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 17477

Title: NMR Structure of the Mouse MFG-E8 C2 Domain   PubMed: 23262193

Deposition date: 2011-02-21 Original release date: 2012-08-31

Authors: Ye, Hong; Subramanian, Vivekanandan; Yu, Liang; Yoon, Ho Sup

Citation: Ye, Hong; Li, Baihong; Subramanian, Vivekanandan; Choi, Bo-Hwa; Yu, Liang; Harikishore, Amaravadhi; Harikishore, Amaravadhi; Chakraborty, Goutam; Baek, Kwanghee; Yoon, Ho Sup. "NMR solution structure of C2 domain of MFG-E8 and insights into its molecular recognition with phosphatidylserine"  Biochim. Biophys. Acta 1828, 1083-1093 (2013).

Assembly members:
MFG-E8_C2_domain, polymer, 170 residues, 18609.027 Da.

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):
MFG-E8_C2_domain: MKSGHGCSEPLGLKNNTIPD SQMSASSSYKTWNLRAFGWY PHLGRLDNQGKINAWTAQSN SAKEWLQVDLGTQRQVTGII TQGARDFGHIQYVASYKVAH SDDGVQWTVYEEQGSSKVFQ GNLDNNSHKKNIFEKPFMAR YVRVLPVSWHNRITLRLELL GCLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts573
15N chemical shifts160
1H chemical shifts973

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MFG-E8_C2_domain1

Entities:

Entity 1, MFG-E8_C2_domain 170 residues - 18609.027 Da.

1   METLYSSERGLYHISGLYCYSSERGLUPRO
2   LEUGLYLEULYSASNASNTHRILEPROASP
3   SERGLNMETSERALASERSERSERTYRLYS
4   THRTRPASNLEUARGALAPHEGLYTRPTYR
5   PROHISLEUGLYARGLEUASPASNGLNGLY
6   LYSILEASNALATRPTHRALAGLNSERASN
7   SERALALYSGLUTRPLEUGLNVALASPLEU
8   GLYTHRGLNARGGLNVALTHRGLYILEILE
9   THRGLNGLYALAARGASPPHEGLYHISILE
10   GLNTYRVALALASERTYRLYSVALALAHIS
11   SERASPASPGLYVALGLNTRPTHRVALTYR
12   GLUGLUGLNGLYSERSERLYSVALPHEGLN
13   GLYASNLEUASPASNASNSERHISLYSLYS
14   ASNILEPHEGLULYSPROPHEMETALAARG
15   TYRVALARGVALLEUPROVALSERTRPHIS
16   ASNARGILETHRLEUARGLEUGLULEULEU
17   GLYCYSLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: sodium phosphate 20 mM; sodium chloride 20 mM; sodium azide 0.01%; MFG-E8 C2 domain, [U-13C; U-15N], 0.8 mM; H2O 90%; D2O 10%

sample_2: sodium phosphate 20 mM; sodium chloride 20 mM; sodium azide 0.01%; MFG-E8 C2 domain, [U-13C; U-15N], 0.8 mM; D2O 100%

sample_conditions_1: ionic strength: 0.02 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D H(CC)(CO)NHsample_1isotropicsample_conditions_1
3D (H)CC(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

BMRB 15558
PDB

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts