BMRB Entry 19005
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19005
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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
Deposition date: 2013-02-05 Original release date: 2013-04-02
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
- assigned_chemical_shifts
Data type | Count |
1H chemical shifts | 261 |
13C chemical shifts | 789 |
15N chemical shifts | 261 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | protein | 1 |
2 | cofactor_HEM | 2 |
3 | cofactor_CYN | 3 |
Entities:
Entity 1, protein 300 residues - Formula weight is not available
N-terminal His tag
1 | MET | HIS | HIS | HIS | HIS | HIS | HIS | LYS | THR | LEU | |
2 | VAL | HIS | VAL | ALA | SER | VAL | GLU | LYS | GLY | ARG | |
3 | SER | TYR | GLU | ASP | PHE | GLN | LYS | VAL | TYR | ASN | |
4 | ALA | ILE | ALA | LEU | LYS | LEU | ARG | GLU | ASP | ASP | |
5 | GLU | TYR | ASP | ASN | TYR | ILE | GLY | TYR | GLY | PRO | |
6 | VAL | LEU | VAL | ARG | LEU | ALA | TRP | HIS | THR | SER | |
7 | GLY | THR | TRP | ASP | LYS | HIS | ASP | ASN | THR | GLY | |
8 | GLY | SER | TYR | GLY | GLY | THR | TYR | ARG | PHE | LYS | |
9 | LYS | GLU | PHE | ASN | ASP | PRO | SER | ASN | ALA | GLY | |
10 | LEU | GLN | ASN | GLY | PHE | LYS | PHE | LEU | GLU | PRO | |
11 | ILE | HIS | LYS | GLU | PHE | PRO | TRP | ILE | SER | SER | |
12 | GLY | ASP | LEU | PHE | SER | LEU | GLY | GLY | VAL | THR | |
13 | ALA | VAL | GLN | GLU | MET | GLN | GLY | PRO | LYS | ILE | |
14 | PRO | TRP | ARG | CYS | GLY | ARG | VAL | ASP | THR | PRO | |
15 | GLU | ASP | THR | THR | PRO | ASP | ASN | GLY | ARG | LEU | |
16 | PRO | ASP | ALA | ASP | LYS | ASP | ALA | ASP | TYR | VAL | |
17 | ARG | THR | PHE | PHE | GLN | ARG | LEU | ASN | MET | ASN | |
18 | ASP | ARG | GLU | VAL | VAL | ALA | LEU | MET | GLY | ALA | |
19 | HIS | ALA | LEU | GLY | LYS | THR | HIS | LEU | LYS | ASN | |
20 | SER | GLY | TYR | GLU | GLY | PRO | TRP | GLY | ALA | ALA | |
21 | ASN | ASN | VAL | PHE | THR | ASN | GLU | PHE | TYR | LEU | |
22 | ASN | LEU | LEU | ASN | GLU | ASP | TRP | LYS | LEU | GLU | |
23 | LYS | ASN | ASP | ALA | ASN | ASN | GLU | GLN | TRP | ASP | |
24 | SER | LYS | SER | GLY | TYR | MET | MET | LEU | PRO | THR | |
25 | ASP | TYR | SER | LEU | ILE | GLN | ASP | PRO | LYS | TYR | |
26 | LEU | SER | ILE | VAL | LYS | GLU | TYR | ALA | ASN | ASP | |
27 | GLN | ASP | LYS | PHE | PHE | LYS | ASP | PHE | SER | LYS | |
28 | ALA | PHE | GLU | LYS | LEU | LEU | GLU | ASN | GLY | ILE | |
29 | THR | PHE | PRO | LYS | ASP | ALA | PRO | SER | PRO | PHE | |
30 | ILE | PHE | LYS | THR | LEU | GLU | GLU | GLN | GLY | LEU |
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:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HN(CA)CB | sample_1 | isotropic | sample_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 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts