BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 30572

Title: Dimer-of-dimer amyloid fibril structure of glucagon   PubMed: 31235909

Deposition date: 2019-02-14 Original release date: 2019-05-28

Authors: Gelenter, M.; Smith, K.; Liao, S.; Mandala, V.; Dregni, A.; Lamm, M.; Tian, Y.; Wei, X.; Pochan, D.; Tucker, T.; Su, Y.; Hong, M.

Citation: Gelenter, M.; Smith, K.; Liao, S.; Mandala, V.; Dregni, A.; Lamm, M.; Tian, Y.; Wei, X.; Pochan, D.; Tucker, T.; Su, Y.; Hong, M.. "The peptide hormone glucagon forms amyloid fibrils with two coexisting beta-strand conformations"  Nat. Struc. Mol. Biol. 26, 592-598 (2019).

Assembly members:
entity_1, polymer, 29 residues, 3486.781 Da.

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

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
entity_1: HSQGTFTSDYSKYLDSRRAQ DFVQWLMNT

Data sets:
Data typeCount
13C chemical shifts306
15N chemical shifts86

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_1, 11
2entity_1, 21
3entity_1, 31
4entity_1, 41
5entity_1, 51
6entity_1, 61
7entity_1, 71
8entity_1, 81
9entity_1, 91
10entity_1, 101
11entity_1, 111
12entity_1, 121
13entity_1, 131
14entity_1, 141
15entity_1, 151
16entity_1, 161

Entities:

Entity 1, entity_1, 1 29 residues - 3486.781 Da.

1   HISSERGLNGLYTHRPHETHRSERASPTYR
2   SERLYSTYRLEUASPSERARGARGALAGLN
3   ASPPHEVALGLNTRPLEUMETASNTHR

Samples:

sample_1: Glucagon, {U-13C; U-15N]-G4,S8,L14,A19,V23, 0.1 ± 0.02 mg/uL

sample_2: Glucagon, {U-13C; U-15N]-S2,Q3,G4,T5,Q24,W25,L26,M27,N28, 0.1 ± 0.02 mg/uL

sample_3: Glucagon, {U-13C; U-15N]-T5,F6,T7,S8,D9,Y10,S11,A19,Q20,D21,F22,V23,Q24, 0.1 ± 0.02 mg/uL

sample_4: Glucagon, {U-13C; U-15N]-S11,K12,Y13,L14,D15,S16,R17,R18,A19, 0.1 ± 0.02 mg/uL

sample_conditions_1: ionic strength: 0.01 M; pH: 2.0; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 13C-13C CORDsample_1isotropicsample_conditions_1
2D 13C-13C CORDsample_2isotropicsample_conditions_1
2D 15N-13C PERSPIRATION-CPsample_2isotropicsample_conditions_1
2D 13C-13C PARsample_2isotropicsample_conditions_1
2D CHHCsample_2isotropicsample_conditions_1
2D 15N-13C NCCXsample_2isotropicsample_conditions_1
3D 15N-13C-13C NCCXsample_4isotropicsample_conditions_1
3D 15N-13C-13C NCACXsample_3isotropicsample_conditions_1
3D 15N-13C-13C NCOCXsample_3isotropicsample_conditions_1
2D 15N-13C NCAsample_1isotropicsample_conditions_1
2D 13C-13C CORDsample_2isotropicsample_conditions_1
2D CHHCsample_4isotropicsample_conditions_1
2D 13C-13C CORDsample_4isotropicsample_conditions_1
2D-13C-13C CORDsample_4isotropicsample_conditions_1
2D 13C-13C CORDsample_3isotropicsample_conditions_1
2D 13C-13C PDSDsample_3isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

SPARKY vNMRFAM-SPARKY 1.412, Goddard - chemical shift assignment, peak picking

TOPSPIN v3.5, Bruker Biospin - processing

NMR spectrometers:

  • Bruker AvanceII 800 MHz
  • Bruker AvanceIII-HD 600 MHz
  • Bruker Avance 900 MHz