BMRB Entry 15193

Name: 1H, 13C, and 15N NMR resonance assignments of Sec95Cys MsrB1 protein
Published: 2007-08-22

Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15193

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

1H, 13C, and 15N NMR resonance assignments of Sec95Cys MsrB1 protein

Deposition date:

2007-03-21

Original release date:

2007-08-22

Authors:

Sal, Lena; Aachmann, Finn; Kim, Hwa-Young; Gladyshev, Vadim; Dikiy, Alexander

Citation:

Citation: Sal, Lena; Aachmann, Finn; Kim, Hwa-Young; Gladyshev, Vadim; Dikiy, Alexander. "NMR assignments of 1H, 13C and 15N spectra of methionine sulfoxide reductase B1 from Mus musculus" Biomol. NMR Assignments 1, 131-133 (2007).
PubMed: 19636847

Assembly members:

Assembly members:
MsrB1, polymer, 124 residues, 13806.5 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: pMR1-SECIS4

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MsrB1: MSFCSFFGGEVFQNHFEPGV YVCAKCSYELFSSHSKYAHS SPWPAFTETIHPDSVTKCPE KNRPEALKVSCGKCGNGLGH EFLNDGPKRGQSRFCIFSSS LKFVPKGKEAAASQGHLEHH HHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	436
15N chemical shifts	113
1H chemical shifts	694

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MsrB1	1

Entities:

Entity 1, MsrB1 124 residues - 13806.5 Da.

1

MET

SER

PHE

CYS

SER

PHE

GLY

GLU

2

VAL

PHE

GLN

ASN

HIS

PHE

GLU

PRO

GLY

VAL

3

TYR

VAL

CYS

ALA

LYS

CYS

SER

TYR

GLU

LEU

4

PHE

SER

HIS

SER

LYS

TYR

ALA

HIS

SER

5

SER

PRO

TRP

PRO

ALA

PHE

THR

GLU

THR

ILE

6

HIS

PRO

ASP

SER

VAL

THR

LYS

CYS

PRO

GLU

7

LYS

ASN

ARG

PRO

GLU

ALA

LEU

LYS

VAL

SER

8

CYS

GLY

LYS

CYS

GLY

ASN

GLY

LEU

GLY

HIS

9

GLU

PHE

LEU

ASN

ASP

GLY

PRO

LYS

ARG

GLY

10

GLN

SER

ARG

PHE

CYS

ILE

PHE

SER

11

LEU

LYS

PHE

VAL

PRO

LYS

GLY

LYS

GLU

ALA

12

ALA

SER

GLN

GLY

HIS

LEU

GLU

HIS

13

HIS

Samples:

H20: MsrB1, [U-98% 13C; U-99% 15N], 1.0 – 1.6 mM; sodium phosphate 20 ± 0.1 mM; DTT 5 ± 0.1 mM; sodium chloride 10 ± 0.1 mM

D2O: MsrB1, [U-98% 13C; U-99% 15N], 1.0 – 1.6 mM; sodium phosphate 20 ± 0.1 mM; DTT 5 ± 0.1 mM; sodium chloride 10 ± 0.1 mM

sample_conditions_1: ionic strength: 0.06 M; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	H20	isotropic	sample_conditions_1
2D 1H-13C HSQC	H20	isotropic	sample_conditions_1
3D HNCA	H20	isotropic	sample_conditions_1
3D HN(CO)CA	H20	isotropic	sample_conditions_1
3D HNCO	H20	isotropic	sample_conditions_1
3D HN(CA)CO	H20	isotropic	sample_conditions_1
3D HNCACB	H20	isotropic	sample_conditions_1
3D CBCA(CO)NH	H20	isotropic	sample_conditions_1
3D HBHA(CO)NH	H20	isotropic	sample_conditions_1
3D HBHANH	H20	isotropic	sample_conditions_1
3D HCCH-COSY	D2O	isotropic	sample_conditions_1
3D HCCH-TOCSY	D2O	isotropic	sample_conditions_1
3D 1H-15N NOESY	H20	isotropic	sample_conditions_1

Software:

xwinnmr v3.5, Bruker Biospin - collection, processing

CARA v1.4, Keller and Wuthrich - chemical shift assignment, data analysis

NMR spectrometers:

Bruker Avance 600 MHz

PDB	2KV1
DBJ	BAC55245 BAC55248 BAC55249 BAE43148
GB	AAF13697 AAH90646 AAI41147 EDL22365 EDL22366
REF	NP_038787
SP	Q9JLC3
AlphaFold	Q9JLC3