BMRB Entry 17432

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17432
MolProbity Validation Chart

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Title:
Solution structure of murine myristoylated msrA
Deposition date:
2011-01-27
Original release date:
2012-01-09
Authors:
Gruschus, James; Lim, Jungchae; Piszczek, Grzegorz; Levine, Rodney; Tjandra, Nico
Citation:

Citation: Lim, Jung Chae; Gruschus, James; Ghesquiere, Bart; Kim, Geumsoo; Piszczek, Grzegorz; Tjandra, Nico; Levine, Rodney. "Characterization and solution structure of mouse myristoylated methionine sulfoxide reductase A."  J. Biol. Chem. 287, 25589-25595 (2012).
PubMed: 22661718

Assembly members:

Assembly members:
msrA, polymer, 212 residues, 23679.752 Da.
MYR, non-polymer, 228.371 Da.

Natural source:

Natural source:   Common Name: house 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: pET17b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
msrA: GDSASKVISAEEALPGRTEP IPVTAKHHVSGNRTVEPFPE GTQMAVFGMGCFWGAERKFW VLKGVYSTQVGFAGGHTRNP TYKEVCSEKTGHAEVVRVVY RPEHISFEELLKVFWENHDP TQGMRQGNDFGTQYRSAVYP TSAVQMEAALRSKEEYQKVL SKHNFGPITTDIREGQVFYY AEDYHQQYLSKNPDGYCGLG GTGVSCPMAIKK

Data sets:
Data typeCount
13C chemical shifts393
15N chemical shifts196
1H chemical shifts421

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1msrA1
2MYRISTIC ACID2

Entities:

Entity 1, msrA 212 residues - 23679.752 Da.

1   GLYASPSERALASERLYSVALILESERALA
2   GLUGLUALALEUPROGLYARGTHRGLUPRO
3   ILEPROVALTHRALALYSHISHISVALSER
4   GLYASNARGTHRVALGLUPROPHEPROGLU
5   GLYTHRGLNMETALAVALPHEGLYMETGLY
6   CYSPHETRPGLYALAGLUARGLYSPHETRP
7   VALLEULYSGLYVALTYRSERTHRGLNVAL
8   GLYPHEALAGLYGLYHISTHRARGASNPRO
9   THRTYRLYSGLUVALCYSSERGLULYSTHR
10   GLYHISALAGLUVALVALARGVALVALTYR
11   ARGPROGLUHISILESERPHEGLUGLULEU
12   LEULYSVALPHETRPGLUASNHISASPPRO
13   THRGLNGLYMETARGGLNGLYASNASPPHE
14   GLYTHRGLNTYRARGSERALAVALTYRPRO
15   THRSERALAVALGLNMETGLUALAALALEU
16   ARGSERLYSGLUGLUTYRGLNLYSVALLEU
17   SERLYSHISASNPHEGLYPROILETHRTHR
18   ASPILEARGGLUGLYGLNVALPHETYRTYR
19   ALAGLUASPTYRHISGLNGLNTYRLEUSER
20   LYSASNPROASPGLYTYRCYSGLYLEUGLY
21   GLYTHRGLYVALSERCYSPROMETALAILE
22   LYSLYS

Entity 2, MYRISTIC ACID - C14 H28 O2 - 228.371 Da.

1   MYR

Samples:

sample_1: msrA, [U-98% 13C; U-98% 15N], 0.3 ± 0.05 mM; DTT 5 ± .2 mM; TRIS 50 ± 1 mM; EDTA 5 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAB22035 BAB26522 BAC33889
GB AAH89311 EDL36048
REF NP_001240641 NP_001240645 NP_080598 XP_006518492 XP_011243223
SP Q9D6Y7
AlphaFold Q9D6Y7

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