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 17629

Title: Yeast Nbp2p SH3 domain in complex with a peptide from Ste20p

Deposition date: 2011-05-07 Original release date: 2011-06-03

Authors: Gorelik, Maryna; Davidson, Alan

Citation: Gorelik, Maryna; Davidson, Alan. "Not known"  Not known ., .-..

Assembly members:
Nbp2_SH3, polymer, 73 residues, 7562.403 Da.
Ste20_peptide, polymer, 16 residues, 1639.933 Da.

Natural source:   Common Name: baker   Taxonomy ID: 4932   Superkingdom: not available   Kingdom: not available   Genus/species: Eukaryota Fungi

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

Entity Sequences (FASTA):
Nbp2_SH3: MAIVNQRAVALYDFEPENDN ELRLAEGDIVFISYKHGQGW LVAENESGSKTGLVPEEFVS YIQPELEHHHHHH
Ste20_peptide: GKFIPSRPAPKPPSSA

Data sets:
Data typeCount
13C chemical shifts280
15N chemical shifts71
1H chemical shifts564

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Nbp2_SH31
2Ste20_peptide2

Entities:

Entity 1, Nbp2_SH3 73 residues - 7562.403 Da.

Residues 1-2 and 66-67 represent non-native residues obtained from cloning. Residues 68-73 represent His tag.

1   METALAILEVALASNGLNARGALAVALALA
2   LEUTYRASPPHEGLUPROGLUASNASPASN
3   GLULEUARGLEUALAGLUGLYASPILEVAL
4   PHEILESERTYRLYSHISGLYGLNGLYTRP
5   LEUVALALAGLUASNGLUSERGLYSERLYS
6   THRGLYLEUVALPROGLUGLUPHEVALSER
7   TYRILEGLNPROGLULEUGLUHISHISHIS
8   HISHISHIS

Entity 2, Ste20_peptide 16 residues - 1639.933 Da.

1   GLYLYSPHEILEPROSERARGPROALAPRO
2   LYSPROPROSERSERALA

Samples:

sample_1: Nbp2 SH3, [U-99% 13C; U-99% 15N], 0.7 ± 0.1 mM; Ste20 peptide 1.4 ± 0.1 mM; sodium chloride 100 mM; sodium phosphate 50 mM; sodium azide 0.05%%; D2O 5%%; H2O 95%%

sample_2: Nbp2 SH3, [U-99% 13C; U-99% 15N], 0.7 ± 0.1 mM; Ste20 peptide 1.4 ± 0.1 mM; sodium chloride 100 mM; sodium phosphate 50 mM; sodium azide 0.05%; D2O 100%

sample_3: Nbp2 SH3, [U-99% 13C; U-99% 15N], 0.7 ± 0.1 mM; Ste20 peptide 0.7 ± 0.1 mM; sodium chloride 100 mM; sodium phosphate 50 mM; sodium azide 0.05%; D2O 5%; H2O 95%

sample_4: Nbp2 SH3, [U-99% 13C; U-99% 15N], 0.7 ± 0.1 mM; Ste20 peptide 0.7 ± 0.1 mM; sodium chloride 100 mM; sodium phosphate 50 mM; sodium azide 0.05%; D2O 100%

sample_conditions_1: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
N15 C13 filtered 2D 1H-1H TOCSYsample_3isotropicsample_conditions_1
15N C13 filtered 2D 1H-1H NOESYsample_3isotropicsample_conditions_1
13C half-filtered 3D 1H-13C NOESYsample_4isotropicsample_conditions_1
13C filtered 2D 1H-1H COSYsample_4isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, data analysis, structure solution

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

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

  • Bruker INOVA 500 MHz
  • Bruker INOVA 800 MHz

Related Database Links:

PDB
DBJ BAA07790 GAA22392 GAA23703
EMBL CAA90382 CAY78665
GB AAS56004 AHY75148 AJP37876 AJU57998 AJU58693 AAA35038 AAA35111 AAB69747 AHY77690 EDN62227
REF NP_010446 NP_011856
SP Q12163 Q03497
TPG DAA12002 DAA06681
BMRB 16970

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