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 19153

Title: NMR solution structure ensemble of 3-4D mutant domain 11 IGF2R

Authors: Strickland, Madeleine; Williams, Chris; Richards, Emily; Minnall, Leanne; Crump, Matthew; Frago, Susana; Hughes, Jennifer; Garner, Lee; Hoppe, Hans-Jurgen; Rezgui, Dellel; Zaccheo, Oliver; Prince, Stuart; Hassan, Andrew; Whittaker, Sara

Citation: Frago, Susana; Strickland, Madeleine; Hughes, Jennifer; Williams, Christopher; Garner, Lee; Hoppe, Hans-Jurgen; Rezgui, Dellel; Zaccheo, Oliver; Prince, Stuart; Crump, Matthew; Hassan, Andrew. "Directed evolution of structurally selected IGF2R domain 11 binding loop residues generates an IGF2 super-antagonist"  EMBO J. ., .-..

Assembly members:
IGF2R, polymer, 142 residues, 15433.671 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
IGF2R: MKSNEHDDCQVTNPSTGHLF DLSSLSGRAGFTAAYAKGWG VYMSICGENENCPPGVGACF GQTRISVGKANKRLRYVDQV LQLVYKDGSPCPSKSGLSYK SVISFVCRPEAGPTNRPMLI SLDKQTCTLFFSWHTPLACE LA

Data typeCount
1H chemical shifts955
13C chemical shifts597
15N chemical shifts151
heteronuclear NOE values266
T1 relaxation values284
T2 relaxation values284

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1IGF2R1

Entities:

Entity 1, IGF2R 142 residues - 15433.671 Da.

1   METLYSSERASNGLUHISASPASPCYSGLN
2   VALTHRASNPROSERTHRGLYHISLEUPHE
3   ASPLEUSERSERLEUSERGLYARGALAGLY
4   PHETHRALAALATYRALALYSGLYTRPGLY
5   VALTYRMETSERILECYSGLYGLUASNGLU
6   ASNCYSPROPROGLYVALGLYALACYSPHE
7   GLYGLNTHRARGILESERVALGLYLYSALA
8   ASNLYSARGLEUARGTYRVALASPGLNVAL
9   LEUGLNLEUVALTYRLYSASPGLYSERPRO
10   CYSPROSERLYSSERGLYLEUSERTYRLYS
11   SERVALILESERPHEVALCYSARGPROGLU
12   ALAGLYPROTHRASNARGPROMETLEUILE
13   SERLEUASPLYSGLNTHRCYSTHRLEUPHE
14   PHESERTRPHISTHRPROLEUALACYSGLU
15   LEUALA

Samples:

sample_1: IGF2R, [U-95% 13C; U-95% 15N], 1 mM; D2O, [U-2H], 7%; H2O 93%; sodium azide 100 uM; EDTA 1 mM; sodium acetate 10 mM

sample_2: IGF2R, [U-95% 15N], 1 mM; D2O, [U-2H], 7%; H2O 93%; sodium azide 100 uM; EDTA 1 mM; sodium acetate 10 mM

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

sample_conditions_2: pH: 5.5; 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 CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
Heteronuclear NOE ratiosample_2isotropicsample_conditions_2
Heteronuclear NOE ratiosample_2isotropicsample_conditions_2
T1 experimentssample_2isotropicsample_conditions_2
T1 experimentssample_2isotropicsample_conditions_2
T2 experimentssample_2isotropicsample_conditions_2
T2 experimentssample_2isotropicsample_conditions_2
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

ARIA v2.2, Linge, O, . - processing, refinement, structure solution

CING viCing, Doreleijers - refinement

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

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

Relax v1.3.9, Palmer, is, him.' - data analysis, processing

SPARKY v2.6, Goddard - data analysis

VNMRJ v0.4, Varian - collection

CCPN_Analysis v2.1, CCPN - chemical shift assignment, data analysis, peak picking

TALOS vTALOS+, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

  • Varian VNMRS 600 MHz
  • Varian VNMRS 900 MHz

Related Database Links:

EMBL P11717
BMRB 17127 17128 19117
PDB