BMRB Entry 30314

Title:
Solution Structure and Dynamics of an Ultra-Stable Single-Chain Insulin Analog STUDIES OF AN ENGINEERED MONOMER AND IMPLICATIONS FOR RECEPTOR BINDING
Deposition date:
2017-06-29
Original release date:
2017-11-08
Authors:
Glidden, M.; Yang, Y.; Wickramasinghe, N.; Weiss, M.
Citation:

Citation: Glidden, Michael; Yang, Yanwu; Smith, Nicholas; Phillips, Nelson; Carr, Kelley; Wickramasinghe, Nalinda; Ismail-Beigi, Faramarz; Lawrence, Michael; Smith, Brian; Weiss, Michael. "Solution structure of an ultra-stable single-chain insulin analog connects protein dynamics to a novel mechanism of receptor binding"  J. Biol. Chem. 293, 69-88 (2018).
PubMed: 29114034

Assembly members:

Assembly members:
Insulin, polymer, 57 residues, 6515.308 Da.

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: Pichia

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts205
15N chemical shifts48
1H chemical shifts299

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 57 residues - 6515.308 Da.

1   PHEVALASNGLNHISLEUCYSGLYSERHIS
2   LEUVALGLUALALEUTYRLEUVALCYSGLY
3   GLUARGGLYPHEPHETYRTHRASPPROTHR
4   GLUGLUGLYPROARGARGGLYILEVALGLU
5   GLNCYSCYSHISSERILECYSSERLEUGLU
6   GLNLEUGLUASNTYRCYSASN

Samples:

sample_1: Single chain insulin SCI-b, [U-13C; U-15N], 1 mM

sample_conditions_1: ionic strength: 0 M; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
4D Time-shared NOESYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCC-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D (H)CC(CO)NHsample_1isotropicsample_conditions_1

Software:

SPARKY - structure solution

TOPSPIN - structure solution

X-PLOR, BRUNGER - refinement, structure solution

NMR spectrometers:

  • Bruker Avance 700 MHz

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