BMRB Entry 34442
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34442
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
Title: Solution structure of the HRP2 IBD PubMed: 33477970
Deposition date: 2019-10-11 Original release date: 2020-11-12
Authors: Veverka, V.
Citation: Van Belle, Siska; El Ashkar, Sara; Cermakova, Katerina; Matthijssens, Filip; Goossens, Steven; Canella, Alessandro; Hodges, Courtney; Christ, Frauke; De Rijck, Jan; Van Vlierberghe, Pieter; Veverka, Vaclav; Debyser, Zeger. "Unlike Its Paralog LEDGF/p75, HRP-2 Is Dispensable for MLL-R Leukemogenesis but Important for Leukemic Cell Survival" Cells 10, 192-192 (2021).
Assembly members:
entity_1, polymer, 86 residues, 9675.237 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: AASPSVEEKLQKLHSEIKFA
LKVDSPDVKRCLNALEELGT
LQVTSQILQKNTDVVATLKK
IRRYKANKDVMEKAAEVYTR
LKSRGS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 384 |
| 15N chemical shifts | 85 |
| 1H chemical shifts | 629 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 86 residues - 9675.237 Da.
| 1 | ALA | ALA | SER | PRO | SER | VAL | GLU | GLU | LYS | LEU | ||||
| 2 | GLN | LYS | LEU | HIS | SER | GLU | ILE | LYS | PHE | ALA | ||||
| 3 | LEU | LYS | VAL | ASP | SER | PRO | ASP | VAL | LYS | ARG | ||||
| 4 | CYS | LEU | ASN | ALA | LEU | GLU | GLU | LEU | GLY | THR | ||||
| 5 | LEU | GLN | VAL | THR | SER | GLN | ILE | LEU | GLN | LYS | ||||
| 6 | ASN | THR | ASP | VAL | VAL | ALA | THR | LEU | LYS | LYS | ||||
| 7 | ILE | ARG | ARG | TYR | LYS | ALA | ASN | LYS | ASP | VAL | ||||
| 8 | MET | GLU | LYS | ALA | ALA | GLU | VAL | TYR | THR | ARG | ||||
| 9 | LEU | LYS | SER | ARG | GLY | SER |
Samples:
sample_1: HRP2, [U-13C; U-15N], 0.5 mM; TRIS 25 mM; NaCl 150 mM; TCEP 1 mM
sample_conditions_1: ionic strength: 175 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | 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 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
TopSpin, Bruker Biospin - collection
Sparky, Goddard - chemical shift assignment
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
YASARA, Yasara - refinement
NMR spectrometers:
- Bruker AVANCE 850 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts