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BMRB Entry 50274

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50274

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Title: Orb2A Prion Like Domain

Deposition date: 2020-05-15 Original release date: 2020-10-21

Authors: Laurents, Douglas; Oroz, Javier

Citation: Oroz, Javier; Sousa Felix, Sara; Cabrito, Eurico; Laurents, Douglas. "pH Changes Trigger Structural Transitions in Drosophila Orb2A PLD Relevant for Functional Aggregation in Memory Consolidation"  J. Biol. Chem. ., .-..

Assembly members:
entity_1, polymer, 90 residues, 10081 Da.

Natural source:   Common Name: fruit fly   Taxonomy ID: 7227   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Drosophila melanogaster

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

Entity Sequences (FASTA):
entity_1: GSMYNKFVNFICGGLPNLNL NKPPQLHQQQHQQQHQQHQQ HQQQQQLHQHQQQLSPNLSA LHHHHQQQQQLRESGGSHSP SSPGGGGGGS

Data sets:
Data typeCount
13C chemical shifts485
15N chemical shifts167
1H chemical shifts254

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Orb2A PLD1

Entities:

Entity 1, Orb2A PLD 90 residues - 10081 Da.

G1 & S2 are from cloning and tag cleavage. The WT Orb2A prion-like domain sequence is: M1YNKFVNFICGGLPNLNLNKPPQLHQQQHQQQHQQHQQHQQQQQLHQHQQQLSPNLSALHHHHQQQQQLRESGGSHSPSSPGGGGGGS88.

1   GLYSERMETTYRASNLYSPHEVALASNPHE
2   ILECYSGLYGLYLEUPROASNLEUASNLEU
3   ASNLYSPROPROGLNLEUHISGLNGLNGLN
4   HISGLNGLNGLNHISGLNGLNHISGLNGLN
5   HISGLNGLNGLNGLNGLNLEUHISGLNHIS
6   GLNGLNGLNLEUSERPROASNLEUSERALA
7   LEUHISHISHISHISGLNGLNGLNGLNGLN
8   LEUARGGLUSERGLYGLYSERHISSERPRO
9   SERSERPROGLYGLYGLYGLYGLYGLYSER

Samples:

sample_1: Orb2A PLD, [U-98% 13C; U-98% 15N], 1.5 ± 0.3 mM; DSS 50 ± 10 uM; D2O 10 ± 1 %; acetic acid, [U-2H], 1.0 ± 0.05 mM

sample_2: Orb2A PLD, [U-98% 13C; U-98% 15N], 1.5 ± 0.3 mM; DSS 50 ± 10 uM; D2O 10 ± 1 %; acetic acid, [U-2H], 1.0 ± 0.05 mM; sodium hydrogen phosphate 25 ± 1 mM; sodium dihydrogen phosphate 25 ± 1 mM; TCEP 1 ± 0.1 mM; potassium chloride 100 ± 5 mM

sample_conditions_1: ionic strength: 0.001 M; pH: 4.0; pressure: 0.93 atm; temperature: 298.2 K

sample_conditions_2: ionic strength: 310 mM; pH: 7.01; pressure: 0.93 atm; temperature: 298.2 K

Experiments:

NameSampleSample stateSample conditions
1D 1Hsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
2D CONsample_1isotropicsample_conditions_1
3D CBCACONsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D hacacoNcaNCOsample_1isotropicsample_conditions_1
3D hacaCOncaNCOsample_1isotropicsample_conditions_1
3D HncocaNHsample_1isotropicsample_conditions_1
1D 1Hsample_2isotropicsample_conditions_2
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
3D HNCOsample_2isotropicsample_conditions_2
3D HNCAsample_2isotropicsample_conditions_2
3D HBHA(CO)NHsample_2isotropicsample_conditions_2

Software:

TOPSPIN v2.1 - collection, processing

SPARKY vNMRFAM version 1.4 - chemical shift assignment

TALOS+ - structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

NCBI Reference Sequence NP_729429.1

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