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
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
Solution structure of alpha-mannosidase binding domain of Atg34
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:

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).
PubMed: 20659891

Assembly members:

Assembly members:
Alpha-mannosidase_binding_domain_of_Atg34, polymer, 107 residues, 12965.639 Da.

Natural source:

Natural source:   Common Name: baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX-6p-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Alpha-mannosidase_binding_domain_of_Atg34: GPHMNDPLLHVEVSNEDNSL HFILYNKTNIIIPGNCTFEF SSQISEVFSIKMGPHEIGIK GQKELWFFPSLPTPLSNYTM KVVNQDGETILVGKCADSNE ITLKSPL

Data sets:
Data typeCount
13C chemical shifts455
15N chemical shifts106
1H chemical shifts742

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Alpha-mannosidase_binding_domain_of_Atg341

Entities:

Entity 1, Alpha-mannosidase_binding_domain_of_Atg34 107 residues - 12965.639 Da.

1   GLYPROHISMETASNASPPROLEULEUHIS
2   VALGLUVALSERASNGLUASPASNSERLEU
3   HISPHEILELEUTYRASNLYSTHRASNILE
4   ILEILEPROGLYASNCYSTHRPHEGLUPHE
5   SERSERGLNILESERGLUVALPHESERILE
6   LYSMETGLYPROHISGLUILEGLYILELYS
7   GLYGLNLYSGLULEUTRPPHEPHEPROSER
8   LEUPROTHRPROLEUSERASNTYRTHRMET
9   LYSVALVALASNGLNASPGLYGLUTHRILE
10   LEUVALGLYLYSCYSALAASPSERASNGLU
11   ILETHRLEULYSSERPROLEU

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)HAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D (Hb)Cb(CgCd)Hdsample_1isotropicsample_conditions_1
2D (Hb)Cb(CgCdCe)Hesample_1isotropicsample_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
AlphaFold Q12292

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks