BMRB Entry 26801
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR26801
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Title: 1H, 13C and 15N Assignment of NFU1 Iron-Sulfur Cluster Scaffold Homolog from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR2876 PubMed: 27818104
Deposition date: 2016-05-16 Original release date: 2016-06-29
Authors: Liu, Gaohua; Xiao, Rong; Janjua, Haleema; Hamilton, Keith; Shastry, Ritu; Kohan, Eitan; Acton, Thomas; Everett, John; Huang, Yuangpeng; Montelione, Gaetano
Citation: Cai, Kai; Liu, Gaohua; Frederick, Ronnie; Xiao, Rong; Montelione, Gaetano; Markley, John. "Structural/Functional Properties of Human NFU1, an Intermediate [4Fe-4S] Carrier in Human Mitochondrial Iron-Sulfur Cluster Biogenesis" Structure 24, 2080-2091 (2016).
Assembly members:
NFU1, polymer, 216 residues, Formula weight is not available
Natural source: Common Name: humans Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
NFU1: MGSSHHHHHHSSGLVPRGSH
MFIQTQDTPNPNSLKFIPGK
PVLETRTMDFPTPAAAFRSP
LARQLFRIEGVKSVFFGPDF
ITVTKENEELDWNLLKPDIY
ATIMDFFASGLPLVTEETPS
GEAGSEEDDEVVAMIKELLD
TRIRPTVQEDGGDVIYKGFE
DGIVQLKLQGSCTSCPSSII
TLKNGIQNMLQFYIPEVEGV
EQVMDDESDEKEANSP
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 680 |
15N chemical shifts | 196 |
1H chemical shifts | 1380 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | NFU1 | 1 |
Entities:
Entity 1, NFU1 216 residues - Formula weight is not available
1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
2 | SER | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | ||||
3 | MET | PHE | ILE | GLN | THR | GLN | ASP | THR | PRO | ASN | ||||
4 | PRO | ASN | SER | LEU | LYS | PHE | ILE | PRO | GLY | LYS | ||||
5 | PRO | VAL | LEU | GLU | THR | ARG | THR | MET | ASP | PHE | ||||
6 | PRO | THR | PRO | ALA | ALA | ALA | PHE | ARG | SER | PRO | ||||
7 | LEU | ALA | ARG | GLN | LEU | PHE | ARG | ILE | GLU | GLY | ||||
8 | VAL | LYS | SER | VAL | PHE | PHE | GLY | PRO | ASP | PHE | ||||
9 | ILE | THR | VAL | THR | LYS | GLU | ASN | GLU | GLU | LEU | ||||
10 | ASP | TRP | ASN | LEU | LEU | LYS | PRO | ASP | ILE | TYR | ||||
11 | ALA | THR | ILE | MET | ASP | PHE | PHE | ALA | SER | GLY | ||||
12 | LEU | PRO | LEU | VAL | THR | GLU | GLU | THR | PRO | SER | ||||
13 | GLY | GLU | ALA | GLY | SER | GLU | GLU | ASP | ASP | GLU | ||||
14 | VAL | VAL | ALA | MET | ILE | LYS | GLU | LEU | LEU | ASP | ||||
15 | THR | ARG | ILE | ARG | PRO | THR | VAL | GLN | GLU | ASP | ||||
16 | GLY | GLY | ASP | VAL | ILE | TYR | LYS | GLY | PHE | GLU | ||||
17 | ASP | GLY | ILE | VAL | GLN | LEU | LYS | LEU | GLN | GLY | ||||
18 | SER | CYS | THR | SER | CYS | PRO | SER | SER | ILE | ILE | ||||
19 | THR | LEU | LYS | ASN | GLY | ILE | GLN | ASN | MET | LEU | ||||
20 | GLN | PHE | TYR | ILE | PRO | GLU | VAL | GLU | GLY | VAL | ||||
21 | GLU | GLN | VAL | MET | ASP | ASP | GLU | SER | ASP | GLU | ||||
22 | LYS | GLU | ALA | ASN | SER | PRO |
Samples:
sample_1: NFU1, [U-100% 13C; U-100% 15N], 0.88 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 100 mM; pH: 7.5; 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-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
XEASY, Bartels et al. - data analysis
TOPSPIN, Bruker Biospin - collection
NMR spectrometers:
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts