BMRB Entry 11491

Title:
Solution structure and siRNA-mediated knockdown analysis of the mitochondrial disease-related protein C12orf65 (ICT2)
Deposition date:
2012-03-28
Original release date:
2012-08-06
Authors:
Enomoto, Mayu; Tochio, Naoya; Tomizawa, Tadashi; Koshiba, Seizo; Guntert, Peter; Kigawa, Takanori; Yokoyama, Shigeyuki; Nameki, Nobukazu
Citation:

Citation: Kogure, H.; Hikawa, Y.; Hagihara, M.; Tochio, N.; Koshiba, S.; Inoue, Y.; Guntert, P.; Kigawa, T.; Yokoyama, S.; Nameki, N.. "Solution structure and siRNA-mediated knockdown analysis of the mitochondrial disease-related protein C12orf65"  Proteins ., .-. (2012).
PubMed: 22821833

Assembly members:

Assembly members:
entity, polymer, 115 residues, 12305.086 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: P070213-30

Data sets:
Data typeCount
13C chemical shifts469
15N chemical shifts104
1H chemical shifts758

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1C12orf651

Entities:

Entity 1, C12orf65 115 residues - 12305.086 Da.

Residues 1-5 and 110-115 represent a non-native affinity tag.

1   GLYSERSERGLYSERSERGLYLYSTRPGLY
2   LEUARGLEUGLNGLULYSPROALALEULEU
3   PHEPROGLYMETALAALASERTHRVALGLN
4   VALALAGLYARGLYSASPTYRPROALALEU
5   LEUPROLEUASNGLUSERGLULEUGLUGLU
6   GLNPHEVALLYSGLYHISGLYPROGLYGLY
7   GLNALATHRASNLYSTHRSERASNCYSVAL
8   VALLEULYSHISVALPROSERGLYILEVAL
9   VALLYSCYSHISGLNTHRARGSERVALASP
10   GLNASNARGLYSILEALAARGLYSVALLEU
11   GLNGLULYSVALASPVALPHETYRASNSER
12   GLYPROSERSERGLY

Samples:

sample_1: entity, [U-13C; U-15N], 0.96 mM; TRIS, [U-2H], 20 mM; sodium chloride 100 mM; DTT, [U-2H], 1 mM; sodium azide 0.02%; D2O, [U-2H], 10%; H2O 90%

sample_conditions_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

NMRView, Johnson, One Moon Scientific - data analysis

Kujira, Kobayashi, N. - chemical shift assignment, data analysis

CYANA v2.0, Guntert, Mumenthaler and Wuthrich - structure solution

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

NMR spectrometers:

  • Bruker Avance 900 MHz

Related Database Links:

PDB
DBJ BAB28408 BAC30294 BAE24439
GB AAH46909 EDL19595 EDL19596
REF NP_001128189 NP_082586
SP Q80VP5
AlphaFold Q80VP5

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