BMRB Entry 34629
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34629
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Title: EB1 bound to MACF peptide
Deposition date: 2021-05-20 Original release date: 2022-05-26
Authors: Almeida, T.; Barsukov, I.
Citation: Almeida, T.; Barsukov, I.. "EB1 bound to MACF peptide" .
Assembly members:
Microtubule-associated protein RP/EB family member 1, polymer, 70 residues, 8049.979 Da.
11MACF, polymer, 11 residues, 1283.561 Da.
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Microtubule-associated protein RP/EB family member 1: DEAAELMQQVKVLKLTVEDL
EKERDFYFGKLRNIELICQE
NEGENDPVLQRIVDILYATD
EGFVIPDEGG
11MACF: KPSKIPTPQRK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 239 |
| 15N chemical shifts | 72 |
| 1H chemical shifts | 538 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
| 2 | unit_2 | 1 |
| 3 | unit_3 | 2 |
| 4 | unit_4 | 2 |
Entities:
Entity 1, unit_1 70 residues - 8049.979 Da.
| 1 | ASP | GLU | ALA | ALA | GLU | LEU | MET | GLN | GLN | VAL | |
| 2 | LYS | VAL | LEU | LYS | LEU | THR | VAL | GLU | ASP | LEU | |
| 3 | GLU | LYS | GLU | ARG | ASP | PHE | TYR | PHE | GLY | LYS | |
| 4 | LEU | ARG | ASN | ILE | GLU | LEU | ILE | CYS | GLN | GLU | |
| 5 | ASN | GLU | GLY | GLU | ASN | ASP | PRO | VAL | LEU | GLN | |
| 6 | ARG | ILE | VAL | ASP | ILE | LEU | TYR | ALA | THR | ASP | |
| 7 | GLU | GLY | PHE | VAL | ILE | PRO | ASP | GLU | GLY | GLY |
Entity 2, unit_3 11 residues - 1283.561 Da.
| 1 | LYS | PRO | SER | LYS | ILE | PRO | THR | PRO | GLN | ARG | ||||
| 2 | LYS |
Samples:
sample_1: cEB1, [U-13C; U-15N], 1.15 mM; 11MACF 1.265 mM
sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger A. T. et.al. - refinement
ARIA, Linge, O'Donoghue and Nilges - structure calculation
CcpNmr Analysis, CCPN - chemical shift assignment, peak picking
NMR spectrometers:
- Bruker AVANCE II 600 MHz
- Bruker AVANCE II 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts