BMRB Entry 16244

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16244
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Backbone NH Assignments for Prp24-RRM23 Bound to AGAGAU RNA
Deposition date:
2009-04-07
Original release date:
2009-09-04
Authors:
Martin-Tumasz, Stephen; Butcher, Samuel
Citation:

Citation: Martin-Tumasz, Stephen; Butcher, Samuel. "(1)H, (13)C and (15)N resonance assignments of a ribonucleoprotein complex consisting of Prp24-RRM2 bound to a fragment of U6 RNA."  Biomol. NMR Assignments 3, 227-230 (2009).
PubMed: 19693704

Assembly members:

Assembly members:
Prp24-RRM23, polymer, 186 residues, 21430 Da.
AGAGAU, polymer, 6 residues, 1922 Da.

Natural source:

Natural source:   Common Name: baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21-b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Prp24-RRM23: MTECTLWMTNFPPSYTQRNI RDLLQDINVVALSIRLPSLR FNTSRRFAYIDVTSKEDARY CVEKLNGLKIEGYTLVTKVS NPLEKSKRTDSATLEGREIM IRNLSTELLDENLLRESFEG FGSIEKINIPAGQKEHSFNN CCAFMVFENKDSAERALQMN RSLLGNREISVSLADKKPLE HHHHHH
AGAGAU: AGAGAU

Data sets:
Data typeCount
15N chemical shifts131
1H chemical shifts131

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Prp24-RRM231
2AGAGAU2

Entities:

Entity 1, Prp24-RRM23 186 residues - 21430 Da.

Final 8 residues are non-native due to 6x His tag

1   METTHRGLUCYSTHRLEUTRPMETTHRASN
2   PHEPROPROSERTYRTHRGLNARGASNILE
3   ARGASPLEULEUGLNASPILEASNVALVAL
4   ALALEUSERILEARGLEUPROSERLEUARG
5   PHEASNTHRSERARGARGPHEALATYRILE
6   ASPVALTHRSERLYSGLUASPALAARGTYR
7   CYSVALGLULYSLEUASNGLYLEULYSILE
8   GLUGLYTYRTHRLEUVALTHRLYSVALSER
9   ASNPROLEUGLULYSSERLYSARGTHRASP
10   SERALATHRLEUGLUGLYARGGLUILEMET
11   ILEARGASNLEUSERTHRGLULEULEUASP
12   GLUASNLEULEUARGGLUSERPHEGLUGLY
13   PHEGLYSERILEGLULYSILEASNILEPRO
14   ALAGLYGLNLYSGLUHISSERPHEASNASN
15   CYSCYSALAPHEMETVALPHEGLUASNLYS
16   ASPSERALAGLUARGALALEUGLNMETASN
17   ARGSERLEULEUGLYASNARGGLUILESER
18   VALSERLEUALAASPLYSLYSPROLEUGLU
19   HISHISHISHISHISHIS

Entity 2, AGAGAU 6 residues - 1922 Da.

1   AGAGAU

Samples:

Fully_Labeled: Prp24-RRM23, [U-99% 13C; U-99% 15N], 500 uM; TRIS 10 mM; potassium chloride 50 mM; DTT 1 mM; AGAGAU 5 mM; H2O 90%; D2O 10%

Referencing: Prp24-RRM23, [U-99% 13C; U-99% 15N], 500 uM; TRIS 10 mM; potassium chloride 50 mM; DTT 1 mM; DSS 10 uM; AGAGAU 5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCFully_Labeledisotropicsample_conditions_1
3D CBCA(CO)NHFully_Labeledisotropicsample_conditions_1
3D HNCACBFully_Labeledisotropicsample_conditions_1
3D HNCAFully_Labeledisotropicsample_conditions_1

Software:

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

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 16243 17589
PDB
DBJ GAA25719
EMBL CAA89251 CAY82100
GB AAU09775 AHY76723 AJP40962 AJS62134 AJS62569
REF NP_013995
SP P49960
TPG DAA10168
AlphaFold P49960

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