BMRB Entry 30500

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30500
MolProbity Validation Chart

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Title:
Structure of a protein complex
Deposition date:
2018-07-20
Original release date:
2019-11-12
Authors:
Buel, G.; Walters, K.
Citation:

Citation: Biancospino, Matteo; Buel, Gwen; Nino, Carlos; Maspero, Elena; Scotto di Perrotolo, Rossella; Raimondi, Andrea; Redlingshofer, Lisa; Weber, Janine; Brodsky, Frances; Walters, Kylie; Polo, Simona. "Clathrin light chain A drives selective myosin VI recruitment to clathrin-coated pits under membrane tension"  Nat. Commun. 10, 4974-4974 (2019).
PubMed: 31672988

Assembly members:

Assembly members:
entity_1, polymer, 87 residues, 9991.648 Da.
entity_2, polymer, 24 residues, 2373.528 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPLGSRPKMTPEQMAKEMSE FLSRGPAVLATKAAAGTKKY DLSKWKYAELRDTINTSCDI ELLAACREEFHRRLKVYHAW KSKNKKR
entity_2: GPLGSPEFIENDEAFAILDG GAPG

Data sets:
Data typeCount
13C chemical shifts431
15N chemical shifts107
1H chemical shifts713

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 87 residues - 9991.648 Da.

1   GLYPROLEUGLYSERARGPROLYSMETTHR
2   PROGLUGLNMETALALYSGLUMETSERGLU
3   PHELEUSERARGGLYPROALAVALLEUALA
4   THRLYSALAALAALAGLYTHRLYSLYSTYR
5   ASPLEUSERLYSTRPLYSTYRALAGLULEU
6   ARGASPTHRILEASNTHRSERCYSASPILE
7   GLULEULEUALAALACYSARGGLUGLUPHE
8   HISARGARGLEULYSVALTYRHISALATRP
9   LYSSERLYSASNLYSLYSARG

Entity 2, entity_2 24 residues - 2373.528 Da.

1   GLYPROLEUGLYSERPROGLUPHEILEGLU
2   ASNASPGLUALAPHEALAILELEUASPGLY
3   GLYALAPROGLY

Samples:

sample_1: Myosin VI 1050-1131, [U-13C; U-15N], 0.36 mM; Clathrin Light Chain Alpha 46-61 0.36 mM; NaCl 50 mM; NaPO4 20 mM

sample_2: Myosin VI 1050-1131 0.4 mM; Clathrin Light Chain Alpha 46-61, [U-13C; U-15N], 0.4 mM; NaCl 50 mM; NaPO4 20 mM

sample_conditions_1: ionic strength: 70 mM; pH: 6.5; pressure: 760 mmHg; temperature: 283.2 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
half-filtered 3D 1H-13C NOESYsample_1isotropicsample_conditions_1
half-filtered 3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

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

XEASY, Bartels et al. - chemical shift assignment, peak picking

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

NMR spectrometers:

  • Bruker AvanceIII 850 MHz
  • Bruker AvanceIII 700 MHz

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