BMRB Entry 15193

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

Data sets:
Data typeCount
13C chemical shifts436
15N chemical shifts113
1H chemical shifts694

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1MsrB11

Entities:

Entity 1, MsrB1 124 residues - 13806.5 Da.

1   METSERPHECYSSERPHEPHEGLYGLYGLU
2   VALPHEGLNASNHISPHEGLUPROGLYVAL
3   TYRVALCYSALALYSCYSSERTYRGLULEU
4   PHESERSERHISSERLYSTYRALAHISSER
5   SERPROTRPPROALAPHETHRGLUTHRILE
6   HISPROASPSERVALTHRLYSCYSPROGLU
7   LYSASNARGPROGLUALALEULYSVALSER
8   CYSGLYLYSCYSGLYASNGLYLEUGLYHIS
9   GLUPHELEUASNASPGLYPROLYSARGGLY
10   GLNSERARGPHECYSILEPHESERSERSER
11   LEULYSPHEVALPROLYSGLYLYSGLUALA
12   ALAALASERGLNGLYHISLEUGLUHISHIS
13   HISHISHISHIS

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCH20isotropicsample_conditions_1
2D 1H-13C HSQCH20isotropicsample_conditions_1
3D HNCAH20isotropicsample_conditions_1
3D HN(CO)CAH20isotropicsample_conditions_1
3D HNCOH20isotropicsample_conditions_1
3D HN(CA)COH20isotropicsample_conditions_1
3D HNCACBH20isotropicsample_conditions_1
3D CBCA(CO)NHH20isotropicsample_conditions_1
3D HBHA(CO)NHH20isotropicsample_conditions_1
3D HBHANHH20isotropicsample_conditions_1
3D HCCH-COSYD2Oisotropicsample_conditions_1
3D HCCH-TOCSYD2Oisotropicsample_conditions_1
3D 1H-15N NOESYH20isotropicsample_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

Related Database Links:

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

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