BMRB Entry 4710

Title:
WT1+KTS/DNA complex
Deposition date:
2000-03-30
Original release date:
2000-05-01
Authors:
Laity, John; Chung, John; Dyson, H.; Wright, Peter
Citation:

Citation: Laity, John; Chung, John; Dyson, H.; Wright, Peter. "Alternative Splicing of Wilms' Tumor Suppressor Protein Modulates DNA Binding Activity Through Isoform-Specific DNA-Induced Conformational Changes"  Biochemistry ., .-. (2000).

Assembly members:

Assembly members:
WT1, polymer, 122 residues, 14766 Da.
DNA, polymer, 14 residues, Formula weight is not available
DNA strand 2, polymer, 14 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Homo Sapiens

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts222
15N chemical shifts97
1H chemical shifts97

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1WT1+KTS1
2DNA strand 12
3DNA strand 23
4Zn 14
5Zn 24
6Zn 34
7Zn 44

Entities:

Entity 1, WT1+KTS 122 residues - 14766 Da.

1   ALASERGLULYSARGPROPHEMETCYSALA
2   TYRPROGLYCYSASNLYSARGTYRPHELYS
3   LEUSERHISLEUGLNMETHISSERARGLYS
4   HISTHRGLYGLULYSPROTYRGLNCYSASP
5   PHELYSASPCYSGLUARGARGPHESERARG
6   SERASPGLNLEULYSARGHISGLNARGARG
7   HISTHRGLYVALLYSPROPHEGLNCYSLYS
8   THRCYSGLNARGLYSPHESERARGSERASP
9   HISLEULYSTHRHISTHRARGTHRHISTHR
10   GLYLYSTHRSERGLULYSPROPHESERCYS
11   ARGTRPPROSERCYSGLNLYSLYSPHEALA
12   ARGSERASPGLULEUVALARGHISHISASN
13   METHIS

Entity 2, DNA strand 1 14 residues - Formula weight is not available

1   DCDGDCDGDGDGDGDGDCDG
2   DTDCDTDG

Entity 3, DNA strand 2 14 residues - Formula weight is not available

1   DCDADGDADCDGDCDCDCDC
2   DCDGDCDG

Entity 4, Zn 1 - Zn - 65.409 Da.

1   ZN

Samples:

free_proteins: WT1, [U-95% 13C; U-95% 15N], 0.15 – 0.3 mM; DNA0.15 – 0.3 mM; DNA strand 20.15 – 0.3 mM

Conditions: pH: 6.70; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
15N-HSQCfree_proteinsnot availableConditions
HNCAfree_proteinsnot availableConditions
HN(CO)CAfree_proteinsnot availableConditions
HNCACBfree_proteinsnot availableConditions
CBCA(CO)NHfree_proteinsnot availableConditions
HNCOfree_proteinsnot availableConditions
HCACO(CA)NHfree_proteinsnot availableConditions
HNCACB (deuterium decoupling)free_proteinsnot availableConditions
HN(CO)CACB (deuterium decoupling)free_proteinsnot availableConditions

Software:

FELIX v95, 97 - processing, peakpicking, analysis

NMR spectrometers:

  • Bruker AMX 500 MHz

Related Database Links:

BMRB 15532 15533 4707 4708 4709
PDB
DBJ BAA28147 BAA76399 BAA94794 BAF84425 BAG52667
EMBL CAA35956 CAA49373 CAA59735 CAA59737 CDG23662
GB AAA40573 AAA61299 AAB27319 AAB33427 AAB70832
PRF 1604420A
REF NP_000369 NP_001001264 NP_001185481 NP_077742 NP_077744
SP B7ZSG3 O62651 P19544 P22561 P49952
TPG DAA21902
AlphaFold P49952 P22561 P19544 O62651 B7ZSG3

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