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 27180

Title: Coheson Domain 5 from Clostridium themocellum   PubMed: 29486159

Deposition date: 2017-07-14 Original release date: 2018-03-28

Authors: Galera-Prat, Albert; ., Laurents; ., .; ., .

Citation: Galera-Prat, Albert; D., Pantoja-Uceda; V., D.; ., .. "Solution conformation of a cohesin module and its scaffoldin linker from a prototypical cellulosome"  Arch. Biochem. Biophys. 644, 1-7 (2018).

Assembly members:
Cohesin Domain 5, polymer, 145 residues, Formula weight is not available

Natural source:   Common Name: not available   Taxonomy ID: 1515   Superkingdom: not available   Kingdom: Clostridium   Genus/species: thermocellum not available

Experimental source:   Production method: recombinant technology' 'Escherichia coli

Entity Sequences (FASTA):
Cohesin Domain 5: GGAVRIKVDTVNAKPGDTVR IPVRFSGIPSKGIANCDFVY SYDPNVLEIIEIEPGDIIVD PNPDKSFDTAVYPDRKIIVF LFAEDSGTGAYAITKDGVFA TIVAKVKSGAPNGLSVIKFV EVGGFANNDLVEQKTQFFDG GVNVGGDTTEPATPTTPVTT PTTTDDLDA

Data sets:
Data typeCount
13C chemical shifts480
1501H chemical shifts

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Cohesin Domain 51

Entities:

Entity 1, Cohesin Domain 5 145 residues - Formula weight is not available

1   GLY.2718056LYS.271801112
2   ALA.271801718VAL.271802324
3   PHE.271802930LYS.271803536
4   ASP.271804142ASP.271804748
5   ILE.271805354GLY.271805960
6   PRO.271806566PHE.271807172
7   PRO.271807778VAL.271808384
8   ASP.271808990TYR.271809596
9   GLY.27180101102VAL.27180107108
10   GLY.27180113114SER.27180119120
11   GLU.27180125126ASN.27180131132
12   GLN.27180137138ASP.27180143144
13   GLY.27180149150PRO.27180155156
14   PRO.27180161162THR.27180167168
15   ALA

Samples:

sample_1: Cohesin Domain 5' '[U-100% 13C; U-100% 15N] 0.04; .; . mM; . 27180

sample_2: linker peptide' '[U-100% 13C; U-100% 15N]; .; . mM; . 27180

sample_conditions_1: ionic strength: 0.02 M; 6.02: 0.02 27180; .: atm temperature; K: 27180

sample_conditions_2: ionic strength: 0.02 M; 6.02: 0.02 27180; .: atm temperature; K: 27180

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
nosotropicnot availablenot available
not availablenot availablenot availablenot available
not availablenot available1not available
not availablenot available$sample_conditions_1not available
not availablesample_conditions_1not availablespectrometer_1
not availablenot availablenot availablenot available
not availablenot availablenot availablenot available
not availablenot available2not available
not availablenot available$spectrometer_2not available

Software:

TOPSPIN v2.1, Bruker Biospin - collection

SPARKY v3.13, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

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