BMRB Entry 17402
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17402
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Title: Structure/function of the LBR Tudor domain PubMed: 22052904
Deposition date: 2011-01-10 Original release date: 2011-12-02
Authors: Liokatis, Stamatios; Edlich, Christian; Soupsana, Katerina; Giannios, Ioannis; Sattler, Michael; Georgatos, Spyros; Politou, Anastasia
Citation: Liokatis, Stamatis; Edlich, Christian; Soupsana, Katerina; Giannios, Ioannis; Panagiotidou, Parthena; Tripsianes, Konstantinos; Sattler, Michael; Georgatos, Spyros; Politou, Anastasia. "Solution structure and molecular interactions of lamin B receptor Tudor domain." J. Biol. Chem. 287, 1032-1042 (2012).
Assembly members:
LBR_Tudor_domain, polymer, 66 residues, 7490.461 Da.
Natural source: Common Name: chicken Taxonomy ID: 9031 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Gallus gallus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
LBR_Tudor_domain: GAMGMPNRKYADGEVVMGRW
PGSVLYYEVQVTSYDDASHL
YTVKYKDGTELALKESDIRL
QSSFKQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 230 |
| 15N chemical shifts | 69 |
| 1H chemical shifts | 451 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | LBR_Tudor_domain | 1 |
Entities:
Entity 1, LBR_Tudor_domain 66 residues - 7490.461 Da.
| 1 | GLY | ALA | MET | GLY | MET | PRO | ASN | ARG | LYS | TYR | ||||
| 2 | ALA | ASP | GLY | GLU | VAL | VAL | MET | GLY | ARG | TRP | ||||
| 3 | PRO | GLY | SER | VAL | LEU | TYR | TYR | GLU | VAL | GLN | ||||
| 4 | VAL | THR | SER | TYR | ASP | ASP | ALA | SER | HIS | LEU | ||||
| 5 | TYR | THR | VAL | LYS | TYR | LYS | ASP | GLY | THR | GLU | ||||
| 6 | LEU | ALA | LEU | LYS | GLU | SER | ASP | ILE | ARG | LEU | ||||
| 7 | GLN | SER | SER | PHE | LYS | GLN |
Samples:
sample_1: LBR_Tudor_domain 0.8 mM; sodium phosphate 20 mM; sodium chloride 100 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 6.9; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | 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 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TALOS, Cornilescu, Delaglio and Bax - dihedral angle restraints
ProcheckNMR, Laskowski and MacArthur - structure quality analysis
WhatIF, Vriend - structure quality analysis
Molmol, Koradi, Billeter and Wuthrich - molecular images
TOPSPIN, Bruker Biospin - collection
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Bruker DRX 500 MHz
- Bruker DRX 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts