BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 26793

Title: Backbone assignment of p24 GOLD domain   PubMed: 27569046

Deposition date: 2016-05-10 Original release date: 2016-10-14

Authors: Yamaguchi, Yoshiki; Nagae, Masamichi

Citation: Nagae, Masamichi; Hirata, Tetsuya; Morita-Matsumoto, Kana; Theiler, Romina; Fujita, Morihisa; Kinoshita, Taroh; Yamaguchi, Yoshiki. "3D structure and interaction of p24beta and p24delta Golgi dynamics domains: implications for p24 complex formation and cargo transport"  J. Mol. Biol. 428, 4087-4099 (2016).

Assembly members:
p24, polymer, 101 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   Vector: pCold

Entity Sequences (FASTA):
p24: GSSGYFVSIDAHAEECFFER VTSGTKMGLIFEVAEGGFLD IDVEITGPDNKGIYKGDRES SGKYTFAAHMDGTYKFCFSN RMSTMTPKIVMFTIDIGEAP K

Data sets:
Data typeCount
13C chemical shifts85
15N chemical shifts48
1H chemical shifts48

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1GOLD domain1

Entities:

Entity 1, GOLD domain 101 residues - Formula weight is not available

1   GLYSERSERGLYTYRPHEVALSERILEASP
2   ALAHISALAGLUGLUCYSPHEPHEGLUARG
3   VALTHRSERGLYTHRLYSMETGLYLEUILE
4   PHEGLUVALALAGLUGLYGLYPHELEUASP
5   ILEASPVALGLUILETHRGLYPROASPASN
6   LYSGLYILETYRLYSGLYASPARGGLUSER
7   SERGLYLYSTYRTHRPHEALAALAHISMET
8   ASPGLYTHRTYRLYSPHECYSPHESERASN
9   ARGMETSERTHRMETTHRPROLYSILEVAL
10   METPHETHRILEASPILEGLYGLUALAPRO
11   LYS

Samples:

sample_1: p24, [U-99% 13C; U-99% 15N], 0.5 mM; H2O 90%; D2O 10%; sodium phosphate 20 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 600 MHz

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