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Biological Magnetic Resonance Data Bank


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BMRB Entry 16970

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16970
MolProbity Validation Chart

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Title: Solution structure of the Bem1p SH3-CI domain from L.elongisporus in complex with Ste20p peptide   PubMed: 21489982

Deposition date: 2010-06-02 Original release date: 2010-07-01

Authors: Gorelik, Maryna; Muhandiram, Ranjith; Davidson, Alan

Citation: Gorelik, Maryna; Stanger, Karen; Davidson, Alan. "A Conserved residue in the yeast Bem1p SH3 domain maintains the high level of binding specificity required for function."  J. Biol. Chem. 286, 19470-19477 (2011).

Assembly members:
Bud_emergence_protein_1, polymer, 120 residues, 13772.617 Da.
Peptide_from_Serine/Threonine_kinase_Ste20, polymer, 16 residues, 1639.933 Da.

Natural source:   Common Name: ascomycetes   Taxonomy ID: 36914   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Lodderomyces elongisporus

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

Entity Sequences (FASTA):
Bud_emergence_protein_1: MAPLFAVTLYEFKAERDDEL DVSPGENLSICAHYDYEWFI AKPINRLGGPGLVPVSYVRI IDLMDPAKYASVDTYDREQV MKIIDEFKIPTVEQWKDQTR RYKESSIQIGNGHGQSQGLE
Peptide_from_Serine/Threonine_kinase_Ste20: GKFIPSRPAPKPPSSA

Data sets:
Data typeCount
13C chemical shifts546
15N chemical shifts122
1H chemical shifts952

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Bud_emergence_protein_11
2Peptide_from_Serine/Threonine_kinase_Ste202

Entities:

Entity 1, Bud_emergence_protein_1 120 residues - 13772.617 Da.

Residues 1-2 and 119-120 represent cloning artifacts

1   METALAPROLEUPHEALAVALTHRLEUTYR
2   GLUPHELYSALAGLUARGASPASPGLULEU
3   ASPVALSERPROGLYGLUASNLEUSERILE
4   CYSALAHISTYRASPTYRGLUTRPPHEILE
5   ALALYSPROILEASNARGLEUGLYGLYPRO
6   GLYLEUVALPROVALSERTYRVALARGILE
7   ILEASPLEUMETASPPROALALYSTYRALA
8   SERVALASPTHRTYRASPARGGLUGLNVAL
9   METLYSILEILEASPGLUPHELYSILEPRO
10   THRVALGLUGLNTRPLYSASPGLNTHRARG
11   ARGTYRLYSGLUSERSERILEGLNILEGLY
12   ASNGLYHISGLYGLNSERGLNGLYLEUGLU

Entity 2, Peptide_from_Serine/Threonine_kinase_Ste20 16 residues - 1639.933 Da.

1   GLYLYSPHEILEPROSERARGPROALAPRO
2   LYSPROPROSERSERALA

Samples:

sample_1: Bem1 SH3-CI protein, [U-99% 13C; U-99% 15N], 0.7 ± 0.05 mM; Ste20 peptide 1.5 ± 0.1 mM; PMSF 0.5 mM; EDTA 0.5 mM; sodium azide 0.05%; HEPES 50 mM; sodium chloride 100 mM; DTT 1 mM; H2O 95%; D2O 5%

sample_2: Bem1 SH3-CI protein, [U-99% 13C; U-99% 15N], 0.7 ± 0.05 mM; Ste20 peptide 1.5 ± 0.1 mM; PMSF 0.5 mM; EDTA 0.5 mM; sodium azide 0.05%; HEPES 50 mM; sodium chloride 100 mM; DTT 1 mM; D2O 100%

sample_3: Bem1 SH3-CI protein, [U-99% 13C; U-99% 15N], 0.5 ± 0.05 mM; Ste20 peptide 0.5 mM; sodium chloride 100 mM; sodium phosphate 50 mM; sodium azide 0.05%; H2O 95%; D2O 5%

sample_4: Bem1 SH3-CI protein, [U-99% 13C; U-99% 15N], 0.5 ± 0.05 mM; Ste20 peptide 0.5 mM; sodium chloride 100 mM; sodium phosphate 50 mM; sodium azide 0.05%; D2O 100%

sample_conditions: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions
3D HNCOsample_1isotropicsample_conditions
3D HN(CO)CAsample_1isotropicsample_conditions
3D HNCACBsample_1isotropicsample_conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions
3D C(CO)NHsample_1isotropicsample_conditions
3D HNCAsample_1isotropicsample_conditions
2D 1H-13C HSQCsample_2isotropicsample_conditions
3D HCCH-TOCSYsample_2isotropicsample_conditions
3D HCCH-COSYsample_2isotropicsample_conditions
3D 1H-15N NOESYsample_2isotropicsample_conditions
3D 1H-13C NOESYsample_2isotropicsample_conditions
15N C13 filtered 2D 1H-1H TOCSYsample_3isotropicsample_conditions
15N C13 filtered 2D 1H-1H NOESYsample_3isotropicsample_conditions
15N C13 filtered 2D 1H-1H COSYsample_4isotropicsample_conditions
13C half-filtered 1H-13C NOESYsample_4isotropicsample_conditions

Software:

SPARKY, Goddard - chemical shift assignment, peak picking

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

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 800 MHz

Related Database Links:

PDB
GB EDK46053 AAA35038 AAA35111 AAB69747 AHY77690 EDN62227
REF XP_001524262 NP_011856
BMRB 17629
DBJ GAA23703
SP Q03497
TPG DAA06681

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