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BMRB Entry 51812

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51812

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Title: 1H, 13C, 15N backbone chemical shift assignments of the extended ARID domain from human AT-rich interactive domain protein 5a (Arid5a)   PubMed: 37129704

Deposition date: 2023-01-30 Original release date: 2023-02-03

Authors: von Ehr, Julian; Korn, Sophie; Schlundt, Andreas

Citation: von Ehr, Julian; Korn, Sophie Marianne; Weiss, Lena; Schlundt, Andreas. "1H, 13C, 15N backbone chemical shift assignments of the extended ARID domain in human AT-rich interactive domain protein 5a (Arid5a)"  Biomol. NMR Assign. 17, 121-127 (2023).

Assembly members:
entity_1, polymer, 151 residues, 17380 Da.

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: pET-Trx1-a

Entity Sequences (FASTA):
entity_1: GAMAISLEDSPEAGGEREEE QEREEEQAFLVSLYKFMKER HTPIERVPHLGFKQINLWKI YKAVEKLGAYELVTGRRLWK NVYDELGGSPGSTSAATCTR RHYERLVLPYVRHLKGEDDK PLPTSKPRKQYKMAKENRGD DGATERPKKAK

Data typeCount
13C chemical shifts283
15N chemical shifts288
1H chemical shifts300

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Arid5a 37-1831

Entities:

Entity 1, Arid5a 37-183 151 residues - 17380 Da.

The first four residues (GAMA) in the protein construct used are cloning artifacts.

1   GLYALAMETALAILESERLEUGLUASPSER
2   PROGLUALAGLYGLYGLUARGGLUGLUGLU
3   GLNGLUARGGLUGLUGLUGLNALAPHELEU
4   VALSERLEUTYRLYSPHEMETLYSGLUARG
5   HISTHRPROILEGLUARGVALPROHISLEU
6   GLYPHELYSGLNILEASNLEUTRPLYSILE
7   TYRLYSALAVALGLULYSLEUGLYALATYR
8   GLULEUVALTHRGLYARGARGLEUTRPLYS
9   ASNVALTYRASPGLULEUGLYGLYSERPRO
10   GLYSERTHRSERALAALATHRCYSTHRARG
11   ARGHISTYRGLUARGLEUVALLEUPROTYR
12   VALARGHISLEULYSGLYGLUASPASPLYS
13   PROLEUPROTHRSERLYSPROARGLYSGLN
14   TYRLYSMETALALYSGLUASNARGGLYASP
15   ASPGLYALATHRGLUARGPROLYSLYSALA
16   LYS

Samples:

sample_1: Arid5a, [U-100% 13C; U-100% 15N], 127 uM; Bis-Tris 20 mM; TCEP 2 mM; NaCl 150 mM

sample_2: Arid5a, [U-100% 13C; U-100% 15N], 471 uM; Bis-Tris 20 mM; TCEP 2 mM; NaCl 150 mM

sample_3: Arid5a, [U-100% 13C; U-100% 15N], 225 uM; Bis-Tris 20 mM; TCEP 2 mM; NaCl 150 mM

sample_4: Arid5a, [U-100% 13C; U-100% 15N], 500 uM; Bis-Tris 20 mM; TCEP 2 mM; NaCl 150 mM

sample_5: Arid5a, [U-100% 13C; U-100% 15N], 700 uM; Bis-Tris 20 mM; TCEP 2 mM; NaCl 150 mM

sample_6: Arid5a, [U-100% 15N], 300 uM; Bis-Tris 20 mM; TCEP 2 mM; NaCl 150 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HNCACBsample_5isotropicsample_conditions_1
3D CBCA(CO)NHsample_5isotropicsample_conditions_1
3D HNCACBsample_4isotropicsample_conditions_1
2D 1H-15N HSQCsample_6isotropicsample_conditions_1

Software:

TOPSPIN v3 + 4 - collection

ANALYSIS v2.5.1 - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE NEO 600 MHz
  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE III 700 MHz
  • Bruker AVANCE III 800 MHz
  • Bruker AVANCE III 950 MHz

Related Database Links:

UNP Q03989-1
AlphaFold Q03989-1

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