BMRB Entry 6658
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6658
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Title: NMR Solution Structure of a ldb1-LID:Lhx3-LIM complex
Deposition date: 2007-08-03 Original release date: 2005-12-14
Authors: Lee, Christopher; Nancarrow, Amy; Mackay, Joel; Matthews, Jacqueline
Citation: Lee, Christopher; Nancarrow, Amy; Bach, Ingolf; Mackay, Joel; Matthews, Jacqueline. "1H, 15N and 13C Assignments of an Intramolecular Lhx3:ldb1 Complex" J. Biomol. NMR 33, 198-198 (2005).
Assembly members:
FLIX3_-_Fusion_of_ldb1-LID_and_Lhx3_LIM_domains, polymer, 182 residues, 20270.156 Da.
ZN, non-polymer, 65.409 Da.
Natural source: Common Name: mouse Taxonomy ID: 10090 Superkingdom: not available Kingdom: not available Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX-2T
Entity Sequences (FASTA):
FLIX3_-_Fusion_of_ldb1-LID_and_Lhx3_LIM_domains: SSQVPDVMVVGEPTLMGGEF
GDEDERLITRLENTQFDAAN
GIDDEGGSGGHMGSGGTPEI
PMCAGCDQHILDRFILKALD
RHWHSKCLKCSDCHVPLAER
CFSRGESVYCKDDFFKRFGT
KCAACQLGIPPTQVVRRAQD
FVYHLHCFACVVCKRQLATG
DEFYLMEDSRLVCKADYETA
KQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 701 |
| 15N chemical shifts | 183 |
| 1H chemical shifts | 1099 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | FLIX3 - Fusion of ldb1-LID and Lhx3 LIM domains | 1 |
| 2 | ZINC ION_1 | 2 |
| 3 | ZINC ION_2 | 2 |
| 4 | ZINC ION_3 | 2 |
| 5 | ZINC ION_4 | 2 |
Entities:
Entity 1, FLIX3 - Fusion of ldb1-LID and Lhx3 LIM domains 182 residues - 20270.156 Da.
Residues 1-45 represent mouse ldb1 residues 295-339 (Swissprot P70662), residues 46-56 is a linker fusing the two proteins (GGSGGHMGSGG), where the HM is encoded by an NdeI restriction site; and residues 57-182 are from mouse Lhx3 residues 28-153 (Swissprot P50481)
| 1 | SER | SER | GLN | VAL | PRO | ASP | VAL | MET | VAL | VAL | ||||
| 2 | GLY | GLU | PRO | THR | LEU | MET | GLY | GLY | GLU | PHE | ||||
| 3 | GLY | ASP | GLU | ASP | GLU | ARG | LEU | ILE | THR | ARG | ||||
| 4 | LEU | GLU | ASN | THR | GLN | PHE | ASP | ALA | ALA | ASN | ||||
| 5 | GLY | ILE | ASP | ASP | GLU | GLY | GLY | SER | GLY | GLY | ||||
| 6 | HIS | MET | GLY | SER | GLY | GLY | THR | PRO | GLU | ILE | ||||
| 7 | PRO | MET | CYS | ALA | GLY | CYS | ASP | GLN | HIS | ILE | ||||
| 8 | LEU | ASP | ARG | PHE | ILE | LEU | LYS | ALA | LEU | ASP | ||||
| 9 | ARG | HIS | TRP | HIS | SER | LYS | CYS | LEU | LYS | CYS | ||||
| 10 | SER | ASP | CYS | HIS | VAL | PRO | LEU | ALA | GLU | ARG | ||||
| 11 | CYS | PHE | SER | ARG | GLY | GLU | SER | VAL | TYR | CYS | ||||
| 12 | LYS | ASP | ASP | PHE | PHE | LYS | ARG | PHE | GLY | THR | ||||
| 13 | LYS | CYS | ALA | ALA | CYS | GLN | LEU | GLY | ILE | PRO | ||||
| 14 | PRO | THR | GLN | VAL | VAL | ARG | ARG | ALA | GLN | ASP | ||||
| 15 | PHE | VAL | TYR | HIS | LEU | HIS | CYS | PHE | ALA | CYS | ||||
| 16 | VAL | VAL | CYS | LYS | ARG | GLN | LEU | ALA | THR | GLY | ||||
| 17 | ASP | GLU | PHE | TYR | LEU | MET | GLU | ASP | SER | ARG | ||||
| 18 | LEU | VAL | CYS | LYS | ALA | ASP | TYR | GLU | THR | ALA | ||||
| 19 | LYS | GLN |
Entity 2, ZINC ION_1 - Zn - 65.409 Da.
| 1 | ZN |
Samples:
sample_1: FLIX3 - Fusion of ldb1-LID and Lhx3 LIM domains, [U-99% 13C; U-99% 15N], 0.75 mM; ZINC ION 3 mM; DSS15 – 30 uM; DTT 1 mM; sodium phosphate 20 mM; sodium chloride 40 mM; D2O, [U-99% 2H], 10%; H2O 90%
sample_3: FLIX3 - Fusion of ldb1-LID and Lhx3 LIM domains 1.2 mM; ZINC ION 4.8 mM; DSS15 – 30 uM; DTT 1 mM; sodium phosphate 20 mM; sodium chloride 40 mM; H2O 90%; D2O, [U-99% 2H], 10%
sample_4: FLIX3 - Fusion of ldb1-LID and Lhx3 LIM domains, [U-10% 13C; U-99% 15N], 0.6 mM; ZINC ION 2.4 mM; DSS15 – 30 uM; DTT 1 mM; sodium phosphate 20 mM; sodium chloride 40 mM; D2O, [U-99% 2H], 90%; H2O 10%
sample_5: FLIX3 - Fusion of ldb1-LID and Lhx3 LIM domains, [U-99% 15N], 0.3 mM; ZINC ION 1.2 mM; DSS15 – 30 uM; DTT 1 mM; sodium phosphate 20 mM; sodium chloride 40 mM; D2O, [U-99% 2H], 90%; H2O 10%
sample_2: FLIX3 - Fusion of ldb1-LID and Lhx3 LIM domains, [U-99% 13C; U-99% 15N], 0.6 mM; ZINC ION 2.4 mM; DSS15 – 30 uM; DTT 1 mM; sodium phosphate 20 mM; sodium chloride 40 mM; D2O, [U-99% 2H], 99%; H2O 1%
sample_conditions_1: ionic strength: 60 mM; pH: 6.8; pressure: 1 atm; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| HNCO | sample_1 | isotropic | sample_conditions_1 |
| HNCA | sample_1 | isotropic | sample_conditions_1 |
| HNCACO | sample_1 | isotropic | sample_conditions_1 |
| HNCOCA | sample_1 | isotropic | sample_conditions_1 |
| HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| HNHA | sample_1 | isotropic | sample_conditions_1 |
| 15N-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 13C-CT-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D-homonuclear TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D-homonuclear NOESY | sample_1 | isotropic | sample_conditions_1 |
| HNCACB | sample_1 | isotropic | sample_conditions_1 |
| CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| 3D 15N-separated NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 13C-separated NOESY | sample_1 | isotropic | sample_conditions_1 |
| 15N-HSQC (optimised for histidine sidechain J-coupling) | sample_1 | isotropic | sample_conditions_1 |
| 13C-CT-HSQC (10% 13C sample) | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
ARIA v1.2, Linge, O'Donoghue and Nilges - chemical shift assignment, refinement
SPARKY, Goddard - data analysis, peak picking
TOPSPIN v1.2, Bruker Biospin - collection, processing
TALOS, Cornilescu, Delaglio and Bax - data analysis
NMR spectrometers:
- Bruker DRX 600 MHz
- Bruker Avance 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts