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Biological Magnetic Resonance Data Bank


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BMRB Entry 17006

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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/BMR17006
MolProbity Validation Chart

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Title: Solution structure of alpha-mannosidase binding domain of Atg19   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:
Atg19, polymer, 118 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):
Atg19: GPHMVEPPNERSLQITMNQR DNSLYFQLFNNTNSVLAGNC KLKFTDAGDKPTTQIIDMGP HEIGIKEYKEYRYFPYALDL EAGSTIEIENQYGEVIFLGK YGSSPMINLRPPSRLSAE

Data sets:
Data typeCount
13C chemical shifts491
15N chemical shifts118
1H chemical shifts808

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Atg191

Entities:

Entity 1, Atg19 118 residues - 12965.639 Da.

1   GLYPROHISMETVALGLUPROPROASNGLU
2   ARGSERLEUGLNILETHRMETASNGLNARG
3   ASPASNSERLEUTYRPHEGLNLEUPHEASN
4   ASNTHRASNSERVALLEUALAGLYASNCYS
5   LYSLEULYSPHETHRASPALAGLYASPLYS
6   PROTHRTHRGLNILEILEASPMETGLYPRO
7   HISGLUILEGLYILELYSGLUTYRLYSGLU
8   TYRARGTYRPHEPROTYRALALEUASPLEU
9   GLUALAGLYSERTHRILEGLUILEGLUASN
10   GLNTYRGLYGLUVALILEPHELEUGLYLYS
11   TYRGLYSERSERPROMETILEASNLEUARG
12   PROPROSERARGLEUSERALAGLU

Samples:

sample_1: sodium phosphate 25 mM; sodium chloride 100 mM; DTT 2 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 GAA26246
EMBL CAA53201 CAA58199 CAA99094 CAY86211
GB AAT93193 AHY77232 AJP41464 AJT70883 AJT71374
REF NP_014559
SP A6ZNC8 P35193
TPG DAA10702

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts