BMRB Entry 50126

Name: PACSIN 1 domain SH3
Published: 2019-12-19

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR50126

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

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Title:

PACSIN 1 domain SH3

Deposition date:

2019-12-13

Original release date:

2019-12-19

Authors:

Boll, Emmanuelle; Cantrelle, Francois-Xavier; Landrieu, Isabelle; Hirel, Matthieu; Sinnaeve, Davy; Levy, Geraldine

Citation:

Citation: Boll, Emmanuelle; Cantrelle, Francois-Xavier; Landrieu, Isabelle; Hirel, Matthieu; Sinnaeve, Davy; Levy, Geraldine. "1H, 13C, and 15N chemical shift assignment of human PACSIN1/syndapin I SH3 domain in solution" Biomol. NMR Assignments 14, 175-178 (2020).
PubMed: 32236802

Assembly members:

Assembly members:
entity_1, polymer, 70 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: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MAKGVRVRALYDYDGQEQDE LSFKAGDELTKLGEEDEQGW CRGRLDSGQLGLYPANYVEA IGSSHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	216
15N chemical shifts	70
1H chemical shifts	304

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PACSIN 1 domain SH3	1

Entities:

Entity 1, PACSIN 1 domain SH3 70 residues - Formula weight is not available

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

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCaCO	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
HNCOCaCB	sample_1	isotropic	sample_conditions_1
BHNCOCaCb	sample_1	isotropic	sample_conditions_1
hCCcoNH	sample_1	isotropic	sample_conditions_1
HNcaNNH	sample_1	isotropic	sample_conditions_1
HNcN	sample_1	isotropic	sample_conditions_1
hbhanh	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
hbhaconh	sample_1	isotropic	sample_conditions_1
HcccoNH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
HcCH-TOCSY	sample_1	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 50126

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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

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

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