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Biological Magnetic Resonance Data Bank


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BMRB Entry 25298

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25298
MolProbity Validation Chart

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Title: Tetramerization domain of the Ciona intestinalis p53/p73-b transcription factor protein   PubMed: 26473758

Deposition date: 2014-10-27 Original release date: 2015-10-26

Authors: Heering, Jan; Jonker, Hendrik; Loehr, Frank; Schwalbe, Harald; Doetsch, Volker

Citation: Heering, Jan; Jonker, Hendrik; Loehr, Frank; Schwalbe, Harald; Doetsch, Volker. "Structural investigations of the p53/p73 homologs from the tunicate species Ciona intestinalis reveal the sequence requirements for the formation of a tetramerization domain"  Protein Sci.' 25, 410-422 (2016).

Assembly members:
entity, polymer, 47 residues, 5528.412 Da.

Natural source:   Common Name: vase tunicate   Taxonomy ID: 7719   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Ciona intestinalis

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

Entity Sequences (FASTA):
entity: SDGDVVYTLNIRGKRKFEKV KEYKEALDLLDYVQPDVKKA CCQRNQI

Data sets:
Data typeCount
13C chemical shifts218
15N chemical shifts46
1H chemical shifts347

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_21
3entity_31
4entity_41

Entities:

Entity 1, entity_1 47 residues - 5528.412 Da.

N-terminal (G)S residue is the remnant of the TEV side

1   SERASPGLYASPVALVALTYRTHRLEUASN
2   ILEARGGLYLYSARGLYSPHEGLULYSVAL
3   LYSGLUTYRLYSGLUALALEUASPLEULEU
4   ASPTYRVALGLNPROASPVALLYSLYSALA
5   CYSCYSGLNARGASNGLNILE

Samples:

sample_1: entity, [U-100% 15N], 2.5 mM; L-arginine 50 mM; L-glutamate 50 mM; DTT 1 mM; H2O 95%; D2O 5%

sample_2: entity, [U-100% 13C; U-100% 15N], 2.5 mM; L-arginine 50 mM; L-glutamate 50 mM; DTT 1 mM; H2O 95%; D2O 5%

sample_3: entity, [U-100% 15N], 2 mM; entity, [U-100% 13C], 2 mM; L-arginine 50 mM; L-glutamate 50 mM; DTT 1 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HCCCONHsample_2isotropicsample_conditions_1
3D CCCONHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_3isotropicsample_conditions_1
3D 1H-13C NOESY 15N-edited intersample_3isotropicsample_conditions_1
3D 1H-13C HMQC-NOESY-15N-1H-TROSYsample_3isotropicsample_conditions_1
3D 1H-13C NOESY J-resolvedsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

CYANA v3.9, Guntert, Mumenthaler and Wuthrich - structure solution

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

ARIA v1.2, Linge, O'Donoghue and Nilges - refinement, structure solution

TOPSPIN v2.1, Bruker Biospin - collection, processing

SPARKY v3.114, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 500 MHz

Related Database Links:

UniProtKB/TrEMBL Q4H2Z8
Aniseed KH2012:KH.C3.713.v1.A.SL1-1
NCBI NP_001071796.1

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts