BMRB Entry 11545

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11545

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Backbone 1H, 13C, and 15N chemical shift assignment for aqMutL-CTD
Deposition date:
2013-11-26
Original release date:
2017-03-13
Authors:
Mizushima, Ryota; Lee, Young-Ho
Citation:

Citation: Mizushima, Ryota; Kim, Ju Yaen; Suetake, Isao; Tanaka, Hiroaki; Takai, Tomoyo; Kamiya, Narutoshi; Takano, Yu; Mishima, Yuichi; Tajima, Shoji; Goto, Yuji; Fukui, Kenji; Lee, Young-Ho. "NMR characterization of the interaction of the endonuclease domain of MutL with divalent metal ions and ATP"  PLoS ONE 9, e98554-e98554 (2014).
PubMed: 24901533

Assembly members:

Assembly members:
aqMutL-CTD_homodimer, polymer, 110 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Aquifex aeolicus   Taxonomy ID: 63363   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Aquifex aeolicus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
aqMutL-CTD_homodimer: PLSQPVKTYKPTYEILGQMD ETFILVKDSEYLYFVDQHLL EERINYEKLKDENLACRISV KAGQKLSEEKIRELIKTWRN LENPHVCPHGRPIYYKIPLR EIYEKVGRNY

Data sets:
Data typeCount
13C chemical shifts283
15N chemical shifts98
1H chemical shifts98

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1C-terminal domain, chain 11
2C-terminal domain, chain 21

Entities:

Entity 1, C-terminal domain, chain 1 110 residues - Formula weight is not available

1   PROLEUSERGLNPROVALLYSTHRTYRLYS
2   PROTHRTYRGLUILELEUGLYGLNMETASP
3   GLUTHRPHEILELEUVALLYSASPSERGLU
4   TYRLEUTYRPHEVALASPGLNHISLEULEU
5   GLUGLUARGILEASNTYRGLULYSLEULYS
6   ASPGLUASNLEUALACYSARGILESERVAL
7   LYSALAGLYGLNLYSLEUSERGLUGLULYS
8   ILEARGGLULEUILELYSTHRTRPARGASN
9   LEUGLUASNPROHISVALCYSPROHISGLY
10   ARGPROILETYRTYRLYSILEPROLEUARG
11   GLUILETYRGLULYSVALGLYARGASNTYR

Samples:

sample_1: MutL, [U-98% 13C; U-99% 15N], 500 uM; potassium phosphate 50 mM; potassium chloride 100 mM; DTT 1 mM; EDTA 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 150 mM; pH: 6.8; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

NMRPipe;_SPARKY, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Goddard - chemical shift assignment, peak picking, processing

NMR spectrometers:

  • Bruker Avance 800 MHz

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