BMRB Entry 16361

Name: NMR structure of the p62 PB1 domain
Published: 2009-06-26

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PDB ID: 2kkc
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16361
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: NMR structure of the p62 PB1 domain PubMed: 19728111

Deposition date: 2009-06-22 Original release date: 2009-06-26

Authors: Yokochi, Masashi; Inagaki, Fuyuhiko

Citation: Saio, Tomohide; Yokochi, Masashi; Inagaki, Fuyuhiko. "The NMR structure of the p62 PB1 domain, a key protein in autophagy and NF-kappaB signaling pathway." J. Biomol. NMR 45, 335-341 (2009).

Assembly members:
p62_PB1, polymer, 100 residues, Formula weight is not available

Natural source: Common Name: Norway Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus

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

Entity Sequences (FASTA):
p62_PB1: HMSLTVKAYLLGKEEAAREI RRFSFCFSPEPEAEAAAGPG PCERLLSRVAVLFPALRPGG FQAHYRAERGDLVAFSSDEE LTMAMSYVKDDIFRIYIKEK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	352
15N chemical shifts	88
1H chemical shifts	692

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	p62_PB1	1

Entities:

Entity 1, p62_PB1 100 residues - Formula weight is not available

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

Samples:

sample_1: p62 PB1, [U-99% 13C; U-99% 15N], 1 mM; H2O 90%; D2O 10%; MES 20 mM; sodium chloride 50 mM; DTT 10 mM

sample_conditions_1: ionic strength: 50 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
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D (H)CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCAHA	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

Software:

Olivia v1.15.2, Masashi Yokochi - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Varian Unity Inova 800 MHz
Varian Unity Inova 600 MHz

BMRB	16736
PDB	2KKC 2KTR
EMBL	CAA69642
GB	AAH61575 AAO15463 EDM04255 EDM04256 EDM04258
REF	NP_787037 NP_853528 XP_006246275 XP_006246276 XP_006246277
SP	O08623

Biological Magnetic Resonance Data Bank