BMRB Entry 6971
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6971
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: NMR assignment of the b' domain of thermophilic fungal protein disulfide isomerase PubMed: 16819589
Deposition date: 2006-02-03 Original release date: 2006-08-07
Authors: Nakano, Michiko; Murakami, Chiho; Yamaguchi, Yoshiki; Sasakawa, Hiroaki; Harada, Takushi; Kurimoto, Eiji; Asami, Osamu; Kajino, Tsutomu; Kato, Koichi
Citation: Nakano, Michiko; Murakami, Chiho; Yamaguchi, Yoshiki; Sasakawa, Hiroaki; Harada, Takushi; Kurimoto, Eiji; Asami, Osamu; Kajino, Tsutomu; Kato, Koichi. "NMR Assignments of the b' and a' Domains of Thermophilic Fungal Protein Disulfide Isomerase" J. Biomol. NMR 36, 44-44 (2006).
Assembly members:
PDI-b', polymer, 133 residues, Formula weight is not available
Natural source: Common Name: thermophilic fungus Taxonomy ID: 34413 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Humicola insolens
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
PDI-b': GPLGSPLIGEIGPETYSDYM
SAGIPLAYIFAETAEERKEL
SDKLKPIAEAQRGVINFGTI
DAKAFGAHAGNLNLKTDKFP
AFAIQEVAKNQKFPFDQEKE
ITFEAIKAFVDDFVAGKIEP
SIKSEPIPEKQEG
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 468 |
15N chemical shifts | 128 |
1H chemical shifts | 816 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | PDI-b' | 1 |
Entities:
Entity 1, PDI-b' 133 residues - Formula weight is not available
1 | GLY | PRO | LEU | GLY | SER | PRO | LEU | ILE | GLY | GLU | ||||
2 | ILE | GLY | PRO | GLU | THR | TYR | SER | ASP | TYR | MET | ||||
3 | SER | ALA | GLY | ILE | PRO | LEU | ALA | TYR | ILE | PHE | ||||
4 | ALA | GLU | THR | ALA | GLU | GLU | ARG | LYS | GLU | LEU | ||||
5 | SER | ASP | LYS | LEU | LYS | PRO | ILE | ALA | GLU | ALA | ||||
6 | GLN | ARG | GLY | VAL | ILE | ASN | PHE | GLY | THR | ILE | ||||
7 | ASP | ALA | LYS | ALA | PHE | GLY | ALA | HIS | ALA | GLY | ||||
8 | ASN | LEU | ASN | LEU | LYS | THR | ASP | LYS | PHE | PRO | ||||
9 | ALA | PHE | ALA | ILE | GLN | GLU | VAL | ALA | LYS | ASN | ||||
10 | GLN | LYS | PHE | PRO | PHE | ASP | GLN | GLU | LYS | GLU | ||||
11 | ILE | THR | PHE | GLU | ALA | ILE | LYS | ALA | PHE | VAL | ||||
12 | ASP | ASP | PHE | VAL | ALA | GLY | LYS | ILE | GLU | PRO | ||||
13 | SER | ILE | LYS | SER | GLU | PRO | ILE | PRO | GLU | LYS | ||||
14 | GLN | GLU | GLY |
Samples:
sample_1: PDI-b', [U-13C; U-15N], 1 mM
conditions_1: pH: 6.0; temperature: 310 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
1H15N HSQC | sample_1 | not available | conditions_1 |
1H13C HSQC | sample_1 | not available | conditions_1 |
HNCA | sample_1 | not available | conditions_1 |
HN(CO)CA | sample_1 | not available | conditions_1 |
HNCO | sample_1 | not available | conditions_1 |
HN(CA)CO | sample_1 | not available | conditions_1 |
CBCA(CO)NH | sample_1 | not available | conditions_1 |
CBCANH | sample_1 | not available | conditions_1 |
HBHA(CO)NH | sample_1 | not available | conditions_1 |
15N-edited TOCSY | sample_1 | not available | conditions_1 |
H(CC)(CO)NH | sample_1 | not available | conditions_1 |
C(CO)NH | sample_1 | not available | conditions_1 |
HCCH-COSY | sample_1 | not available | conditions_1 |
HCCH-TOCSY | sample_1 | not available | conditions_1 |
1H-1H TOCSY | sample_1 | not available | conditions_1 |
1H-1H NOESY | sample_1 | not available | conditions_1 |
Software:
No software information available
NMR spectrometers:
- Bruker DRX 800 MHz
- Bruker Avance 600 MHz
- Bruker DMX 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts