BMRB Entry 19771

Title:
Solution structure of CPEB1 ZZ domain in the free state
Deposition date:
2014-02-06
Original release date:
2014-07-21
Authors:
Afroz, Tariq; Skrisovska, Lenka; Belloc, Eulalia; Boixet, Jordina; Mendez, Raul; Allain, Frederic
Citation:

Citation: Afroz, Tariq; Skrisovska, Lenka; Belloc, Eulalia; Boixet, Jordina; Mendez, Raul; Allain, Frederic. "A fly trap mechanism provides sequence-specific RNA recognition by CPEB proteins"  Genes Dev. 28, 1498-1514 (2014).
PubMed: 24990967

Assembly members:

Assembly members:
CPEB1ZZ, polymer, 61 residues, 7387.450 Da.
ZINC ION, non-polymer, 65.409 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: pET28A(+)

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts173
15N chemical shifts59
1H chemical shifts334

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CPEB1ZZ1
2ZINC ION_12
3ZINC ION_22

Entities:

Entity 1, CPEB1ZZ 61 residues - 7387.450 Da.

1   ILEASPPROTYRLEUGLUASPSERLEUCYS
2   HISILECYSSERSERGLNPROGLYPROPHE
3   PHECYSARGASPGLNVALCYSPHELYSTYR
4   PHECYSARGSERCYSTRPHISTRPARGHIS
5   SERMETGLUGLYLEUARGHISHISSERPRO
6   LEUMETARGASNGLNLYSASNARGASPSER
7   SER

Entity 2, ZINC ION_1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: CPEB1ZZ, [U-100% 13C; U-100% 15N], 0.4 – 0.6 mM; H2O 90%; D2O 10%; sodium phosphate 50 mM; NaCl 100 mM; Arg 50 mM; Glu 50 mM; DTT 1 mM

sample_2: CPEB1ZZ, [U-100% 15N], 0.4 – 0.6 mM; H2O 90%; D2O 10%; sodium phosphate 50 mM; NaCl 100 mM; Arg 50 mM; Glu 50 mM; DTT 1 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1

Software:

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

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

Related Database Links:

BMRB 18840
PDB
DBJ BAB14496 BAB33089 BAC37017 BAG63194 BAH11723
EMBL CAA69588 CAH92427
GB AAH35348 AAH50629 AAI25477 AAK01239 AAK01240
REF NP_001073001 NP_001073002 NP_001073003 NP_001099746 NP_001126432
SP P0C279 P70166 Q5R733 Q9BZB8
TPG DAA17635
AlphaFold Q5R733 Q9BZB8 P70166 P0C279

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