BMRB Entry 17200
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PDB ID: 2l3r
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17200
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
Citation: Nady, Nataliya; Lemak, Alexander; Walker, John; Avvakumov, George; Kareta, Michael; Achour, Mayada; Xue, Sheng; Duan, Shili; Allali-Hassani, Abdellah; Zuo, Xiaobing; Wang, Yun-Xing; Bronner, Christian; Chedin, Frederic; Arrowsmith, Cheryl; Dhe-Paganon, Sirano. "Recognition of multivalent histone states associated with heterochromatin by UHRF1 protein." J. Biol. Chem. 286, 24300-24311 (2011).
PubMed: 21489993
Assembly members:
UHRF1 Tandem Tudor Domains, polymer, 162 residues, 18824.107 Da.
Histone H3, polymer, 11 residues, 1293.529 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a
Entity Sequences (FASTA):
UHRF1 Tandem Tudor Domains: GGMWDETELGLYKVNEYVDA
RDTNMGAWFEAQVVRVTRKA
PSRDEPCSSTSRPALEEDVI
YHVKYDDYPENGVVQMNSRD
VRARARTIIKWQDLEVGQVV
MLNYNPDNPKERGFWYDAEI
SRKRETRTARELYANVVLGD
DSLNDCRIIFVDEVFKIERP
GE
Histone H3: ARTKQTARXST
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 644 |
| 15N chemical shifts | 160 |
| 1H chemical shifts | 1122 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | UHRF1 Tandem Tudor Domains | 1 |
| 2 | Histone H3 | 2 |
Entities:
Entity 1, UHRF1 Tandem Tudor Domains 162 residues - 18824.107 Da.
| 1 | GLY | GLY | MET | TRP | ASP | GLU | THR | GLU | LEU | GLY | ||||
| 2 | LEU | TYR | LYS | VAL | ASN | GLU | TYR | VAL | ASP | ALA | ||||
| 3 | ARG | ASP | THR | ASN | MET | GLY | ALA | TRP | PHE | GLU | ||||
| 4 | ALA | GLN | VAL | VAL | ARG | VAL | THR | ARG | LYS | ALA | ||||
| 5 | PRO | SER | ARG | ASP | GLU | PRO | CYS | SER | SER | THR | ||||
| 6 | SER | ARG | PRO | ALA | LEU | GLU | GLU | ASP | VAL | ILE | ||||
| 7 | TYR | HIS | VAL | LYS | TYR | ASP | ASP | TYR | PRO | GLU | ||||
| 8 | ASN | GLY | VAL | VAL | GLN | MET | ASN | SER | ARG | ASP | ||||
| 9 | VAL | ARG | ALA | ARG | ALA | ARG | THR | ILE | ILE | LYS | ||||
| 10 | TRP | GLN | ASP | LEU | GLU | VAL | GLY | GLN | VAL | VAL | ||||
| 11 | MET | LEU | ASN | TYR | ASN | PRO | ASP | ASN | PRO | LYS | ||||
| 12 | GLU | ARG | GLY | PHE | TRP | TYR | ASP | ALA | GLU | ILE | ||||
| 13 | SER | ARG | LYS | ARG | GLU | THR | ARG | THR | ALA | ARG | ||||
| 14 | GLU | LEU | TYR | ALA | ASN | VAL | VAL | LEU | GLY | ASP | ||||
| 15 | ASP | SER | LEU | ASN | ASP | CYS | ARG | ILE | ILE | PHE | ||||
| 16 | VAL | ASP | GLU | VAL | PHE | LYS | ILE | GLU | ARG | PRO | ||||
| 17 | GLY | GLU |
Entity 2, Histone H3 11 residues - 1293.529 Da.
| 1 | ALA | ARG | THR | LYS | GLN | THR | ALA | ARG | M3L | SER | ||||
| 2 | THR |
Related Database Links:
| PDB | 2L3R 3DB3 3DB4 4GY5 4QQD |
| DBJ | BAF36719 BAF36720 BAF82078 BAG37156 |
| GB | AAF28469 AAI13876 AAK55744 AAV40831 ABQ59043 |
| REF | NP_001041666 NP_001276979 NP_001276980 NP_001276981 NP_037414 |
| SP | Q96T88 |
| AlphaFold | Q96T88 Q3BDD9 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
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SPARKY: Backbone
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