BMRB Entry 51379

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51379

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Title:
1H, 13C, and 15N resonance assignments of human glutathione peroxidase 4
Deposition date:
2022-03-22
Original release date:
2022-05-27
Authors:
Furuita, Kyoko; Inomata, Kouki; Sugiki, Toshihiko; Kobayashi, Naohiro; Fujiwara, Toshimichi; Kojima, Chojiro
Citation:

Citation: Furuita, Kyoko; Inomata, Kouki; Sugiki, Toshihiko; Kobayashi, Naohiro; Fujiwara, Toshimichi; Kojima, Chojiro. "1H, 13C, and 15N resonance assignments of human glutathione peroxidase 4"  Biomol. NMR Assignments 16, 267-271 (2022).
PubMed: 35616778

Assembly members:

Assembly members:
entity_1, polymer, 174 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pCold-GST

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPGHMSASRDDWRAARSMHE FSAKDIDGHMVNLDKYRGFV SIVTNVASQCGKTEVNYTQL VDLHARYAERGLRILAFPSN QFGKQEPGSNEEIKEFAAGY NVKFDMFSKIEVNGDDAHPL WKWMKIQPKGKGILGNAIKW NFTKFLIDKNGVVVKRYGPM EEPLVIEKDLPHYF

Data sets:
Data typeCount
13C chemical shifts757
15N chemical shifts171
1H chemical shifts1181

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Glutathione peroxidase 41

Entities:

Entity 1, Glutathione peroxidase 4 174 residues - Formula weight is not available

1   GLYPROGLYHISMETSERALASERARGASP
2   ASPTRPARGALAALAARGSERMETHISGLU
3   PHESERALALYSASPILEASPGLYHISMET
4   VALASNLEUASPLYSTYRARGGLYPHEVAL
5   SERILEVALTHRASNVALALASERGLNCYS
6   GLYLYSTHRGLUVALASNTYRTHRGLNLEU
7   VALASPLEUHISALAARGTYRALAGLUARG
8   GLYLEUARGILELEUALAPHEPROSERASN
9   GLNPHEGLYLYSGLNGLUPROGLYSERASN
10   GLUGLUILELYSGLUPHEALAALAGLYTYR
11   ASNVALLYSPHEASPMETPHESERLYSILE
12   GLUVALASNGLYASPASPALAHISPROLEU
13   TRPLYSTRPMETLYSILEGLNPROLYSGLY
14   LYSGLYILELEUGLYASNALAILELYSTRP
15   ASNPHETHRLYSPHELEUILEASPLYSASN
16   GLYVALVALVALLYSARGTYRGLYPROMET
17   GLUGLUPROLEUVALILEGLULYSASPLEU
18   PROHISTYRPHE

Samples:

sample_1: Glutathione peroxidase 4, [U-100% 13C; U-100% 15N], 0.4 mM; potassium phosphate 50 mM; potassium chloride 50 mM; DTT 1 mM; H2O 95%; D2O, [U-99% 2H], 5%

sample_2: Glutathione peroxidase 4, [U-100% 15N], 0.4 mM; potassium phosphate 50 mM; potassium chloride 50 mM; DTT 1 mM; H2O 95%; D2O, [U-99% 2H], 5%

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 15N-separated NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1

Software:

NMRPipe - processing

istHMS - processing

MAGRO - chemical shift assignment, data analysis, peak picking

CYANA v3.98.13 - chemical shift assignment

TOPSPIN - collection

NMRViewJ - data analysis

NMR spectrometers:

  • Bruker AVANCE III HD 800 MHz

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