BMRB Entry 11012

Title:
1H, 13C and 15N resonance assignments for the 25.8 kDa DNA binding domain of the human p63 protein
Deposition date:
2007-11-01
Original release date:
2015-06-16
Authors:
Enthart, Andreas; Kessler, Horst
Citation:

Citation: Enthart, Andreas; Furrer, Julien; Dehner, Alexander; Kessler, Horst. "Solution structure and binding studies of the p63 DNA binding domain"  .

Assembly members:

Assembly members:
p63BDB, polymer, 233 residues, 25883.586 Da.
ZN, non-polymer, 65.409 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: p20020

Data sets:
Data typeCount
13C chemical shifts877
15N chemical shifts215
1H chemical shifts1418

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1p63BDB1
2ZINC ION2

Entities:

Entity 1, p63BDB 233 residues - 25883.586 Da.

1   GLYSERSERTHRPHEASPALALEUSERPRO
2   SERPROALAILEPROSERASNTHRASPTYR
3   PROGLYPROHISSERPHEASPVALSERPHE
4   GLNGLNSERSERTHRALALYSSERALATHR
5   TRPTHRTYRSERTHRGLULEULYSLYSLEU
6   TYRCYSGLNILEALALYSTHRCYSPROILE
7   GLNILELYSVALMETTHRPROPROPROGLN
8   GLYALAVALILEARGALAMETPROVALTYR
9   LYSLYSALAGLUHISVALTHRGLUVALVAL
10   LYSARGCYSPROASNHISGLULEUSERARG
11   GLUPHEASNGLUGLYGLNILEALAPROPRO
12   SERHISLEUILEARGVALGLUGLYASNSER
13   HISALAGLNTYRVALGLUASPPROILETHR
14   GLYARGGLNSERVALLEUVALPROTYRGLU
15   PROPROGLNVALGLYTHRGLUPHETHRTHR
16   VALLEUTYRASNPHEMETCYSASNSERSER
17   CYSVALGLYGLYMETASNARGARGPROILE
18   LEUILEILEVALTHRLEUGLUTHRARGASP
19   GLYGLNVALLEUGLYARGARGCYSPHEGLU
20   ALAARGILECYSALACYSPROGLYARGASP
21   ARGLYSALAASPGLUASPSERILEARGLYS
22   GLNGLNVALSERASPSERTHRLYSASNGLY
23   ASPALAPHEARGGLNASNTHRHISGLYILE
24   GLNMETTHR

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: p63BDB, [U-15N], 0.7 ± 0.1 mM; potassium chloride 50 mM; potassium phosphate 50 mM; DTT 5 mM

sample_2: p63BDB, [U-13C; U-15N], 0.7 ± 0.1 mM; potassium chloride 50 mM; potassium phosphate 50 mM; DTT 5 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D HNHAsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D CNH NOESYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1

Software:

SPARKY v3.110, Goddard - chemical shift assignment, data analysis, peak picking

X-PLOR NIH v2.16.0, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

xwinnmr, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 900 MHz
  • Bruker DMX 600 MHz

Related Database Links:

PDB
DBJ BAA32432 BAA32433 BAA32592 BAA32593 BAB20631
EMBL CAA76562 CAB88216 CAC37098 CAC37099 CAC37100
GB AAC24830 AAC43038 AAC62633 AAC62634 AAC62635
REF NP_001079107 NP_001108450 NP_001108451 NP_001108452 NP_001108453
SP O88898 Q9H3D4 Q9JJP6
TPG DAA33389
AlphaFold Q9JJP6 O88898 Q9H3D4

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