BMRB Entry 27045
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27045
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Title: Solid-state NMR chemical shifts of amyloid-like fibrils formed by huntingtin exon 1 with a 44-residue polyQ domain. PubMed: 28537272
Deposition date: 2017-03-09 Original release date: 2017-05-19
Authors: Hoop, Cody; Kar, Karunakar; Wetzel, Ronald; van der Wel, Patrick; Lin, Hsiang-Kai; Poirier, Michelle; Boatz, Jennifer
Citation: Lin, Hsiang-Kai; Boatz, Jennifer; Krabbendam, Inge; Kodali, Ravindra; Hou, Zhipeng; Wetzel, Ronald; Dolga, Amalia; Poirier, Michelle; van der Wel, Patrick. "Fibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon1 rather than its polyglutamine core" Nat Commun. 8, 15462-15462 (2017).
Assembly members:
huntingtin_exon1_Q44, polymer, 120 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
huntingtin_exon1_Q44: MATLEKLMKAFESLKSFQQQ
QQQQQQQQQQQQQQQQQQQQ
QQQQQQQQQQQQQQQQQQQQ
QPPPPPPPPPPPQLPQPPPQ
AQPLLPQPQPPPPPPPPPPG
PAVAEEPLHRPSGSHHHHHH
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 130 |
15N chemical shifts | 8 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | HttExon1, Chain A | 1 |
2 | HttExon1, Chain B | 1 |
Entities:
Entity 1, HttExon1, Chain A 120 residues - Formula weight is not available
1 | MET | ALA | THR | LEU | GLU | LYS | LEU | MET | LYS | ALA | |
2 | PHE | GLU | SER | LEU | LYS | SER | PHE | GLN | GLN | GLN | |
3 | GLN | GLN | GLN | GLN | GLN | GLN | GLN | GLN | GLN | GLN | |
4 | GLN | GLN | GLN | GLN | GLN | GLN | GLN | GLN | GLN | GLN | |
5 | GLN | GLN | GLN | GLN | GLN | GLN | GLN | GLN | GLN | GLN | |
6 | GLN | GLN | GLN | GLN | GLN | GLN | GLN | GLN | GLN | GLN | |
7 | GLN | PRO | PRO | PRO | PRO | PRO | PRO | PRO | PRO | PRO | |
8 | PRO | PRO | GLN | LEU | PRO | GLN | PRO | PRO | PRO | GLN | |
9 | ALA | GLN | PRO | LEU | LEU | PRO | GLN | PRO | GLN | PRO | |
10 | PRO | PRO | PRO | PRO | PRO | PRO | PRO | PRO | PRO | GLY | |
11 | PRO | ALA | VAL | ALA | GLU | GLU | PRO | LEU | HIS | ARG | |
12 | PRO | SER | GLY | SER | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: huntingtin_exon1_Q44, [U-99% 13C; U-99% 15N], 5 mg
275_K: temperature: 275 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 13C-13C DARR | sample_1 | solid | 275_K |
2D 13C-13C DARR | sample_1 | solid | 275_K |
2D 13C-13C INEPT/TOBSY | sample_1 | solid | 275_K |
2D 13C-13C PDSD | sample_1 | solid | 275_K |
1H-13C DIPSHIFT | sample_1 | solid | 275_K |
Software:
SPARKY, Goddard - chemical shift assignment
TOPSPIN, Bruker Biospin, CCPN - chemical shift assignment, collection
CcpNMR_Analysis, Bruker Biospin, CCPN - chemical shift assignment, collection
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 750 MHz