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 25838

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for the C-terminal intrinsically disordered domain of Alb3   PubMed: 26568381

Deposition date: 2015-10-06 Original release date: 2016-01-06

Authors: Sattler, Michael; Hennig, Janosch

Citation: Horn, Annemarie; Hennig, Janosch; Ahmed, Yasar; Stier, Gunter; Wild, Klemens; Sattler, Michael; Hennig, Janosch. "Structural basis for cpSRP43 chromodomain selectivity and dynamics in Alb3 insertase interaction"  Nat. Commun. 6, 8875-8875 (2015).

Assembly members:
Alb3-A3CT, polymer, 101 residues, Formula weight is not available

Natural source:   Common Name: Thale cress   Taxonomy ID: 3702   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Arabidopsis thaliana

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21d

Entity Sequences (FASTA):
Alb3-A3CT: MDENASKIISAGRAKRSIAQ PDDAGERFRQLKEQEKRSKK NKAVAKDTVELVEESQSESE EGSDDEEEEAREGALASSTT SKPLPEVGQRRSKRSKRKRT V

Data sets:
Data typeCount
13C chemical shifts153
15N chemical shifts79
1H chemical shifts119

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1A3CT monomer1

Entities:

Entity 1, A3CT monomer 101 residues - Formula weight is not available

1   METASPGLUASNALASERLYSILEILESER
2   ALAGLYARGALALYSARGSERILEALAGLN
3   PROASPASPALAGLYGLUARGPHEARGGLN
4   LEULYSGLUGLNGLULYSARGSERLYSLYS
5   ASNLYSALAVALALALYSASPTHRVALGLU
6   LEUVALGLUGLUSERGLNSERGLUSERGLU
7   GLUGLYSERASPASPGLUGLUGLUGLUALA
8   ARGGLUGLYALALEUALASERSERTHRTHR
9   SERLYSPROLEUPROGLUVALGLYGLNARG
10   ARGSERLYSARGSERLYSARGLYSARGTHR
11   VAL

Samples:

sample_1: Alb3-A3CT, [U-100% 13C; U-100% 15N], 0.45 mM; sodium phosphate 20 mM; sodium chloride 150 mM; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance III 800 MHz

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