BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 18277

Title: Solution structures of KmAtg10   PubMed: 22682742

Deposition date: 2012-02-19 Original release date: 2012-06-13

Authors: Yamaguchi, Masaya; Noda, Nobuo; Yamamoto, Hayashi; Shima, Takayuki; Kumeta, Hiroyuki; Kobashigawa, Yoshihiro; Akada, Rinji; Ohsumi, Yoshinori; Inagaki, Fuyuhiko

Citation: Yamaguchi, Masaya; Noda, Nobuo; Yamamoto, Hayashi; Shima, Takayuki; Kumeta, Hiroyuki; Kobashigawa, Yoshihiro; Akada, Rinji; Ohsumi, Yoshinori; Inagaki, Fuyuhiko. "Structural insights into Atg10-mediated formation of the autophagy-essential Atg12-Atg5 conjugate."  Structure 20, 1244-1254 (2012).

Assembly members:
entity, polymer, 148 residues, 17413.861 Da.

Natural source:   Common Name: ascomycetes   Taxonomy ID: 4911   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Kluyveromyces marxianus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX6p

Entity Sequences (FASTA):
entity: SMLTLPEYNEQIPNVRSLLT KWAKVERIQDVQDGLQLDVR LKTDTLLELHIYYDHVYHVP SIKFRLWSLDTEEDISSLRL LTLSDSELRSILNLGTFSVT LSTDMEMKSVYYYINNCDTD ANVGSDVEHYLTRWISLYIR IFDLNFVP

Data sets:
Data typeCount
13C chemical shifts688
15N chemical shifts162
1H chemical shifts1111

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1KmAtg101

Entities:

Entity 1, KmAtg10 148 residues - 17413.861 Da.

1   SERMETLEUTHRLEUPROGLUTYRASNGLU
2   GLNILEPROASNVALARGSERLEULEUTHR
3   LYSTRPALALYSVALGLUARGILEGLNASP
4   VALGLNASPGLYLEUGLNLEUASPVALARG
5   LEULYSTHRASPTHRLEULEUGLULEUHIS
6   ILETYRTYRASPHISVALTYRHISVALPRO
7   SERILELYSPHEARGLEUTRPSERLEUASP
8   THRGLUGLUASPILESERSERLEUARGLEU
9   LEUTHRLEUSERASPSERGLULEUARGSER
10   ILELEUASNLEUGLYTHRPHESERVALTHR
11   LEUSERTHRASPMETGLUMETLYSSERVAL
12   TYRTYRTYRILEASNASNCYSASPTHRASP
13   ALAASNVALGLYSERASPVALGLUHISTYR
14   LEUTHRARGTRPILESERLEUTYRILEARG
15   ILEPHEASPLEUASNPHEVALPRO

Samples:

13C_15N: KmAtg10, [U-99% 13C; U-99% 15N], 0.5 mM; sodium phosphate 50 mM; sodium chloride 100 mM; DTT 5 mM; H20 90%; D20 10%

sample_conditions_1: ionic strength: 150 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC13C_15Nisotropicsample_conditions_1
2D 1H-13C HSQC aliphatic13C_15Nisotropicsample_conditions_1
2D 1H-13C HSQC aromatic13C_15Nisotropicsample_conditions_1
3D HNCO13C_15Nisotropicsample_conditions_1
3D HN(CO)CA13C_15Nisotropicsample_conditions_1
3D HNCA13C_15Nisotropicsample_conditions_1
3D HBHA(CO)NH13C_15Nisotropicsample_conditions_1
3D HN(CA)HA13C_15Nisotropicsample_conditions_1
3D CBCA(CO)NH13C_15Nisotropicsample_conditions_1
3D HNCACB13C_15Nisotropicsample_conditions_1
3D C(CO)NH13C_15Nisotropicsample_conditions_1
3D HCCH-TOCSY aliphatic13C_15Nisotropicsample_conditions_1
2D HbCbCgCdHd13C_15Nisotropicsample_conditions_1
2D HbCbCgCdCeHe13C_15Nisotropicsample_conditions_1
3D HCCH-TOCSY aromatic13C_15Nisotropicsample_conditions_1
3D 1H-15N NOESY13C_15Nisotropicsample_conditions_1
3D 1H-13C NOESY aliphatic13C_15Nisotropicsample_conditions_1
3D 1H-13C NOESY aromatic13C_15Nisotropicsample_conditions_1

Software:

VNMR v6.1C, Varian - collection

NMRPipe v2010.176.13.55, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.113, Goddard - chemical shift assignment, peak picking, refinement

TALOS+ v1.01, Shen, Delaglio, Cornilescu, Bax - structure solution

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

NMR spectrometers:

  • Agilent Unity INOVA 800 MHz
  • Agilent Unity INOVA 600 MHz

Related Database Links:

PDB
DBJ BAO42720 BAP74090

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