Biological Magnetic Resonance Data Bank

A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 19822

Title: NMR structure of B25-(alpha, beta)-dehydro-phenylalanine insulin   PubMed: 25092300

Deposition date: 2014-02-27 Original release date: 2014-08-25

Authors: Yang, yanwu; Weiss, Michael

Citation: Menting, John; Yang, Yanwu; Chan, ShuJin; Phillips, Nelson; Smith, Brian; Whittaker, Jonathan; Wickramasinghe, Nalinda; Whittaker, Linda; Pandyarajan, Vijay; Wan, Zhu-li; Yadav, Satya; Carroll, Julie; Strokes, Natalie; Roberts, Charles; Ismail-Beigi, Faramarz; Milewski, Wieslawa; Steiner, Donald; Chauhan, Virander; Ward, Colin; Weiss, Michael; Lawrence, Michael. "Protective hinge in insulin opens to enable its receptor engagement"  Proc. Natl. Acad. Sci. USA 111, E3395-E3404 (2014).

Assembly members:
entity_1, polymer, 21 residues, 2383.700 Da.
entity_2, polymer, 30 residues, 3958.224 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: Pichia pastoris   Vector: pPICZalpha

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts138
15N chemical shifts39
1H chemical shifts333

Additional metadata:

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


Entity Assembly IDEntity NameEntity ID


Entity 1, Insulin_1 21 residues - 2383.700 Da.

3   ASN

Entity 2, Insulin_2 30 residues - 3958.224 Da.



sample_1: entity_1, [U-13C; U-15N], 0.5 mM; entity_2, [U-13C; U-15N], 0.5 mM; H2O 90%; D2O 10%

sample_2: entity_1 0.5 mM; entity_2 0.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.01 M; pH: 7; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.01 M; pH: 7; temperature: 298 K


NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
4D 13C, 13C-NOESYsample_1isotropicsample_conditions_1
4D 15N, 13C-NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2anisotropicsample_conditions_2
2D 1H-1H TOCSYsample_2anisotropicsample_conditions_2


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

PIPP, Garrett - chemical shift assignment, data analysis, peak picking

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

InsightII, Accelrys Software Inc. - structure solution

Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Thornton - structure solution

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

BMRB 1000 1002 1004 1006 1008 1010 1012 1014 1016 1018 1020 1022 1023 11016 1344 15464 1585 1587 16026 16027 1632 16343 16608 16663 16915 17107 1761 17803 18858 18859 18921 18923 18924 18925 19978 19979 20052 20053 25260 25261 4266
DBJ BAH59081 BAJ17943 BAM29044
EMBL CAA23424 CAA23475 CAA23828 CAA43403 CAA43405
GB AAA17540 AAA19033 AAA36849 AAA59172 AAA59173
PRF 0601246A 1006230A 550086A 560164B 580107B
REF NP_000198 NP_001008996 NP_001075804 NP_001103242 NP_001123565
SP P01308 P01311 P01315 P01321 P30406
AlphaFold P01311 P01308 P01315 P01321 P30406

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