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 30010

Title: Amphiphysin SH3 in complex with Chikungunya virus nsP3 peptide   PubMed: 27268056

Deposition date: 2016-02-04 Original release date: 2016-06-13

Authors: Tossavainen, H.; Aitio, O.; Hellman, M.; Saksela, K.; Permi, P.

Citation: Tossavainen, H.; Aitio, O.; Hellman, M.; Saksela, K.; Permi, P.. "Structural Basis of the High Affinity Interaction between the Alphavirus Nonstructural Protein-3 (nsP3) and the SH3 Domain of Amphiphysin-2"  J. Biol. Chem. 291, 16307-16317 (2016).

Assembly members:
entity_1, polymer, 81 residues, 9356.412 Da.
entity_2, polymer, 17 residues, 1938.266 Da.

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

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

Entity Sequences (FASTA):
entity_1: GRLDLPPGFMFKVQAQHDYT ATDTDELQLKAGDVVLVIPF QNPEEQDEGWLMGVKESDWN QHKELEKCRGVFPENFTERV P
entity_2: STVPVAPPRRRRGRNLT

Data sets:
Data typeCount
13C chemical shifts334
15N chemical shifts105
1H chemical shifts704

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 81 residues - 9356.412 Da.

1   GLYARGLEUASPLEUPROPROGLYPHEMET
2   PHELYSVALGLNALAGLNHISASPTYRTHR
3   ALATHRASPTHRASPGLULEUGLNLEULYS
4   ALAGLYASPVALVALLEUVALILEPROPHE
5   GLNASNPROGLUGLUGLNASPGLUGLYTRP
6   LEUMETGLYVALLYSGLUSERASPTRPASN
7   GLNHISLYSGLULEUGLULYSCYSARGGLY
8   VALPHEPROGLUASNPHETHRGLUARGVAL
9   PRO

Entity 2, entity_2 17 residues - 1938.266 Da.

1   SERTHRVALPROVALALAPROPROARGARG
2   ARGARGGLYARGASNLEUTHR

Samples:

sample_1: CHIKV nsP3 peptide, [U-13C; U-15N], 0.5 mM; amphiphysin 2 SH3, [U-13C; U-15N], 0.5 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HEsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1

Software:

AMBER, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

SPARKY, Goddard - chemical shift assignment, peak picking

VNMR, Varian - processing

NMR spectrometers:

  • Varian INOVA 800 MHz

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