BMRB Entry 15710

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15710
MolProbity Validation Chart

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Title:
Structural Basis of PxxDY Motif Recognition in SH3 Binding
Deposition date:
2008-04-02
Original release date:
2008-08-28
Authors:
Aitio, Olli; Hellman, Maarit; Kesti, Tapio; Kleino, Iivari; Samuilova, Olga; Tossavainen, Helena; Saksela, Kalle; Permi, Perttu
Citation:

Citation: Aitio, Olli; Hellman, Maarit; Kesti, Tapio; Kleino, Iivari; Samuilova, Olga; Paakkonen, Kimmo; Tossavainen, Helena; Saksela, Kalle; Permi, Perttu. "Structural basis of PxxDY motif recognition in SH3 binding"  J. Mol. Biol. 382, 167-178 (2008).
PubMed: 18644376

Assembly members:

Assembly members:
Eps8L1SH3, polymer, 68 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX6P

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Eps8L1SH3: GPLGSGALKWVLCNYDFQAR NSSELSVKQRDVLEVLDDSR KWWKVRDPAGQEGYVPYNIL TPYPAAAS

Data sets:
Data typeCount
13C chemical shifts235
15N chemical shifts62
1H chemical shifts452

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1component 11

Entities:

Entity 1, component 1 68 residues - Formula weight is not available

1   GLYPROLEUGLYSERGLYALALEULYSTRP
2   VALLEUCYSASNTYRASPPHEGLNALAARG
3   ASNSERSERGLULEUSERVALLYSGLNARG
4   ASPVALLEUGLUVALLEUASPASPSERARG
5   LYSTRPTRPLYSVALARGASPPROALAGLY
6   GLNGLUGLYTYRVALPROTYRASNILELEU
7   THRPROTYRPROALAALAALASER

Samples:

sample_1: Eps8L1SH3, [U-13C; U-15N], 0.8 mM

sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D iHNCACBsample_1isotropicsample_conditions_1
3D iHNCAsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D CC(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HEsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

VNMR, Varian - collection, processing

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

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAA91041 BAC11399 BAG59319
GB AAG03038 AAG03039 AAH15763 AAL76117 AAQ15231
REF NP_060199 NP_573441 XP_005259077 XP_011525352
SP Q8TE68
AlphaFold Q8TE68

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks