BMRB Entry 18798

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18798

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Title:
Backbone assignments of the apo and Zn(II) protoporphyrin IX-bound states of the soluble form of rat heme oxygenase-1
Deposition date:
2012-10-22
Original release date:
2015-05-07
Authors:
Harada, Erisa; Sugishima, Masakazu; Harada, Jiro; Noguchi, Masato; Fukuyama, Keiichi; Sugase, Kenji
Citation:

Citation: Harada, Erisa; Sugishima, Masakazu; Harada, Jiro; Noguchi, Masato; Fukuyama, Keiichi; Sugase, Kenji. "Backbone assignments of the apo and Zn(II) protoporphyrin IX-bound states of the soluble form of rat heme oxygenase-1"  Biomol. NMR Assign. 9, 197-200 (2015).
PubMed: 25209143

Assembly members:

Assembly members:
., polymer, 232 residues, 26800 Da.

Natural source:

Natural source:   Common Name: Rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
.: MERPQLDSMSQDLSEALKEA TKEVHIRAENSEFMRNFQKG QVSREGFKLVMASLYHIYTA LEEEIERNKQNPVYAPLYFP EELHRRAALEQDMAFWYGPH WQEAIPYTPATQHYVKRLHE VGGTHPELLVAHAYTRYLGD LSGGQVLKKIAQKAMALPSS GEGLAFFTFPSIDNPTKFKQ LYRARMNTLEMTPEVKHRVT EEAKTAFLLNIELFEELQAL LTEEHKDQSPSQ

Data sets:
Data typeCount
13C chemical shifts672
15N chemical shifts218
1H chemical shifts218

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HO-1_WT1

Entities:

Entity 1, HO-1_WT 232 residues - 26800 Da.

1   METGLUARGPROGLNLEUASPSERMETSER
2   GLNASPLEUSERGLUALALEULYSGLUALA
3   THRLYSGLUVALHISILEARGALAGLUASN
4   SERGLUPHEMETARGASNPHEGLNLYSGLY
5   GLNVALSERARGGLUGLYPHELYSLEUVAL
6   METALASERLEUTYRHISILETYRTHRALA
7   LEUGLUGLUGLUILEGLUARGASNLYSGLN
8   ASNPROVALTYRALAPROLEUTYRPHEPRO
9   GLUGLULEUHISARGARGALAALALEUGLU
10   GLNASPMETALAPHETRPTYRGLYPROHIS
11   TRPGLNGLUALAILEPROTYRTHRPROALA
12   THRGLNHISTYRVALLYSARGLEUHISGLU
13   VALGLYGLYTHRHISPROGLULEULEUVAL
14   ALAHISALATYRTHRARGTYRLEUGLYASP
15   LEUSERGLYGLYGLNVALLEULYSLYSILE
16   ALAGLNLYSALAMETALALEUPROSERSER
17   GLYGLUGLYLEUALAPHEPHETHRPHEPRO
18   SERILEASPASNPROTHRLYSPHELYSGLN
19   LEUTYRARGALAARGMETASNTHRLEUGLU
20   METTHRPROGLUVALLYSHISARGVALTHR
21   GLUGLUALALYSTHRALAPHELEULEUASN
22   ILEGLULEUPHEGLUGLULEUGLNALALEU
23   LEUTHRGLUGLUHISLYSASPGLNSERPRO
24   SERGLN

Samples:

sample_1: heme oxygenase 1, [U-100% 13C; U-100% 15N; U-80% 2H], 0.4 mM; potassium phosphate 50 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis, processing

NMRView, Johnson, One Moon Scientific - data analysis

Kujira, RIKEN, Naohiro Kobayashi - automated peak assignment, chemical shift assignment

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker DMX 750 MHz

Related Database Links:

PDB
BMRB 18799 18800
GB AAA41346 AAH91164 ADD84876 EDL87376
REF NP_036712
SP P06762
AlphaFold P06762

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