BMRB Entry 25282

Name: Backbone assignment of native and 8M urea-denatured MJ0366
Published: 2015-09-04

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25282

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

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Title:

Backbone assignment of native and 8M urea-denatured MJ0366

Deposition date:

2014-10-12

Original release date:

2015-09-04

Authors:

Wang, Iren; Chen, Szu-Yu; Hsu, Shang-Te

Citation:

Citation: Wang, Iren; Chen, Szu-Yu; Hsu, Shang-Te. "Unraveling the folding mechanism of the smallest knotted protein, MJ0366" J. Phys. Chem. B. 119, 4359-4370 (2015).
PubMed: 25741995

Assembly members:

Assembly members:
MJ0366, polymer, 92 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Euryarchaeotes Taxonomy ID: 2190 Superkingdom: Archaea Kingdom: not available Genus/species: Methanococcus jannaschii

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pETz2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MJ0366: MPLVGFMKEKKRATFYLYKN IDGRKLRYLLHKLENVENVD IDTLRRAIEAEKKYKRSITL TEEEEVIIQRLGKSANLLLN CELVKLDEGERA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_2

Data type	Count
13C chemical shifts	533
15N chemical shifts	179
1H chemical shifts	270

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MJ0366	1

Entities:

Entity 1, MJ0366 92 residues - Formula weight is not available

1

MET

PRO

LEU

VAL

GLY

PHE

MET

LYS

GLU

LYS

2

LYS

ARG

ALA

THR

PHE

TYR

LEU

TYR

LYS

ASN

3

ILE

ASP

GLY

ARG

LYS

LEU

ARG

TYR

LEU

4

HIS

LYS

LEU

GLU

ASN

VAL

GLU

ASN

VAL

ASP

5

ILE

ASP

THR

LEU

ARG

ALA

ILE

GLU

ALA

6

GLU

LYS

TYR

LYS

ARG

SER

ILE

THR

LEU

7

THR

GLU

VAL

ILE

GLN

ARG

8

LEU

GLY

LYS

SER

ALA

ASN

LEU

ASN

9

CYS

GLU

LEU

VAL

LYS

LEU

ASP

GLU

GLY

GLU

10

ARG

ALA

Samples:

sample_1: MJ0366, [U-99% 13C; U-99% 15N], 0.55 mM; potassium phosphate 50 mM; sodium chloride 50 mM; H2O 90%; D2O 10%

sample_2: MJ0366, [U-99% 13C; U-99% 15N], 0.5 mM; potassium phosphate 50 mM; sodium chloride 50 mM; urea 8 M; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 6; pressure: 1 atm; temperature: 310 K

sample_conditions_2: pH: 6; temperature: 298 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 HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_2
3D HNCO	sample_2	isotropic	sample_conditions_2
3D HNCA	sample_2	isotropic	sample_conditions_2
3D HN(CO)CA	sample_2	isotropic	sample_conditions_2
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_2

Software:

TOPSPIN, Bruker Biospin - collection

SPARKY, Goddard - data analysis, peak picking

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Bruker Avance 600 MHz

PDB	2EFV
GB	AAB98357
SP	Q57812
AlphaFold	Q57812