BMRB Entry 15763
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15763
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Title: The solution structure of human Mia40 PubMed: 19182799
Deposition date: 2008-05-08 Original release date: 2009-02-09
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
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 240 |
| 15N chemical shifts | 66 |
| 1H chemical shifts | 393 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Human Mia40 | 1 |
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 | GLY | SER | PHE | THR | MET | SER | TYR | CYS | ARG | GLN | ||||
| 2 | GLU | GLY | LYS | ASP | ARG | ILE | ILE | PHE | VAL | THR | ||||
| 3 | LYS | GLU | ASP | HIS | GLU | THR | PRO | SER | SER | ALA | ||||
| 4 | GLU | LEU | VAL | ALA | ASP | ASP | PRO | ASN | ASP | PRO | ||||
| 5 | TYR | GLU | GLU | HIS | GLY | LEU | ILE | LEU | PRO | ASN | ||||
| 6 | GLY | ASN | ILE | ASN | TRP | ASN | CYS | PRO | CYS | LEU | ||||
| 7 | GLY | GLY | MET | ALA | SER | GLY | PRO | CYS | GLY | GLU | ||||
| 8 | GLN | PHE | LYS | SER | ALA | PHE | SER | CYS | PHE | HIS | ||||
| 9 | TYR | SER | THR | GLU | GLU | ILE | LYS | GLY | SER | ASP | ||||
| 10 | CYS | VAL | ASP | GLN | PHE | ARG | ALA | MET | GLN | GLU | ||||
| 11 | CYS | MET | GLN | LYS | TYR | PRO | ASP | LEU | TYR | PRO | ||||
| 12 | GLN | GLU | ASP | GLU | ASP | GLU | GLU | GLU | GLU | ARG | ||||
| 13 | GLU | LYS | LYS | PRO | ALA | GLU | GLN | ALA | GLU | GLU | ||||
| 14 | THR | ALA | PRO | ILE | GLU | ALA | THR | ALA | THR | LYS | ||||
| 15 | GLU | GLU | GLU | GLY | SER | SER |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_2 | isotropic | sample_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 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts