BMRB Entry 27168

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27168

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

1H, 15N, and 13C chemical shift assignments of the micelle immersed C-terminal FATC domain of the human DNA-dependent protein kinase catalytic subunit (DNA-PKcs) fused to the B1 domain of streptococcal protein G (GB1)

Deposition date:

2017-07-06

Original release date:

2018-02-02

Authors:

Abd Rahim, Munirah Sufiyah; Dames, Sonja; Sommer, Lisa; Shaad, Martin

Citation:

Citation: Rahim, M.; Sommer, L.; Wacker, A.; Schaad, M.; Dames, S.. "1H, 15N, and 13C chemical shift assignments of the micelle immersed FAT C-terminal (FATC) domains of the human protein kinases ataxia-telangiectasia mutated (ATM) and DNA-dependent protein kinase catalytic subunit (DNA-PKcs) fused to the B1 domain of streptococcal protein G (GB1)" Biomol. NMR Assign. 12, 149-154 (2018).
PubMed: 29349619

Assembly members:

Assembly members:
hdnapkfatc, polymer, 100 residues, 11170.25 Da.

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: pGEV2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hdnapkfatc: MQYKLALNGKTLKGETTTEA VDAATAEKVVKQFANDNGVD GEWTYDDATKTFTVTELVPR GSDDDDKSGLSEETQVKCLM DQATDPNILGRTWEGWEPWM

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	288
15N chemical shifts	105
1H chemical shifts	569

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	gb1ent-dnapkfatc	1

Entities:

Entity 1, gb1ent-dnapkfatc 100 residues - 11170.25 Da.

Residue 1-56 represent the GB1 tag and are followed by a thrombin (LVPRGS) and an enterokinase (DDDDK) site. Residue 68-100 correspond to the FATC domain.

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

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	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
3D HNCA	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
15N T1	sample_2	isotropic	sample_conditions_1
15N T2	sample_2	isotropic	sample_conditions_1
{1H}-15N-NOE	sample_2	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 27168

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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

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

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