Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18518
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Rogov, Vladimir; Suzuki, Hironori; Fiskin, Evgenij; Wild, Philipp; Kniss, Andreas; Rozenknop, Alexis; Kato, Ryuichi; Kawasaki, Masato; McEwan, David; Lohr, Frank; Guntert, Peter; Dikic, Ivan; Wakatsuki, Soichi; Dotsch, Volker. "Structural basis for phosphorylation-triggered autophagic clearance of Salmonella." Biochem. J. 454, 459-466 (2013).
PubMed: 23805866
Assembly members:
entity_1, polymer, 119 residues, 13965.232 Da.
entity_2, polymer, 17 residues, 2245.827 Da.
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 Vector: pETm60_UB3
Entity Sequences (FASTA):
entity_1: GAMGKTFKQRRTFEQRVEDV
RLIREQHPTKIPVIIERYKG
EKQLPVLDKTKFLVPDHVNM
SELIKIIRRRLQLNANQAFF
LLVNGHSMVSVSTPISEVYE
SEKDEDGFLYMVYASQETF
entity_2: NXXGXXEDXFVEIRMAE
Data type | Count |
13C chemical shifts | 548 |
15N chemical shifts | 141 |
1H chemical shifts | 1028 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | entity_1 | 1 |
2 | entity_2 | 2 |
Entity 1, entity_1 119 residues - 13965.232 Da.
Residues 1-4 are expression tag. Residues 5-119 correspond to residues 5-119 of human Microtubule-associated proteins 1A/1B light chain 3B (UniProtKB entry Q9GZQ8)
1 | GLY | ALA | MET | GLY | LYS | THR | PHE | LYS | GLN | ARG | ||||
2 | ARG | THR | PHE | GLU | GLN | ARG | VAL | GLU | ASP | VAL | ||||
3 | ARG | LEU | ILE | ARG | GLU | GLN | HIS | PRO | THR | LYS | ||||
4 | ILE | PRO | VAL | ILE | ILE | GLU | ARG | TYR | LYS | GLY | ||||
5 | GLU | LYS | GLN | LEU | PRO | VAL | LEU | ASP | LYS | THR | ||||
6 | LYS | PHE | LEU | VAL | PRO | ASP | HIS | VAL | ASN | MET | ||||
7 | SER | GLU | LEU | ILE | LYS | ILE | ILE | ARG | ARG | ARG | ||||
8 | LEU | GLN | LEU | ASN | ALA | ASN | GLN | ALA | PHE | PHE | ||||
9 | LEU | LEU | VAL | ASN | GLY | HIS | SER | MET | VAL | SER | ||||
10 | VAL | SER | THR | PRO | ILE | SER | GLU | VAL | TYR | GLU | ||||
11 | SER | GLU | LYS | ASP | GLU | ASP | GLY | PHE | LEU | TYR | ||||
12 | MET | VAL | TYR | ALA | SER | GLN | GLU | THR | PHE |
Entity 2, entity_2 17 residues - 2245.827 Da.
Residues 169-185 correspond to residues 169-185 of human Optineurin sequence (UniProtKB entry Q96CV9). All serines in the peptide are phosphoserines (SEP).
1 | ASN | SEP | SEP | GLY | SEP | SEP | GLU | ASP | SEP | PHE | ||||
2 | VAL | GLU | ILE | ARG | MET | ALA | GLU |
sample_1: entity_1, [U-98% 13C; U-98% 15N], 0.6 ± 0.05 mM; entity_2 4.9 ± 0.5 mM; sodium phosphate 70 mM; sodium chloride 30 mM; DSS 0.3 mM; Protease inhibitors cocktail 5 mM; H2O 95%; D2O 5%
sample_2: entity_1, [U-98% 13C; U-98% 15N], 2.5 ± 0.05 mM; entity_2 0.4 ± 0.04 mM; sodium phosphate 70 mM; sodium chloride 30 mM; DSS 0.3 mM; Protease inhibitors cocktail 5 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 0.05 M; pH: 6.8; pressure: 1 atm; temperature: 288 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | 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 aliphatic | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
3D NOESY-[13C,1H]-HSQC 13C/15N filtered in F1 | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY F1,F2 13C/15N filtered | sample_2 | isotropic | sample_conditions_1 |
3D NOESY-[15N,1H]-FHSQC | sample_1 | isotropic | sample_conditions_1 |
TOPSPIN v2, Bruker Biospin - chemical shift calculation, collection, processing
SPARKY v3.114, Goddard - chemical shift assignment, data analysis, peak picking
CYANA v2, Guntert, Mumenthaler and Wuthrich - structure solution
OPALp, Koradi, Billeter and Guntert - refinement
UNP | Q9GZQ8 Q96CV9 |
BMRB | 15877 |
PDB | |
DBJ | BAB15169 BAB22364 BAB22569 BAB22641 BAB22855 |
EMBL | CAD38970 CAG31435 CAL38438 |
GB | AAA20645 AAB72082 AAG09686 AAG23182 AAH18634 |
REF | NP_001001169 NP_001026632 NP_001078950 NP_001177219 NP_001180554 |
SP | A6NCE7 O41515 Q62625 Q9CQV6 Q9GZQ8 |
TPG | DAA20021 |
AlphaFold | Q6NW02 Q9Y218 A6NCE7 O41515 Q62625 Q9CQV6 Q9GZQ8 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks