BMRB Entry 25467

Name: Backbone H, N and C assignments for PLAT domain of human polycystin-1, W3128A mutant
Published: 2016-06-30

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25467

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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: Backbone H, N and C assignments for PLAT domain of human polycystin-1, W3128A mutant PubMed: 25943267

Deposition date: 2015-02-05 Original release date: 2016-06-30

Authors: Williamson, Mike; Ong, Albert; Xu, Yaoxian; Hounslow, Andrea

Citation: Xu, Yaoxian; Ong, Albert; Williamson, Mike; Hounslow, Andrea. "Backbone assignment and secondary structure of the PLAT domain of human polycystin-1" Biomol. NMR Assign. 9, 369-373 (2015).

Assembly members:
PKD1_PLAT, polymer, 210 residues, Formula weight is not available

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: GEVS2

Entity Sequences (FASTA):
PKD1_PLAT: AAAAAAAAMQYKLALNGKTL KGETTTEAVDAATAEKVFKQ YANDNGVDGEWTYDDATKTF TVTELVPRGSCGQRGRFKYE ILVKTGAGRGSGTTAHVGIM LYGVDSRSGHRHLDGDRAFH RNSLDIFRIATPHSLGSVWK IRVWHDNKGLSPAWFLQHVI VRDLQTARSAFFLVNDWLSV ETEANGGLVEKEVLAASDAA LLRFHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	325
15N chemical shifts	109
1H chemical shifts	109

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PKD1_PLAT	1

Entities:

Entity 1, PKD1_PLAT 210 residues - Formula weight is not available

This has a polyalanine tag followed by the GB1 domain, a short linker, residues 3112-3245 of human PKD1 PLAT, and a His tag.

1	ALA	ALA	ALA	ALA	ALA	ALA	ALA	ALA	MET	GLN
2	TYR	LYS	LEU	ALA	LEU	ASN	GLY	LYS	THR	LEU
3	LYS	GLY	GLU	THR	THR	THR	GLU	ALA	VAL	ASP
4	ALA	ALA	THR	ALA	GLU	LYS	VAL	PHE	LYS	GLN
5	TYR	ALA	ASN	ASP	ASN	GLY	VAL	ASP	GLY	GLU
6	TRP	THR	TYR	ASP	ASP	ALA	THR	LYS	THR	PHE
7	THR	VAL	THR	GLU	LEU	VAL	PRO	ARG	GLY	SER
8	CYS	GLY	GLN	ARG	GLY	ARG	PHE	LYS	TYR	GLU
9	ILE	LEU	VAL	LYS	THR	GLY	ALA	GLY	ARG	GLY
10	SER	GLY	THR	THR	ALA	HIS	VAL	GLY	ILE	MET
11	LEU	TYR	GLY	VAL	ASP	SER	ARG	SER	GLY	HIS
12	ARG	HIS	LEU	ASP	GLY	ASP	ARG	ALA	PHE	HIS
13	ARG	ASN	SER	LEU	ASP	ILE	PHE	ARG	ILE	ALA
14	THR	PRO	HIS	SER	LEU	GLY	SER	VAL	TRP	LYS
15	ILE	ARG	VAL	TRP	HIS	ASP	ASN	LYS	GLY	LEU
16	SER	PRO	ALA	TRP	PHE	LEU	GLN	HIS	VAL	ILE
17	VAL	ARG	ASP	LEU	GLN	THR	ALA	ARG	SER	ALA
18	PHE	PHE	LEU	VAL	ASN	ASP	TRP	LEU	SER	VAL
19	GLU	THR	GLU	ALA	ASN	GLY	GLY	LEU	VAL	GLU
20	LYS	GLU	VAL	LEU	ALA	ALA	SER	ASP	ALA	ALA
21	LEU	LEU	ARG	PHE	HIS	HIS	HIS	HIS	HIS	HIS

Samples:

sample_1: GB1-PLAT, [U-13C; U-15N; U-2H], 200 uM; DTT 10 mM; sodium chloride 500 mM; TRIS 50 mM

sample_conditions_1: ionic strength: 550 mM; 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 HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

Felix, Accelrys Software Inc. - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 900 MHz
Bruker Avance 600 MHz

Uniprot	P98161
AlphaFold	Q15141

Biological Magnetic Resonance Data Bank