BMRB Entry 52244
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52244
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NMR-STAR v3 text file.
XML gzip file.
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Citation: Lorton, Benjamin; Warren, Christopher; Ilyas, Humaira; Nandigrami, Prithviraj; Hegde, Subray; Cahill, Sean; Lehman, Stephanie; Shabanowitz, Jeffrey; Hunt, Donald; Fiser, Andras; Cowburn, David; Shechter, David. "Glutamylation of Npm2 and Nap1 acidic disordered regions increases DNA mimicry and histone chaperone efficiency" iScience ., .-. (2024).
PubMed: 37790377
Assembly members:
entity_1, polymer, 129 residues, 13950 Da.
entity_2, polymer, 125 residues, 13817 Da.
Natural source: Common Name: African clawed frog Taxonomy ID: 8355 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Xenopus laevis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-histone expression plasmid
Entity Sequences (FASTA):
entity_1: SGRGKQGGKTRAKAKTRSSR
AGLQFPVGRVHRLLRKGNYA
ERVGAGAPVYLAAVLEYLTA
EILELAGNAARDNKKTRIIP
RHLQLAVRNDEELNKLLGRV
TIAQGGVLPNIQSVLLPKKT
ESSKSAKSK
entity_2: PEPAKSAPAPKKGSKKAVTK
TQKKDGKKRRKTRKESYAIY
VYKVLKQVHPDTGISSKAMS
IMNSFVNDVFERIAGEASRL
AHYNKRSTITSREIQTAVRL
LLPGELAKHAVSEGTKAVTK
YTSAK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 580 |
| 15N chemical shifts | 186 |
| 1H chemical shifts | 186 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | H2A | 1 |
| 2 | H2B | 2 |
Entities:
Entity 1, H2A 129 residues - 13950 Da.
Uniprot accesion number for H2A used in this study: P06897
| 1 | SER | GLY | ARG | GLY | LYS | GLN | GLY | GLY | LYS | THR | ||||
| 2 | ARG | ALA | LYS | ALA | LYS | THR | ARG | SER | SER | ARG | ||||
| 3 | ALA | GLY | LEU | GLN | PHE | PRO | VAL | GLY | ARG | VAL | ||||
| 4 | HIS | ARG | LEU | LEU | ARG | LYS | GLY | ASN | TYR | ALA | ||||
| 5 | GLU | ARG | VAL | GLY | ALA | GLY | ALA | PRO | VAL | TYR | ||||
| 6 | LEU | ALA | ALA | VAL | LEU | GLU | TYR | LEU | THR | ALA | ||||
| 7 | GLU | ILE | LEU | GLU | LEU | ALA | GLY | ASN | ALA | ALA | ||||
| 8 | ARG | ASP | ASN | LYS | LYS | THR | ARG | ILE | ILE | PRO | ||||
| 9 | ARG | HIS | LEU | GLN | LEU | ALA | VAL | ARG | ASN | ASP | ||||
| 10 | GLU | GLU | LEU | ASN | LYS | LEU | LEU | GLY | ARG | VAL | ||||
| 11 | THR | ILE | ALA | GLN | GLY | GLY | VAL | LEU | PRO | ASN | ||||
| 12 | ILE | GLN | SER | VAL | LEU | LEU | PRO | LYS | LYS | THR | ||||
| 13 | GLU | SER | SER | LYS | SER | ALA | LYS | SER | LYS |
Entity 2, H2B 125 residues - 13817 Da.
Uniprot accesion number for H2B used in this study: P02281
| 1 | PRO | GLU | PRO | ALA | LYS | SER | ALA | PRO | ALA | PRO | ||||
| 2 | LYS | LYS | GLY | SER | LYS | LYS | ALA | VAL | THR | LYS | ||||
| 3 | THR | GLN | LYS | LYS | ASP | GLY | LYS | LYS | ARG | ARG | ||||
| 4 | LYS | THR | ARG | LYS | GLU | SER | TYR | ALA | ILE | TYR | ||||
| 5 | VAL | TYR | LYS | VAL | LEU | LYS | GLN | VAL | HIS | PRO | ||||
| 6 | ASP | THR | GLY | ILE | SER | SER | LYS | ALA | MET | SER | ||||
| 7 | ILE | MET | ASN | SER | PHE | VAL | ASN | ASP | VAL | PHE | ||||
| 8 | GLU | ARG | ILE | ALA | GLY | GLU | ALA | SER | ARG | LEU | ||||
| 9 | ALA | HIS | TYR | ASN | LYS | ARG | SER | THR | ILE | THR | ||||
| 10 | SER | ARG | GLU | ILE | GLN | THR | ALA | VAL | ARG | LEU | ||||
| 11 | LEU | LEU | PRO | GLY | GLU | LEU | ALA | LYS | HIS | ALA | ||||
| 12 | VAL | SER | GLU | GLY | THR | LYS | ALA | VAL | THR | LYS | ||||
| 13 | TYR | THR | SER | ALA | LYS |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks