BMRB Entry 19076

Title:
1H, 13C, and 15N backbone chemical shift assignments of the resting-state yeast cytochrome c peroxidase with the N-terminal His-tag
Deposition date:
2013-03-06
Original release date:
2013-09-10
Authors:
Volkov, Alexander; van Nuland, Nico; Vanwetswinkel, Sophie
Citation:

Citation: Vanwetswinkel, Sophie; van Nuland, Nico; Volkov, Alexander. "Paramagnetic properties of the low- and high-spin states of yeast cytochrome c peroxidase."  J. Biomol. NMR 57, 21-26 (2013).
PubMed: 23832496

Assembly members:

Assembly members:
cytochrome_c_peroxidase, polymer, 300 residues, Formula weight is not available
HEME B/C, non-polymer, 618.503 Da.

Natural source:

Natural source:   Common Name: baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET24a(+)

Data sets:
Data typeCount
13C chemical shifts515
1H chemical shifts195
15N chemical shifts195

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CcP1
2cofactor2

Entities:

Entity 1, CcP 300 residues - Formula weight is not available

N-terminal His tag

1   METHISHISHISHISHISHISLYSTHRLEU
2   VALHISVALALASERVALGLULYSGLYARG
3   SERTYRGLUASPPHEGLNLYSVALTYRASN
4   ALAILEALALEULYSLEUARGGLUASPASP
5   GLUTYRASPASNTYRILEGLYTYRGLYPRO
6   VALLEUVALARGLEUALATRPHISTHRSER
7   GLYTHRTRPASPLYSHISASPASNTHRGLY
8   GLYSERTYRGLYGLYTHRTYRARGPHELYS
9   LYSGLUPHEASNASPPROSERASNALAGLY
10   LEUGLNASNGLYPHELYSPHELEUGLUPRO
11   ILEHISLYSGLUPHEPROTRPILESERSER
12   GLYASPLEUPHESERLEUGLYGLYVALTHR
13   ALAVALGLNGLUMETGLNGLYPROLYSILE
14   PROTRPARGCYSGLYARGVALASPTHRPRO
15   GLUASPTHRTHRPROASPASNGLYARGLEU
16   PROASPALAASPLYSASPALAASPTYRVAL
17   ARGTHRPHEPHEGLNARGLEUASNMETASN
18   ASPARGGLUVALVALALALEUMETGLYALA
19   HISALALEUGLYLYSTHRHISLEULYSASN
20   SERGLYTYRGLUGLYPROTRPGLYALAALA
21   ASNASNVALPHETHRASNGLUPHETYRLEU
22   ASNLEULEUASNGLUASPTRPLYSLEUGLU
23   LYSASNASPALAASNASNGLUGLNTRPASP
24   SERLYSSERGLYTYRMETMETLEUPROTHR
25   ASPTYRSERLEUILEGLNASPPROLYSTYR
26   LEUSERILEVALLYSGLUTYRALAASNASP
27   GLNASPLYSPHEPHELYSASPPHESERLYS
28   ALAPHEGLULYSLEULEUGLUASNGLYILE
29   THRPHEPROLYSASPALAPROSERPROPHE
30   ILEPHELYSTHRLEUGLUGLUGLNGLYLEU

Entity 2, cofactor - 618.503 Da.

1   HEB

Samples:

sample_1: cytochrome c peroxidase, [U-13C; U-15N; U-2H], 1.25 mM; sodium phosphate 20 mM; sodium chloride 100 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 115 mM; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)CBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

No software information available

NMR spectrometers:

  • Varian Uniform NMR System 800 MHz

Related Database Links:

BMRB 1839 19004 19005 19075 19884 25551
PDB
DBJ GAA24787
EMBL CAA44288 CAA82145 CAY81144
GB AAA88709 AAS56247 AHY76301 AJP40095 AJS30293
REF NP_012992
SP P00431
TPG DAA09217
AlphaFold P00431

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