BMRB Entry 17306
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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/BMR17306
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Aksel, Tural; Majumdar, Ananya; Barrick, Doug. "The contribution of entropy, enthalpy, and hydrophobic desolvation to cooperativity in repeat-protein folding." Structure 19, 349-360 (2011).
PubMed: 21397186
Assembly members:
NR1C, polymer, 115 residues, Formula weight is not available
Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: T7
Entity Sequences (FASTA):
NR1C: GHMWGSKDGNTPLHNAAKNG
HAEEVKKLLSKGADVNARSK
DGNTPLHLAAKNGHAEIVKL
LLAKGADVNARSKDGNTPEH
LAKKNGHHEIVKLLDAKGAD
VNARSWGSSHHHHHH
- assigned_chemical_shifts
- heteronucl_NOEs
- heteronucl_T1_relaxation
- heteronucl_T2_relaxation
- order_parameters
| Data type | Count |
| 13C chemical shifts | 413 |
| 15N chemical shifts | 103 |
| 1H chemical shifts | 661 |
| heteronuclear NOE values | 94 |
| order parameters | 85 |
| T1 relaxation values | 94 |
| T2 relaxation values | 94 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NR1C_assembly | 1 |
Entities:
Entity 1, NR1C_assembly 115 residues - Formula weight is not available
| 1 | GLY | HIS | MET | TRP | GLY | SER | LYS | ASP | GLY | ASN | ||||
| 2 | THR | PRO | LEU | HIS | ASN | ALA | ALA | LYS | ASN | GLY | ||||
| 3 | HIS | ALA | GLU | GLU | VAL | LYS | LYS | LEU | LEU | SER | ||||
| 4 | LYS | GLY | ALA | ASP | VAL | ASN | ALA | ARG | SER | LYS | ||||
| 5 | ASP | GLY | ASN | THR | PRO | LEU | HIS | LEU | ALA | ALA | ||||
| 6 | LYS | ASN | GLY | HIS | ALA | GLU | ILE | VAL | LYS | LEU | ||||
| 7 | LEU | LEU | ALA | LYS | GLY | ALA | ASP | VAL | ASN | ALA | ||||
| 8 | ARG | SER | LYS | ASP | GLY | ASN | THR | PRO | GLU | HIS | ||||
| 9 | LEU | ALA | LYS | LYS | ASN | GLY | HIS | HIS | GLU | ILE | ||||
| 10 | VAL | LYS | LEU | LEU | ASP | ALA | LYS | GLY | ALA | ASP | ||||
| 11 | VAL | ASN | ALA | ARG | SER | TRP | GLY | SER | SER | HIS | ||||
| 12 | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: NR1C, [U-100% 13C; U-100% 15N], 2 mM; sodium phosphate 25 mM; sodium chloride 25 mM; H2O 90%; D2O 10%
NR1C_conditions: ionic strength: 63 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | NR1C_conditions |
| 3D CBCA(CO)NH | sample_1 | isotropic | NR1C_conditions |
| 3D HNCACB | sample_1 | isotropic | NR1C_conditions |
| 3D HBHA(CO)NH | sample_1 | isotropic | NR1C_conditions |
| 3D HNCO | sample_1 | isotropic | NR1C_conditions |
| 3D HNHA | sample_1 | isotropic | NR1C_conditions |
| 3D 1H-15N NOESY | sample_1 | isotropic | NR1C_conditions |
| 3D 1H-13C NOESY | sample_1 | isotropic | NR1C_conditions |
| 3D HCCH-TOCSY | sample_1 | isotropic | NR1C_conditions |
| 3D H(CCO)NH | sample_1 | isotropic | NR1C_conditions |
| 2D 1H-15N HSQC | sample_1 | anisotropic | NR1C_conditions |
Software:
CYANA v2, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, refinement, structure solution
UNIO v2.0.1, Dr. Torsten Herrmann - chemical shift assignment, structure solution
CARA v1.8.4, Kurt Wuthrich - chemical shift assignment, data analysis
X-PLOR NIH v2.24, Schwieters, Kuszewski, Tjandra and Clore - refinement
ModelFree v4.2, Palmer - data analysis
NMRPipe v5.5, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TALOS, Cornilescu, Delaglio and Bax - data analysis
NMR spectrometers:
- Bruker Avance 600 MHz
- Varian INOVA 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks