BMRB Entry 27180

Name: Coheson Domain 5 from Clostridium themocellum
Published: 2018-03-28

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27180

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

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

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

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	480
15N chemical shifts	150
1H chemical shifts	186

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Cohesin Domain 5	1

Entities:

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

1

GLY

ALA

VAL

ARG

ILE

LYS

VAL

ASP

THR

2

VAL

ASN

ALA

LYS

PRO

GLY

ASP

THR

VAL

ARG

3

ILE

PRO

VAL

ARG

PHE

SER

GLY

ILE

PRO

SER

4

LYS

GLY

ILE

ALA

ASN

CYS

ASP

PHE

VAL

TYR

5

SER

TYR

ASP

PRO

ASN

VAL

LEU

GLU

ILE

6

GLU

ILE

GLU

PRO

GLY

ASP

ILE

VAL

ASP

7

PRO

ASN

PRO

ASP

LYS

SER

PHE

ASP

THR

ALA

8

VAL

TYR

PRO

ASP

ARG

LYS

ILE

VAL

PHE

9

LEU

PHE

ALA

GLU

ASP

SER

GLY

THR

GLY

ALA

10

TYR

ALA

ILE

THR

LYS

ASP

GLY

VAL

PHE

ALA

11

THR

ILE

VAL

ALA

LYS

VAL

LYS

SER

GLY

ALA

12

PRO

ASN

GLY

LEU

SER

VAL

ILE

LYS

PHE

VAL

13

GLU

VAL

GLY

PHE

ALA

ASN

ASP

LEU

14

VAL

GLU

GLN

LYS

THR

GLN

PHE

ASP

GLY

15

GLY

VAL

ASN

VAL

GLY

ASP

THR

GLU

16

PRO

ALA

THR

PRO

THR

PRO

VAL

THR

17

PRO

THR

ASP

LEU

ASP

ALA

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:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
2D TOCSY	sample_2	isotropic	sample_conditions_2
2D NOESY	sample_2	isotropic	sample_conditions_2
2D 1H-13C HSQC	sample_2	isotropic	sample_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