BMRB Entry 15279

Title:
Structure of the EH-domain of EHD1
Deposition date:
2007-06-01
Original release date:
2007-10-16
Authors:
KIEKEN, Fabien; JOVIC, Marko; CAPLAN, Steve; SORGEN, Paul
Citation:

Citation: Kieken, Fabien; Jovic, Marko; Naslavsky, N.; Caplan, Steve; Sorgen, Paul. "EH domain of EHD1"  J. Biomol. NMR 39, 323-329 (2007).
PubMed: 17899392

Assembly members:

Assembly members:
EH domain of EHD1, polymer, 139 residues, 15004.205 Da.
CA, non-polymer, 40.078 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: Pgex 6P-2

Data sets:
Data typeCount
13C chemical shifts602
15N chemical shifts131
1H chemical shifts967

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1EH domain of EHD11
2CALCIUM ION2

Entities:

Entity 1, EH domain of EHD1 139 residues - 15004.205 Da.

1   GLYPROLEUGLYSERGLUSERLEUMETPRO
2   SERGLNVALVALLYSGLYGLYALAPHEASP
3   GLYTHRMETASNGLYPROPHEGLYHISGLY
4   TYRGLYGLUGLYALAGLYGLUGLYILEASP
5   ASPVALGLUTRPVALVALGLYLYSASPLYS
6   PROTHRTYRASPGLUILEPHETYRTHRLEU
7   SERPROVALASNGLYLYSILETHRGLYALA
8   ASNALALYSLYSGLUMETVALLYSSERLYS
9   LEUPROASNTHRVALLEUGLYLYSILETRP
10   LYSLEUALAASPVALASPLYSASPGLYLEU
11   LEUASPASPGLUGLUPHEALALEUALAASN
12   HISLEUILELYSVALLYSLEUGLUGLYHIS
13   GLULEUPROALAASPLEUPROPROHISLEU
14   VALPROPROSERLYSARGARGHISGLU

Entity 2, CALCIUM ION - Ca - 40.078 Da.

1   CA

Samples:

sample_1: EH Domain of EHD-1, [U-99% 13C; U-99% 15N], 1 ± 0.05 mM; CALCIUM ION 3 mM; PBS 150 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - data analysis

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 16179 16180 16181 16671
PDB
DBJ BAB28540 BAC40684 BAE32742 BAE35499 BAE35852
EMBL CAH90816
GB AAB81204 AAD45423 AAD45866 AAF24223 AAG02009
REF NP_001011939 NP_001015578 NP_001125465 NP_001162473 NP_001248124
SP Q5E9R3 Q5RBP4 Q641Z6 Q9H4M9 Q9WVK4
AlphaFold Q5RBP4 Q641Z6 Q9H4M9 Q9WVK4 Q5E9R3

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