BMRB Entry 18951
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18951
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Title: NMR solution structure of a MYB-like DNA binding domain of KNL-2 from C. Elegans
Deposition date: 2013-01-15 Original release date: 2014-03-31
Authors: Osborne, Michael; Borden, Katherine
Citation: De Rop, Valerie; Dorn, Jonas; Osborne, Michael; Boisvert, Jacques; Ryan, Joel; Padeganeh, Abbas; Moevus, Corentin; Borden, Katherine; Maddox, Amy; Maddox, Paul. "Centromere epigenome stability is mediated by structural recognition by the Centromere Licensing Complex" Science ., .-..
Assembly members:
KNL2, polymer, 134 residues, 15216.123 Da.
Natural source: Common Name: Caenorhabditis elegans Taxonomy ID: 6239 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Caenorhabditis elegans
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
KNL2: GPLGSVAKKITWRKQDLDRL
KRVIALKKPSASDADWTEVL
RLLAKEGVVEPEVVRQIAIT
RLKWVEPGPLGSVAKKITWR
KQDLDRLKRVIALKKPSASD
ADWTEVLRLLAKEGVVEPEV
VRQIAITRLKWVEP
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 170 |
15N chemical shifts | 47 |
1H chemical shifts | 351 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | MYB-like DNA binding domain of KNL-2 from C. Elegans | 1 |
Entities:
Entity 1, MYB-like DNA binding domain of KNL-2 from C. Elegans 134 residues - 15216.123 Da.
Residues 1-5 (GPLGS) are a cloning artefact
1 | GLY | PRO | LEU | GLY | SER | VAL | ALA | LYS | LYS | ILE | ||||
2 | THR | TRP | ARG | LYS | GLN | ASP | LEU | ASP | ARG | LEU | ||||
3 | LYS | ARG | VAL | ILE | ALA | LEU | LYS | LYS | PRO | SER | ||||
4 | ALA | SER | ASP | ALA | ASP | TRP | THR | GLU | VAL | LEU | ||||
5 | ARG | LEU | LEU | ALA | LYS | GLU | GLY | VAL | VAL | GLU | ||||
6 | PRO | GLU | VAL | VAL | ARG | GLN | ILE | ALA | ILE | THR | ||||
7 | ARG | LEU | LYS | TRP | VAL | GLU | PRO | GLY | PRO | LEU | ||||
8 | GLY | SER | VAL | ALA | LYS | LYS | ILE | THR | TRP | ARG | ||||
9 | LYS | GLN | ASP | LEU | ASP | ARG | LEU | LYS | ARG | VAL | ||||
10 | ILE | ALA | LEU | LYS | LYS | PRO | SER | ALA | SER | ASP | ||||
11 | ALA | ASP | TRP | THR | GLU | VAL | LEU | ARG | LEU | LEU | ||||
12 | ALA | LYS | GLU | GLY | VAL | VAL | GLU | PRO | GLU | VAL | ||||
13 | VAL | ARG | GLN | ILE | ALA | ILE | THR | ARG | LEU | LYS | ||||
14 | TRP | VAL | GLU | PRO |
Samples:
sample_1: KNL2, [U-99% 13C; U-99% 15N], 0.2 mM; sodium phosphate 20 mM; sodium chloride 100 mM; DTT 2 mM; sodium azide 0.02%; Magnesium Sulphate 5 mM
sample_2: KNL2, [U-99% 13C; U-99% 15N], 0.2 mM; sodium phosphate 20 mM; sodium chloride 100 mM; DTT 2 mM; sodium azide 0.02%; Magnesium Sulphate 5 mM
sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 273 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aromatic | sample_2 | isotropic | sample_conditions_1 |
Software:
CYANA v3,0, Guntert, Mumenthaler and Wuthrich - automated structure calculation
NMRView, Johnson, One Moon Scientific - data analysis
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
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