BMRB Entry 19949

Name: The proline-rich region of 18.5-kDa myelin basic protein requires long-range interactions with residues upstream to interact with the SH3-domain of Fyn
Published: 2019-07-11

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19949

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

The proline-rich region of 18.5-kDa myelin basic protein requires long-range interactions with residues upstream to interact with the SH3-domain of Fyn

Deposition date:

2014-04-30

Original release date:

2019-07-11

Authors:

De Avila, Miguel; Vassall, Kenrick; Smith, Graham; Bamm, Vladimir; Harauz, George

Citation:

Citation: De Avila, Miguel; Vassall, Kenrick; Smith, Graham; Bamm, Vladimir; Harauz, George. "The proline-rich region of 18.5 kDa myelin basic protein binds to the SH3-domain of Fyn tyrosine kinase with the aid of an upstream segment to form a dynamic complex in vitro" Biosci. Rep. 34, e00157-e00157 (2014).
PubMed: 25343306

Assembly members:

Assembly members:
MBP_S38-S107_peptide, polymer, 70 residues, Formula weight is not available
Fyn_SH3_domain, polymer, 80 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-SUMO vector

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MBP_S38-S107_peptide: SIGRFFSGDRGAPKRGSGKD SHTRTTHYGSLPQKSQHGRT QDENPVVHFFKNIVTPRTPP PSQGKGRGLS
Fyn_SH3_domain: MVQISVTLFVALYDYEARTE DDLSFHKGEKFQILNSSEGD WWEARSLTTGETGYIPSNYV APVDRLDYKDDDDKHHHHHH

Data sets:

assigned_chemical_shifts
- EPPH+Fyn_Assignments
heteronucl_T1_relaxation
- heteronuclear_T1_list_EPPH+Fyn
heteronucl_T2_relaxation
- heteronuclear_T2_list_EPPH+Fyn

Data type	Count
13C chemical shifts	164
15N chemical shifts	62
1H chemical shifts	63
T1 relaxation values	56
T2 relaxation values	56

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MBP peptide	1
2	Fyn peptide	2

Entities:

Entity 1, MBP peptide 70 residues - Formula weight is not available

1	SER	ILE	GLY	ARG	PHE	PHE	SER	GLY	ASP	ARG
2	GLY	ALA	PRO	LYS	ARG	GLY	SER	GLY	LYS	ASP
3	SER	HIS	THR	ARG	THR	THR	HIS	TYR	GLY	SER
4	LEU	PRO	GLN	LYS	SER	GLN	HIS	GLY	ARG	THR
5	GLN	ASP	GLU	ASN	PRO	VAL	VAL	HIS	PHE	PHE
6	LYS	ASN	ILE	VAL	THR	PRO	ARG	THR	PRO	PRO
7	PRO	SER	GLN	GLY	LYS	GLY	ARG	GLY	LEU	SER

Entity 2, Fyn peptide 80 residues - Formula weight is not available

1	MET	VAL	GLN	ILE	SER	VAL	THR	LEU	PHE	VAL
2	ALA	LEU	TYR	ASP	TYR	GLU	ALA	ARG	THR	GLU
3	ASP	ASP	LEU	SER	PHE	HIS	LYS	GLY	GLU	LYS
4	PHE	GLN	ILE	LEU	ASN	SER	SER	GLU	GLY	ASP
5	TRP	TRP	GLU	ALA	ARG	SER	LEU	THR	THR	GLY
6	GLU	THR	GLY	TYR	ILE	PRO	SER	ASN	TYR	VAL
7	ALA	PRO	VAL	ASP	ARG	LEU	ASP	TYR	LYS	ASP
8	ASP	ASP	ASP	LYS	HIS	HIS	HIS	HIS	HIS	HIS

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	MBP+Fyn_sample	isotropic	sample_conditions_1
3D HNCO	MBP+Fyn_sample	isotropic	sample_conditions_1
3D HN(CA)CO	MBP+Fyn_sample	isotropic	sample_conditions_1
3D CBCA(CO)NH	MBP+Fyn_sample	isotropic	sample_conditions_1
3D HNCACB	MBP+Fyn_sample	isotropic	sample_conditions_1
3D HACAN	MBP+Fyn_sample	isotropic	sample_conditions_1

