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 25919

Title: LC3 FUNDC1 complex structure   PubMed: 27653272

Authors: Xia, Bin; Kuang, Yao

Citation: Kuang, Yao; Ma, Kaili; Zhou, Changqian; Ding, Pengfei; Zhu, Yushan; Chen, Quan; Xia, Bin. "Structural basis for the phosphorylation of FUNDC1 LIR as a molecular switch of mitophagy"  Autophagy 12, 2363-2373 (2016).

Assembly members:
entity_1, polymer, 120 residues, 14150.413 Da.
entity_2, polymer, 17 residues, 2071.041 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
entity_1: MPSEKTFKQRRTFEQRVEDV RLIREQHPTKIPVIIERYKG EKQLPVLDKTKFLVPDHVNM SELIKIIRRRLQLNANQAFF LLVNGHSMVSVSTPISEVYE SEKDEDGFLYMVYASQETFG
entity_2: DYESDDDSYEVLDLTEY

Data sets:
Data typeCount
13C chemical shifts533
15N chemical shifts132
1H chemical shifts955

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 120 residues - 14150.413 Da.

1   METPROSERGLULYSTHRPHELYSGLNARG
2   ARGTHRPHEGLUGLNARGVALGLUASPVAL
3   ARGLEUILEARGGLUGLNHISPROTHRLYS
4   ILEPROVALILEILEGLUARGTYRLYSGLY
5   GLULYSGLNLEUPROVALLEUASPLYSTHR
6   LYSPHELEUVALPROASPHISVALASNMET
7   SERGLULEUILELYSILEILEARGARGARG
8   LEUGLNLEUASNALAASNGLNALAPHEPHE
9   LEULEUVALASNGLYHISSERMETVALSER
10   VALSERTHRPROILESERGLUVALTYRGLU
11   SERGLULYSASPGLUASPGLYPHELEUTYR
12   METVALTYRALASERGLNGLUTHRPHEGLY

Entity 2, entity_2 17 residues - 2071.041 Da.

1   ASPTYRGLUSERASPASPASPSERTYRGLU
2   VALLEUASPLEUTHRGLUTYR

Samples:

sample_1: entity_1, [U-13C; U-15N], 0.9 mM; entity_2 1.8 mM; sodium chloride 100 mM; sodium phosphate 25 mM; D2O, [U-2H], 10%; DSS 1%

sample_conditions_1: ionic strength: 0.15 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz

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