BMRB Entry 50793

Title:
ular mechanisms underlying the role of the centriolar CEP164-TTBK2 complex in ciliopathies
Deposition date:
2021-02-25
Original release date:
2021-09-07
Authors:
Rosa e Silva, Ivan; Bino, Lucia; Johnson, Christopher; Rutherford, Trevor; Neuhaus, David; Andreeva, Antonina; Cajanek, Lukas; van Breugel, Mark
Citation:

Citation: Rosa e Silva, Ivan; Bino, Lucia; Johnson, Christopher; Rutherford, Trevor; Neuhaus, David; Andreeva, Antonina; Cajanek, Lukas; van Breugel, Mark. "Molecular mechanisms underlying the role of the centriolar CEP164-TTBK2 complex in ciliopathies"  Structure 30, 114-128 (2022).
PubMed: 34499853

Assembly members:

Assembly members:
entity_1, polymer, 109 residues, Formula weight is not available

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: pGEX6P1

Data sets:
Data typeCount
13C chemical shifts441
15N chemical shifts103
1H chemical shifts755

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CEP1641

Entities:

Entity 1, CEP164 109 residues - Formula weight is not available

1   METALAGLYARGPROLEUARGILEGLYASP
2   GLNLEUVALLEUGLUGLUASPTYRASPGLU
3   THRTYRILEPROSERGLUGLNGLUILELEU
4   GLUPHEALAARGGLUILEGLYILEASPPRO
5   ILELYSGLUPROGLULEUMETTRPLEUALA
6   ARGGLUGLYILEVALALAPROLEUPROGLY
7   GLUTRPLYSPROCYSGLNASPILETHRGLY
8   ASPILETYRTYRPHEASNPHEALAASNGLY
9   GLNSERMETTRPASPHISPROCYSASPGLU
10   HISTYRARGSERLEUVALILEGLNGLUARG
11   ALALYSLEUSERTHRSERGLYALAILE

Samples:

sample_1: CEP164 N-terminal domain, [U-100% 13C; U-100% 15N], 120 uM; sodium phosphate 25 mM; sodium chloride 125 mM; DTT 4 mM; complete protease inhibitor cocktail, EDTA free 0.4 tablet/100mL

sample_2: CEP164 N-terminal domain, [U-100% 15N], 500 uM; sodium phosphate 25 mM; sodium chloride 125 mM; DTT 4 mM; complete protease inhibitor cocktail, EDTA free 0.4 tablet/100mL

sample_conditions_1: ionic strength: 185 mM; pH: 7.4; pressure: 1 atm; temperature: 293 K

sample_conditions_2: ionic strength: 185 mM; pH: 7.4; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.2 - collection, processing

SPARKY v3.12 - chemical shift assignment

X-PLOR NIH v2.28 - structure solution

AMBER11 - structure solution

TALOS+ v3.80F1 Rev 2012.080.14.41 - structure solution

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE III 700 MHz
  • Bruker AVANCE III 800 MHz

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