BMRB Entry 19949

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19949

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Title:
The proline-rich region of 18.5-kDa myelin basic protein requires long-range interactions with residues upstream to interact with the SH3-domain of Fyn
Deposition date:
2014-04-30
Original release date:
2019-07-11
Authors:
De Avila, Miguel; Vassall, Kenrick; Smith, Graham; Bamm, Vladimir; Harauz, George
Citation:

Citation: De Avila, Miguel; Vassall, Kenrick; Smith, Graham; Bamm, Vladimir; Harauz, George. "The proline-rich region of 18.5 kDa myelin basic protein binds to the SH3-domain of Fyn tyrosine kinase with the aid of an upstream segment to form a dynamic complex in vitro"  Biosci. Rep. 34, e00157-e00157 (2014).
PubMed: 25343306

Assembly members:

Assembly members:
MBP_S38-S107_peptide, polymer, 70 residues, Formula weight is not available
Fyn_SH3_domain, polymer, 80 residues, Formula weight is not available

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MBP_S38-S107_peptide: SIGRFFSGDRGAPKRGSGKD SHTRTTHYGSLPQKSQHGRT QDENPVVHFFKNIVTPRTPP PSQGKGRGLS
Fyn_SH3_domain: MVQISVTLFVALYDYEARTE DDLSFHKGEKFQILNSSEGD WWEARSLTTGETGYIPSNYV APVDRLDYKDDDDKHHHHHH

Data sets:
Data typeCount
13C chemical shifts164
15N chemical shifts62
1H chemical shifts63
T1 relaxation values56
T2 relaxation values56

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MBP peptide1
2Fyn peptide2

Entities:

Entity 1, MBP peptide 70 residues - Formula weight is not available

1   SERILEGLYARGPHEPHESERGLYASPARG
2   GLYALAPROLYSARGGLYSERGLYLYSASP
3   SERHISTHRARGTHRTHRHISTYRGLYSER
4   LEUPROGLNLYSSERGLNHISGLYARGTHR
5   GLNASPGLUASNPROVALVALHISPHEPHE
6   LYSASNILEVALTHRPROARGTHRPROPRO
7   PROSERGLNGLYLYSGLYARGGLYLEUSER

Entity 2, Fyn peptide 80 residues - Formula weight is not available

1   METVALGLNILESERVALTHRLEUPHEVAL
2   ALALEUTYRASPTYRGLUALAARGTHRGLU
3   ASPASPLEUSERPHEHISLYSGLYGLULYS
4   PHEGLNILELEUASNSERSERGLUGLYASP
5   TRPTRPGLUALAARGSERLEUTHRTHRGLY
6   GLUTHRGLYTYRILEPROSERASNTYRVAL
7   ALAPROVALASPARGLEUASPTYRLYSASP
8   ASPASPASPLYSHISHISHISHISHISHIS

Samples:

MBP+Fyn_sample: MBP S38-S107 peptide, [U-100% 13C; U-100% 15N], 675 mM; Fyn SH3 domain 675 mM; D2O, [U-2H], 10%; HEPES-NaOH 20 mM; NaCl 100 mM; H2O 90%

sample_conditions_1: ionic strength: 0.1 M; pH: 7.4; pressure: 1 atm; temperature: 295 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCMBP+Fyn_sampleisotropicsample_conditions_1
3D HNCOMBP+Fyn_sampleisotropicsample_conditions_1
3D HN(CA)COMBP+Fyn_sampleisotropicsample_conditions_1
3D CBCA(CO)NHMBP+Fyn_sampleisotropicsample_conditions_1
3D HNCACBMBP+Fyn_sampleisotropicsample_conditions_1
3D HACANMBP+Fyn_sampleisotropicsample_conditions_1

Software:

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

TOPSPIN, Bruker Biospin - collection

SPARKY, Goddard - data analysis

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 600 MHz

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