BMRB Entry 11473

Title:
Solution structure of the CERT PH domain
Deposition date:
2012-02-25
Original release date:
2012-08-13
Authors:
Sugiki, Toshihiko; Takeuchi, Koh; Tokunaga, Yuji; Kumagai, Keigo; Kawano, Miyuki; Nishijima, Masahiro; Hanada, Kentaro; Takahashi, Hideo; Shimada, Ichio
Citation:

Citation: Sugiki, Toshihiko; Takeuchi, Koh; Tokunaga, Yuji; Terasawa, Hiroaki; Kumagai, Keigo; Kawano, Miyuki; Nishijima, Masahiro; Hanada, Kentaro; Takahashi, Hideo; Shimada, Ichio. "Structural basis for the Golgi-association by the pleckstrin homology domain of the ceramide trafficking protein CERT"  J. Biol. Chem. ., .-. (2012).
PubMed: 22869376

Assembly members:

Assembly members:
CERT, polymer, 94 residues, 11180.480 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

Data sets:
Data typeCount
13C chemical shifts369
15N chemical shifts98
1H chemical shifts587

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CERT PH domain1

Entities:

Entity 1, CERT PH domain 94 residues - 11180.480 Da.

1   VALGLUARGCYSGLYVALLEUSERLYSTRP
2   THRASNTYRILEHISGLYTRPGLNASPARG
3   TRPVALVALLEULYSASNASNALALEUSER
4   TYRTYRLYSSERGLUASPGLUTHRGLUTYR
5   GLYCYSARGGLYSERILECYSLEUSERLYS
6   ALAVALILETHRPROHISASPPHEASPGLU
7   CYSARGPHEASPILESERVALASNASPSER
8   VALTRPTYRLEUARGALAGLNASPPROASP
9   HISARGGLNGLNTRPILEASPALAILEGLU
10   GLNHISLYSTHR

Samples:

sample_1: CERT, [U-98% 15N], 0.2 mM; HEPES 10 mM; sodium chloride 100 mM; DTT 5 mM; H2O 93%; D2O 7%

sample_2: CERT, [U-98% 13C; U-98% 15N], 0.2 mM; HEPES 10 mM; sodium chloride 100 mM; DTT 5 mM; H2O 93%; D2O 7%

sample_conditions_1: pH: 7.20; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
4D 13C 15N NOESYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAC03762 BAF84776 BAG53379 BAI45568
EMBL CAH92584
GB AAD30288 AAG42046 AAG42047 AAG42049 AAH00102
REF NP_001102405 NP_001123577 NP_001126514 NP_001230955 NP_005704
SP Q5R6M6 Q6VVX2 Q9GKI7 Q9Y5P4
TPG DAA25918
AlphaFold Q9GKI7 Q5R6M6 Q6VVX2 Q9Y5P4

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