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 16198

Title: 1H, 13C and 15N backbone and side chain chemical shift assignments of N-terminal domain of Tim23.

Deposition date: 2009-03-06 Original release date: 2010-11-19

Authors: Thakur, Anushikha; Balasubramanyam, Chittoor; Silva, Patrick; Atreya, Hanudatta

Citation: Thakur, Anushikha; Balasubramanyam, Chittoor; Silva, Patrick; Atreya, Hanudatta. "1H.13C and 15N backbone and side-chain resonance assignments of N-terminal domain of a mitochondrial inner membrane translocase (TIM23) from S. cerevisiae"  . ., .-..

Assembly members:
Tim23, polymer, 104 residues, Formula weight is not available

Natural source:   Common Name: baker   Taxonomy ID: 4932   Superkingdom: not available   Kingdom: not available   Genus/species: Eukaryota Fungi

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

Entity Sequences (FASTA):
Tim23: MSWLFGDKTPTDDANAAVGG QDTTKPKELSLKQSLGFEPN INNIISGPGGMHVDTARLHP LAGLDKGVEYLDLEEEQLSS LEGSQGLIPSRGWTDDLCHH HHHH

Data sets:
Data typeCount
13C chemical shifts359
15N chemical shifts90
1H chemical shifts555

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Tim231

Entities:

Entity 1, Tim23 104 residues - Formula weight is not available

1   METSERTRPLEUPHEGLYASPLYSTHRPRO
2   THRASPASPALAASNALAALAVALGLYGLY
3   GLNASPTHRTHRLYSPROLYSGLULEUSER
4   LEULYSGLNSERLEUGLYPHEGLUPROASN
5   ILEASNASNILEILESERGLYPROGLYGLY
6   METHISVALASPTHRALAARGLEUHISPRO
7   LEUALAGLYLEUASPLYSGLYVALGLUTYR
8   LEUASPLEUGLUGLUGLUGLNLEUSERSER
9   LEUGLUGLYSERGLNGLYLEUILEPROSER
10   ARGGLYTRPTHRASPASPLEUCYSHISHIS
11   HISHISHISHIS

Samples:

sample_1: Tim23, [U-100% 13C; U-100% 15N], 1 mM; potassium phosphate 50 mM; sodium chloride 50 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1

Software:

XEASY, Bartels et al. - data analysis

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

DBJ GAA26110
EMBL CAA50640 CAA52274 CAA96296 CAY82210
GB AHY77105 AJP41342 AJT01777 AJT02149 AJT02522
REF NP_014414
SP P32897
TPG DAA10558

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