BMRB Entry 1889
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR1889
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Title: Proton Homonuclear Correlated Spectroscopy as an Assignment Tool for Hyperfine-Shifted Resonances in Medium-Sized Paramagnetic Proteins: Cyanide-Ligated Yeast Cytochrome c Peroxidase as an Example
Deposition date: 1995-07-31 Original release date: 1999-06-14
Authors: Satterlee, James; Russell, David; Erman, James
Citation: Satterlee, James; Russell, David; Erman, James. "Proton Homonuclear Correlated Spectroscopy as an Assignment Tool for Hyperfine-Shifted Resonances in Medium-Sized Paramagnetic Proteins: Cyanide-Ligated Yeast Cytochrome c Peroxidase as an Example" Biochemistry 30, 9072-9077 (1991).
Assembly members:
cytochrome c peroxidase, polymer, 232 residues, Formula weight is not available
Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available
Experimental source: Production method: not available
Entity Sequences (FASTA):
cytochrome c peroxidase: XXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXX
XXXXXXXRXXXHXXXXXXXX
XXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXHXXXXT
XXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXL
- assigned_chemical_shifts
Data type | Count |
1H chemical shifts | 16 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | cytochrome c peroxidase | 1 |
Entities:
Entity 1, cytochrome c peroxidase 232 residues - Formula weight is not available
1 | X | X | X | X | X | X | X | X | X | X | ||||
2 | X | X | X | X | X | X | X | X | X | X | ||||
3 | X | X | X | X | X | X | X | X | X | X | ||||
4 | X | X | X | X | X | X | X | X | X | X | ||||
5 | X | X | X | X | X | X | X | ARG | X | X | ||||
6 | X | HIS | X | X | X | X | X | X | X | X | ||||
7 | X | X | X | X | X | X | X | X | X | X | ||||
8 | X | X | X | X | X | X | X | X | X | X | ||||
9 | X | X | X | X | X | X | X | X | X | X | ||||
10 | X | X | X | X | X | X | X | X | X | X | ||||
11 | X | X | X | X | X | X | X | X | X | X | ||||
12 | X | X | X | X | X | X | X | X | X | X | ||||
13 | X | X | X | X | X | X | X | X | X | X | ||||
14 | X | X | X | X | X | X | X | X | X | X | ||||
15 | X | X | X | X | X | X | X | X | X | X | ||||
16 | X | X | X | X | X | X | X | X | X | X | ||||
17 | X | X | X | X | X | X | X | X | X | X | ||||
18 | X | X | X | X | HIS | X | X | X | X | THR | ||||
19 | X | X | X | X | X | X | X | X | X | X | ||||
20 | X | X | X | X | X | X | X | X | X | X | ||||
21 | X | X | X | X | X | X | X | X | X | X | ||||
22 | X | X | X | X | X | X | X | X | X | X | ||||
23 | X | X | X | X | X | X | X | X | X | X | ||||
24 | X | LEU |
Samples:
sample_one:
sample_condition_set_one: pH: 7 na; temperature: 300 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|
Software:
No software information available
NMR spectrometers:
- unknown unknown 0 MHz