BMRB Entry 16930

Name: Chemical shift assignments of the Talin F2 domain (residues 196-309)
Published: 2010-10-14

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16930

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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:

Chemical shift assignments of the Talin F2 domain (residues 196-309)

Deposition date:

2010-05-14

Original release date:

2010-10-14

Authors:

Goult, Ben

Citation:

Citation: Kalli, Antreas; Wegener, Kate; Goult, Benjamin; Anthis, Nicholas; Campbell, Iain; Sansom, Mark. "The structure of the talin/integrin complex at a lipid bilayer: an NMR and MD simulation study." Structure 18, 1280-1288 (2010).
PubMed: 20947017

Assembly members:

Assembly members:
F2, polymer, 120 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-151

Entity Sequences (FASTA):

Entity Sequences (FASTA):
F2: GIDPFTKFFYSDQNVDSRDP VQLNLLYVQARDDILNGSHP VSFDKACEFAGFQCQIQFGP HNEQKHKAGFLDLKDFLPKE YVKQKGERKIFQAHKNCGQM SEIEAKVRYVKLARSLKTYG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	343
15N chemical shifts	113
1H chemical shifts	113

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	F2	1

Entities:

Entity 1, F2 120 residues - Formula weight is not available

Residues 1-6 (190-195) represent a non-native affinity tag

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

Samples:

sample_1: F2 1 ± 0.05 mM; DTT 2 ± 0.05 mM; sodium chloride 50 ± 0.05 mM; sodium phosphate 20 ± 0.05 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 M; 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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v2, Bruker Biospin - collection, processing

Analysis v2.1.3, CCPN - chemical shift assignment, data analysis

NMR spectrometers:

Bruker DRX 600 MHz

BMRB	15792 16932 16959
PDB	1Y19 3IVF
DBJ	BAA82979 BAC30516 BAC65702 BAE27781 BAG09941
EMBL	CAA39588
GB	AAD13152 AAF23322 AAF27330 AAH42923 AAI22767
PRF	1617167A
REF	NP_001034114 NP_001192357 NP_006280 NP_035732 XP_001084941
SP	P26039 Q9Y490
TPG	DAA26829
AlphaFold	P26039 Q9Y490

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

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