BMRB Entry 17007
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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/BMR17007
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Title: Solution structure of alpha-mannosidase binding domain of Atg34 PubMed: 20659891
Deposition date: 2010-06-18 Original release date: 2010-08-12
Authors: Watanabe, Yasunori; Noda, Nobuo N; Kumeta, Hiroyuki; Suzuki, Kuninori; Ohsumi, Yoshinori; Inagaki, Fuyuhiko
Citation: Watanabe, Yasunori; Noda, Nobuo; Kumeta, Hiroyuki; Suzuki, Kuninori; Ohsumi, Yoshinori; Inagaki, Fuyuhiko. "Selective Transport of {alpha}-Mannosidase by Autophagic Pathways: STRUCTURAL BASIS FOR CARGO RECOGNITION BY Atg19 AND Atg34." J. Biol. Chem. 285, 30026-30033 (2010).
Assembly members:
Alpha-mannosidase_binding_domain_of_Atg34, polymer, 107 residues, 12965.639 Da.
Natural source: Common Name: baker Taxonomy ID: 4932 Superkingdom: not available Kingdom: not available Genus/species: Eukaryota Fungi
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Alpha-mannosidase_binding_domain_of_Atg34: GPHMNDPLLHVEVSNEDNSL
HFILYNKTNIIIPGNCTFEF
SSQISEVFSIKMGPHEIGIK
GQKELWFFPSLPTPLSNYTM
KVVNQDGETILVGKCADSNE
ITLKSPL
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 455 |
15N chemical shifts | 106 |
1H chemical shifts | 742 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Alpha-mannosidase_binding_domain_of_Atg34 | 1 |
Entities:
Entity 1, Alpha-mannosidase_binding_domain_of_Atg34 107 residues - 12965.639 Da.
1 | GLY | PRO | HIS | MET | ASN | ASP | PRO | LEU | LEU | HIS | ||||
2 | VAL | GLU | VAL | SER | ASN | GLU | ASP | ASN | SER | LEU | ||||
3 | HIS | PHE | ILE | LEU | TYR | ASN | LYS | THR | ASN | ILE | ||||
4 | ILE | ILE | PRO | GLY | ASN | CYS | THR | PHE | GLU | PHE | ||||
5 | SER | SER | GLN | ILE | SER | GLU | VAL | PHE | SER | ILE | ||||
6 | LYS | MET | GLY | PRO | HIS | GLU | ILE | GLY | ILE | LYS | ||||
7 | GLY | GLN | LYS | GLU | LEU | TRP | PHE | PHE | PRO | SER | ||||
8 | LEU | PRO | THR | PRO | LEU | SER | ASN | TYR | THR | MET | ||||
9 | LYS | VAL | VAL | ASN | GLN | ASP | GLY | GLU | THR | ILE | ||||
10 | LEU | VAL | GLY | LYS | CYS | ALA | ASP | SER | ASN | GLU | ||||
11 | ILE | THR | LEU | LYS | SER | PRO | LEU |
Samples:
sample_1: sodium phosphate 25 mM; sodium chloride 100 mM; DTT 2 mM; Alpha-mannosidase binding domain of Atg34, [U-99% 13C; U-99% 15N], 0.7 mM; H2O 90%; D2O 10%
sample_conditions_1: 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 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | 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 HN(CO)HA | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
2D (Hb)Cb(CgCd)Hd | sample_1 | isotropic | sample_conditions_1 |
2D (Hb)Cb(CgCdCe)He | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment, peak picking
VNMR, Varian - collection
NMR spectrometers:
- Varian INOVA 600 MHz
- Varian INOVA 800 MHz
Related Database Links:
PDB | |
DBJ | GAA26245 |
EMBL | CAA58197 CAA99095 CAY86209 |
GB | AHY77231 AJP41463 AJT70882 AJT71373 AJT71861 |
REF | NP_014558 |
SP | Q12292 |
TPG | DAA10701 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts