BMRB Entry 30087

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30087
MolProbity Validation Chart

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Title:
NMR solution structure of a thermophilic lysine methyl transferase from Sulfolobus islandicus
Deposition date:
2016-05-12
Original release date:
2017-05-19
Authors:
de Lichtenberg, C.; Stiefler-Jensen, D.; Schwarz-Linnet, T.; She, Q.; Teilum, K.
Citation:

Citation: de Lichtenberg, C.; Stiefler-Jensen, D.; Schwarz-Linnet, T.; She, Q.; Teilum, K.. "NMR solution structure of a thermophilic lysine methyl transferase from Sulfolobus islandicus"  .

Assembly members:

Assembly members:
Protein-lysine N-methyltransferase, polymer, 172 residues, 19420.371 Da.

Natural source:

Natural source:   Common Name: crenarchaeotes   Taxonomy ID: 930945   Superkingdom: Archaea   Kingdom: not available   Genus/species: sulfolobus sulfolobus islandicus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)   Vector: pET30a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Protein-lysine N-methyltransferase: MSYVPHVPYVPTPEKVVRRM LEIAKVSQDDIVYALGCGDG RIIITAAKDFNVKKAVGVEI NDERIREALANIEKNGVTGR ASIVKGNFFEVDISEATVVT MFLLTNVNEMLKPKLEKELK PGTRVVSHEFEIRGWNPKEV IKVEDGNMNHTVYLYVIGEH KAAALEHHHHHH

Data sets:
Data typeCount
13C chemical shifts631
15N chemical shifts154
1H chemical shifts1001

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 172 residues - 19420.371 Da.

1   METSERTYRVALPROHISVALPROTYRVAL
2   PROTHRPROGLULYSVALVALARGARGMET
3   LEUGLUILEALALYSVALSERGLNASPASP
4   ILEVALTYRALALEUGLYCYSGLYASPGLY
5   ARGILEILEILETHRALAALALYSASPPHE
6   ASNVALLYSLYSALAVALGLYVALGLUILE
7   ASNASPGLUARGILEARGGLUALALEUALA
8   ASNILEGLULYSASNGLYVALTHRGLYARG
9   ALASERILEVALLYSGLYASNPHEPHEGLU
10   VALASPILESERGLUALATHRVALVALTHR
11   METPHELEULEUTHRASNVALASNGLUMET
12   LEULYSPROLYSLEUGLULYSGLULEULYS
13   PROGLYTHRARGVALVALSERHISGLUPHE
14   GLUILEARGGLYTRPASNPROLYSGLUVAL
15   ILELYSVALGLUASPGLYASNMETASNHIS
16   THRVALTYRLEUTYRVALILEGLYGLUHIS
17   LYSALAALAALALEUGLUHISHISHISHIS
18   HISHIS

Samples:

sample_1: DSS 0.5 mM; Na-acetate 20 mM; aKMT_D34A, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O 10%

sample_2: DSS 0.5 mM; Na-acetate 20 mM; aKMT_D34A, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O 10%

sample_3: C12E5 0.123 M; DSS 0.5 mM; Na-acetate 20 mM; aKMT_D34A, [U-100% 13C; U-100% 15N], 1 mM; hexanol 0.111 M; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.02 M; pH: 5; pressure: 1 atm; temperature: 313 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 HN(CA)COsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D IPAP HSQCsample_1isotropicsample_conditions_1
3D HCCH-TOCSY aromaticsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
2D IPAP HSQCsample_3anisotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1

Software:

Analysis, CCPN - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Agilent DD2 800 MHz
  • Bruker AvanceIII 800 MHz

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