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 19653

Title: RRM domain from C. elegans SUP-12   PubMed: 23334698

Authors: Amrane, S.; Mackereth, Cameron

Citation: Amrane, Samir; Mackereth, Cameron. "Protein chemical shift assignments of the unbound and RNA-bound forms of the alternative splicing factor SUP-12 from C. elegans."  Biomol. NMR Assignments 8, 109-112 (2013).

Assembly members:
PROTEIN_SUP-12_ISOFORM_B, polymer, 97 residues, 10819.1904 Da.
GGTGTGC, polymer, 7 residues, 2106.4793 Da.

Natural source:   Common Name: nematodes   Taxonomy ID: 6239   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Caenorhabditis elegans

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

Entity Sequences (FASTA):
PROTEIN_SUP-12_ISOFORM_B: GAMGSRDTMFTKIFVGGLPY HTSDKTLHEYFEQFGDIEEA VVITDRNTQKSRGYGFVTMK DRASAERACKDPNPIIDGRK ANVNLAYLGAKPRTNVQ
GGTGTGC: GGTGTGC

Data sets:
Data typeCount
13C chemical shifts420
15N chemical shifts99
1H chemical shifts731

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PROTEIN SUP-12, ISOFORM B1
2GGTGTGC2

Entities:

Entity 1, PROTEIN SUP-12, ISOFORM B 97 residues - 10819.1904 Da.

1   GLYALAMETGLYSERARGASPTHRMETPHE
2   THRLYSILEPHEVALGLYGLYLEUPROTYR
3   HISTHRSERASPLYSTHRLEUHISGLUTYR
4   PHEGLUGLNPHEGLYASPILEGLUGLUALA
5   VALVALILETHRASPARGASNTHRGLNLYS
6   SERARGGLYTYRGLYPHEVALTHRMETLYS
7   ASPARGALASERALAGLUARGALACYSLYS
8   ASPPROASNPROILEILEASPGLYARGLYS
9   ALAASNVALASNLEUALATYRLEUGLYALA
10   LYSPROARGTHRASNVALGLN

Entity 2, GGTGTGC 7 residues - 2106.4793 Da.

1   DGDGDTDGDTDGDC

Samples:

sample_1: PROTEIN SUP-12, ISOFORM B, [U-13C; U-15N], 0.8 mM; GGTGTGC 0.8 mM; sodium phosphate 20 mM; sodium chloride 300 mM; H2O 10%; D2O, [U-100% 2H], 90%

sample_2: PROTEIN SUP-12, ISOFORM B, [U-13C; U-15N], 0.4 mM; GGTGTGC 0.4 mM; sodium phosphate 20 mM; sodium chloride 300 mM; D2O, [U-100% 2H], 100%

sample_3: PROTEIN SUP-12, ISOFORM B, [U-100% 2H], 0.6 mM; GGTGTGC 0.6 mM; sodium phosphate 20 mM; sodium chloride 300 mM; D2O, [U-100% 2H], 100%

sample_conditions_1: ionic strength: 300.000 mM; pH: 6.500; pressure: 1.000 atm; temperature: 298.000 K

Experiments:

NameSampleSample stateSample conditions
15N-NOESYsample_1solutionsample_conditions_1
13C-NOESYsample_2solutionsample_conditions_1
double-filtered 1Hsample_2solutionsample_conditions_1
1H-NOESYsample_2solutionsample_conditions_1
1H-TOCSYsample_2solutionsample_conditions_1
1Hsample_3solutionsample_conditions_1
1H-NOESYsample_3solutionsample_conditions_1

Software:

CNS1.1 vany, Brunger, Adams, Clore, Gros, Nilges and Read - chemical shift assignment

NMRPipe vany, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift assignment

SPARKY vany, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz

Related Database Links:

UNP O45189 H2L051_CAEEL
BMRB 11541 18845 18846
PDB
EMBL CCD71425 CCD71429
GB KIH66793
REF NP_001129938 NP_508674