BMRB Entry 16361

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16361
MolProbity Validation Chart

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Title:
NMR structure of the p62 PB1 domain
Deposition date:
2009-06-22
Original release date:
2009-06-26
Authors:
Yokochi, Masashi; Inagaki, Fuyuhiko
Citation:

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).
PubMed: 19728111

Assembly members:

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

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

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

Data sets:
Data typeCount
13C chemical shifts352
15N chemical shifts88
1H chemical shifts692

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1p62_PB11

Entities:

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

1   HISMETSERLEUTHRVALLYSALATYRLEU
2   LEUGLYLYSGLUGLUALAALAARGGLUILE
3   ARGARGPHESERPHECYSPHESERPROGLU
4   PROGLUALAGLUALAALAALAGLYPROGLY
5   PROCYSGLUARGLEULEUSERARGVALALA
6   VALLEUPHEPROALALEUARGPROGLYGLY
7   PHEGLNALAHISTYRARGALAGLUARGGLY
8   ASPLEUVALALAPHESERSERASPGLUGLU
9   LEUTHRMETALAMETSERTYRVALLYSASP
10   ASPILEPHEARGILETYRILELYSGLULYS

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCAHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_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

Related Database Links:

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

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