BMRB Entry 17490

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17490
MolProbity Validation Chart

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Title:
Solution Structure of the C-terminal domain of Prp24
Deposition date:
2011-02-25
Original release date:
2011-06-22
Authors:
Martin-Tumasz, Stephen; Butcher, Samuel
Citation:

Citation: Martin-Tumasz, Stephen; Richie, Ashley; Clos, Lawrence; Brow, David; Butcher, Samuel. "A novel occluded RNA recognition motif in Prp24 unwinds the U6 RNA internal stem loop."  Nucleic Acids Res. 39, 7837-7847 (2011).
PubMed: 21653550

Assembly members:

Assembly members:
L4W, polymer, 117 residues, 12568.729 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: pET-21b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
L4W: MFLERNEVKRLLASRNSKEL ETLICLFPLSDKVSPSLICQ FLQEEIHINEKDIRKILLVS DFNGAIIIFRDSKFAAKMLM ILNGSQFQGKVIRSGTINDM KRYYNNQQNHWHHHHHH

Data sets:
Data typeCount
13C chemical shifts492
15N chemical shifts121
1H chemical shifts807

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1L4W1

Entities:

Entity 1, L4W 117 residues - 12568.729 Da.

1   METPHELEUGLUARGASNGLUVALLYSARG
2   LEULEUALASERARGASNSERLYSGLULEU
3   GLUTHRLEUILECYSLEUPHEPROLEUSER
4   ASPLYSVALSERPROSERLEUILECYSGLN
5   PHELEUGLNGLUGLUILEHISILEASNGLU
6   LYSASPILEARGLYSILELEULEUVALSER
7   ASPPHEASNGLYALAILEILEILEPHEARG
8   ASPSERLYSPHEALAALALYSMETLEUMET
9   ILELEUASNGLYSERGLNPHEGLNGLYLYS
10   VALILEARGSERGLYTHRILEASNASPMET
11   LYSARGTYRTYRASNASNGLNGLNASNHIS
12   TRPHISHISHISHISHISHIS

Samples:

13C15N_H2O: L4W, [U-99% 13C; U-99% 15N], 600 uM; potassium phosphate pH 6 18 mM; potassium chloride 45 mM; DTT 0.9 mM; H2O 9%; D2O 10%

13C15N_D2O: L4W, [U-99% 13C; U-99% 15N], 600 uM; potassium phosphate pH 6, [U-99% 2H], 18 mM; potassium chloride, [U-99% 2H], 45 mM; D2O 100%

Reference: L4W, [U-99% 13C; U-99% 15N], 600 uM; potassium phosphate pH 6 18 mM; potassium chloride 45 mM; DSS 1 uM; H2O 90%; D2O 10%

Unlabeled_D2O: L4W 600 uM; potassium phosphate pH 6, [U-99% 2H], 18 mM; potassium chloride, [U-99% 2H], 45 mM; D2O 100%

Aligned: L4W, [U-99% 13C; U-99% 15N], 600 uM; potassium phosphate pH 6 18 mM; potassium chloride 45 mM; DTT 0.9 mM; DMPC/DHPC q=3 6.5%; CTAB 0.67 mg/mL; H2O 90%; D2O 10%

sample_conditions_1: pH: 6; pressure: 1 atm; temperature: 273 K

RDCs: pH: 6; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC13C15N_H2Oisotropicsample_conditions_1
3D CBCA(CO)NH13C15N_H2Oisotropicsample_conditions_1
3D 1H-15N NOESY13C15N_H2Oisotropicsample_conditions_1
3D HNCACB13C15N_H2Oisotropicsample_conditions_1
3D HNCO13C15N_H2Oisotropicsample_conditions_1
3D HBHA(CO)NH13C15N_H2Oisotropicsample_conditions_1
3D C(CO)NH13C15N_H2Oisotropicsample_conditions_1
3D H(CCO)NH13C15N_H2Oisotropicsample_conditions_1
2D 1H-13C HSQC aliphatic13C15N_D2Oisotropicsample_conditions_1
2D 1H-13C HSQC aromatic13C15N_D2Oisotropicsample_conditions_1
2D 1H-1H NOESYUnlabeled_D2Oisotropicsample_conditions_1
3D HCCH-TOCSY13C15N_D2Oisotropicsample_conditions_1
3D 1H-13C NOESY aliphatic13C15N_D2Oisotropicsample_conditions_1
3D 1H-13C NOESY aromatic13C15N_D2Oisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticReferenceisotropicsample_conditions_1
2D-NHSQC-IPAP13C15N_H2OisotropicRDCs
2D-NHSQC-IPAPAlignedanisotropicRDCs
3D-Jmodulated-CHSQC13C15N_H2OisotropicRDCs
3D-Jmodulated-CHSQCAlignedanisotropicRDCs

Software:

VNMRJ, Varian - collection

xwinnmr, Bruker Biospin - collection

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

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

TALOS, Cornilescu, Delaglio and Bax - data analysis

HADDOCK v2.0, Alexandre Bonvin - data analysis, refinement

UNIO v08, Torsten Herrmann - structure solution

nmr_structure_tools, Lawrence J Clos - data analysis

NMR spectrometers:

  • Varian Uniform NMR System 600 MHz
  • Bruker DMX 750 MHz
  • Varian Uniform NMR System 900 MHz

Related Database Links:

BMRB 17491
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