BMRB Entry 19602

Zinc induced dimer of the metal binding domain 1-16 of human amyloid beta-peptide with Alzheimer`s disease pathogenic English mutation H6R
Deposition date:
Original release date:
Polshakov, Vladimir; Istrate, Andrey; Kozin, Sergey

Citation: Istrate, Andrey; Makarov, Alexander; Kozin, Sergey; Polshakov, Vladimir. "Optimization of the methods for small peptide solution structure determination by NMR spectroscopy"  Mol. Biol. (Mosk) 44, 1075-1085 (2010).
PubMed: 21290829

Assembly members:

Assembly members:
entity_1, polymer, 18 residues, 1977.121 Da.
ZINC ION, non-polymer, 65.409 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):

Data typeCount
13C chemical shifts157
15N chemical shifts38
1H chemical shifts331

Additional metadata:

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


Entity Assembly IDEntity NameEntity ID


Entity 1, Human-amyloid-peptide_1 18 residues - 1977.121 Da.


Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN


sample_1: entity_1 2 mM; bis-Tris, [U-99% 2H], 20 mM; TSP, d4 (100%), 40 uM; H2O 90%; D2O 10%

sample_2: entity_1 2 mM; bis-Tris, [U-99% 2H], 20 mM; TSP, d4 (100%), 40 uM; D2O 100%

sample_3: entity_1 2 mM; zinc cloride 1 mM; bis-Tris, [U-99% 2H], 20 mM; TSP, d4 (100%), 40 uM; H2O 90%; D2O 10%

sample_4: entity_1 2 mM; zinc cloride 1 mM; bis-Tris, [U-99% 2H], 20 mM; TSP, d4 (100%), 40 uM; D2O 100%

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 274 K

sample_conditions_2: pD: 7.2; pressure: 1 atm; temperature: 278 K


NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_2
2D 1H-1H TOCSYsample_2isotropicsample_conditions_2
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
2D 1H-1H TOCSYsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
2D 1H-1H NOESYsample_4isotropicsample_conditions_2
2D 1H-1H TOCSYsample_4isotropicsample_conditions_2


NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN, Bruker Biospin - collection

SPARKY, Goddard - chemical shift assignment

NMRest, Polshakov V. I. - data analysis

GROMACS v4.5.4, Van Der Spoel, Lindahl Hess, Groenhof, Mark and Berendsen - refinement

CPMD, CPMD consortium - geometry optimization

PyMol, DeLano - data analysis

InsightII, Accelrys Software Inc. - data analysis

ProcheckNMR, Laskowski and MacArthur - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:


Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks