BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 17134

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17134

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Title: Solution structure of Opossum Domain 11   PubMed: 23197533

Deposition date: 2010-08-18 Original release date: 2014-03-04

Authors: Williams, Christopher; Hoppe, Hans; Rezgui, Dellel; Rezgui, Madeline; Frago, Susana; Ellis, Rosamund; Wattana-Amorn, Pakorn; Prince, Stuart; Zaccheo, Oliver; Forbes, Briony; Jones, E.; Crump, Matthew; Bassim, A.

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).

Assembly members:
IGF2R, polymer, 151 residues, 16103.299 Da.

Natural source:   Common Name: Gray Short-tailed Opossum   Taxonomy ID: 13616   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Monodelphis domestica

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

Entity Sequences (FASTA):
IGF2R: MKSNIQDNCQVTNPATGHLF DLNSLKNDSGYSVAYSEKGL IYIGICGGTKNCPSGVGVCF GLTKINAGSWNSQLMYVDQV LQLVYDDGAPCPSKNALKYK SVISFVCTHDSGANNKPVFV SLDKQTCTLYFSWHTPLACE KEEPRHHHHHH

Data sets:
Data typeCount
13C chemical shifts596
15N chemical shifts150
1H chemical shifts937

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1IGF2R1

Entities:

Entity 1, IGF2R 151 residues - 16103.299 Da.

Domain 11 of the IGF2R from Monodelphis domestica. The C-terminal residues EEVPRHHHHHH are a non-native affinity tag

1   METLYSSERASNILEGLNASPASNCYSGLN
2   VALTHRASNPROALATHRGLYHISLEUPHE
3   ASPLEUASNSERLEULYSASNASPSERGLY
4   TYRSERVALALATYRSERGLULYSGLYLEU
5   ILETYRILEGLYILECYSGLYGLYTHRLYS
6   ASNCYSPROSERGLYVALGLYVALCYSPHE
7   GLYLEUTHRLYSILEASNALAGLYSERTRP
8   ASNSERGLNLEUMETTYRVALASPGLNVAL
9   LEUGLNLEUVALTYRASPASPGLYALAPRO
10   CYSPROSERLYSASNALALEULYSTYRLYS
11   SERVALILESERPHEVALCYSTHRHISASP
12   SERGLYALAASNASNLYSPROVALPHEVAL
13   SERLEUASPLYSGLNTHRCYSTHRLEUTYR
14   PHESERTRPHISTHRPROLEUALACYSGLU
15   LYSGLUGLUPROARGHISHISHISHISHIS
16   HIS

Samples:

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

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

sample_conditions_1: pH: 5.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

VNMRJ, Varian - collection

ARIA v1.2, Linge, O, . - refinement, structure solution

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

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

CcpNMR v2.13, CCPN - chemical shift assignment, data analysis, peak picking

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

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

  • Varian INOVA 600 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