BMRB Entry 34000

Title:
D11 bound IGF-II
Deposition date:
2016-05-23
Original release date:
2016-08-01
Authors:
Hexnerova, R.
Citation:

Citation: Hexnerova, Rozalie; Krizkova, Kvetoslava; Fabry, Milan; Sieglova, Irena; Kedrova, Katerina; Collinsova, Michaela; Ullrichova, Pavlina; Srb, Pavel; Williams, Christopher; Crump, Matthew; Tosner, Zdenek; Jiracek, Jiri; Veverka, Vaclav; Zakova, Lenka. "Probing Receptor Specificity by Sampling the Conformational Space of the Insulin-like Growth Factor II C-domain"  J. Biol. Chem. 291, 21234-21245 (2016).
PubMed: 27510031

Assembly members:

Assembly members:
Insulin-like growth factor II, polymer, 67 residues, 7484.472 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: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Insulin-like growth factor II: AYRPSETLCGGELVDTLQFV CGDRGFYFSRPASRVSRRSR GIVEECCFRSCDLALLETYC ATPAKSE

Data sets:
Data typeCount
13C chemical shifts174
15N chemical shifts72
1H chemical shifts448

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 67 residues - 7484.472 Da.

1   ALATYRARGPROSERGLUTHRLEUCYSGLY
2   GLYGLULEUVALASPTHRLEUGLNPHEVAL
3   CYSGLYASPARGGLYPHETYRPHESERARG
4   PROALASERARGVALSERARGARGSERARG
5   GLYILEVALGLUGLUCYSCYSPHEARGSER
6   CYSASPLEUALALEULEUGLUTHRTYRCYS
7   ALATHRPROALALYSSERGLU

Samples:

sample_1: acetic acid, d4, 20 uM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0 mM; pH: 4.2; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

SPARKY, Goddard - chemical shift assignment

TOPSPIN, Bruker Biospin - collection, processing

YASARA, Hoegenauer, Koraimann, Kungl, Vriend - refinement

NMR spectrometers:

  • Bruker AvanceIII 600 MHz
  • Bruker AvanceIII 850 MHz

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