BMRB Entry 18654

Title:
NMR Structures of Single-chain Insulin
Deposition date:
2012-08-09
Original release date:
2012-09-07
Authors:
Weiss, Michael; Yang, Yanwu
Citation:

Citation: Yang, Yanwu; Wan, Zhu-li; Hua, Qing-xin; Phillips, Nelson; Huang, Kun; Yeh, I-Ju; Liu, Yule; Hu, Shi-Quan; Hattier, Thomas; Whittaker, Jonathan; Weiss, Michael. "Dynamic repair of an amyloidogenic protein: insulin fibrillation is blocked by tethering a nascent alpha-helix"  .

Assembly members:

Assembly members:
Single-chain Insulin, polymer, 57 residues, 6382.218 Da.

Natural source:

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: pPICz

Experimental source:

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: pPICz

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Single-chain Insulin: FVNQHLCGSDLVEALYLVCG ERGFFYTDPTGGGPRRGIVE QCCHSICSLYQLENYCN

Data sets:
Data typeCount
13C chemical shifts191
15N chemical shifts54
1H chemical shifts368

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Single-chain Insulin1

Entities:

Entity 1, Single-chain Insulin 57 residues - 6382.218 Da.

1   PHEVALASNGLNHISLEUCYSGLYSERASP
2   LEUVALGLUALALEUTYRLEUVALCYSGLY
3   GLUARGGLYPHEPHETYRTHRASPPROTHR
4   GLYGLYGLYPROARGARGGLYILEVALGLU
5   GLNCYSCYSHISSERILECYSSERLEUTYR
6   GLNLEUGLUASNTYRCYSASN

Samples:

sample_1: Single Chain Insulin, [U-100% 13C; U-100% 15N], 0.9 mM; H2O 93%; H2O 7%

sample_conditions_1: ionic strength: 0.1 M; pH: 7.0; pressure: 1 atm; temperature: 273 K

Experiments:

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 HNCOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
4D Time-shared NOESY (4D-N15,C13-edited and 4D-C13,C13-edited NOESY)sample_1isotropicsample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

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

PIPP, Garrett - peak picking

xwinnmr, Bruker Biospin - collection

InsightII, Accelrys Software Inc. - data analysis

Molmol, Koradi, Billeter and Wuthrich - structure display

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz

Related Database Links:

PDB

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