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

BMRB Entry 19949

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

1	SER	ILE	GLY	ARG	PHE	PHE	SER	GLY	ASP	ARG
2	GLY	ALA	PRO	LYS	ARG	GLY	SER	GLY	LYS	ASP
3	SER	HIS	THR	ARG	THR	THR	HIS	TYR	GLY	SER
4	LEU	PRO	GLN	LYS	SER	GLN	HIS	GLY	ARG	THR
5	GLN	ASP	GLU	ASN	PRO	VAL	VAL	HIS	PHE	PHE
6	LYS	ASN	ILE	VAL	THR	PRO	ARG	THR	PRO	PRO
7	PRO	SER	GLN	GLY	LYS	GLY	ARG	GLY	LEU	SER

1	MET	VAL	GLN	ILE	SER	VAL	THR	LEU	PHE	VAL
2	ALA	LEU	TYR	ASP	TYR	GLU	ALA	ARG	THR	GLU
3	ASP	ASP	LEU	SER	PHE	HIS	LYS	GLY	GLU	LYS
4	PHE	GLN	ILE	LEU	ASN	SER	SER	GLU	GLY	ASP
5	TRP	TRP	GLU	ALA	ARG	SER	LEU	THR	THR	GLY
6	GLU	THR	GLY	TYR	ILE	PRO	SER	ASN	TYR	VAL
7	ALA	PRO	VAL	ASP	ARG	LEU	ASP	TYR	LYS	ASP
8	ASP	ASP	ASP	LYS	HIS	HIS	HIS	HIS	HIS	HIS

1	SER	ILE	GLY	ARG	PHE	PHE	SER	GLY	ASP	ARG
2	GLY	ALA	PRO	LYS	ARG	GLY	SER	GLY	LYS	ASP
3	SER	HIS	THR	ARG	THR	THR	HIS	TYR	GLY	SER
4	LEU	PRO	GLN	LYS	SER	GLN	HIS	GLY	ARG	THR
5	GLN	ASP	GLU	ASN	PRO	VAL	VAL	HIS	PHE	PHE
6	LYS	ASN	ILE	VAL	THR	PRO	ARG	THR	PRO	PRO
7	PRO	SER	GLN	GLY	LYS	GLY	ARG	GLY	LEU	SER

1	MET	VAL	GLN	ILE	SER	VAL	THR	LEU	PHE	VAL
2	ALA	LEU	TYR	ASP	TYR	GLU	ALA	ARG	THR	GLU
3	ASP	ASP	LEU	SER	PHE	HIS	LYS	GLY	GLU	LYS
4	PHE	GLN	ILE	LEU	ASN	SER	SER	GLU	GLY	ASP
5	TRP	TRP	GLU	ALA	ARG	SER	LEU	THR	THR	GLY
6	GLU	THR	GLY	TYR	ILE	PRO	SER	ASN	TYR	VAL
7	ALA	PRO	VAL	ASP	ARG	LEU	ASP	TYR	LYS	ASP
8	ASP	ASP	ASP	LYS	HIS	HIS	HIS	HIS	HIS	HIS

1	SER	ILE	GLY	ARG	PHE	PHE	SER	GLY	ASP	ARG
2	GLY	ALA	PRO	LYS	ARG	GLY	SER	GLY	LYS	ASP
3	SER	HIS	THR	ARG	THR	THR	HIS	TYR	GLY	SER
4	LEU	PRO	GLN	LYS	SER	GLN	HIS	GLY	ARG	THR
5	GLN	ASP	GLU	ASN	PRO	VAL	VAL	HIS	PHE	PHE
6	LYS	ASN	ILE	VAL	THR	PRO	ARG	THR	PRO	PRO
7	PRO	SER	GLN	GLY	LYS	GLY	ARG	GLY	LEU	SER

1	MET	VAL	GLN	ILE	SER	VAL	THR	LEU	PHE	VAL
2	ALA	LEU	TYR	ASP	TYR	GLU	ALA	ARG	THR	GLU
3	ASP	ASP	LEU	SER	PHE	HIS	LYS	GLY	GLU	LYS
4	PHE	GLN	ILE	LEU	ASN	SER	SER	GLU	GLY	ASP
5	TRP	TRP	GLU	ALA	ARG	SER	LEU	THR	THR	GLY
6	GLU	THR	GLY	TYR	ILE	PRO	SER	ASN	TYR	VAL
7	ALA	PRO	VAL	ASP	ARG	LEU	ASP	TYR	LYS	ASP
8	ASP	ASP	ASP	LYS	HIS	HIS	HIS	HIS	HIS	HIS