BMRB Entry 18029
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18029
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Title: 1H, 13C, and 15N Chemical Shift Assignments for sf-ALR PubMed: 21383138
Deposition date: 2011-10-31 Original release date: 2011-11-04
Authors: Ivano, Bertini; Simone, Ciofi-Baffoni; Angelo, Gallo
Citation: Banci, Lucia; Bertini, Ivano; Calderone, Vito; Cefaro, Chiara; Ciofi-Baffoni, Simone; Gallo, Angelo; Kallergi, Emmanouela; Lionaki, Eirini; Pozidis, Charalambos; Tokatlidis, Kostas. "Molecular recognition and substrate mimicry drive the electron-transfer process between MIA40 and ALR." Proc. Natl. Acad. Sci. U.S.A. 108, 4811-4816 (2011).
Assembly members:
sf-ALR, polymer, 129 residues, 14991.9 Da.
FAD, non-polymer, 785.550 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):
sf-ALR: GSFTMRTQQKRDTKFREDCP
PDREELGRHSWAVLHTLAAY
YPDLPTPEQQQDMAQFIHLF
SKFYPCEECAEDLRKRLARN
HPDTRTRAAFTQWLCHLHNE
VNRKLGKPDFDCSKVDERWR
DGWKDGSCD
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 411 |
15N chemical shifts | 107 |
1H chemical shifts | 503 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | sf-ALR, chain 1 | 1 |
2 | sf-ALR, chain 2 | 1 |
3 | FAD, 1 | 2 |
4 | FAD, 2 | 2 |
Entities:
Entity 1, sf-ALR, chain 1 129 residues - 14991.9 Da.
The first four residue (GSFT) are remaining from the TEV cleavage site
1 | GLY | SER | PHE | THR | MET | ARG | THR | GLN | GLN | LYS | ||||
2 | ARG | ASP | THR | LYS | PHE | ARG | GLU | ASP | CYS | PRO | ||||
3 | PRO | ASP | ARG | GLU | GLU | LEU | GLY | ARG | HIS | SER | ||||
4 | TRP | ALA | VAL | LEU | HIS | THR | LEU | ALA | ALA | TYR | ||||
5 | TYR | PRO | ASP | LEU | PRO | THR | PRO | GLU | GLN | GLN | ||||
6 | GLN | ASP | MET | ALA | GLN | PHE | ILE | HIS | LEU | PHE | ||||
7 | SER | LYS | PHE | TYR | PRO | CYS | GLU | GLU | CYS | ALA | ||||
8 | GLU | ASP | LEU | ARG | LYS | ARG | LEU | ALA | ARG | ASN | ||||
9 | HIS | PRO | ASP | THR | ARG | THR | ARG | ALA | ALA | PHE | ||||
10 | THR | GLN | TRP | LEU | CYS | HIS | LEU | HIS | ASN | GLU | ||||
11 | VAL | ASN | ARG | LYS | LEU | GLY | LYS | PRO | ASP | PHE | ||||
12 | ASP | CYS | SER | LYS | VAL | ASP | GLU | ARG | TRP | ARG | ||||
13 | ASP | GLY | TRP | LYS | ASP | GLY | SER | CYS | ASP |
Entity 2, FAD, 1 - C27 H33 N9 O15 P2 - 785.550 Da.
1 | FAD |
Samples:
sample_1: sf-ALR, [U-100% 13C; U-100% 15N], 1 mM; potassium phosphate 50 mM; EDTA 0.5 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 50 mM; pH: 7.2; pressure: 1 atm; temperature: 308 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1, Bruker Biospin - collection, processing
CARA v2.0, Keller and Wuthrich - chemical shift assignment, data analysis
NMR spectrometers:
- Bruker Avance 900 MHz
- Bruker Avance 500 MHz
Related Database Links:
BMRB | 26515 26533 |
PDB | |
DBJ | BAI46852 |
EMBL | CAB87993 |
GB | AAA96390 AAD17328 AAD36986 AAG43494 AAH02429 |
REF | NP_005253 XP_004057029 XP_007980253 |
SP | P55789 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts