BMRB Entry 50457

Name: Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain complexed to talazoparib
Published: 2020-09-15

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50457

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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:

Backbone amide group 15N and 1H assignments and 15N relaxation data for human PARP-1 CAT domain complexed to talazoparib

Deposition date:

2020-09-03

Original release date:

2020-09-15

Authors:

Ogden, Tom; Yang, Ji-Chun; Neuhaus, David

Citation:

Citation: Ogden, Tom; Yang, Ji-Chun; Schimpl, Marianne; Easton, Laura; Underwood, Elizabeth; Rawlins, Philip; McCauley, Michael; Langelier, Marie-France; Pascal, John; Embrey, Kevin; Neuhaus, David. "Dynamics of the HD regulatory subdomain of PARP-1; substrate access and allostery in PARP activation and inhibition" Nucleic Acids Res. 49, 2266-2288 (2021).
PubMed: 33511412

Assembly members:

Assembly members:
entity_1, polymer, 360 residues, Formula weight is not available
entity_2YQ, non-polymer, 380.351 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: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GTVNPGTKSKLPKPVQDLIK MIFDVESMKKAMVEYEIDLQ KMPLGKLSKRQIQAAYSILS EVQQAVSQGSSDSQILDLSN RFYTLIPHDFGMKKPPLLNN ADSVQAKAEMLDNLLDIEVA YSLLRGGSDDSSKDPIDVNY EKLKTDIKVVDRDSEEAEII RKYVKNTHATTHNAYDLEVI DIFKIEREGECQRYKPFKQL HNRRLLWHGSRTTNFAGILS QGLRIAPPEAPVTGYMFGKG IYFADMVSKSANYCHTSQGD PIGLILLGEVALGNMYELKH ASHISKLPKGKHSVKGLGKT TPDPSANISLDGVDVPLGTG ISSGVNDTSLLYNEYIVYDI AQVNLKYLLKLKFNFKTSLW

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
heteronucl_NOEs
- heteronuclear_noe_list_1
heteronucl_T1_relaxation
- heteronuclear_T1_list_1
heteronucl_T1rho_relaxation
- heteronuclear_T1rho_list_1

Data type	Count
15N chemical shifts	324
1H chemical shifts	324
T1 relaxation values	297
T1rho relaxation values	289
heteronuclear NOE values	316

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PARP-1_CAT_domain	1
2	talazoparib	2

Entities:

Entity 1, PARP-1_CAT_domain 360 residues - Formula weight is not available

The first residue in the sequence supplied here is a non-native glycine arising from cloning. The remaining residues are residues 656-1014 of human PARP-1 (the isoform having Ala at position 762).

1	GLY	THR	VAL	ASN	PRO	GLY	THR	LYS	SER	LYS
2	LEU	PRO	LYS	PRO	VAL	GLN	ASP	LEU	ILE	LYS
3	MET	ILE	PHE	ASP	VAL	GLU	SER	MET	LYS	LYS
4	ALA	MET	VAL	GLU	TYR	GLU	ILE	ASP	LEU	GLN
5	LYS	MET	PRO	LEU	GLY	LYS	LEU	SER	LYS	ARG
6	GLN	ILE	GLN	ALA	ALA	TYR	SER	ILE	LEU	SER
7	GLU	VAL	GLN	GLN	ALA	VAL	SER	GLN	GLY	SER
8	SER	ASP	SER	GLN	ILE	LEU	ASP	LEU	SER	ASN
9	ARG	PHE	TYR	THR	LEU	ILE	PRO	HIS	ASP	PHE
10	GLY	MET	LYS	LYS	PRO	PRO	LEU	LEU	ASN	ASN
11	ALA	ASP	SER	VAL	GLN	ALA	LYS	ALA	GLU	MET
12	LEU	ASP	ASN	LEU	LEU	ASP	ILE	GLU	VAL	ALA
13	TYR	SER	LEU	LEU	ARG	GLY	GLY	SER	ASP	ASP
14	SER	SER	LYS	ASP	PRO	ILE	ASP	VAL	ASN	TYR
15	GLU	LYS	LEU	LYS	THR	ASP	ILE	LYS	VAL	VAL
16	ASP	ARG	ASP	SER	GLU	GLU	ALA	GLU	ILE	ILE
17	ARG	LYS	TYR	VAL	LYS	ASN	THR	HIS	ALA	THR
18	THR	HIS	ASN	ALA	TYR	ASP	LEU	GLU	VAL	ILE
19	ASP	ILE	PHE	LYS	ILE	GLU	ARG	GLU	GLY	GLU
20	CYS	GLN	ARG	TYR	LYS	PRO	PHE	LYS	GLN	LEU
21	HIS	ASN	ARG	ARG	LEU	LEU	TRP	HIS	GLY	SER
22	ARG	THR	THR	ASN	PHE	ALA	GLY	ILE	LEU	SER
23	GLN	GLY	LEU	ARG	ILE	ALA	PRO	PRO	GLU	ALA
24	PRO	VAL	THR	GLY	TYR	MET	PHE	GLY	LYS	GLY
25	ILE	TYR	PHE	ALA	ASP	MET	VAL	SER	LYS	SER
26	ALA	ASN	TYR	CYS	HIS	THR	SER	GLN	GLY	ASP
27	PRO	ILE	GLY	LEU	ILE	LEU	LEU	GLY	GLU	VAL
28	ALA	LEU	GLY	ASN	MET	TYR	GLU	LEU	LYS	HIS
29	ALA	SER	HIS	ILE	SER	LYS	LEU	PRO	LYS	GLY
30	LYS	HIS	SER	VAL	LYS	GLY	LEU	GLY	LYS	THR
31	THR	PRO	ASP	PRO	SER	ALA	ASN	ILE	SER	LEU
32	ASP	GLY	VAL	ASP	VAL	PRO	LEU	GLY	THR	GLY
33	ILE	SER	SER	GLY	VAL	ASN	ASP	THR	SER	LEU
34	LEU	TYR	ASN	GLU	TYR	ILE	VAL	TYR	ASP	ILE
35	ALA	GLN	VAL	ASN	LEU	LYS	TYR	LEU	LEU	LYS
36	LEU	LYS	PHE	ASN	PHE	LYS	THR	SER	LEU	TRP

Entity 2, talazoparib - C19 H14 F2 N6 O - 380.351 Da.

1

2YQ

Samples:

sample_1: human PARP-1 CAT domain, [U-15N], 0.4 mM; TRIS, [U-2H], 50 mM; sodium chloride 50 mM; DTT, [U-2H], 2 mM; talazoparib 0.2 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
3D 15N-separated NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N TROSY-based steady-state 15N{1H} NOE measurement	sample_1	isotropic	sample_conditions_1
2D 1H-15N TROSY-based 15N T1 measurement	sample_1	isotropic	sample_conditions_1
2D 1H-15N TROSY-based 15N T1rho measurement	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.2 and 3.5 - processing

MddNMR v2.4 - processing

NMRPipe v8.7 - processing

ANALYSIS v2.4.2 - data analysis

SPARKY v3.115 - data analysis

NMR spectrometers:

Bruker AVANCE III HD 800 MHz

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

1	GLY	THR	VAL	ASN	PRO	GLY	THR	LYS	SER	LYS
2	LEU	PRO	LYS	PRO	VAL	GLN	ASP	LEU	ILE	LYS
3	MET	ILE	PHE	ASP	VAL	GLU	SER	MET	LYS	LYS
4	ALA	MET	VAL	GLU	TYR	GLU	ILE	ASP	LEU	GLN
5	LYS	MET	PRO	LEU	GLY	LYS	LEU	SER	LYS	ARG
6	GLN	ILE	GLN	ALA	ALA	TYR	SER	ILE	LEU	SER
7	GLU	VAL	GLN	GLN	ALA	VAL	SER	GLN	GLY	SER
8	SER	ASP	SER	GLN	ILE	LEU	ASP	LEU	SER	ASN
9	ARG	PHE	TYR	THR	LEU	ILE	PRO	HIS	ASP	PHE
10	GLY	MET	LYS	LYS	PRO	PRO	LEU	LEU	ASN	ASN
11	ALA	ASP	SER	VAL	GLN	ALA	LYS	ALA	GLU	MET
12	LEU	ASP	ASN	LEU	LEU	ASP	ILE	GLU	VAL	ALA
13	TYR	SER	LEU	LEU	ARG	GLY	GLY	SER	ASP	ASP
14	SER	SER	LYS	ASP	PRO	ILE	ASP	VAL	ASN	TYR
15	GLU	LYS	LEU	LYS	THR	ASP	ILE	LYS	VAL	VAL
16	ASP	ARG	ASP	SER	GLU	GLU	ALA	GLU	ILE	ILE
17	ARG	LYS	TYR	VAL	LYS	ASN	THR	HIS	ALA	THR
18	THR	HIS	ASN	ALA	TYR	ASP	LEU	GLU	VAL	ILE
19	ASP	ILE	PHE	LYS	ILE	GLU	ARG	GLU	GLY	GLU
20	CYS	GLN	ARG	TYR	LYS	PRO	PHE	LYS	GLN	LEU
21	HIS	ASN	ARG	ARG	LEU	LEU	TRP	HIS	GLY	SER
22	ARG	THR	THR	ASN	PHE	ALA	GLY	ILE	LEU	SER
23	GLN	GLY	LEU	ARG	ILE	ALA	PRO	PRO	GLU	ALA
24	PRO	VAL	THR	GLY	TYR	MET	PHE	GLY	LYS	GLY
25	ILE	TYR	PHE	ALA	ASP	MET	VAL	SER	LYS	SER
26	ALA	ASN	TYR	CYS	HIS	THR	SER	GLN	GLY	ASP
27	PRO	ILE	GLY	LEU	ILE	LEU	LEU	GLY	GLU	VAL
28	ALA	LEU	GLY	ASN	MET	TYR	GLU	LEU	LYS	HIS
29	ALA	SER	HIS	ILE	SER	LYS	LEU	PRO	LYS	GLY
30	LYS	HIS	SER	VAL	LYS	GLY	LEU	GLY	LYS	THR
31	THR	PRO	ASP	PRO	SER	ALA	ASN	ILE	SER	LEU
32	ASP	GLY	VAL	ASP	VAL	PRO	LEU	GLY	THR	GLY
33	ILE	SER	SER	GLY	VAL	ASN	ASP	THR	SER	LEU
34	LEU	TYR	ASN	GLU	TYR	ILE	VAL	TYR	ASP	ILE
35	ALA	GLN	VAL	ASN	LEU	LYS	TYR	LEU	LEU	LYS
36	LEU	LYS	PHE	ASN	PHE	LYS	THR	SER	LEU	TRP

1	GLY	THR	VAL	ASN	PRO	GLY	THR	LYS	SER	LYS
2	LEU	PRO	LYS	PRO	VAL	GLN	ASP	LEU	ILE	LYS
3	MET	ILE	PHE	ASP	VAL	GLU	SER	MET	LYS	LYS
4	ALA	MET	VAL	GLU	TYR	GLU	ILE	ASP	LEU	GLN
5	LYS	MET	PRO	LEU	GLY	LYS	LEU	SER	LYS	ARG
6	GLN	ILE	GLN	ALA	ALA	TYR	SER	ILE	LEU	SER
7	GLU	VAL	GLN	GLN	ALA	VAL	SER	GLN	GLY	SER
8	SER	ASP	SER	GLN	ILE	LEU	ASP	LEU	SER	ASN
9	ARG	PHE	TYR	THR	LEU	ILE	PRO	HIS	ASP	PHE
10	GLY	MET	LYS	LYS	PRO	PRO	LEU	LEU	ASN	ASN
11	ALA	ASP	SER	VAL	GLN	ALA	LYS	ALA	GLU	MET
12	LEU	ASP	ASN	LEU	LEU	ASP	ILE	GLU	VAL	ALA
13	TYR	SER	LEU	LEU	ARG	GLY	GLY	SER	ASP	ASP
14	SER	SER	LYS	ASP	PRO	ILE	ASP	VAL	ASN	TYR
15	GLU	LYS	LEU	LYS	THR	ASP	ILE	LYS	VAL	VAL
16	ASP	ARG	ASP	SER	GLU	GLU	ALA	GLU	ILE	ILE
17	ARG	LYS	TYR	VAL	LYS	ASN	THR	HIS	ALA	THR
18	THR	HIS	ASN	ALA	TYR	ASP	LEU	GLU	VAL	ILE
19	ASP	ILE	PHE	LYS	ILE	GLU	ARG	GLU	GLY	GLU
20	CYS	GLN	ARG	TYR	LYS	PRO	PHE	LYS	GLN	LEU
21	HIS	ASN	ARG	ARG	LEU	LEU	TRP	HIS	GLY	SER
22	ARG	THR	THR	ASN	PHE	ALA	GLY	ILE	LEU	SER
23	GLN	GLY	LEU	ARG	ILE	ALA	PRO	PRO	GLU	ALA
24	PRO	VAL	THR	GLY	TYR	MET	PHE	GLY	LYS	GLY
25	ILE	TYR	PHE	ALA	ASP	MET	VAL	SER	LYS	SER
26	ALA	ASN	TYR	CYS	HIS	THR	SER	GLN	GLY	ASP
27	PRO	ILE	GLY	LEU	ILE	LEU	LEU	GLY	GLU	VAL
28	ALA	LEU	GLY	ASN	MET	TYR	GLU	LEU	LYS	HIS
29	ALA	SER	HIS	ILE	SER	LYS	LEU	PRO	LYS	GLY
30	LYS	HIS	SER	VAL	LYS	GLY	LEU	GLY	LYS	THR
31	THR	PRO	ASP	PRO	SER	ALA	ASN	ILE	SER	LEU
32	ASP	GLY	VAL	ASP	VAL	PRO	LEU	GLY	THR	GLY
33	ILE	SER	SER	GLY	VAL	ASN	ASP	THR	SER	LEU
34	LEU	TYR	ASN	GLU	TYR	ILE	VAL	TYR	ASP	ILE
35	ALA	GLN	VAL	ASN	LEU	LYS	TYR	LEU	LEU	LYS
36	LEU	LYS	PHE	ASN	PHE	LYS	THR	SER	LEU	TRP

