BMRB Entry 19186

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR19186

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Title:
Chemical shift assignments of a S72-S107 peptide of 18.5kDa murine myelin basic protein (MBP)
Deposition date:
2013-04-23
Original release date:
2013-08-16
Authors:
Vassall, Kenrick; Bessonov, Kyrylo; De Avila, Miguel; Polverini, Eugenia; Harauz, George
Citation:

Citation: Vassall, Kenrick; Bessonov, Kyrylo; De Avila, Miguel; Polverini, Eugenia; Harauz, George. "The Effects of Threonine Phosphorylation on the Stability and Dynamics of the Central Molecular Switch Region of 18.5-kDa Myelin Basic Protein."  PLoS ONE 8, e68175-e68175 (2013).
PubMed: 23861868

Assembly members:

Assembly members:
S72-S107, polymer, 36 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):
S72-S107: SQHGRTQDENPVVHFFKNIV TPRTPPPSQGKGRGLS

Data sets:
Data typeCount
13C chemical shifts114
15N chemical shifts34
1H chemical shifts70

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1S72-S107 peptide of 18.5 kDa MBP1

Entities:

Entity 1, S72-S107 peptide of 18.5 kDa MBP 36 residues - Formula weight is not available

1   SERGLNHISGLYARGTHRGLNASPGLUASN
2   PROVALVALHISPHEPHELYSASNILEVAL
3   THRPROARGTHRPROPROPROSERGLNGLY
4   LYSGLYARGGLYLEUSER

Samples:

sample_1: S72-S107 peptide of 18.5 kDa MBP, [U-100% 13C; U-100% 15N], 1.7 mM; HEPES 20 mM; sodium chloride 100 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 0.1 M; pH: 7.5; pressure: 1 atm; temperature: 295 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HACANsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

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

CARA, Keller and Wuthrich - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 15131 18520
PDB
DBJ BAB23830 BAC37705 BAE28256 BAE87162 BAE87443
EMBL CAA10804 CAA10805 CAA10806 CAA10807 CAA35179
GB AAA37720 AAA39496 AAA39497 AAA39499 AAA39500
REF NP_001020252 NP_001020261 NP_001020263 NP_001020272 NP_001020422
SP P02686 P02688 P04370 P06906
AlphaFold P02686 P02688 P04370 P06906

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