BMRB Entry 30469
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30469
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Title: NMR structure of the second qRRM2 domain of human hnRNP H PubMed: 30122033
Deposition date: 2018-05-16 Original release date: 2018-08-31
Authors: Srinivasa, R.
Citation: Penumutchu, Srinivasa; Chiu, Liang-Yuan; Meagher, Jennifer; Hansen, Alexandar; Stuckey, Jeanne; Tolbert, Blanton. "Differential Conformational Dynamics Encoded by the Linker between Quasi RNA Recognition Motifs of Heterogeneous Nuclear Ribonucleoprotein H." J. Am. Chem. Soc. 140, 11661-11673 (2018).
Assembly members:
qRRM2 domain of Heterogeneous nuclear ribonucleoprotein H2, polymer, 105 residues, 11791.324 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):
qRRM2 domain of Heterogeneous nuclear ribonucleoprotein H2: SNAMDWVLKHTGPNSPDTAN
DGFVRLRGLPFGCSKEEIVQ
FFSGLEIVPNGITLPVDFQG
RSTGEAFVQFASQEIAEKAL
KKHKERIGHRYIEIFKSSRA
EVRTH
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 380 |
| 15N chemical shifts | 97 |
| 1H chemical shifts | 617 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 105 residues - 11791.324 Da.
| 1 | SER | ASN | ALA | MET | ASP | TRP | VAL | LEU | LYS | HIS | ||||
| 2 | THR | GLY | PRO | ASN | SER | PRO | ASP | THR | ALA | ASN | ||||
| 3 | ASP | GLY | PHE | VAL | ARG | LEU | ARG | GLY | LEU | PRO | ||||
| 4 | PHE | GLY | CYS | SER | LYS | GLU | GLU | ILE | VAL | GLN | ||||
| 5 | PHE | PHE | SER | GLY | LEU | GLU | ILE | VAL | PRO | ASN | ||||
| 6 | GLY | ILE | THR | LEU | PRO | VAL | ASP | PHE | GLN | GLY | ||||
| 7 | ARG | SER | THR | GLY | GLU | ALA | PHE | VAL | GLN | PHE | ||||
| 8 | ALA | SER | GLN | GLU | ILE | ALA | GLU | LYS | ALA | LEU | ||||
| 9 | LYS | LYS | HIS | LYS | GLU | ARG | ILE | GLY | HIS | ARG | ||||
| 10 | TYR | ILE | GLU | ILE | PHE | LYS | SER | SER | ARG | ALA | ||||
| 11 | GLU | VAL | ARG | THR | HIS |
Samples:
sample_1: qRRM2 domain of hnRNP H, C13_N15, 1.5 ± 0.1 mM
sample_conditions_1: ionic strength: 40 mM; pH: 6.2; pressure: 760 mmHg; temperature: 305 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| HNCA | sample_1 | isotropic | sample_conditions_1 |
| HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| HNCACB | sample_1 | isotropic | sample_conditions_1 |
| CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| HNCO | sample_1 | isotropic | sample_conditions_1 |
| HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| (H)CCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| H(C)CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D NOESY-(13C-1H)-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D NOESY-(15N-1H)-HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment, peak picking
ARIA, Linge, O'Donoghue and Nilges - structure calculation
NMR spectrometers:
- Bruker AvanceIII 900 MHz
- Bruker AvanceIII 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts