BMRB Entry 50405

Title:
WT1(-KTS) backbone and side chain 13C, 15N and 1H assignments
Deposition date:
2020-07-22
Original release date:
2020-07-27
Authors:
Nishikawa, Tadateru; Wojciak, Jonathan; Dyson, Helen Jane; Wright, Peter
Citation:

Citation: Laity, J.; Chung, J.; Dyson, H.; Wright, P.. "Alternative splicing of Wilms' tumor suppressor protein modulates DNA binding activity through isoform-specific DNA-induced conformational changes."  Biochemistry 39, 5341-5348 (2000).
PubMed: 10820004

Assembly members:

Assembly members:
entity_1, polymer, 119 residues, 14450 Da.
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:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: PET21

Data sets:
Data typeCount
13C chemical shifts395
15N chemical shifts109
1H chemical shifts724

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1WT1-KTS1
2Zn 12
3Zn 22
4Zn 32
5Zn 42

Entities:

Entity 1, WT1-KTS 119 residues - 14450 Da.

1   ALASERGLULYSARGPROPHEMETCYSALA
2   TYRPROGLYCYSASNLYSARGTYRPHELYS
3   LEUSERHISLEUGLNMETHISSERARGLYS
4   HISTHRGLYGLULYSPROTYRGLNCYSASP
5   PHELYSASPCYSGLUARGARGPHESERARG
6   SERASPGLNLEULYSARGHISGLNARGARG
7   HISTHRGLYVALLYSPROPHEGLNCYSLYS
8   THRCYSGLNARGLYSPHESERARGSERASP
9   HISLEULYSTHRHISTHRARGTHRHISTHR
10   GLYGLULYSPROPHESERCYSARGTRPPRO
11   SERCYSGLNLYSLYSPHEALAARGSERASP
12   GLULEUVALARGHISHISASNMETHIS

Entity 2, Zn 1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: WT1, [U-95% 13C; U-95% 15N], 0.55 mM; deuterated Tris 10 mM; KCl 20 mM; DTT 2 mM; NaN3 1 mM

sample_conditions_1: pH: 6.8; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
15N-HSQCsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
3D H(CCO)NH-sample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
3D 13C-separated NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1

Software:

NMRView vNMRviewJ implemented in NMRBox - peak picking, analysis

NMR spectrometers:

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

Related Database Links:

BMRB 15532 15533 4708 4709 4710
PDB
DBJ BAA11522 BAA28147 BAA94793 BAF84425
EMBL CAA35956 CAA43819 CDG23662
GB AAA36810 AAA61299 AAB33443 AAB53152 AAH32861
PRF 1604420A
REF NP_000369 NP_001001264 NP_001079057 NP_001079336 NP_001135625
SP B5DE03 O62651 P19544 P79958
TPG DAA21902
AlphaFold O62651 B5DE03 P79958 Q8IYZ5

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