BMRB

Biological Magnetic Resonance Data Bank


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BMRB Entry 30099

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30099
MolProbity Validation Chart

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Title: Structure of human islet amyloid polypeptide in complex with an engineered binding protein   PubMed: 27641459

Deposition date: 2016-05-23 Original release date: 2016-09-22

Authors: Mirecka, E.; Feuerstein, S.; Gremer, L.; Schroeder, G.; Stoldt, M.; Willbold, D.; Hoyer, W.

Citation: Mirecka, E.; Feuerstein, S.; Gremer, L.; Schroeder, G.; Stoldt, M.; Willbold, D.; Hoyer, W.. "beta-Hairpin of Islet Amyloid Polypeptide Bound to an Aggregation Inhibitor"  Sci. Rep. 6, 33474-33474 (2016).

Assembly members:
Islet amyloid polypeptide, polymer, 37 residues, 3909.304 Da.
HI18, polymer, 69 residues, 7804.660 Da.

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 BL21(DE3)

Entity Sequences (FASTA):
Islet amyloid polypeptide: KCNTATCATQRLANFLVHSS NNFGAILSSTNVGSNTY
HI18: MHHHHHHVNSVDNKFNKEME SAGGEIVYLPNLNPDQLCAF IHSIHDDPSQSANLLAEAKK LNDAQAPKW

Data sets:
Data typeCount
13C chemical shifts320
15N chemical shifts98
1H chemical shifts656

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_2, 12
3entity_2, 22

Entities:

Entity 1, entity_1 37 residues - 3909.304 Da.

1   LYSCYSASNTHRALATHRCYSALATHRGLN
2   ARGLEUALAASNPHELEUVALHISSERSER
3   ASNASNPHEGLYALAILELEUSERSERTHR
4   ASNVALGLYSERASNTHRTYR

Entity 2, entity_2, 1 69 residues - 7804.660 Da.

1   METHISHISHISHISHISHISVALASNSER
2   VALASPASNLYSPHEASNLYSGLUMETGLU
3   SERALAGLYGLYGLUILEVALTYRLEUPRO
4   ASNLEUASNPROASPGLNLEUCYSALAPHE
5   ILEHISSERILEHISASPASPPROSERGLN
6   SERALAASNLEULEUALAGLUALALYSLYS
7   LEUASNASPALAGLNALAPROLYSTRP

Samples:

sample_1: HI18 0.48 mM; ISLET AMYLOID POLYPEPTIDE, [U-13C; U-15N], 0.40 mM; sodium phosphate 20 mM; H2O 93%; D2O 7%

sample_2: HI18, [U-13C; U-15N], 0.40 mM; ISLET AMYLOID POLYPEPTIDE 0.48 mM; sodium phosphate 20 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 20 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

ARIA v2.3.2, Linge, O'Donoghue and Nilges - structure calculation

Analysis v2.3, CCPN - chemical shift assignment, peak picking

CNS v1.21, Brunger A. T. et.al. - refinement

NMRPipe v7.9, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMRJ v2.3A, Varian - collection

NMR spectrometers:

  • Varian VNMRS 800 MHz
  • Varian VNMRS 900 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts