BMRB Entry 11548
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR11548
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
Title: DESIGNED ARMADILLO REPEAT PROTEIN FRAGMENT (MAII) PubMed: 24931467
Deposition date: 2013-12-09 Original release date: 2014-07-21
Authors: Zerbe, Oliver; Christen, Martin; Plueckthun, Andreas; Watson, Randall
Citation: Watson, Randall; Christen, Martin; Ewald, Christina; Bumback, Fabian; Reichen, Christian; Mihajlovic, Maja; Schmidt, E.; Guntert, Peter; Caflisch, Amedeo; Plueckthun, Andreas; Zerbe, Oliver. "Spontaneous Self-Assembly of Fragments of Engineered Armadillo Repeat Proteins into Folded Proteins" Structure 22, 985-995 (2014).
Assembly members:
MA, polymer, 84 residues, 9104.170 Da.
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: pLIC_CR
Entity Sequences (FASTA):
MA: GNEQIQAVIDAGALPALVQL
LSSPNEQILQEALWALSNIA
SGGNEQKQAVKEAGALEKLE
QLQSHENEKIQKEAQEALEK
LQSH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 281 |
| 15N chemical shifts | 64 |
| 1H chemical shifts | 456 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | MA | 1 |
Entities:
Entity 1, MA 84 residues - 9104.170 Da.
| 1 | GLY | ASN | GLU | GLN | ILE | GLN | ALA | VAL | ILE | ASP | ||||
| 2 | ALA | GLY | ALA | LEU | PRO | ALA | LEU | VAL | GLN | LEU | ||||
| 3 | LEU | SER | SER | PRO | ASN | GLU | GLN | ILE | LEU | GLN | ||||
| 4 | GLU | ALA | LEU | TRP | ALA | LEU | SER | ASN | ILE | ALA | ||||
| 5 | SER | GLY | GLY | ASN | GLU | GLN | LYS | GLN | ALA | VAL | ||||
| 6 | LYS | GLU | ALA | GLY | ALA | LEU | GLU | LYS | LEU | GLU | ||||
| 7 | GLN | LEU | GLN | SER | HIS | GLU | ASN | GLU | LYS | ILE | ||||
| 8 | GLN | LYS | GLU | ALA | GLN | GLU | ALA | LEU | GLU | LYS | ||||
| 9 | LEU | GLN | SER | HIS |
Samples:
sample_1: MA, [U-13C; U-15N], 0.75 mM; sodium phosphate 50 mM; sodium chloride 150 mM; glycerol 2%; TMSP 1 mM; sodium azide 0.02%; H2O 88%; D2O 10%
sample_conditions_1: ionic strength: 285 mM; pH: 7.4; pressure: 1 atm; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1, Bruker Biospin - collection, processing
CARA v1.8.4, Keller and Wuthrich - chemical shift assignment
CcpNMR v2.3.1, CCPN - chemical shift assignment, data analysis, peak picking
UNIO v2.0.2, (UNIO) Herrmann - data analysis, peak picking, structure solution
CYANA v3.96a, Guntert, Mumenthaler and Wuthrich - geometry optimization, structure solution
X-PLOR_NIH v2.32, Schwieters, Kuszewski, Tjandra and Clore - refinement
TALOS-N v4.01, Shen and Bax - data analysis
NMR spectrometers:
- Bruker Avance 700 MHz
- Bruker Avance 600 MHz
Related Database Links:
| PDB |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts