BMRB Entry 27119

Title:
SH2B1 SH2 Domain
Deposition date:
2017-05-30
Original release date:
2017-11-16
Authors:
McKercher, Marissa; Guan, Xiaoyang; Tan, Zhongping; Wuttke, Deborah
Citation:

Citation: McKercher, Marissa; Guan, Xiaoyang; Tan, Zhongping; Wuttke, Deborah. "Diversity in Peptide Recognition by the SH2 Domain of SH2B1"  Proteins 86, 164-176 (2018).
PubMed: 29127727

Assembly members:

Assembly members:
SH2B1_SH2_Domain, polymer, 114 residues, 12811.5 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: pET15b

Data sets:
Data typeCount
13C chemical shifts97
15N chemical shifts97
1H chemical shifts97

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SH2B1 SH2 Domain1

Entities:

Entity 1, SH2B1 SH2 Domain 114 residues - 12811.5 Da.

First four residues (GSHM) are carried over after thrombin protease cleavage of the 6X-His affinity tag

1   GLYSERHISMETASPGLNPROLEUSERGLY
2   TYRPROTRPPHEHISGLYMETLEUSERARG
3   LEULYSALAALAGLNLEUVALLEUTHRGLY
4   GLYTHRGLYSERHISGLYVALPHELEUVAL
5   ARGGLNSERGLUTHRARGARGGLYGLUTYR
6   VALLEUTHRPHEASNPHEGLNGLYLYSALA
7   LYSHISLEUARGLEUSERLEUASNGLUGLU
8   GLYGLNCYSARGVALGLNHISLEUTRPPHE
9   GLNSERILEPHEASPMETLEUGLUHISPHE
10   ARGVALHISPROILEPROLEUGLUSERGLY
11   GLYSERSERASPVALVALLEUVALSERTYR
12   VALPROSERSER

Samples:

sample_1: SH2B1 SH2 Domain, [U-100% 13C; U-100% 15N], 1 mM; TRIS 50 mM; sodium chloride 50 mM; EDTA 1 mM; DTT 1 mM; TSP 0.15 mM

sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

VNMRJ, Varian - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Oxford INOVA 600 MHz

Related Database Links:

UNP Q9NRF2-1
AlphaFold Q9Y3Y3

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