BMRB Entry 7036

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PDB ID: 2fry
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR7036
MolProbity Validation Chart

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Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for 3rd SH3 domain of human NCK2 adaptor protein
Deposition date:
2006-03-29
Original release date:
2011-08-11
Authors:
Liu, Jingxian
Citation:

Citation: Liu, Jingxian; Li, Minfen; Ran, Xiaoyuan; Fan, Jing-song; Song, Jianxing. "Structural Insight into the Binding Diversity between the Human Nck2 SH3 Domains and Proline-Rich Proteins(,)"  Biochemistry 45, 7171-7184 (2006).
PubMed: 16752908

Assembly members:

Assembly members:
NCK2 3rd SH3, polymer, 61 residues, 6822 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   Vector: pET32a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NCK2 3rd SH3: GSHVVQTLYPFSSVTEEELN FEKGETMEVIEKPENDPEWW KCKNARGQVGLVPKNYVVVL S

Data sets:
Data typeCount
13C chemical shifts177
15N chemical shifts55
1H chemical shifts338
T1 relaxation values54
T2 relaxation values54

Additional metadata:

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Assembly:

Entity Assembly IDEntity NameEntity ID
1NCK2 3rd SH31

Entities:

Entity 1, NCK2 3rd SH3 61 residues - 6822 Da.

1   GLYSERHISVALVALGLNTHRLEUTYRPRO
2   PHESERSERVALTHRGLUGLUGLULEUASN
3   PHEGLULYSGLYGLUTHRMETGLUVALILE
4   GLULYSPROGLUASNASPPROGLUTRPTRP
5   LYSCYSLYSASNALAARGGLYGLNVALGLY
6   LEUVALPROLYSASNTYRVALVALVALLEU
7   SER

Related Database Links:

PDB 1U5S 1WX6 2FRY
GB AAC04831 AAY24332 EPQ18601
PIR B46243
REF XP_006103064

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks