BMRB Entry 19117

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19117
MolProbity Validation Chart

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Title:
NMR solution structure ensemble of 3-4D mutant domain 11 IGF2R in complex with IGF2 (domain 11 structure only)
Deposition date:
2013-03-27
Original release date:
2014-10-13
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:

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:

Assembly members:
Domain_11, polymer, 142 residues, 15433.671 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   Vector: pET26a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Domain_11: MKSNEHDDCQVTNPSTGHLF DLSSLSGRAGFTAAYAKGWG VYMSICGENENCPPGVGACF GQTRISVGKANKRLRYVDQV LQLVYKDGSPCPSKSGLSYK SVISFVCRPEAGPTNRPMLI SLDKQTCTLFFSWHTPLACE LA

Data typeCount
13C chemical shifts558
15N chemical shifts150
1H chemical shifts932
heteronuclear NOE values238
T1 relaxation values238
T2 relaxation values237

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Domain_111

Entities:

Entity 1, Domain_11 142 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: Domain_11 1 mM; H2O 93%; D2O 7%

sample_2: Domain_11 1 mM; H2O 93%; D2O 7%

sample_conditions_1: pH: 4; temperature: 310.15 K

sample_conditions_2: pH: 4; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
2D 1H-13C HSQCsample_2isotropicsample_conditions_2
3D CBCA(CO)NHsample_2isotropicsample_conditions_2
3D C(CO)NHsample_2isotropicsample_conditions_2
3D HNCOsample_2isotropicsample_conditions_2
3D HNCAsample_2isotropicsample_conditions_2
3D HN(CO)CAsample_2isotropicsample_conditions_2
3D H(CCO)NHsample_2isotropicsample_conditions_2
3D HCCH-TOCSYsample_2isotropicsample_conditions_2
3D 1H-15N NOESYsample_2isotropicsample_conditions_2
3D 1H-15N TOCSYsample_2isotropicsample_conditions_2
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_2
Heteronuclear NOE ratiosample_1isotropicsample_conditions_1
Heteronuclear NOE ratiosample_1isotropicsample_conditions_1
T1 experimentssample_1isotropicsample_conditions_1
T1 experimentssample_1isotropicsample_conditions_1
T2 experimentssample_1isotropicsample_conditions_1
T2 experimentssample_1isotropicsample_conditions_1

Software:

ARIA v2.2 -

NMR spectrometers:

  • Varian VNMRS 600 MHz
  • Varian VNMRS 900 MHz

Related Database Links:

EMBL P11717 P01344
BMRB 17127 17128 19153
PDB

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