BMRB Entry 34095

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34095
MolProbity Validation Chart

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Title:
Structure Of P63 SAM Domain L514F Mutant Causative Of AEC Syndrome
Deposition date:
2017-02-08
Original release date:
2018-02-02
Authors:
Rinnenthal, J.; Wuerz, J.; Osterburg, C.; Guentert, P.; Doetsch, V.
Citation:

Citation: Russo, Claudia; Osterburg, Christian; Sirico, Anna; Antonini, Dario; Ambrosio, Raffaele; Wurz, Julia Maren; Rinnenthal, Jorg; Ferniani, Marco; Kehrloesser, Sebastian; Schafer, Birgit; Guntert, Peter; Sinha, Satrajit; Dotsch, Volker; Missero, Caterina. "Protein aggregation of the p63 transcription factor underlies severe skin fragility in AEC syndrome"  Proc. Natl. Acad. Sci. U. S. A. 115, E906-E915 (2018).
PubMed: 29339502

Assembly members:

Assembly members:
entity_1, polymer, 70 residues, 7957.985 Da.

Natural source:

Natural source:   Common Name: House Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPLGSTDCSIVSFFARLGCS SCLDYFTTQGLTTIYQIEHY SMDDLASLKIPEQFRHAIWK GILDHRQLHD

Data sets:
Data typeCount
13C chemical shifts113
15N chemical shifts61
1H chemical shifts413

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 70 residues - 7957.985 Da.

1   GLYPROLEUGLYSERTHRASPCYSSERILE
2   VALSERPHEPHEALAARGLEUGLYCYSSER
3   SERCYSLEUASPTYRPHETHRTHRGLNGLY
4   LEUTHRTHRILETYRGLNILEGLUHISTYR
5   SERMETASPASPLEUALASERLEULYSILE
6   PROGLUGLNPHEARGHISALAILETRPLYS
7   GLYILELEUASPHISARGGLNLEUHISASP

Samples:

sample_2: Tumor protein 63 350 uM; NaCl 100 mM; HEPES 20 mM

sample_1: Tumor protein 63, [U-13C; U-15N], 350 uM; NaCl 100 mM; HEPES 20 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1

Software:

CYANA 3.97, Guntert, Mumenthaler and Wuthrich - chemical shift assignment

CYANA 3.97 v3.98, Guntert, Mumenthaler and Wuthrich - structure calculation

OPALp 1.4, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

SPARKY, Goddard - chemical shift assignment, peak picking

TALOS+, Cornilescu, Delaglio and Bax - data analysis

xwinnmr, Bruker Biospin - processing

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

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