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 16176

Title: Prp40 FF4 domain   PubMed: 19722265

Deposition date: 2009-02-18 Original release date: 2009-08-10

Authors: Bonet, Roman; Ruiz, Lidia; Morales, Begonya; Macias, Maria

Citation: Bonet, Roman; Ruiz, Lidia; Morales, Begona; Macias, Maria. "Solution structure of the fourth FF domain of yeast Prp40 splicing factor."  Proteins 77, 1000-1003 (2009).

Assembly members:
yeast_Prp40_FF4_domain, polymer, 69 residues, 7900.010 Da.

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

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

Entity Sequences (FASTA):
yeast_Prp40_FF4_domain: GAMGNERRILEQKKHYFWLL LQRTYTKTGKPKPSTWDLAS KELGESLEYKALGDEDNIRR QIFEDFKPE

Data sets:
Data typeCount
13C chemical shifts249
15N chemical shifts61
1H chemical shifts497

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1yeast_Prp40_FF4_domain1

Entities:

Entity 1, yeast_Prp40_FF4_domain 69 residues - 7900.010 Da.

FF4 domain correspond to residues 488-552 of Prp40.Residues 1-4 in the chem.shift list remain from the cloning after cleavage of the tag

1   GLYALAMETGLYASNGLUARGARGILELEU
2   GLUGLNLYSLYSHISTYRPHETRPLEULEU
3   LEUGLNARGTHRTYRTHRLYSTHRGLYLYS
4   PROLYSPROSERTHRTRPASPLEUALASER
5   LYSGLULEUGLYGLUSERLEUGLUTYRLYS
6   ALALEUGLYASPGLUASPASNILEARGARG
7   GLNILEPHEGLUASPPHELYSPROGLU

Samples:

yeast_Prp40_FF4_domain_unlabeled: yeast Prp40 FF4 domain 0.5 mM; sodium phosphate 20 mM; sodium chloride 130 mM; sodium azide 0.5 mM; H20 90%; D20 10%

yeast_Prp40_FF4_domain_labeled: yeast Prp40 FF4 domain, [U-100% 15N], 0.5 mM; yeast Prp40 FF4 domain, [U-100% 13C], 0.5 mM; sodium phosphate 20 mM; sodium chloride 130 mM; sodium azide 0.5 mM; D20 100%

sample_conditions_1: ionic strength: 150 mM; pH: 5.8; pressure: 1.0 atm; temperature: 285 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYyeast_Prp40_FF4_domain_unlabeledisotropicsample_conditions_1
2D 1H-1H TOCSYyeast_Prp40_FF4_domain_unlabeledisotropicsample_conditions_1
3D CBCA(CO)NHyeast_Prp40_FF4_domain_labeledisotropicsample_conditions_1
3D HNCACByeast_Prp40_FF4_domain_labeledisotropicsample_conditions_1
3D H(CCO)NHyeast_Prp40_FF4_domain_labeledisotropicsample_conditions_1
3D HCCH-TOCSYyeast_Prp40_FF4_domain_labeledisotropicsample_conditions_1
3D 1H-15N NOESYyeast_Prp40_FF4_domain_labeledisotropicsample_conditions_1
3D 1H-13C NOESYyeast_Prp40_FF4_domain_labeledisotropicsample_conditions_1
2D 1H-15N HSQCyeast_Prp40_FF4_domain_labeledisotropicsample_conditions_1
2D 1H-13C HSQCyeast_Prp40_FF4_domain_labeledisotropicsample_conditions_1

Software:

ARIA v2.0, Linge, O, . - refinement, structure solution

XEASY, Bartels et al. - chemical shift assignment, peak picking

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

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

ProcheckNMR, Laskowski and MacArthur - data analysis

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker DRX 800 MHz

Related Database Links:

PDB
DBJ GAA24712
EMBL CAA81847 CAY81071
GB AAB24902 AHY76231 AJP40025 AJS30223 AJS30524
REF NP_012913
SP P33203
TPG DAA09144

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts