BMRB Entry 19157
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR19157
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Title: ATOMIC-RESOLUTION STRUCTURE OF A CROSS-BETA QUADRUPLET AMYLOID FIBRIL DETERMINED BY SOLID-STATE MAGIC ANGLE SPINNING NMR AND CRYO-EM PubMed: 23513222
Deposition date: 2013-04-10 Original release date: 2013-05-14
Authors: Fitzpatrick, Anthony; Debelouchina, G.; Bayro, M.; Clare, D.; Caporini, M.; Bajaj, V.; Jaroniec, C.; Wang, L.; Ladizhansky, V.; Muller, S.; Macphee, C.; Waudby, C.; Mott, H.; De simone, A.; Knowles, T.; Saibil, H.; Vendruscolo, M.; Orlova, E.; Griffin, R.; Dobson, C.; Bajaj, M.; De-simone, A.
Citation: Fitzpatrick, Anthony; Debelouchina, G.; Bayro, M.; Clare, D.; Caporini, M.; Bajaj, V.; Jaroniec, C.; Wang, L.; Ladizhansky, V.; Muller, S.; Macphee, C.; Waudby, C.; Mott, H.; De simone, A.; Knowles, T.; Saibil, H.; Vendruscolo, M.; Orlova, E.; Griffin, R.; Dobson, C.. "ATOMIC STRUCTURE AND HIERARCHICAL ASSEMBLY OF A CROSS-BETA AMYLOID FIBRIL." Proc. Natl. Acad. Sci. U. S. A. 110, 5468-5473 (2013).
Assembly members:
TRANSTHYRETIN_(chain_A), polymer, 11 residues, 1198.3778 Da.
Natural source: Common Name: unknown 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):
TRANSTHYRETIN_(chain_A): YTIAALLSPYS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 52 |
| 15N chemical shifts | 9 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | TRANSTHYRETIN (chain A), 1 | 1 |
| 2 | TRANSTHYRETIN (chain A), 2 | 1 |
| 3 | TRANSTHYRETIN (chain A), 3 | 1 |
| 4 | TRANSTHYRETIN (chain A), 4 | 1 |
| 5 | TRANSTHYRETIN (chain A), 5 | 1 |
| 6 | TRANSTHYRETIN (chain A), 6 | 1 |
| 7 | TRANSTHYRETIN (chain A), 7 | 1 |
| 8 | TRANSTHYRETIN (chain A), 8 | 1 |
| 9 | TRANSTHYRETIN (chain A), 9 | 1 |
| 10 | TRANSTHYRETIN (chain A), 10 | 1 |
| 11 | TRANSTHYRETIN (chain A), 11 | 1 |
| 12 | TRANSTHYRETIN (chain A), 12 | 1 |
| 13 | TRANSTHYRETIN (chain A), 13 | 1 |
| 14 | TRANSTHYRETIN (chain A), 14 | 1 |
| 15 | TRANSTHYRETIN (chain A), 15 | 1 |
| 16 | TRANSTHYRETIN (chain A), 16 | 1 |
| 17 | TRANSTHYRETIN (chain A), 17 | 1 |
| 18 | TRANSTHYRETIN (chain A), 18 | 1 |
| 19 | TRANSTHYRETIN (chain A), 19 | 1 |
| 20 | TRANSTHYRETIN (chain A), 20 | 1 |
| 21 | TRANSTHYRETIN (chain A), 21 | 1 |
| 22 | TRANSTHYRETIN (chain A), 22 | 1 |
| 23 | TRANSTHYRETIN (chain A), 23 | 1 |
| 24 | TRANSTHYRETIN (chain A), 24 | 1 |
| 25 | TRANSTHYRETIN (chain A), 25 | 1 |
| 26 | TRANSTHYRETIN (chain A), 26 | 1 |
| 27 | TRANSTHYRETIN (chain A), 27 | 1 |
| 28 | TRANSTHYRETIN (chain A), 28 | 1 |
| 29 | TRANSTHYRETIN (chain A), 29 | 1 |
| 30 | TRANSTHYRETIN (chain A), 30 | 1 |
| 31 | TRANSTHYRETIN (chain A), 31 | 1 |
| 32 | TRANSTHYRETIN (chain A), 32 | 1 |
| 33 | TRANSTHYRETIN (chain A), 33 | 1 |
| 34 | TRANSTHYRETIN (chain A), 34 | 1 |
| 35 | TRANSTHYRETIN (chain A), 35 | 1 |
| 36 | TRANSTHYRETIN (chain A), 36 | 1 |
| 37 | TRANSTHYRETIN (chain A), 37 | 1 |
| 38 | TRANSTHYRETIN (chain A), 38 | 1 |
| 39 | TRANSTHYRETIN (chain A), 39 | 1 |
| 40 | TRANSTHYRETIN (chain A), 40 | 1 |
| 41 | TRANSTHYRETIN (chain A), 41 | 1 |
| 42 | TRANSTHYRETIN (chain A), 42 | 1 |
| 43 | TRANSTHYRETIN (chain A), 43 | 1 |
| 44 | TRANSTHYRETIN (chain A), 44 | 1 |
| 45 | TRANSTHYRETIN (chain A), 45 | 1 |
| 46 | TRANSTHYRETIN (chain A), 46 | 1 |
| 47 | TRANSTHYRETIN (chain A), 47 | 1 |
| 48 | TRANSTHYRETIN (chain A), 48 | 1 |
Entities:
Entity 1, TRANSTHYRETIN (chain A), 1 11 residues - 1198.3778 Da.
| 1 | TYR | THR | ILE | ALA | ALA | LEU | LEU | SER | PRO | TYR | ||||
| 2 | SER |
Samples:
sample_1: TRANSTHYRETIN (chain A) na mM
sample_conditions_1: pH: .; pressure: 1.000 atm; temperature: 288.150 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1D DQ-DRAWS | sample_1 | solid | sample_conditions_1 |
| REDOR | sample_1 | solid | sample_conditions_1 |
| ZF-TEDOR | sample_1 | solid | sample_conditions_1 |
| 2D PDSD | sample_1 | solid | sample_conditions_1 |
| 1D DQ-DRAWS | sample_1 | solid | sample_conditions_1 |
| REDOR | sample_1 | solid | sample_conditions_1 |
Software:
AutoDep v4.3 -
CNSSOLVE vany, BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- -
NMR spectrometers:
- Bruker Custom built 750 MHz
- VARIAN CUSTOM BUILT 500 MHz