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 19948

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   PubMed: 25343306

Authors: De Avila, Miguel; Vassall, Kenrick; Smith, Graham; Bamm, Vladimir; Harauz, George

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).

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

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

Entity Sequences (FASTA):
MBP_S38-S107_peptide: SIGRFFSGDRGAPKRGSGKD SHTRTTHYGSLPQKSQHGRT QDENPVVHFFKNIVTPRTPP PSQGKGRGLS

Data sets:
Data typeCount
13C chemical shifts164
15N chemical shifts62
1H chemical shifts63
T1 relaxation values57
T2 relaxation values57

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1MBP S38-S107 peptide1

Entities:

Entity 1, MBP S38-S107 peptide 70 residues - Formula weight is not available

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

Samples:

MBP_sample: MBP S38-S107 peptide, [U-100% 13C; U-100% 15N], 0.75 mM; D2O, [U-100% 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_sampleisotropicsample_conditions_1
3D HNCOMBP_sampleisotropicsample_conditions_1
3D HN(CA)COMBP_sampleisotropicsample_conditions_1
3D CBCA(CO)NHMBP_sampleisotropicsample_conditions_1
3D HNCACBMBP_sampleisotropicsample_conditions_1
3D HACANMBP_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

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