyr-phosphorylated Human EphrinBs and Nck2 SH2 Domain."  J. Biol. Chem. 280, 19205-19212 (2005).

Assembly members:
Nck2 SH2 domain, polymer, 98 residues, Formula weight is not available

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

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
Nck2 SH2 domain: REWYYGNVTRHQAECALNER GVEGDFLIRDSESSPSDFSV SLKASGKNKHFKVQLVDNVY CIGQRRFHTMDELVEHYKKA PIFTSEHGEKLYLVRALQ

Data sets:
Data typeCount
13C chemical shifts370
15N chemical shifts92
1H chemical shifts433

Additional metadata:

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  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Nck2 SH2 domain1

Entities:

Entity 1, Nck2 SH2 domain 98 residues - Formula weight is not available

1   ARGGLUTRPTYRTYRGLYASNVALTHRARG
2   HISGLNALAGLUCYSALALEUASNGLUARG
3   GLYVALGLUGLYASPPHELEUILEARGASP
4   SERGLUSERSERPROSERASPPHESERVAL
5   SERLEULYSALASERGLYLYSASNLYSHIS
6   PHELYSVALGLNLEUVALASPASNVALTYR
7   CYSILEGLYGLNARGARGPHEHISTHRMET
8   ASPGLULEUVALGLUHISTYRLYSLYSALA
9   PROILEPHETHRSERGLUHISGLYGLULYS
10   LEUTYRLEUVALARGALALEUGLN