1	GLY	THR	VAL	ASN	PRO	GLY	THR	LYS	SER	LYS
2	LEU	PRO	LYS	PRO	VAL	GLN	ASP	LEU	ILE	LYS
3	MET	ILE	PHE	ASP	VAL	GLU	SER	MET	LYS	LYS
4	ALA	MET	VAL	GLU	TYR	GLU	ILE	ASP	LEU	GLN
5	LYS	MET	PRO	LEU	GLY	LYS	LEU	SER	LYS	ARG
6	GLN	ILE	GLN	ALA	ALA	TYR	SER	ILE	LEU	SER
7	GLU	VAL	GLN	GLN	ALA	VAL	SER	GLN	GLY	SER
8	SER	ASP	SER	GLN	ILE	LEU	ASP	LEU	SER	ASN
9	ARG	PHE	TYR	THR	LEU	ILE	PRO	HIS	ASP	PHE
10	GLY	MET	LYS	LYS	PRO	PRO	LEU	LEU	ASN	ASN
11	ALA	ASP	SER	VAL	GLN	ALA	LYS	ALA	GLU	MET
12	LEU	ASP	ASN	LEU	LEU	ASP	ILE	GLU	VAL	ALA
13	TYR	SER	LEU	LEU	ARG	GLY	GLY	SER	ASP	ASP
14	SER	SER	LYS	ASP	PRO	ILE	ASP	VAL	ASN	TYR
15	GLU	LYS	LEU	LYS	THR	ASP	ILE	LYS	VAL	VAL
16	ASP	ARG	ASP	SER	GLU	GLU	ALA	GLU	ILE	ILE
17	ARG	LYS	TYR	VAL	LYS	ASN	THR	HIS	ALA	THR
18	THR	HIS	ASN	ALA	TYR	ASP	LEU	GLU	VAL	ILE
19	ASP	ILE	PHE	LYS	ILE	GLU	ARG	GLU	GLY	GLU
20	CYS	GLN	ARG	TYR	LYS	PRO	PHE	LYS	GLN	LEU
21	HIS	ASN	ARG	ARG	LEU	LEU	TRP	HIS	GLY	SER
22	ARG	THR	THR	ASN	PHE	ALA	GLY	ILE	LEU	SER
23	GLN	GLY	LEU	ARG	ILE	ALA	PRO	PRO	GLU	ALA
24	PRO	VAL	THR	GLY	TYR	MET	PHE	GLY	LYS	GLY
25	ILE	TYR	PHE	ALA	ASP	MET	VAL	SER	LYS	SER
26	ALA	ASN	TYR	CYS	HIS	THR	SER	GLN	GLY	ASP
27	PRO	ILE	GLY	LEU	ILE	LEU	LEU	GLY	GLU	VAL
28	ALA	LEU	GLY	ASN	MET	TYR	GLU	LEU	LYS	HIS
29	ALA	SER	HIS	ILE	SER	LYS	LEU	PRO	LYS	GLY
30	LYS	HIS	SER	VAL	LYS	GLY	LEU	GLY	LYS	THR
31	THR	PRO	ASP	PRO	SER	ALA	ASN	ILE	SER	LEU
32	ASP	GLY	VAL	ASP	VAL	PRO	LEU	GLY	THR	GLY
33	ILE	SER	SER	GLY	VAL	ASN	ASP	THR	SER	LEU
34	LEU	TYR	ASN	GLU	TYR	ILE	VAL	TYR	ASP	ILE
35	ALA	GLN	VAL	ASN	LEU	LYS	TYR	LEU	LEU	LYS
36	LEU	LYS	PHE	ASN	PHE	LYS	THR	SER	LEU	TRP