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 27102

Title: Backbone assignments for the Val66 prodomain of BDNF   PubMed: 28933046

Deposition date: 2017-05-09 Original release date: 2021-07-22

Authors: Wang, Jing; Bracken, Clay; Bains, Henrietta; Anastasia, Agustin

Citation: Wang, Jing; Bains, Henrietta; Anastasia, Agustin; Bracken, Clay. "NMR backbone resonance assignments of the prodomain variants of BDNF in the urea denatured state"  Biomol. NMR Assign. 12, 43-45 (2018).

Assembly members:
Val66_BDNF_Prodomain, polymer, 112 residues, Formula weight is not available

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28

Entity Sequences (FASTA):
Val66_BDNF_Prodomain: SMAPMKEANIRGQGGLAYPG VRTHGTLESVNGPKAGSRGL TSLADTFEHVIEELLDEDQK VRPNEENNKDADLYTSRVML SSQVPLEPPLLFLLEEYKNY LDAANMSMRVRR

Data sets:
Data typeCount
13C chemical shifts303
15N chemical shifts102
1H chemical shifts102

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Val66 BDNF Prodomain1

Entities:

Entity 1, Val66 BDNF Prodomain 112 residues - Formula weight is not available

1   SERMETALAPROMETLYSGLUALAASNILE
2   ARGGLYGLNGLYGLYLEUALATYRPROGLY
3   VALARGTHRHISGLYTHRLEUGLUSERVAL
4   ASNGLYPROLYSALAGLYSERARGGLYLEU
5   THRSERLEUALAASPTHRPHEGLUHISVAL
6   ILEGLUGLULEULEUASPGLUASPGLNLYS
7   VALARGPROASNGLUGLUASNASNLYSASP
8   ALAASPLEUTYRTHRSERARGVALMETLEU
9   SERSERGLNVALPROLEUGLUPROPROLEU
10   LEUPHELEULEUGLUGLUTYRLYSASNTYR
11   LEUASPALAALAASNMETSERMETARGVAL
12   ARGARG

Samples:

sample_1: Val66 BDNF Prodomain, [U-95% 13C; U-95% 15N], 0.3 mM; urea 2 M; sodium chloride 100 mM; TRIS 10 mM; glycine 10 mM; PIPES 10 mM; DSS 0.1 mM; D2O 7%; H2O 93%; EDTA 0.5 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.2; pressure: 1 atm; temperature: 278 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1

Software:

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

SPARKY, Goddard - 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 shifts
SPARKY: Backbone or all simulated shifts