BMRB Entry 18846

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18846
MolProbity Validation Chart

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Title:
SUP-12 + GGUGUGC
Deposition date:
2012-11-19
Original release date:
2013-01-29
Authors:
Amrane, Samir; Mackereth, Cameron
Citation:

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 ., .-. (2013).
PubMed: 23334698

Assembly members:

Assembly members:
SUP-12, polymer, 97 residues, 10815.1 Da.
GGUGUGC, polymer, 7 residues, 2236.4 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-His1a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SUP-12: GAMGSRDTMFTKIFVGGLPY HTSDKTLHEYFEQFGDIEEA VVITDRNTQKSRGYGFVTMK DRASAERACKDPNPIIDGRK ANVNLAYLGAKPRTNVQ
GGUGUGC: GGUGUGC

Data sets:
Data typeCount
13C chemical shifts430
15N chemical shifts99
1H chemical shifts668

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SUP-121
2RNA2

Entities:

Entity 1, SUP-12 97 residues - 10815.1 Da.

The N-terminal Gly-Ala-Met remains following removal of the His6-tag by TEV potease

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

Entity 2, RNA 7 residues - 2236.4 Da.

1   GGUGUGC

Samples:

sample_1: SUP-12, [U-99% 13C; U-99% 15N], 0.2 mM; GGUGUGC 0.24 mM; sodium phosphate 20 mM; sodium chloride 300 mM; H2O 90%; D2O 10%

sample_2: SUP-12, [U-99% 13C; U-99% 15N], 0.4 mM; GGUGUGC 0.42 mM; sodium phosphate 20 mM; sodium chloride 300 mM; D2O 100%

sample_3: SUP-12, [U-10% 13C; U-99% 15N], 50 uM; GGUGUGC 75 uM; sodium phosphate 20 mM; sodium chloride 300 mM; D2O 100%

sample_conditions_1: ionic strength: 320 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D CBHDsample_2isotropicsample_conditions_1
3D CBHEsample_2isotropicsample_conditions_1
3D HCACOsample_2isotropicsample_conditions_1
3D H(C)CH-TOCSYsample_2isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_2isotropicsample_conditions_1
2D 1H-13C HSQC CTsample_3isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

NMRPipe v2007, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.113, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz

Related Database Links:

UNP O45189 H2L051
BMRB 11541 18845 19653
PDB
EMBL CCD71425 CCD71429
GB KIH66793
REF NP_001129938 NP_508674
AlphaFold H2L051 O45189

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