BMRB Entry 26551

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26551

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Title:
Backbone resonance assignments of the human p73 DNA binding domain
Deposition date:
2015-03-31
Original release date:
2015-08-18
Authors:
Cino, Elio; Soares, Iaci; de Freitas, Monica; Silva, Jerson
Citation:

Citation: Cino, Elio; Soares, Iaci; de Freitas, Monica; Silva, Jerson. "Backbone resonance assignments of the human p73 DNA binding domain"  Biomol. NMR Assign. 10, 49-51 (2016).
PubMed: 26294377

Assembly members:

Assembly members:
p73_DBD, polymer, 208 residues, 23313.5 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: pNIC-CTHF

Entity Sequences (FASTA):

Entity Sequences (FASTA):
p73_DBD: MAPVIPSNTDYPGPHHFEVT FQQSSTAKSATWTYSPLLKK LYCQIAKTCPIQIKVSTPPP PGTAIRAMPVYKKAEHVTDV VKRCPNHELGRDFNEGQSAP ASHLIRVEGNNLSQYVDDPV TGRQSVVVPYEPPQVGTEFT TILYNFMCNSSCVGGMNRRP ILIIITLEMRDGQVLGRRSF EGRICACPGRDRKADEDHYR EAENLYFQ

Data sets:
Data typeCount
13C chemical shifts573
15N chemical shifts175
1H chemical shifts175

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1DNA binding domain1

Entities:

Entity 1, DNA binding domain 208 residues - 23313.5 Da.

The M1 and C-terminal AENLYFQ sequence are non-native (initiator M and TEV consensus)

1   METALAPROVALILEPROSERASNTHRASP
2   TYRPROGLYPROHISHISPHEGLUVALTHR
3   PHEGLNGLNSERSERTHRALALYSSERALA
4   THRTRPTHRTYRSERPROLEULEULYSLYS
5   LEUTYRCYSGLNILEALALYSTHRCYSPRO
6   ILEGLNILELYSVALSERTHRPROPROPRO
7   PROGLYTHRALAILEARGALAMETPROVAL
8   TYRLYSLYSALAGLUHISVALTHRASPVAL
9   VALLYSARGCYSPROASNHISGLULEUGLY
10   ARGASPPHEASNGLUGLYGLNSERALAPRO
11   ALASERHISLEUILEARGVALGLUGLYASN
12   ASNLEUSERGLNTYRVALASPASPPROVAL
13   THRGLYARGGLNSERVALVALVALPROTYR
14   GLUPROPROGLNVALGLYTHRGLUPHETHR
15   THRILELEUTYRASNPHEMETCYSASNSER
16   SERCYSVALGLYGLYMETASNARGARGPRO
17   ILELEUILEILEILETHRLEUGLUMETARG
18   ASPGLYGLNVALLEUGLYARGARGSERPHE
19   GLUGLYARGILECYSALACYSPROGLYARG
20   ASPARGLYSALAASPGLUASPHISTYRARG
21   GLUALAGLUASNLEUTYRPHEGLN

Samples:

sample_1: p73 DBD, [U-95% 13C; U-95% 15N], 0.35 mM; sodium phosphate 50 mM; NaCl 100 mM; DTT 2 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7; pressure: 1 atm; temperature: 298 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 HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz

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