BMRB Entry 11562
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11562
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Title: Redox protein (reduced form)
Deposition date: 2014-03-31 Original release date: 2015-05-18
Authors: Inagaki, Koya; Satoh, Tadashi; Kato, Koichi
Citation: Inagaki, Koya; Satoh, Tadashi; Kato, Koichi. "1H , 13C and 15N Assigned Chemical Shifts for PDI" Not known ., .-..
Assembly members:
PDI, polymer, 121 residues, 13124.035 Da.
Natural source: Common Name: Soft-rot fungus Taxonomy ID: 34413 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Humicola isolens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
PDI: GPLGSEGPVTVVVAKNYNEI
VLDDTKDVLIEFYAPWCGHC
KALAPKYEELGALYAKSEFK
DRVVIAKVDATANDVPDEIQ
GFPTIKLYPAGAKGQPVTYS
GSRTVEDLIKFIAENGKYKA
A
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 448 |
| 15N chemical shifts | 115 |
| 1H chemical shifts | 679 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 121 residues - 13124.035 Da.
Residues 1-5 represent a non-native affinity tag
| 1 | GLY | PRO | LEU | GLY | SER | GLU | GLY | PRO | VAL | THR | ||||
| 2 | VAL | VAL | VAL | ALA | LYS | ASN | TYR | ASN | GLU | ILE | ||||
| 3 | VAL | LEU | ASP | ASP | THR | LYS | ASP | VAL | LEU | ILE | ||||
| 4 | GLU | PHE | TYR | ALA | PRO | TRP | CYS | GLY | HIS | CYS | ||||
| 5 | LYS | ALA | LEU | ALA | PRO | LYS | TYR | GLU | GLU | LEU | ||||
| 6 | GLY | ALA | LEU | TYR | ALA | LYS | SER | GLU | PHE | LYS | ||||
| 7 | ASP | ARG | VAL | VAL | ILE | ALA | LYS | VAL | ASP | ALA | ||||
| 8 | THR | ALA | ASN | ASP | VAL | PRO | ASP | GLU | ILE | GLN | ||||
| 9 | GLY | PHE | PRO | THR | ILE | LYS | LEU | TYR | PRO | ALA | ||||
| 10 | GLY | ALA | LYS | GLY | GLN | PRO | VAL | THR | TYR | SER | ||||
| 11 | GLY | SER | ARG | THR | VAL | GLU | ASP | LEU | ILE | LYS | ||||
| 12 | PHE | ILE | ALA | GLU | ASN | GLY | LYS | TYR | LYS | ALA | ||||
| 13 | ALA |
Samples:
sample_1: PDI, [U-15N], 0.1 mM; sodium phosphate 10 mM; potassium chloride 100 mM; H2O 90%; D2O 10%
sample_2: PDI, [U-13C; U-15N], 0.1 mM; sodium phosphate 10 mM; potassium chloride 100 mM; D2O 100%
sample_conditions_1: ionic strength: 0.16 M; pH: 6.0; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement
SPARKY v3.1, Goddard - chemical shift assignment
xwinnmr v2.6, Bruker Biospin - processing
NMR spectrometers:
- Bruker Avance 800 MHz
- JEOL ECA 920 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts