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Biological Magnetic Resonance Data Bank


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BMRB Entry 51342

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51342
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Title: SH2 domain from mouse SH2B1   PubMed: 37311460

Deposition date: 2022-03-01 Original release date: 2023-05-19

Authors: Fowler, Nicholas; Albalwi, Marym; Lee, Subin; Hounslow, Andrea; Williamson, Mike

Citation: Fowler, Nicholas; Albalwi, Marym; Lee, Subin; Hounslow, Andrea; Williamson, Mike. "Improved methodology for protein NMR structure calculation using hydrogen bond restraints and ANSURR validation: The SH2 domain of SH2B1"  Structure 31, 975-986 (2023).

Assembly members:
entity_1, polymer, 119 residues, 13664 Da.

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-4

Entity Sequences (FASTA):
entity_1: MKIHHHHHHDQPLSGYPWFH GMLSRLKAAQLVLEGGTGSH GVFLVRQSETRRGEYVLTFN FQGKAKHLRLSLNEEGQCRV QHLWFQSIFDMLEHFRVHPI PLESGGSSDVVLVSYVPSQ

Data sets:
Data typeCount
13C chemical shifts541
15N chemical shifts140
1H chemical shifts843

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1SH2 domain1

Entities:

Entity 1, SH2 domain 119 residues - 13664 Da.

This sequence corresponds to residues 519-628 from mouse SH2B1 (Uniprot Q91ZM2) with the addition of a 9-residue His tag at the N terminus. Thus the first included residue of the mouse sequence (D519) is Asp-10.

1   METLYSILEHISHISHISHISHISHISASP
2   GLNPROLEUSERGLYTYRPROTRPPHEHIS
3   GLYMETLEUSERARGLEULYSALAALAGLN
4   LEUVALLEUGLUGLYGLYTHRGLYSERHIS
5   GLYVALPHELEUVALARGGLNSERGLUTHR
6   ARGARGGLYGLUTYRVALLEUTHRPHEASN
7   PHEGLNGLYLYSALALYSHISLEUARGLEU
8   SERLEUASNGLUGLUGLYGLNCYSARGVAL
9   GLNHISLEUTRPPHEGLNSERILEPHEASP
10   METLEUGLUHISPHEARGVALHISPROILE
11   PROLEUGLUSERGLYGLYSERSERASPVAL
12   VALLEUVALSERTYRVALPROSERGLN

Samples:

sample_1: SH2, [U-100% 13C; U-100% 15N], 1 ± 0.05 mM; potassium phosphate 100 ± 1 mM; DSS 1 ± 0.05 mM

sample_conditions_1: ionic strength: 200 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_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
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HC(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
2D HBCBCGCDHDsample_1isotropicsample_conditions_1
2D HBCBCGCDCEHEsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v4.05 - collection

Felix - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE NEO 800 MHz

Related Database Links:

UNP Q91ZM2
AlphaFold Q9WVM5

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