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 15532

Title: Structure of the Wilms Tumor Suppressor Protein Zinc Finger Domain Bound to DNA   PubMed: 17716689

Deposition date: 2007-10-18 Original release date: 2008-02-14

Authors: Stoll, Raphael; Lee, Brian; Debler, Erik; Laity, John; Wilson, Ian; Dyson, Helen; Wright, Peter

Citation: Stoll, Raphael; Lee, Brian; Debler, Erik; Laity, John; Wilson, Ian; Dyson, Helen; Wright, Peter. "Structure of the Wilms' Tumor Suppressor Protein Zinc Finger Domain Bound to DNA"  J. Mol. Biol. 372, 1227-1245 (2007).

Assembly members:
wt1-17mer, polymer, 119 residues, 14494.849 Da.
ZN, non-polymer, 65.409 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

Entity Sequences (FASTA):
wt1-17mer: ASEKRPFMCAYPGCNKRYFK LSHLQMHSRKHTGEKPYQCD FKDCERRFSRSDQLKRHQRR HTGVKPFQCKTCQRKFSRSD HLKTHTRTHTGEKPFSCRWP SCQKKFARSDELVRHHNMH

Data sets:
Data typeCount
15N chemical shifts110
1H chemical shifts110

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1wt1-17mer1
2zn12
3zn22
4zn32
5zn42

Entities:

Entity 1, wt1-17mer 119 residues - 14494.849 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, zn1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: wt1, [U-100% 13C; U-100% 15N], 0.6 mM; Tris/HCl 10 mM; KCl 20 mM; ZnSO4 5 uM; NaN3 2 mM

sample_conditions_1: ionic strength: 20 mM; pH: 6.7; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
IPAPsample_1anisotropicsample_conditions_1

Software:

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Koll - structure solution

NMR spectrometers:

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

Related Database Links:

BMRB 15533 4707 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

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