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.
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:

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).
PubMed: 28537272

Assembly members:

Assembly members:
huntingtin_exon1_Q44, polymer, 120 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pMal_c2x

Entity Sequences (FASTA):

Entity Sequences (FASTA):
huntingtin_exon1_Q44: MATLEKLMKAFESLKSFQQQ QQQQQQQQQQQQQQQQQQQQ QQQQQQQQQQQQQQQQQQQQ QPPPPPPPPPPPQLPQPPPQ AQPLLPQPQPPPPPPPPPPG PAVAEEPLHRPSGSHHHHHH

Data typeCount
13C chemical shifts130
15N chemical shifts8

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1HttExon1, Chain A1
2HttExon1, Chain B1

Entities:

Entity 1, HttExon1, Chain A 120 residues - Formula weight is not available

1   METALATHRLEUGLULYSLEUMETLYSALA
2   PHEGLUSERLEULYSSERPHEGLNGLNGLN
3   GLNGLNGLNGLNGLNGLNGLNGLNGLNGLN
4   GLNGLNGLNGLNGLNGLNGLNGLNGLNGLN
5   GLNGLNGLNGLNGLNGLNGLNGLNGLNGLN
6   GLNGLNGLNGLNGLNGLNGLNGLNGLNGLN
7   GLNPROPROPROPROPROPROPROPROPRO
8   PROPROGLNLEUPROGLNPROPROPROGLN
9   ALAGLNPROLEULEUPROGLNPROGLNPRO
10   PROPROPROPROPROPROPROPROPROGLY
11   PROALAVALALAGLUGLUPROLEUHISARG
12   PROSERGLYSERHISHISHISHISHISHIS

Samples:

sample_1: huntingtin_exon1_Q44, [U-99% 13C; U-99% 15N], 5 mg

275_K: temperature: 275 K

Experiments:

NameSampleSample stateSample conditions
2D 13C-13C DARRsample_1solid275_K
2D 13C-13C DARRsample_1solid275_K
2D 13C-13C INEPT/TOBSYsample_1solid275_K
2D 13C-13C PDSDsample_1solid275_K
1H-13C DIPSHIFTsample_1solid275_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