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BMRB: 17007

2KZK

Solution structure of alpha-mannosidase binding domain of Atg34

Authors

Watanabe, Y., Noda, N., Kumeta, H., Suzuki, K., Ohsumi, Y., Inagaki, F.

Assembly

Alpha-mannosidase binding domain of Atg34

Entity

1. Alpha-mannosidase binding domain of Atg34 (polymer, Thiol state: all free), 107 monomers, 11946.51 Da Detail

GPHMNDPLLH VEVSNEDNSL HFILYNKTNI IIPGNCTFEF SSQISEVFSI KMGPHEIGIK GQKELWFFPS LPTPLSNYTM KVVNQDGETI LVGKCADSNE ITLKSPL

Formula weight

11946.51 Da

Source organism

Saccharomyces cerevisiae

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 97.2 %, Completeness: 92.1 %, Completeness (bb): 94.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	92.1 % (1168 of 1268)	93.3 % (615 of 659)	89.7 % (446 of 497)	95.5 % (107 of 112)
Backbone	94.2 % (590 of 626)	94.8 % (202 of 213)	93.0 % (292 of 314)	97.0 % (96 of 99)
Sidechain	91.0 % (675 of 742)	92.6 % (413 of 446)	88.7 % (251 of 283)	84.6 % (11 of 13)
Aromatic	64.4 % (67 of 104)	76.9 % (40 of 52)	52.9 % (27 of 51)	0.0 % (0 of 1)
Methyl	99.2 % (117 of 118)	98.3 % (58 of 59)	100.0 % (59 of 59)

1. Alpha-mannosidase binding domain of Atg34

GPHMNDPLLH VEVSNEDNSL HFILYNKTNI IIPGNCTFEF SSQISEVFSI KMGPHEIGIK GQKELWFFPS LPTPLSNYTM KVVNQDGETI LVGKCADSNE ITLKSPL

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Concentration
1	sodium phosphate	natural abundance	25 mM
2	sodium chloride	natural abundance	100 mM
3	DTT	natural abundance	2 mM
4	Alpha-mannosidase binding domain of Atg34	[U-99% 13C; U-99% 15N]	0.7 mM
5	H2O	natural abundance	90 %
6	D2O	natural abundance	10 %

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.05 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.05 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: -0.13 ppm, Outliers: 4 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.73 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2KZK, Strand ID: A Detail

Release date

2010-08-11

Citation

Selective transport of alpha-mannosidase by autophagic pathways: structural basis for cargo recognition by Atg19 and Atg34
Watanabe, Y., Noda, N.N., Kumeta, H., Suzuki, K., Ohsumi, Y., Inagaki, F.
J. Biol. Chem. (2010), 285, 30026-30033, PubMed 20659891 , DOI 10.1074/jbc.M110.143545 , Abstract

Related entities 1. Alpha-mannosidase binding domain of Atg34, : 1 : 2 : 4 entities Detail

Interaction partners 1. Alpha-mannosidase binding domain of Atg34, : 20 interactors Detail

More details for 20 interactors identified by 6 citations

Experiments performed 14 experiments Detail

1 2D 1H-15N HSQC