BMRB Entry 50236

Title:
WT1-KTS RNA complex   PubMed: 32955251
Deposition date:
2020-04-14
Original release date:
2021-03-01
Authors:
Nishikawa, Tadateru; Wojciak, Jonathan; Dyson, Helen Jane; Wright, Peter
Citation:

Citation: Nishikawa, Tadateru; Wojciak, Jonathan; Dyson, Helen Jane; Wright, Peter. "RNA Binding by the KTS Splice Variants of Wilms' Tumor Suppressor Protein WT1"  Biochemistry 59, 3889-3901 (2020).

Assembly members:

Assembly members:
entity_1, polymer, 117 residues, Formula weight is not available
entity_2, polymer, 29 residues, Formula weight is not available
entity_ZN, non-polymer, 65.409 Da.

Natural source:

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: pWT1-4-

Experimental source:

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: pWT1-4-

Data sets:
Data typeCount
13C chemical shifts473
15N chemical shifts109
1H chemical shifts264

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1protein1
2RNA2
3ZN, 13
4ZN, 23
5ZN, 33

Entities:

Entity 1, protein 117 residues - Formula weight is not available

1   GLULYSARGPROPHEMETCYSALATYRPRO
2   GLYCYSASNLYSARGTYRPHELYSLEUSER
3   HISLEUGLNMETHISSERARGLYSHISTHR
4   GLYGLULYSPROTYRGLNCYSASPPHELYS
5   ASPCYSGLUARGARGPHESERARGSERASP
6   GLNLEULYSARGHISGLNARGARGHISTHR
7   GLYVALLYSPROPHEGLNCYSLYSTHRCYS
8   GLNARGLYSPHESERARGSERASPHISLEU
9   LYSTHRHISTHRARGTHRHISTHRGLYGLU
10   LYSPROPHESERCYSARGTRPPROSERCYS
11   GLNLYSLYSPHEALAARGSERASPGLULEU
12   VALARGHISHISASNMETHIS

Entity 2, RNA 29 residues - Formula weight is not available

1   GGGCCACCAA
2   CGACAUUGAU
3   AUGGUGCCC

Entity 3, ZN, 1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: WT1(-KTS), [U-100% 13C; U-100% 15N; U-90% 2H], 0.55 ± 0.1 mM; aptamer RNA 0.55 ± 0.1 mM; TRIS, [U-100% 2H], 10 ± 0.1 mM; potassium chloride 350 ± 0.5 mM; DTT 10 ± 0.1 mM; ZnSO4 5 ± 0.1 uM; sodium azide 2 ± 0.1 mM

sample_2: WT1(-KTS), [U-100% 13C; U-100% 15N; U-65% 2H], 0.55 ± 0.1 mM; aptamer RNA 0.55 ± 0.1 mM; TRIS, [U-100% 2H], 10 ± 0.1 mM; potassium chloride 350 ± 0.5 mM; DTT 10 ± 0.1 mM; ZnSO4 5 ± 0.1 uM; sodium azide 2 ± 0.1 mM

sample_3: WT1(-KTS) 0.55 ± 0.1 mM; aptamer RNA, [U-99% 13C; U-99% 15N], 0.55 ± 0.1 mM; TRIS, [U-100% 2H], 10 ± 0.1 mM; potassium chloride 350 ± 0.5 mM; DTT 10 ± 0.1 mM; ZnSO4 5 ± 0.1 uM; sodium azide 2 ± 0.1 mM

sample_4: WT1(-KTS) 0.55 ± 0.1 mM; aptamer RNA, [U-100% 15N], 0.55 ± 0.1 mM; TRIS, [U-100% 2H], 10 ± 0.1 mM; potassium chloride 350 ± 0.5 mM; DTT 10 ± 0.1 mM; ZnSO4 5 ± 0.1 uM; sodium azide 2 ± 0.1 mM

sample_conditions_1: ionic strength: 350 mM; pH: 7.1; pressure: 1 atm; temperature: 310 K

sample_conditions_2: ionic strength: 350 mM; pH: 7.1; pressure: 1 atm; temperature: 280 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HMQCsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_3isotropicsample_conditions_1
3D HMQC-NOESYsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
2D 1H-13C HMQCsample_3isotropicsample_conditions_1
2D 13C[F1,F2]filtered NOESYsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_4isotropicsample_conditions_2
3D 1H-15N NOESYsample_4isotropicsample_conditions_2

Software:

NMRPipe - processing

NMRView - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 750 MHz
  • Bruker Avance 500 MHz
  • Bruker DRX 800 MHz
  • Bruker DRX 600 MHz

Related Database Links:

UNP P19544

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