BMRB Entry 30010

Name: Amphiphysin SH3 in complex with Chikungunya virus nsP3 peptide
Published: 2016-06-13

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PDB ID: 5i22
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR30010
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	334
15N chemical shifts	105
1H chemical shifts	704

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	2

Entities:

Entity 1, entity_1 81 residues - 9356.412 Da.

1

GLY

ARG

LEU

ASP

LEU

PRO

GLY

PHE

MET

2

PHE

LYS

VAL

GLN

ALA

GLN

HIS

ASP

TYR

THR

3

ALA

THR

ASP

THR

ASP

GLU

LEU

GLN

LEU

LYS

4

ALA

GLY

ASP

VAL

LEU

VAL

ILE

PRO

PHE

5

GLN

ASN

PRO

GLU

GLN

ASP

GLU

GLY

TRP

6

LEU

MET

GLY

VAL

LYS

GLU

SER

ASP

TRP

ASN

7

GLN

HIS

LYS

GLU

LEU

GLU

LYS

CYS

ARG

GLY

8

VAL

PHE

PRO

GLU

ASN

PHE

THR

GLU

ARG

VAL

9

PRO

Entity 2, entity_2 17 residues - 1938.266 Da.

1

SER

THR

VAL

PRO

VAL

ALA

PRO

ARG

2

ARG

GLY

ARG

ASN

LEU

THR

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
2D (HB)CB(CGCDCE)HE	sample_1	isotropic	sample_conditions_1
2D (HB)CB(CGCD)HD	sample_1	isotropic	sample_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