BMRB Entry 51491

Name: MEC-2 C-terminal disordered region (residues 372-481)
Published: 2023-07-13

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51491

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:

MEC-2 C-terminal disordered region (residues 372-481)

Deposition date:

2022-06-14

Original release date:

2023-07-13

Authors:

Mateos, Borja; Sanfeliu-Cerdan, Neus; Salvatella, Xavier; Krieg, Michael

Citation:

Citation: Sanfeliu-Cerdan, Neus; Mateos, Borja; Garcia-Cabau, Carla; Catala-Castro, Frederic; Ribera, Maria; Porta-de-la-Riva, Montserrat; Wieser, Stefan; Salvatella, Xavier; Krieg, Michael. "A viscoelastic switch of Stomatin condensatesgoverns transport and mechanotransduction" Nat. Cell Biol. ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 111 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: PPKVEEPPSLPKKIRSCCLY KYPDWVQGMVGSEGGGGHGH SHGGGGGGLGSSQGAFHPSQ AGSGPSTTTTSGRPLLRSMR EAQFHSAAPPISAPNQSQTS VSQLDPALLIR

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	201
15N chemical shifts	76
1H chemical shifts	75

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MEC-2 C-terminal domain	1

Entities:

Entity 1, MEC-2 C-terminal domain 111 residues - Formula weight is not available

1

PRO

LYS

VAL

GLU

PRO

SER

LEU

2

PRO

LYS

ILE

ARG

SER

CYS

LEU

TYR

3

LYS

TYR

PRO

ASP

TRP

VAL

GLN

GLY

MET

VAL

4

GLY

SER

GLU

GLY

HIS

GLY

HIS

5

SER

HIS

GLY

LEU

GLY

6

SER

GLN

GLY

ALA

PHE

HIS

PRO

SER

GLN

7

ALA

GLY

SER

GLY

PRO

SER

THR

8

SER

GLY

ARG

PRO

LEU

ARG

SER

MET

ARG

9

GLU

ALA

GLN

PHE

HIS

SER

ALA

PRO

10

ILE

SER

ALA

PRO

ASN

GLN

SER

GLN

THR

SER

11

VAL

SER

GLN

LEU

ASP

PRO

ALA

LEU

ILE

12

ARG

Samples:

sample_1: MEC-2 C-terminal domain, [U-99% 13C; U-99% 15N], 0.4 mM; D2O, [U-2H], 10%; DSS 10 uM; TCEP 1 mM

sample_conditions_1: ionic strength: 0 M; pH: 7.4; pressure: 1 atm; temperature: 278 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe - processing

TOPSPIN - collection

MddNMR - processing

CcpNMR - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 600 MHz

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