BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 4491

Title: Solution structure of the apo EH1 domain of mouse Eps15   PubMed: 9835057

Authors: Whitehead, B.; Tessari, M.; Carotenuto, A.; van Bergen en Henegouwen, P.; Vuister, G.

Citation: Whitehead, B.; Tessari, M.; Versteeg, H.; van Delft, S.; van Bergen en Henegouwen, P.; Vuister, G.. "Sequence-specific 1H, 13C and 15N assignment of the EH1 domain of mouse Eps15"  J. Biomol. NMR 12, 465-466 (1998).

Assembly members:
Eps15, polymer, 120 residues, Formula weight is not available

Natural source:   Common Name: house mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

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

Entity Sequences (FASTA):
Eps15: MAAAAQLSLTQLSSGNPVYE KYYRQVEAGNTGRVLALDAA AFLKKSGLPDLILGKIWDLA DTDGKGVLSKQEFFVALRLV ACAQNGLEVSLSSLSLAVPP PRFHDSSSPLLTSGPSVAEL

Data sets:
Data typeCount
13C chemical shifts501
15N chemical shifts124
1H chemical shifts774

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Eps151

Entities:

Entity 1, Eps15 120 residues - Formula weight is not available

1   METALAALAALAALAGLNLEUSERLEUTHR
2   GLNLEUSERSERGLYASNPROVALTYRGLU
3   LYSTYRTYRARGGLNVALGLUALAGLYASN
4   THRGLYARGVALLEUALALEUASPALAALA
5   ALAPHELEULYSLYSSERGLYLEUPROASP
6   LEUILELEUGLYLYSILETRPASPLEUALA
7   ASPTHRASPGLYLYSGLYVALLEUSERLYS
8   GLNGLUPHEPHEVALALALEUARGLEUVAL
9   ALACYSALAGLNASNGLYLEUGLUVALSER
10   LEUSERSERLEUSERLEUALAVALPROPRO
11   PROARGPHEHISASPSERSERSERPROLEU
12   LEUTHRSERGLYPROSERVALALAGLULEU

Samples:

sample_one: Eps15, [U-15N], 1.0 mM; potassium phosphate 100 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_two: Eps15, [U-15N; U-13C], 1.0 mM; potassium phosphate 100 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_cond_1: ionic strength: 100 mM; pH: 5.2; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions

Software:

No software information available

NMR spectrometers:

  • Varian UnityInova 500 MHz
  • Varian UnityInova 750 MHz

Related Database Links:

BMRB 4140
PDB