BMRB Entry 17646
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17646
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Title: Solution structure of the N-terminal domain of human anamorsin PubMed: 21700214
Deposition date: 2011-05-13 Original release date: 2011-06-30
Authors: Banci, Lucia; Bertini, Ivano; Ciofi-Baffoni, Simone; Boscaro, Francesca; Chatzi, Afroditi; Mikolajczyk, Maciej; Tokatlidis, Kostas; Winkelmann, Julia
Citation: Banci, Lucia; Bertini, Ivano; Ciofi-Baffoni, Simone; Boscaro, Francesca; Chatzi, Afroditi; Mikolajczyk, Maciej; Tokatlidis, Kostas; Winkelmann, Julia. "Anamorsin Is a [2Fe-2S] Cluster-Containing Substrate of the Mia40-Dependent Mitochondrial Protein Trapping Machinery." Chem. Biol. 18, 794-804 (2011).
Assembly members:
Anamorsin, polymer, 172 residues, 18539.293 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):
Anamorsin: MADFGISAGQFVAVVWDKSS
PVEALKGLVDKLQALTGNEG
RVSVENIKQLLQSAHKESSF
DIILSGLVPGSTTLHSAEIL
AEIARILRPGGCLFLKEPVE
TAVDNNSKVKTASKLCSALT
LSGLVEVKELQREPLTPEEV
QSVREHLGHESDNLLFVQIT
GKKPNFEVGSSR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 707 |
| 15N chemical shifts | 181 |
| 1H chemical shifts | 1141 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Anamorsin | 1 |
Entities:
Entity 1, Anamorsin 172 residues - 18539.293 Da.
This is the N-terminal folded domain (from 1 to 172 residues) of anamorsin
| 1 | MET | ALA | ASP | PHE | GLY | ILE | SER | ALA | GLY | GLN | ||||
| 2 | PHE | VAL | ALA | VAL | VAL | TRP | ASP | LYS | SER | SER | ||||
| 3 | PRO | VAL | GLU | ALA | LEU | LYS | GLY | LEU | VAL | ASP | ||||
| 4 | LYS | LEU | GLN | ALA | LEU | THR | GLY | ASN | GLU | GLY | ||||
| 5 | ARG | VAL | SER | VAL | GLU | ASN | ILE | LYS | GLN | LEU | ||||
| 6 | LEU | GLN | SER | ALA | HIS | LYS | GLU | SER | SER | PHE | ||||
| 7 | ASP | ILE | ILE | LEU | SER | GLY | LEU | VAL | PRO | GLY | ||||
| 8 | SER | THR | THR | LEU | HIS | SER | ALA | GLU | ILE | LEU | ||||
| 9 | ALA | GLU | ILE | ALA | ARG | ILE | LEU | ARG | PRO | GLY | ||||
| 10 | GLY | CYS | LEU | PHE | LEU | LYS | GLU | PRO | VAL | GLU | ||||
| 11 | THR | ALA | VAL | ASP | ASN | ASN | SER | LYS | VAL | LYS | ||||
| 12 | THR | ALA | SER | LYS | LEU | CYS | SER | ALA | LEU | THR | ||||
| 13 | LEU | SER | GLY | LEU | VAL | GLU | VAL | LYS | GLU | LEU | ||||
| 14 | GLN | ARG | GLU | PRO | LEU | THR | PRO | GLU | GLU | VAL | ||||
| 15 | GLN | SER | VAL | ARG | GLU | HIS | LEU | GLY | HIS | GLU | ||||
| 16 | SER | ASP | ASN | LEU | LEU | PHE | VAL | GLN | ILE | THR | ||||
| 17 | GLY | LYS | LYS | PRO | ASN | PHE | GLU | VAL | GLY | SER | ||||
| 18 | SER | ARG |
Samples:
sample_1: Anamorsin, [U-100% 15N], 0.5 – 1 mM; sodium phosphate 50 mM; DTT 2 mM; H2O 90%; D2O 10%
sample_2: anamorsin, [U-100% 13C; U-100% 15N], 0.5 – 1 mM; sodium phosphate 50 mM; DTT 2 mM; H2O 90%; D2O 10%
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 TOCSY | 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 HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection, processing
CARA v2.0, Keller and Wuthrich - chemical shift assignment
CANDID, Herrmann, Guntert and Wuthrich - automatic NOEs assignment
TALOS, Cornilescu, Delaglio and Bax - Backbone torsion angle calculation
CYANA v1.3, Guntert, Mumenthaler and Wuthrich - structure solution
AMBER v10.0, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement
ProcheckNMR, Laskowski and MacArthur - data analysis
WhatIF, Vriend - data analysis
PSVS, Bhattacharya and Montelione - data analysis
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 900 MHz
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAG58080 BAK62448 |
| GB | AAC24311 AAG44562 AAH02568 AAH24196 AAH67303 |
| REF | NP_001233553 NP_001295287 NP_064709 XP_003263147 XP_003823791 |
| SP | Q6FI81 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts