BMRB Entry 4800
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR4800
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Title: Chemical shifts of 1H resonances of the heme protons and of the side chain protons of the two axial ligands, His69 and Met106, and of Trp109 of the isolated c domain of Paracoccus pantotrophus in the reduced state
Deposition date: 2000-08-04 Original release date: 2001-03-12
Authors: Steensma, Elles; Gordon, Euan; Oster, Linda; Ferguson, Stuart; Hajdu, Janos
Citation: Steensma, Elles; Gordon, Euan; Oster, Linda; Ferguson, Stuart; Hajdu, Janos. "Heme Ligation and Conformational Plasticity in the Isolated c Domain of Cytochrome cd1 Nitrite Reductase" J. Biol. Chem. 276, 5846-5855 (2001).
Assembly members:
isolated reduced c domain, polymer, 133 residues, 14855 Da.
HEME C, non-polymer, 618.503 Da.
Natural source: Common Name: Paracoccus pantotrophus Taxonomy ID: 82367 Superkingdom: Eubacteria Kingdom: not available Genus/species: Paracoccus pantotrophus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
isolated reduced c domain: QEQVAPPKDPAAALEDHKTR
TDNRYEPSLDNLAQQDVAAP
GAPEGVSALSDAQYNEANKI
YFERCAGCHGVLRKGATGKA
LTPDLTRDLGFDYLQSFITY
GSPAGMPNWGTSGELSAEQV
DLMANYLLLDPAA
- assigned_chemical_shifts
Data type | Count |
1H chemical shifts | 55 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | isolated reduced c domain monomer | 1 |
2 | reduced heme | 2 |
Entities:
Entity 1, isolated reduced c domain monomer 133 residues - 14855 Da.
1 | GLN | GLU | GLN | VAL | ALA | PRO | PRO | LYS | ASP | PRO | ||||
2 | ALA | ALA | ALA | LEU | GLU | ASP | HIS | LYS | THR | ARG | ||||
3 | THR | ASP | ASN | ARG | TYR | GLU | PRO | SER | LEU | ASP | ||||
4 | ASN | LEU | ALA | GLN | GLN | ASP | VAL | ALA | ALA | PRO | ||||
5 | GLY | ALA | PRO | GLU | GLY | VAL | SER | ALA | LEU | SER | ||||
6 | ASP | ALA | GLN | TYR | ASN | GLU | ALA | ASN | LYS | ILE | ||||
7 | TYR | PHE | GLU | ARG | CYS | ALA | GLY | CYS | HIS | GLY | ||||
8 | VAL | LEU | ARG | LYS | GLY | ALA | THR | GLY | LYS | ALA | ||||
9 | LEU | THR | PRO | ASP | LEU | THR | ARG | ASP | LEU | GLY | ||||
10 | PHE | ASP | TYR | LEU | GLN | SER | PHE | ILE | THR | TYR | ||||
11 | GLY | SER | PRO | ALA | GLY | MET | PRO | ASN | TRP | GLY | ||||
12 | THR | SER | GLY | GLU | LEU | SER | ALA | GLU | GLN | VAL | ||||
13 | ASP | LEU | MET | ALA | ASN | TYR | LEU | LEU | LEU | ASP | ||||
14 | PRO | ALA | ALA |
Entity 2, reduced heme - C34 H34 Fe N4 O4 - 618.503 Da.
1 | HEC |
Samples:
sample_1: isolated reduced c domain1 2 mM; sodium phosphate 50 mM; sodium chloride 100 mM; sodium ascorbate mM
Cond_1: pH*: 6.7; temperature: 278 K
Cond_2: pH*: 6.7; temperature: 300 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
1H-1H NOESY | not available | not available | not available |
1H-1H cl-TOCSY | not available | not available | not available |
1H-1H DQF-COSY | not available | not available | not available |
1D NOESY | not available | not available | not available |
Software:
XEASY -
NMR spectrometers:
- Bruker DMX 500.13 MHz
- Bruker DMX 500.03 MHz