BMRB Entry 27180

Title:
Coheson Domain 5 from Clostridium themocellum
Deposition date:
2017-07-14
Original release date:
2018-03-28
Authors:
Galera-Prat, Albert; Laurents, Douglas; Carri n-V zquez, Mariano; Pantoja-Uceda, David
Citation:

Citation: Galera-Prat, Albert; Pantoja-Uceda, David; Laurents, Douglas; Carrion Vazquez, Mariano. "Solution conformation of a cohesin module and its scaffoldin linker from a prototypical cellulosome"  Arch. Biochem. Biophys. 644, 1-7 (2018).
PubMed: 29486159

Assembly members:

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

Natural source:

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

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts480
15N chemical shifts150
1H chemical shifts186

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   GLYGLYALAVALARGILELYSVALASPTHR
2   VALASNALALYSPROGLYASPTHRVALARG
3   ILEPROVALARGPHESERGLYILEPROSER
4   LYSGLYILEALAASNCYSASPPHEVALTYR
5   SERTYRASPPROASNVALLEUGLUILEILE
6   GLUILEGLUPROGLYASPILEILEVALASP
7   PROASNPROASPLYSSERPHEASPTHRALA
8   VALTYRPROASPARGLYSILEILEVALPHE
9   LEUPHEALAGLUASPSERGLYTHRGLYALA
10   TYRALAILETHRLYSASPGLYVALPHEALA
11   THRILEVALALALYSVALLYSSERGLYALA
12   PROASNGLYLEUSERVALILELYSPHEVAL
13   GLUVALGLYGLYPHEALAASNASNASPLEU
14   VALGLUGLNLYSTHRGLNPHEPHEASPGLY
15   GLYVALASNVALGLYGLYASPTHRTHRGLU
16   PROALATHRPROTHRTHRPROVALTHRTHR
17   PROTHRTHRTHRASPASPLEUASPALA

Samples:

sample_1: Cohesin Domain 5, [U-100% 13C; U-100% 15N], 1.26 ± 0.04 mM; KH2PO5 8.5 mM; KH2PO4 1.5 mM; sodium azide 0.7 mM

sample_2: linker peptide, [U-100% 13C; U-100% 15N], 2 mM; KH2PO5 8.5 mM; KH2PO4 1.5 mM; sodium azide 0.7 mM

sample_conditions_1: ionic strength: 0.02 M; pH: 6.02; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.02 M; pH: 6.02; pressure: 1 atm; temperature: 278 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D TOCSYsample_2isotropicsample_conditions_2
2D NOESYsample_2isotropicsample_conditions_2
2D 1H-13C HSQCsample_2isotropicsample_conditions_2

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