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 27417

Title: Putative methyltransferase WBSCR27 in complex with S-adenosyl-L-methionine   PubMed: 29868988

Deposition date: 2018-03-06 Original release date: 2018-06-20

Authors: Mariasina, Sofia; Polshakov, Vladimir; Chang, Chi-Fon

Citation: Mariasina, Sofia; Petrova, Olga; Osterman, Ilya; Sergeeva, Olga; Efimov, Sergey; Klochkov, Vladimir; Sergiev, Petr; Dontsova, Olga; Huang, Tai-Huang; Chang, Chi-Fon; Polshakov, Vladimir. "NMR assignments of the WBSCR27 protein related to Williams-Beuren syndrome"  Biomol. NMR Assignments 12, 303-308 (2018).

Assembly members:
WBSCR27_putative_methyltransferase, polymer, 240 residues, 25963 Da.
entity_SAM, non-polymer, 398.437 Da.

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

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

Entity Sequences (FASTA):
WBSCR27_putative_methyltransferase: GAMAQEEAGRLPQVLARVGT SHGITDLACKLRFYDDWAPE YDQDVAALKYRAPRLAVDCL SRAFRGSPHDALILDVACGT GLVAVELQARGFLQVQGVDG SPEMLKQARARGLYHHLSLC TLGQEPLPDPEGTFDAVIIV GALSEGQVPCSAIPELLRVT KPGGLVCLTTRTNPSNLPYK ETLEATLDSLERAGVWECLV TQPVDHWELATSEQETGLGT CANDGFISGIIYLYRKQETV

Data sets:
Data typeCount
13C chemical shifts779
15N chemical shifts214
1H chemical shifts1173

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1WBSCR271
2SAM2

Entities:

Entity 1, WBSCR27 240 residues - 25963 Da.

Residues 1-2 represent a non-native affinity tag;

1   GLYALAMETALAGLNGLUGLUALAGLYARG
2   LEUPROGLNVALLEUALAARGVALGLYTHR
3   SERHISGLYILETHRASPLEUALACYSLYS
4   LEUARGPHETYRASPASPTRPALAPROGLU
5   TYRASPGLNASPVALALAALALEULYSTYR
6   ARGALAPROARGLEUALAVALASPCYSLEU
7   SERARGALAPHEARGGLYSERPROHISASP
8   ALALEUILELEUASPVALALACYSGLYTHR
9   GLYLEUVALALAVALGLULEUGLNALAARG
10   GLYPHELEUGLNVALGLNGLYVALASPGLY
11   SERPROGLUMETLEULYSGLNALAARGALA
12   ARGGLYLEUTYRHISHISLEUSERLEUCYS
13   THRLEUGLYGLNGLUPROLEUPROASPPRO
14   GLUGLYTHRPHEASPALAVALILEILEVAL
15   GLYALALEUSERGLUGLYGLNVALPROCYS
16   SERALAILEPROGLULEULEUARGVALTHR
17   LYSPROGLYGLYLEUVALCYSLEUTHRTHR
18   ARGTHRASNPROSERASNLEUPROTYRLYS
19   GLUTHRLEUGLUALATHRLEUASPSERLEU
20   GLUARGALAGLYVALTRPGLUCYSLEUVAL
21   THRGLNPROVALASPHISTRPGLULEUALA
22   THRSERGLUGLNGLUTHRGLYLEUGLYTHR
23   CYSALAASNASPGLYPHEILESERGLYILE
24   ILETYRLEUTYRARGLYSGLNGLUTHRVAL

Entity 2, SAM - C15 H22 N6 O5 S - 398.437 Da.

1   SAM

Samples:

sample_N: WBSCR27 putative methyltransferase, [U-99% 15N], 0.8 mM; S-Adenosyl-L-methionine 5 mM; NaCl 50 mM; Sodium phosphate buffer (pH 7) 50 mM; DL-Dithiothreitol (DTT) 10 mM; Sodium azide (NaN3) 0.02%

sample_CN_D2O: WBSCR27 putative methyltransferase, [U-99% 13C; U-99% 15N], 0.4 mM; S-Adenosyl-L-methionine 2 mM; NaCl 50 mM; Sodium phosphate buffer (pH 7) 50 mM; DL-Dithiothreitol (DTT) 10 mM; Sodium azide (NaN3) 0.02%

sample_CN: WBSCR27 putative methyltransferase, [U-99% 13C; U-99% 15N], 0.6 mM; S-Adenosyl-L-methionine 5 mM; NaCl 50 mM; Sodium phosphate buffer (pH 7) 50 mM; DL-Dithiothreitol (DTT) 10 mM; Sodium azide (NaN3) 0.02%

sample_conditions_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_Nisotropicsample_conditions_1
2D 1H-13C HSQCsample_CNisotropicsample_conditions_1
3D HNCOsample_CNisotropicsample_conditions_1
3D HCACOsample_CNisotropicsample_conditions_1
3D HN(CO)CAsample_CNisotropicsample_conditions_1
3D HNCAsample_CNisotropicsample_conditions_1
3D CBCA(CO)NHsample_CNisotropicsample_conditions_1
3D HNCACBsample_CNisotropicsample_conditions_1
3D HBHA(CO)NHsample_Nisotropicsample_conditions_1
3D HNHAHBsample_Nisotropicsample_conditions_1
3D 1H-15N NOESYsample_Nisotropicsample_conditions_1
3D 1H-13C NOESYsample_CNisotropicsample_conditions_1
3D 1H-13C NOESYsample_CN_D2Oisotropicsample_conditions_1
3D HCCH-TOCSYsample_CNisotropicsample_conditions_1
2D 15{1H}NOEsample_CNisotropicsample_conditions_1

Software:

SPARKY vNMRFAM, (NMRFAM Sparky) W. Lee, Goddard - chemical shift assignment, data analysis, peak picking

TOPSPIN vv3.1, Bruker Biospin - collection

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

TALOS vTALOS+, Cornilescu, Delaglio and Bax - data analysis

NMRest, Polshakov - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 850 MHz

Related Database Links:

Q8BGM4-1 WBSCR27

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