BMRB Entry 30200

Title:
Sparse-restraint solution NMR structure of micelle-solubilized cytosolic amino terminal domain of C. elegans mechanosensory ion channel MEC-4 refined by restrained Rosetta
Deposition date:
2016-11-04
Original release date:
2017-01-26
Authors:
Everett, J.; Liu, G.; Mao, B.; Driscoll, M.; Montelione, G.
Citation:

Citation: Everett, J.; Liu, G.; Mao, B.; Driscoll, M.; Montelione, G.. "Sparse-restraint solution NMR structure of micelle-solubilized cytosolic amino terminal domain of C. elegans mechanosensory ion channel MEC-4 refined by restrained Rosetta"  .

Assembly members:

Assembly members:
entity_1, polymer, 111 residues, 13296.793 Da.

Natural source:

Natural source:   Common Name: C. elegans   Taxonomy ID: 6239   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Caenorhabditis elegans

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts287
15N chemical shifts91
1H chemical shifts91

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 111 residues - 13296.793 Da.

1   METSERTRPMETGLNASNLEULYSASNTYR
2   GLNHISLEUARGASPPROSERGLUTYRMET
3   SERGLNVALTYRGLYASPPROLEUALATYR
4   LEUGLNGLUTHRTHRLYSPHEVALTHRGLU
5   ARGGLUTYRTYRGLUASPPHEGLYTYRGLY
6   GLUCYSPHEASNSERTHRGLUSERGLUVAL
7   GLNCYSGLULEUILETHRGLYGLUPHEASP
8   PROLYSLEULEUPROTYRASPLYSARGLEU
9   ALATRPHISPHELYSGLUPHECYSTYRLYS
10   THRSERALAHISGLYILEPROMETILEGLY
11   GLUALAPROLEUGLUHISHISHISHISHIS
12   HIS

Samples:

sample_1: Degenerin mec-4, [U-13C; U-15N; U-2H], 1.5 mM

sample_conditions_1: ionic strength: 0.025 M; pH: 6.8; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

AutoAssign v2.4.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

Restrained Rosetta, Mao, Baker, Montelione - refinement

SPARKY, Goddard - peak picking

TALOS, Cornilescu, Delaglio and Bax - structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz

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