BMRB Entry 27599

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27599

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Backbone chemical shifts for super-stable p53 DNA-Binding Domain C5xS
Deposition date:
2018-09-05
Original release date:
2018-11-07
Authors:
Krois, Alexander; Dyson, Jane; Wright, Peter
Citation:

Citation: Krois, Alexander; Dyson, Jane; Wright, Peter. "Long-range regulation of p53 DNA binding by its intrinsically disordered N-terminal transactivation domain"  Proc. Natl. Acad. Sci. U.S.A. 115, E11302-E11310 (2018).
PubMed: 30420502

Assembly members:

Assembly members:
p53(DBD)_super-stable_C5xS, polymer, 228 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
p53(DBD)_super-stable_C5xS: GSHAPSWPLSSSVPSQKTYQ GSYGFRLGFLHSGTAKSVTS TYSPALNKLFCQLAKTCPVQ LWVDSTPPPGTRVRAMAIYK QSQHMTEVVRRCPHHERSSD SDGLAPPQHLIRVEGNLRAE YLDDRNTFRHSVVVPYEPPE VGSDSTTIHYNYMCYSSCMG GMNRRPILTIITLEDSSGNL LGRDSFEVRVSASPGRDRRT EEENLRKKGEPHHELPPGST KRALPNNT

Data sets:
Data typeCount
13C chemical shifts375
15N chemical shifts176
1H chemical shifts176

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1p53(DBD)1

Entities:

Entity 1, p53(DBD) 228 residues - Formula weight is not available

Residues 85, 86, and 87 are from expression/cloning and are not a part of the native sequence.

1   GLYSERHISALAPROSERTRPPROLEUSER
2   SERSERVALPROSERGLNLYSTHRTYRGLN
3   GLYSERTYRGLYPHEARGLEUGLYPHELEU
4   HISSERGLYTHRALALYSSERVALTHRSER
5   THRTYRSERPROALALEUASNLYSLEUPHE
6   CYSGLNLEUALALYSTHRCYSPROVALGLN
7   LEUTRPVALASPSERTHRPROPROPROGLY
8   THRARGVALARGALAMETALAILETYRLYS
9   GLNSERGLNHISMETTHRGLUVALVALARG
10   ARGCYSPROHISHISGLUARGSERSERASP
11   SERASPGLYLEUALAPROPROGLNHISLEU
12   ILEARGVALGLUGLYASNLEUARGALAGLU
13   TYRLEUASPASPARGASNTHRPHEARGHIS
14   SERVALVALVALPROTYRGLUPROPROGLU
15   VALGLYSERASPSERTHRTHRILEHISTYR
16   ASNTYRMETCYSTYRSERSERCYSMETGLY
17   GLYMETASNARGARGPROILELEUTHRILE
18   ILETHRLEUGLUASPSERSERGLYASNLEU
19   LEUGLYARGASPSERPHEGLUVALARGVAL
20   SERALASERPROGLYARGASPARGARGTHR
21   GLUGLUGLUASNLEUARGLYSLYSGLYGLU
22   PROHISHISGLULEUPROPROGLYSERTHR
23   LYSARGALALEUPROASNASNTHR

Samples:

sample_1: p53(DBD) super-stable C5xS, [U-100% 13C; U-100% 15N; U-80% 2H], 300 uM; Tris 20 mM; NaCl 150 mM; DTT 2 mM

sample_conditions_1: ionic strength: 170 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment, collection, data analysis

NMR spectrometers:

  • Bruker DRX 800 MHz

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