BMRB Entry 27903

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27903

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Title:
Clr4 1-191
Deposition date:
2019-05-13
Original release date:
2019-07-09
Authors:
Akoury, Elias
Citation:

Citation: Akoury, Elias; Ma, Guoli; Demolin, Segolene; Bronner, Cornelia; Zocco, Manuel; Cirilo, Alexandre; Ivic, Nives; Halic, Mario. "Disordered region of H3K9 methyltransferase Clr4 binds the nucleosome and contributes to its activity"  Nucleic Acids Res. 47, 6726-6736 (2019).
PubMed: 31165882

Assembly members:

Assembly members:
protein, polymer, 190 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: bl21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
protein: MSPKQEEYEVERIVDEKLDR NGAVKLYRIRWLNYSSRSDT WEPPENLSGCSAVLAEWKRR KRRLKGSNSDSDSPHHASNP HPNSRQKHQHQTSKSVPRSQ RFSRELNVKKENKKVFSSQT TKRQSRKQSTALTTNDTSII LDDSLHTNSKKLGKTRNEVK EESQKRELVSNSIKEATSPK TSSILTKXRN

Data sets:
Data typeCount
15N chemical shifts173
1H chemical shifts173

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1crr1

Entities:

Entity 1, crr 190 residues - Formula weight is not available

1   METSERPROLYSGLNGLUGLUTYRGLUVAL
2   GLUARGILEVALASPGLULYSLEUASPARG
3   ASNGLYALAVALLYSLEUTYRARGILEARG
4   TRPLEUASNTYRSERSERARGSERASPTHR
5   TRPGLUPROPROGLUASNLEUSERGLYCYS
6   SERALAVALLEUALAGLUTRPLYSARGARG
7   LYSARGARGLEULYSGLYSERASNSERASP
8   SERASPSERPROHISHISALASERASNPRO
9   HISPROASNSERARGGLNLYSHISGLNHIS
10   GLNTHRSERLYSSERVALPROARGSERGLN
11   ARGPHESERARGGLULEUASNVALLYSLYS
12   GLUASNLYSLYSVALPHESERSERGLNTHR
13   THRLYSARGGLNSERARGLYSGLNSERTHR
14   ALALEUTHRTHRASNASPTHRSERILEILE
15   LEUASPASPSERLEUHISTHRASNSERLYS
16   LYSLEUGLYLYSTHRARGASNGLUVALLYS
17   GLUGLUSERGLNLYSARGGLULEUVALSER
18   ASNSERILELYSGLUALATHRSERPROLYS
19   THRSERSERILELEUTHRLYSXARGASN

Samples:

sample_1: protein, [U-100% 13C; U-100% 15N], 500 uM

sample_conditions_1: pH: 6.8

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

CCPN, CCPN - chemical shift assignment

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