BMRB Entry 17110

Title:
chicken IGF2R domain 11
Deposition date:
2010-08-10
Original release date:
2012-08-30
Authors:
Williams, Christopher; Hoppe, Hans; Strickland, Madeline; Frago, Susana; Ellis, Rosamund; Wattana-Amorn, Pakorn; Prince, Stuart; Zaccheo, Oliver; Forbes, Briony; Jones, Yvonne; Rezgui, Dellel; Crump, Matthew; Hassan, Bassim
Citation:

Citation: Williams, Christopher; Hoppe, Hans; Rezgui, Dellel; Strickland, Madeline; Frago, Susana; Ellis, Rosamund; Wattana-Amorn, Pakorn; Prince, Stuart; Zaccheo, Oliver; Forbes, Briony; Jones, E.; Crump, Matthew; Hassan, A.; Grutzner, Frank; Nolan, Catherine; Mungall, Andrew. "An exon splice enhancer primes IGF2:IGF2R binding site structure and function evolution"  Science 338, 1209-1213 (2012).
PubMed: 23197533

Assembly members:

Assembly members:
IGF2R, polymer, 154 residues, 16408.426 Da.

Natural source:

Natural source:   Common Name: chicken   Taxonomy ID: 9031   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Gallus gallus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET26a

Data sets:
Data typeCount
13C chemical shifts592
15N chemical shifts154
1H chemical shifts959

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1IGF2R1

Entities:

Entity 1, IGF2R 154 residues - 16408.426 Da.

Domain 11 of the IGF2R from Gallus gallus (chicken). The C-terminal residues EEVPRHHHHHH are a non-native affinity tag

1   METLYSSERASNVALGLNASNASPCYSARG
2   VALTHRASNPROALATHRGLYHISLEUPHE
3   ASPLEUTHRSERLEULYSARGGLUSERGLY
4   TYRTHRILETHRASPSERHISASNARGLYS
5   ILEGLULEUASNVALCYSALAGLUALALYS
6   SERSERCYSALAASNGLYALAALAVALCYS
7   ILETHRASPGLYPROLYSTHRLEUASNALA
8   GLYLYSLEUSERLYSTHRLEUTHRTYRGLU
9   ASPGLNVALLEULYSLEUVALTYRGLUASP
10   GLYASPPROCYSPROTHRASPLEULYSMET
11   LYSHISLYSSERTYRPHESERPHEVALCYS
12   LYSSERASPALAGLYASPASPSERGLNPRO
13   VALPHELEUSERPHEASPGLUGLNTHRCYS
14   THRSERTYRPHESERTRPHISTHRSERLEU
15   ALACYSGLUGLUGLUVALPROARGHISHIS
16   HISHISHISHIS

Samples:

sample_1: D2O 5 ± 0.1 %; sodium acetate 20 ± 0.1 mM; EDTA 0.1 ± 0.01 mM; sodium azide 100 ± 0.1 uM; IGF2R, [U-98% 15N], 0.5 – 1 mM; H2O 95%

sample_2: D2O 5 ± 0.1 %; sodium phosphate 20 ± 0.1 mM; EDTA 0.1 ± 0.01 mM; sodium azide 100 ± 0.1 uM; IGF2R, [U-98% 13C; U-98% 15N], 0.5 – 1 mM; H2O 95%

sample_conditions_1: ionic strength: 0 M; pH: 5.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

VNMRJ, Varian - collection

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

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

TALOS, Cornilescu, Delaglio and Bax - data analysis, geometry optimization

ARIA v1.2, Linge, O'Donoghue and Nilges - refinement, structure solution

iCing vr765, Vuister, Doreleijers, Sousa da Silva - refinement

ANALYSIS v2.13, Vranken, Boucher, Stevens, Fogh, Pajon, Llinas, Ulrich, Markley, Ionides, Laue - chemical shift assignment, data analysis

NMR spectrometers:

  • Varian VNMRS 600 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB

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