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
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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: 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:
Domain_11, 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):
Domain_11: MKSNEHDDCQVTNPSTGHLF
DLSSLSGRAGFTAAYAKGWG
VYMSICGENENCPPGVGACF
GQTRISVGKANKRLRYVDQV
LQLVYKDGSPCPSKSGLSYK
SVISFVCRPEAGPTNRPMLI
SLDKQTCTLFFSWHTPLACE
LA
- assigned_chemical_shifts
- heteronucl_NOEs
- heteronucl_T1_relaxation
- heteronucl_T2_relaxation
| Data type | Count |
| 13C chemical shifts | 558 |
| 15N chemical shifts | 150 |
| 1H chemical shifts | 932 |
| heteronuclear NOE values | 238 |
| T1 relaxation values | 238 |
| T2 relaxation values | 237 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Domain_11 | 1 |
Entities:
Entity 1, Domain_11 142 residues - 15433.671 Da.
| 1 | MET | LYS | SER | ASN | GLU | HIS | ASP | ASP | CYS | GLN | ||||
| 2 | VAL | THR | ASN | PRO | SER | THR | GLY | HIS | LEU | PHE | ||||
| 3 | ASP | LEU | SER | SER | LEU | SER | GLY | ARG | ALA | GLY | ||||
| 4 | PHE | THR | ALA | ALA | TYR | ALA | LYS | GLY | TRP | GLY | ||||
| 5 | VAL | TYR | MET | SER | ILE | CYS | GLY | GLU | ASN | GLU | ||||
| 6 | ASN | CYS | PRO | PRO | GLY | VAL | GLY | ALA | CYS | PHE | ||||
| 7 | GLY | GLN | THR | ARG | ILE | SER | VAL | GLY | LYS | ALA | ||||
| 8 | ASN | LYS | ARG | LEU | ARG | TYR | VAL | ASP | GLN | VAL | ||||
| 9 | LEU | GLN | LEU | VAL | TYR | LYS | ASP | GLY | SER | PRO | ||||
| 10 | CYS | PRO | SER | LYS | SER | GLY | LEU | SER | TYR | LYS | ||||
| 11 | SER | VAL | ILE | SER | PHE | VAL | CYS | ARG | PRO | GLU | ||||
| 12 | ALA | GLY | PRO | THR | ASN | ARG | PRO | MET | LEU | ILE | ||||
| 13 | SER | LEU | ASP | LYS | GLN | THR | CYS | THR | LEU | PHE | ||||
| 14 | PHE | SER | TRP | HIS | THR | PRO | LEU | ALA | CYS | GLU | ||||
| 15 | LEU | ALA |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_2 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_2 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_2 |
| 3D C(CO)NH | sample_2 | isotropic | sample_conditions_2 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_2 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_2 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_2 |
| 3D H(CCO)NH | sample_2 | isotropic | sample_conditions_2 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_2 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_2 |
| 3D 1H-15N TOCSY | sample_2 | isotropic | sample_conditions_2 |
| 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_2 |
| Heteronuclear NOE ratio | sample_1 | isotropic | sample_conditions_1 |
| Heteronuclear NOE ratio | sample_1 | isotropic | sample_conditions_1 |
| T1 experiments | sample_1 | isotropic | sample_conditions_1 |
| T1 experiments | sample_1 | isotropic | sample_conditions_1 |
| T2 experiments | sample_1 | isotropic | sample_conditions_1 |
| T2 experiments | sample_1 | isotropic | sample_conditions_1 |
Software:
ARIA v2.2 -
NMR spectrometers:
- Varian VNMRS 600 MHz
- Varian VNMRS 900 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts