BMRB Entry 16213

Name: A Complete NMR Spectral Assignment of the MESD Protein
Published: 2010-06-28

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16213

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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:

A Complete NMR Spectral Assignment of the MESD Protein

Deposition date:

2009-03-12

Original release date:

2010-06-28

Authors:

Chen, Jianglei; Wang, Jianjun

Citation:

Citation: Chen, Jianglei; Li, Qianqian; Liu, Chia-Chen; Zhou, Bei; Bu, Guojun; Wang, Jianjun. "NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6." J. Biomol. NMR 47, 283-288 (2010).
PubMed: 20506034

Assembly members:

Assembly members:
MESD, polymer, 195 residues, 22037.7 Da.

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pTWIN1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MESD: ADTPGEATPPPRKKKDIRDY NDADMARLLEQWEKDDDIEE GDLPEHKRPSAPIDFSKLDP GKPESILKMTKKGKTLMMFV TVSGNPTEKETEEITSLWQG SLFNANYDVQRFIVGSDRAI FMLRDGSYAWEIKDFLVSQD RCAEVTLEGQMYPGKGGGSK EKNKTKPEKAKKKEGDPKPR ASKEDNRAGSRREDL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	599
15N chemical shifts	190
1H chemical shifts	1277

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MESD	1

Entities:

Entity 1, MESD 195 residues - 22037.7 Da.

1

ALA

ASP

THR

PRO

GLY

GLU

ALA

THR

PRO

2

PRO

ARG

LYS

ASP

ILE

ARG

ASP

TYR

3

ASN

ASP

ALA

ASP

MET

ALA

ARG

LEU

GLU

4

GLN

TRP

GLU

LYS

ASP

ILE

GLU

5

GLY

ASP

LEU

PRO

GLU

HIS

LYS

ARG

PRO

SER

6

ALA

PRO

ILE

ASP

PHE

SER

LYS

LEU

ASP

PRO

7

GLY

LYS

PRO

GLU

SER

ILE

LEU

LYS

MET

THR

8

LYS

GLY

LYS

THR

LEU

MET

PHE

VAL

9

THR

VAL

SER

GLY

ASN

PRO

THR

GLU

LYS

GLU

10

THR

GLU

ILE

THR

SER

LEU

TRP

GLN

GLY

11

SER

LEU

PHE

ASN

ALA

ASN

TYR

ASP

VAL

GLN

12

ARG

PHE

ILE

VAL

GLY

SER

ASP

ARG

ALA

ILE

13

PHE

MET

LEU

ARG

ASP

GLY

SER

TYR

ALA

TRP

14

GLU

ILE

LYS

ASP

PHE

LEU

VAL

SER

GLN

ASP

15

ARG

CYS

ALA

GLU

VAL

THR

LEU

GLU

GLY

GLN

16

MET

TYR

PRO

GLY

LYS

GLY

SER

LYS

17

GLU

LYS

ASN

LYS

THR

LYS

PRO

GLU

LYS

ALA

18

LYS

GLU

GLY

ASP

PRO

LYS

PRO

ARG

19

ALA

SER

LYS

GLU

ASP

ASN

ARG

ALA

GLY

SER

20

ARG

GLU

ASP

LEU

Samples:

sample_1: MESD, [U-13C; U-15N], 0.8 – 1.0 mM; sodium chloride 25 mM; EDTA 10 mM; DTT 10 mM; sodium azide 0.1 mM; sodium phosphate 25 mM

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
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 HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HCCTOCSY	sample_1	isotropic	sample_conditions_1
3D CCCTOCSY	sample_1	isotropic	sample_conditions_1
4D 13C/15N-edited NOESY	sample_1	isotropic	sample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

Varian INOVA 600 MHz

BMRB	11076
PDB	2KGL 2KMI 2RQK 2RQM
DBJ	BAB25865 BAC27617 BAC36471 BAC36476
GB	AAG33621 AAH14742 AAH85892 EDL06865 EDL06866
REF	NP_001008346 NP_075892
SP	Q5U2R7 Q9ERE7
AlphaFold	Q5U2R7 Q9ERE7