BMRB Entry 16736

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16736

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
NMR STRUCTURE OF P62 PB1 DIMER DETERMINED BASED ON PCS
Deposition date:
2010-02-19
Original release date:
2010-05-03
Authors:
Saio, Tomohide; Yokochi, Masashi; Kumeta, Hiroyuki; Inagaki, Fuyuhiko
Citation:

Citation: Saio, Tomohide; Yokochi, Masashi; Kumeta, Hiroyuki; Inagaki, Fuyuhiko. "PCS-based structure determination of protein-protein complexes."  J. Biomol. NMR 46, 271-280 (2010).
PubMed: 20300805

Assembly members:

Assembly members:
entity_1, polymer, 117 residues, 11119.817 Da.
entity_2, polymer, 100 residues, 11019.478 Da.
TB, non-polymer, 158.925 Da.

Natural source:

Natural source:   Common Name: 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: pET21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: CYVDTNNDGAYEGDELHMGS LTVKAYLLGKEEAAREIRRF SFCFSPEPEAEAAAGPGPSE RLLSRVAVLFPALRPGGFQA HYRAERGDLVAFSSDEELTM AMSYVKDDIFRIYIKEK
entity_2: HMSLTVEAYLLGKEEAAREI RRFSFSFSPEPEAEAAAGPG PSERLLSRVAVLFPALRPGG FQAHYRDEDGDLVAFSSDEE LTMAMSYVKDDIFAIYIKEK

Data sets:
Data typeCount
15N chemical shifts192
1H chemical shifts192

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22
3TERBIUM(III) ION3

Entities:

Entity 1, entity_1 117 residues - 11119.817 Da.

1   CYSTYRVALASPTHRASNASNASPGLYALA
2   TYRGLUGLYASPGLULEUHISMETGLYSER
3   LEUTHRVALLYSALATYRLEULEUGLYLYS
4   GLUGLUALAALAARGGLUILEARGARGPHE
5   SERPHECYSPHESERPROGLUPROGLUALA
6   GLUALAALAALAGLYPROGLYPROSERGLU
7   ARGLEULEUSERARGVALALAVALLEUPHE
8   PROALALEUARGPROGLYGLYPHEGLNALA
9   HISTYRARGALAGLUARGGLYASPLEUVAL
10   ALAPHESERSERASPGLUGLULEUTHRMET
11   ALAMETSERTYRVALLYSASPASPILEPHE
12   ARGILETYRILELYSGLULYS

Entity 2, entity_2 100 residues - 11019.478 Da.

1   HISMETSERLEUTHRVALGLUALATYRLEU
2   LEUGLYLYSGLUGLUALAALAARGGLUILE
3   ARGARGPHESERPHESERPHESERPROGLU
4   PROGLUALAGLUALAALAALAGLYPROGLY
5   PROSERGLUARGLEULEUSERARGVALALA
6   VALLEUPHEPROALALEUARGPROGLYGLY
7   PHEGLNALAHISTYRARGASPGLUASPGLY
8   ASPLEUVALALAPHESERSERASPGLUGLU
9   LEUTHRMETALAMETSERTYRVALLYSASP
10   ASPILEPHEALAILETYRILELYSGLULYS

Entity 3, TERBIUM(III) ION - Tb - 158.925 Da.

1   TB

Samples:

sample_1: entity_1, [U-99% 13C; U-99% 15N], 0.5 mM; entity_2 0.5 mM; MES 20 mM; sodium chloride 50 mM; TERBIUM(III) ION 0.5 mM

sample_2: entity_1 0.5 mM; entity_2, [U-99% 13C; U-99% 15N], 0.5 mM; MES 20 mM; sodium chloride 50 mM; TERBIUM(III) ION 0.5 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1

Software:

Olivia, Masashi Yokochi - chemical shift assignment, data analysis

X-PLOR NIH v2.9.20, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

BMRB 16361
PDB

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