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 27148

Title: Backbone and side chain chemical shift assignments of wild-type PACT-D3.   PubMed: 29045748

Deposition date: 2017-06-19 Original release date: 2019-04-15

Authors: Heyam, Alex

Citation: Heyam, Alex; Coupland, Claire; Degut, Clement; Haley, Ruth; Baxter, Nicola; Jakob, Leonhard; Aguiar, Pedro; Meister, Gunter; Williamson, Michael; Lagos, Dimitris; Plevin, Michael. "Conserved asymmetry underpins homodimerization of Dicer-associated double-stranded RNA-binding proteins."  Nucleic Acids Res. 45, 12577-12584 (2017).

Assembly members:
PACT-D3_wt, polymer, 79 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

Entity Sequences (FASTA):
PACT-D3_wt: GPAMTDYIQLLSEIAKEQGF NITYLDIDELSANGQYQCLA ELSTSPITVCHGSGISCGNA QSDAAHNALQYLKIIAERK

Data sets:
Data typeCount
13C chemical shifts584
15N chemical shifts155
1H chemical shifts893

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PACT-D3 state_A1
2PACT-D3 state_B1

Entities:

Entity 1, PACT-D3 state_A 79 residues - Formula weight is not available

The first four residues (GPAM) are non-native, and remain after cleavage of an affinity tag. This is followed by PACT residues 239-313.

1   GLYPROALAMETTHRASPTYRILEGLNLEU
2   LEUSERGLUILEALALYSGLUGLNGLYPHE
3   ASNILETHRTYRLEUASPILEASPGLULEU
4   SERALAASNGLYGLNTYRGLNCYSLEUALA
5   GLULEUSERTHRSERPROILETHRVALCYS
6   HISGLYSERGLYILESERCYSGLYASNALA
7   GLNSERASPALAALAHISASNALALEUGLN
8   TYRLEULYSILEILEALAGLUARGLYS

Samples:

backbone_assignment: PACT-D3_wt, [U-13C; U-15N], 1.3 mM; sodium chloride 50 mM; MES 20 mM; TCEP 10 mM; DSS 50 uM

sidechain_assignment: PACT-D3_wt, [U-13C; U-15N], 2.4 mM; sodium chloride 50 mM; MES 20 mM; TCEP 10 mM; DSS 50 uM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1H-15N SOFAST-HMQCbackbone_assignmentisotropicsample_conditions_1
HNCACBbackbone_assignmentisotropicsample_conditions_1
CBCACONHbackbone_assignmentisotropicsample_conditions_1
HNCOsidechain_assignmentisotropicsample_conditions_1
CC(CO)NH-TOCSYsidechain_assignmentisotropicsample_conditions_1
HCCH-TOCSYsidechain_assignmentisotropicsample_conditions_1
1H-13C HSQCsidechain_assignmentisotropicsample_conditions_1

Software:

TOPSPIN v3.0-3.5, Bruker Biospin - collection, processing

CcpNmr_Analysis v2.4, CCPN - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

UNP O75569

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