BMRB Entry 19910
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19910
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Title: Solution structure of the P22S mutant of N-terminal CS domain of human Shq1 PubMed: 25553844
Deposition date: 2014-04-16 Original release date: 2015-01-12
Authors: Singh, Mahavir; Wang, Zhonghua; Cascio, Duilio; Feigon, Juli
Citation: Singh, Mahavir; Wang, Zhonghua; Cascio, Duilio; Feigon, Juli. "Structure and interactions of the CS domain of human H/ACA RNP assembly protein Shq1" J. Mol. Biol. ., .-..
Assembly members:
P22S_mutant_of_human_Shq1_CS_domain, polymer, 133 residues, 10870.401 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):
P22S_mutant_of_human_Shq1_CS_domain: GSTAIGMKETAAAKFERQHM
DSPDLGTGGGSGDDDDKMLT
PAFDLSQDPDFLTIAIRVSY
ARVSEFDVYFEGSDFKFYAK
PYFLRLTLPGRIVENGSEQG
SYDADKGIFTIRLPKETPGQ
HFEGLNMLTALLA
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 549 |
| 13C chemical shifts | 366 |
| 15N chemical shifts | 90 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | P22S mutant of N-terminal CS domain of human Shq1 | 1 |
Entities:
Entity 1, P22S mutant of N-terminal CS domain of human Shq1 133 residues - 10870.401 Da.
Residues -36 to 0 represent a non-native residues after removal of Gst affinity tag by thrombin
| 1 | GLY | SER | THR | ALA | ILE | GLY | MET | LYS | GLU | THR | ||||
| 2 | ALA | ALA | ALA | LYS | PHE | GLU | ARG | GLN | HIS | MET | ||||
| 3 | ASP | SER | PRO | ASP | LEU | GLY | THR | GLY | GLY | GLY | ||||
| 4 | SER | GLY | ASP | ASP | ASP | ASP | LYS | MET | LEU | THR | ||||
| 5 | PRO | ALA | PHE | ASP | LEU | SER | GLN | ASP | PRO | ASP | ||||
| 6 | PHE | LEU | THR | ILE | ALA | ILE | ARG | VAL | SER | TYR | ||||
| 7 | ALA | ARG | VAL | SER | GLU | PHE | ASP | VAL | TYR | PHE | ||||
| 8 | GLU | GLY | SER | ASP | PHE | LYS | PHE | TYR | ALA | LYS | ||||
| 9 | PRO | TYR | PHE | LEU | ARG | LEU | THR | LEU | PRO | GLY | ||||
| 10 | ARG | ILE | VAL | GLU | ASN | GLY | SER | GLU | GLN | GLY | ||||
| 11 | SER | TYR | ASP | ALA | ASP | LYS | GLY | ILE | PHE | THR | ||||
| 12 | ILE | ARG | LEU | PRO | LYS | GLU | THR | PRO | GLY | GLN | ||||
| 13 | HIS | PHE | GLU | GLY | LEU | ASN | MET | LEU | THR | ALA | ||||
| 14 | LEU | LEU | ALA |
Samples:
sample_1: P22S mutant of human Shq1 CS domain, [U-15N], 0.5 – 1 mM; sodium phosphate 20 mM; sodium chloride 100 mM; DTT 1 mM; H2O 95%; D2O 5%
sample_2: P22S mutant of human Shq1 CS domain, [U-99% 13C; U-99% 15N], 0.5 – 1 mM; sodium phosphate 20 mM; sodium chloride 100 mM; DTT 1 mM; H2O 95%; D2O 5%
sample_3: P22S mutant of human Shq1 CS domain, [U-99% 13C; U-99% 15N], 0.5 – 1 mM; sodium phosphate 20 mM; sodium chloride 100 mM; DTT 1 mM; D2O 100%
sample_conditions_1: temperature: 298 K; pH: 7; pressure: 1 atm; ionic strength: 100 mM
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_3 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_2 | isotropic | sample_conditions_1 |
Software:
xwinnmr, Bruker Biospin - collection, processing, data analysis
TOPSPIN, Bruker Biospin - collection, data analysis, processing
X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis, chemical shift assignment, processing
SPARKY, Goddard - data analysis, chemical shift assignment, chemical shift calculation
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift calculation, data analysis, processing
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker DRX 600 MHz
- Bruker DRX 500 MHz
Related Database Links:
| BMRB | 25167 |
| PDB | |
| GB | AAH17204 AAH17274 AAH25270 AAH32671 AAH39830 |
| REF | NP_060600 XP_001082636 XP_001141951 XP_003264945 XP_003780373 |
| SP | Q6PI26 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts