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.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: NRC consensus ankyrin repeat protein backbone and sidechain assignments PubMed: 21397186
Deposition date: 2010-11-17 Original release date: 2011-03-21
Authors: Aksel, Tural; Majumdar, Ananya; Barrick, Doug
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).
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
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:
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts