BMRB Entry 16023
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16023
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Title: Tetramer of KIA7H peptide
Deposition date: 2008-11-06 Original release date: 2012-07-19
Authors: Lopez-Alonso, Jorge; Pardo-Cea, Miguel; Lopez de la Osa, Jaime; Chakrabartty, Avijit; Gonzalez, Carlos; Laurents, Douglas
Citation: Lopez-Alonso, Jorge; Pardo-Cea, Miguel; Lopez de la Osa, Jaime; Chakrabartty, Avijit; Gonzalez, Carlos; Laurents, Douglas. "Terminal amino acid in KIA7 determines its stability" Not known ., .-..
Assembly members:
KIA7H, polymer, 22 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: chemical synthesis
Entity Sequences (FASTA):
KIA7H: XAKAAAAAIKAIAAIIKAGG
HX
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 22 |
| 1H chemical shifts | 134 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | KIA7H peptide, chain 1 | 1 |
| 2 | KIA7H peptide, chain 2 | 1 |
| 3 | KIA7H peptide, chain 3 | 1 |
| 4 | KIA7H peptide, chain 4 | 1 |
Entities:
Entity 1, KIA7H peptide, chain 1 22 residues - Formula weight is not available
| 1 | ACE | ALA | LYS | ALA | ALA | ALA | ALA | ALA | ILE | LYS | ||||
| 2 | ALA | ILE | ALA | ALA | ILE | ILE | LYS | ALA | GLY | GLY | ||||
| 3 | HIS | NH2 |
Samples:
H2O: KIA7H 2.8 mM; sodium chloride 200 mM; sodium phosphate 1 mM; boric acid 1 mM; H2O 90%; D2O 10%
D2O: KIA7H 1 mM; sodium chloride 200 mM; sodium phosphate 1 mM; boric acid 1 mM; D2O 100%
sample_conditions_H2O: pH: 7.45; pressure: 1 atm; temperature: 278 K
sample_conditions_D2O: pH: 7.49; pressure: 1 atm; temperature: 278 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-13C HSQC | H2O | isotropic | sample_conditions_H2O |
| 2D 1H-1H TOCSY | H2O | isotropic | sample_conditions_H2O |
| 2D 1H-1H NOESY | H2O | isotropic | sample_conditions_H2O |
| 2D 1H-13C HSQC | D2O | isotropic | sample_conditions_D2O |
| 2D 1H-1H NOESY | D2O | isotropic | sample_conditions_D2O |
Software:
TOPSPIN, Bruker Biospin - processing
SPARKY, Goddard - chemical shift assignment
DYANA, Guntert, Braun and Wuthrich - structure solution
AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement
NMR spectrometers:
- Bruker Avance 800 MHz