BMRB Entry 17306
Click here to enlarge.
PDB ID: 2l6b
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 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks