BMRB Entry 16230

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16230
MolProbity Validation Chart

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Title:
Solution Structure of Yeast Prp24-RRM2 Bound to a Fragment of U6 RNA
Deposition date:
2009-03-27
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 Assign 3, 227-230 (2009).
PubMed: 19693704

Assembly members:

Assembly members:
Prp24-RRM2, polymer, 92 residues, 10012.586 Da.
AGAGAU, polymer, 6 residues, 1826.235 Da.

Natural source:

Natural source:   Common Name: 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-RRM2: MTECTLWMTNFPPSYTQRNI RDLLQDINVVALSIRLPSLR FNTSRRFAYIDVTSKEDARY CVEKLNGLKIEGYTLVTKVS NPLELEHHHHHH
AGAGAU: AGAGAU

Data sets:
Data typeCount
13C chemical shifts367
15N chemical shifts91
1H chemical shifts642

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Prp24-RRM21
2AGAGAU2

Entities:

Entity 1, Prp24-RRM2 92 residues - 10012.586 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   ASNPROLEUGLULEUGLUHISHISHISHIS
10   HISHIS

Entity 2, AGAGAU 6 residues - 1826.235 Da.

1   AGAGAU

Samples:

Unlabeled: Prp24-RRM2 300 uM; AGAGAU 3 mM; TRIS, [U-2H], 10 mM; potassium chloride 50 mM; D20 100%

Fully_Labeled_D2O: Prp24-RRM2, [U-99% 15N], 500 uM; AGAGAU 5 mM; TRIS, [U-2H], 10 mM; potassium chloride 50 mM; D20 100%

Fully_Labeled: Prp24-RRM2, [U-99% 13C; U-99% 15N], 500 mM; AGAGAU 5 mM; TRIS 10 mM; potassium chloride 50 mM; DTT 1 mM; H20 90%; D20 10%

Referencing: Prp24-RRM2, [U-99% 13C; U-99% 15N], 500 uM; AGAGAU 5 mM; TRIS 10 mM; potassium chloride 50 mM; DTT 1 mM; DSS 10 uM; H20 90%; D20 10%

Aligned: Prp24-RRM2, [U-99% 13C; U-99% 15N], 300 uM; AGAGAU 3 mM; TRIS 10 mM; potassium chloride 50 mM; DTT 1 mM; DMPC/DHPC 3:1 6.5%; H20 90%; D20 10%

sample_conditions_1: ionic strength: 50 mM; pH: 7; pressure: 1.0 atm; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C HSQCReferencingisotropicsample_conditions_1
2D 1H-15N HSQCFully_Labeledisotropicsample_conditions_1
2D 1H-13C HSQCFully_Labeled_D2Oisotropicsample_conditions_1
3D CBCA(CO)NHFully_Labeledisotropicsample_conditions_1
3D C(CO)NHFully_Labeledisotropicsample_conditions_1
3D HNCOFully_Labeledisotropicsample_conditions_1
3D HNCACBFully_Labeledisotropicsample_conditions_1
3D HBHA(CO)NHFully_Labeledisotropicsample_conditions_1
3D HCCH-TOCSYFully_Labeledisotropicsample_conditions_1
3D 1H-15N NOESYFully_Labeledisotropicsample_conditions_1
3D 1H-13C NOESYFully_Labeled_D2Oisotropicsample_conditions_1
2D 1H-1H NOESYFully_Labeled_D2Oisotropicsample_conditions_1
2D 1H-1H NOESYUnlabeledisotropicsample_conditions_1
2D 1H-15N HSQC-IPAPFully_Labeledisotropicsample_conditions_1
2D 1H-15N HSQC-IPAPAlignedanisotropicsample_conditions_1
3D J modulated CHSQCFully_Labeledisotropicsample_conditions_1
3D J modulated CHSQCAlignedisotropicsample_conditions_1

Software:

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

xwinnmr, Bruker Biospin - collection

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

ATHNOS-CANDID, Herrmann, T; Guentert, P; Wuethrich, K - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

TALOS, Cornilescu, Delaglio and Bax - data analysis

HADDOCK v2, Dominguez, C; Boelens, R; Bonvin, A M M J - refinement, structure solution

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian DMX 750 MHz
  • Varian INOVA 900 MHz
  • Varian INOVA 800 MHz

Related Database Links:

BMRB 16243 16244 16246
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