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 15763

Title: The solution structure of human Mia40   PubMed: 19182799

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

Citation: Banci, Lucia; Bertini, Ivano; Cefaro, Chiara; Ciofi-Baffoni, Simone; Gallo, Angelo; Martinelli, Manuele; Dionisia, Sideris; Nitsa, Katrakili; Tokatlidis, Kostas. "MIA40 is an oxidoreductase that catalyzes oxidative protein folding in mitochondria"  Nat. Struct. Mol. Biol. 16, 198-206 (2009).

Assembly members:
Human_Mia40, polymer, 146 residues, 15996.3 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):
Human_Mia40: GSFTMSYCRQEGKDRIIFVT KEDHETPSSAELVADDPNDP YEEHGLILPNGNINWNCPCL GGMASGPCGEQFKSAFSCFH YSTEEIKGSDCVDQFRAMQE CMQKYPDLYPQEDEDEEEER EKKPAEQAEETAPIEATATK EEEGSS

Data sets:
Data typeCount
13C chemical shifts240
15N chemical shifts66
1H chemical shifts393

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Human Mia401

Entities:

Entity 1, Human Mia40 146 residues - 15996.3 Da.

Residues 1-4 (not present in wild type gene) are non native as a consequence of gene cloning.

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

Samples:

sample_1: Human Mia40, [U-100% 15N], 0.5-1 mM; DTT 2 mM; potassium phosphate 50 mM; EDTA 0.5 mM

sample_2: Human Mia40, [U-100% 13C; U-100% 15N], 0.5-1 mM; DTT 2 mM; potassium phosphate 50 mM; EDTA 0.5 mM

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-1H NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

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

AMBER v8.0, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - geometry optimization, refinement

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

PECAN, Eghbalnia - Prediction of secondary structure

WhatIF, Vriend - Structure validation

ProcheckNMR, Laskowski and MacArthur - Structure validation

ATHNOS-CANDID v1.2, Herrmann, Guntert and Wuthrich - NOEs assignment, peak picking

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz

Related Database Links:

BMRB 17067
PDB
DBJ BAB71132 BAF83453
GB AAH17082 AAH33775 AIC53061 EAW64180 EAW64181
REF NP_001091972 NP_001185638 NP_653237 XP_001157417 XP_002813171
SP Q8N4Q1