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 51359

Title: Backbone resonance assignments of the N-terminal domain of Sam68   PubMed: 36537190

Deposition date: 2022-03-11 Original release date: 2022-11-23

Authors: Malki, Idir; Dominguez, Cyril

Citation: Malki, Idir; Liepina, Inara; Kogelnik, Nora; Watmuff, Hollie; Robinson, Sue; Lightfoot, Adam; Gonchar, Oksana; Bottrill, Andrew; Fry, Andrew; Dominguez, Cyril. "Cdk1-mediated threonine phosphorylation of Sam68 modulates its RNA binding, alternative splicing activity and cellular functions"  Nucleic Acids Res. 50, 13045-13062 (2022).

Assembly members:
entity_1, polymer, 97 residues, Formula weight is not available

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pLEICS-01

Entity Sequences (FASTA):
entity_1: SMQRRDDPAARMSRSSGRSG SMDPSGAHPSVRQTPSRQPP LPHRSRGGGGGSRGGARASP ATQPPPLLPPSATGPDATVG GPAPTPLLPPSATASVK

Data sets:
Data typeCount
13C chemical shifts91
15N chemical shifts50
1H chemical shifts50

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Sam68 N-terminal domain1

Entities:

Entity 1, Sam68 N-terminal domain 97 residues - Formula weight is not available

1   SERMETGLNARGARGASPASPPROALAALA
2   ARGMETSERARGSERSERGLYARGSERGLY
3   SERMETASPPROSERGLYALAHISPROSER
4   VALARGGLNTHRPROSERARGGLNPROPRO
5   LEUPROHISARGSERARGGLYGLYGLYGLY
6   GLYSERARGGLYGLYALAARGALASERPRO
7   ALATHRGLNPROPROPROLEULEUPROPRO
8   SERALATHRGLYPROASPALATHRVALGLY
9   GLYPROALAPROTHRPROLEULEUPROPRO
10   SERALATHRALASERVALLYS

Samples:

sample_1: N-terminal domain of Sam68, [U-99% 13C; U-99% 15N], 500 uM

sample_conditions_1: ionic strength: 0.25 M; pH: 7.0; pressure: 1 atm; temperature: 278 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCACONHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

CcpNMR v2.4.2 - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 600 MHz

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