BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 19005

Title: 1H, 13C, and 15N backbone chemical shift assignments of the low-spin CN-bound yeast cytochrome c peroxidase with the N-terminal His-tag   PubMed: 23517193

Authors: Volkov, Alexander; van Nuland, Nico

Citation: Volkov, Alexander; Wohlkonig, Alexandre; Soror, Sameh; van Nuland, Nico. "Expression, Purification, Characterization, and Solution Nuclear Magnetic Resonance Study of Highly Deuterated Yeast Cytochrome c Peroxidase with Enhanced Solubility"  Biochemistry 52, 2165-2175 (2013).

Assembly members:
cytochrome_c_peroxidase, polymer, 300 residues, Formula weight is not available
PROTOPORPHYRIN IX CONTAINING FE, non-polymer, 616.487 Da.
CYANIDE ION, non-polymer, 26.017 Da.

Natural source:   Common Name: baker   Taxonomy ID: 4932   Superkingdom: not available   Kingdom: not available   Genus/species: Eukaryota Fungi

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

Entity Sequences (FASTA):
cytochrome_c_peroxidase: MHHHHHHKTLVHVASVEKGR SYEDFQKVYNAIALKLREDD EYDNYIGYGPVLVRLAWHTS GTWDKHDNTGGSYGGTYRFK KEFNDPSNAGLQNGFKFLEP IHKEFPWISSGDLFSLGGVT AVQEMQGPKIPWRCGRVDTP EDTTPDNGRLPDADKDADYV RTFFQRLNMNDREVVALMGA HALGKTHLKNSGYEGPWGAA NNVFTNEFYLNLLNEDWKLE KNDANNEQWDSKSGYMMLPT DYSLIQDPKYLSIVKEYAND QDKFFKDFSKAFEKLLENGI TFPKDAPSPFIFKTLEEQGL

Data sets:
Data typeCount
1H chemical shifts261
13C chemical shifts789
15N chemical shifts261

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1protein1
2cofactor_HEM2
3cofactor_CYN3

Entities:

Entity 1, protein 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_HEM - C34 H32 Fe N4 O4 - 616.487 Da.

1   HEM

Entity 3, cofactor_CYN - C N - 26.017 Da.

1   CYN

Samples:

sample_1: cytochrome c peroxidase, [U-13C; U-15N; U-2H], 1.25 – 1.5 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

Software:

VNMRJ, Varian - collection

CCPN, CCPN - chemical shift assignment, data analysis, peak picking

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

NMR spectrometers:

  • Varian Uniform NMR System 800 MHz

Related Database Links:

BMRB 1839 19004 19075 19076 19884 25551
PDB
DBJ GAA24787
EMBL CAA44288 CAA82145 CAY81144
GB AAA88709 AAS56247 AHY76301 AJP40095 AJS30293
REF NP_012992
SP P00431
TPG DAA09217