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BMRB Entry 17067

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17067
MolProbity Validation Chart

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Title: Complex hMia40-hCox17   PubMed: 21059946

Deposition date: 2010-07-20 Original release date: 2010-11-15

Authors: Bertini, Ivano; Ciofi-Baffoni, Simone; Gallo, Angelo

Citation: Banci, Lucia; Bertini, Ivano; Cefaro, Chiara; Cenacchi, Lucia; Ciofi-Baffoni, Simone; Felli, Isabella Caterina; Gallo, Angelo; Gonnelli, Leonardo; Luchinat, Enrico; Sideris, Dionisia; Tokatlidis, Kostas. "Molecular chaperone function of Mia40 triggers consecutive induced folding steps of the substrate in mitochondrial protein import."  Proc. Natl. Acad. Sci. U.S.A. 107, 20190-20195 (2010).

Assembly members:
Mia40, polymer, 146 residues, 6727.517 Da.
Cox17, polymer, 67 residues, 2412.846 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):
Mia40: GSFTMSYCRQEGKDRIIFVT KEDHETPSSAELVADDPNDP YEEHGLILPNGNINWNSPCL GGMASGPCGEQFKSAFSCFH YSTEEIKGSDCVDQFRAMQE CMQKYPDLYPQEDEDEEEER EKKPAEQAEETAPIEATATK EEEGSS
Cox17: GSFTMPGLVDSNPAPPESQE KKPLKPCCASPETKKARDAS IIEKGEEHCGHLIEAHKESM RALGFKI

Data sets:
Data typeCount
13C chemical shifts526
15N chemical shifts148
1H chemical shifts461

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Mia401
2Cox172

Entities:

Entity 1, Mia40 146 residues - 6727.517 Da.

1   GLYSERPHETHRMETSERTYRCYSARGGLN
2   GLUGLYLYSASPARGILEILEPHEVALTHR
3   LYSGLUASPHISGLUTHRPROSERSERALA
4   GLULEUVALALAASPASPPROASNASPPRO
5   TYRGLUGLUHISGLYLEUILELEUPROASN
6   GLYASNILEASNTRPASNSERPROCYSLEU
7   GLYGLYMETALASERGLYPROCYSGLYGLU
8   GLNPHELYSSERALAPHESERCYSPHEHIS
9   TYRSERTHRGLUGLUILELYSGLYSERASP
10   CYSVALASPGLNPHEARGALAMETGLNGLU
11   CYSMETGLNLYSTYRPROASPLEUTYRPRO
12   GLNGLUASPGLUASPGLUGLUGLUGLUARG
13   GLULYSLYSPROALAGLUGLNALAGLUGLU
14   THRALAPROILEGLUALATHRALATHRLYS
15   GLUGLUGLUGLYSERSER

Entity 2, Cox17 67 residues - 2412.846 Da.

1   GLYSERPHETHRMETPROGLYLEUVALASP
2   SERASNPROALAPROPROGLUSERGLNGLU
3   LYSLYSPROLEULYSPROCYSCYSALASER
4   PROGLUTHRLYSLYSALAARGASPALASER
5   ILEILEGLULYSGLYGLUGLUHISCYSGLY
6   HISLEUILEGLUALAHISLYSGLUSERMET
7   ARGALALEUGLYPHELYSILE

Samples:

sample_1: Mia40, [U-100% 13C; U-100% 15N], 0.5 mM; Cox17 0.5 mM; Phosphate 50 mM; EDTA 0.5 mM; H2O 90%; D2O 10%

sample_2: Cox17, [U-100% 13C; U-100% 15N], 0.5 mM; Mia40 0.5 mM; Phosphate 50 mM; EDTA 0.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D ω1- 13C-edited, ω2-13C-filtered NOESYsample_1isotropicsample_conditions_1
3D ω1- 13C-edited, ω2-13C-filtered NOESYsample_2isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CARA v2, Keller and Wuthrich - chemical shift assignment, data analysis

AMBER v10.0, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 500 MHz

Related Database Links:

BMRB 15763 17821
PDB
DBJ BAB71132 BAF83453
GB AAH17082 AAH33775 AIC53061 EAW64180 EAW64181
REF NP_001091972 NP_001185638 NP_653237 XP_001157417 XP_002813171
SP Q8N4Q1

Download simulated HSQC data in one of the following formats:
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