BMRB Entry 19626
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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/BMR19626
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Title: 1H,13C and 15N assignment of Rsa1p(317-352)/Hit1p((70-164) PubMed: 25170085
Deposition date: 2013-11-21 Original release date: 2014-09-08
Authors: Quinternet, Marc; Roth, Benjamin; Back, Regis; Jacquemin, Clemence; Manival, Xavier
Citation: Rothe, Benjamin; Saliou, Jean-Michel; Quinternet, Marc; Back, Regis; Tiotiu, Decebal; Jacquemin, Clemence; Loegler, Christine; Schlotter, Florence; Pena, Vlad; Eckert, Kelvin; Morera, Solange; Dorsselaer, Alain Van; Branlant, Christiane; Massenet, Severine; Sanglier-Cianferani, Sarah; Manival, Xavier; Charpentier, Bruno. "Protein Hit1, a novel box C/D snoRNP assembly factor, controls cellular concentration of the scaffolding protein Rsa1 by direct interaction." Nucleic Acids Res. 42, 10731-10747 (2014).
Assembly members:
rsa, polymer, 63 residues, Formula weight is not available
hit, polymer, 122 residues, Formula weight is not available
Natural source: Common Name: baker Taxonomy ID: 4932 Superkingdom: not available Kingdom: not available Genus/species: Eukaryota Fungi
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
rsa: GPHMFANENSQLLDFIRELG
DVGLLEYELSQQEKDVLFGS
SEDNNKNHYKPNYKNRKPNL
SRA
hit: MSEQPRAGTEANVEVVNNDK
IINSSLAMNKTLKTKAFDDI
YQNSAELQELLKYNTVKFHL
AKVYRILSSTVNDGSSGKMN
SDLQKELAVNYLNTLRYGGI
HYNEAIEEFCQILLDKLNAV
KK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 596 |
| 15N chemical shifts | 149 |
| 1H chemical shifts | 970 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | rsa | 1 |
| 2 | hit | 2 |
Entities:
Entity 1, rsa 63 residues - Formula weight is not available
| 1 | GLY | PRO | HIS | MET | PHE | ALA | ASN | GLU | ASN | SER | ||||
| 2 | GLN | LEU | LEU | ASP | PHE | ILE | ARG | GLU | LEU | GLY | ||||
| 3 | ASP | VAL | GLY | LEU | LEU | GLU | TYR | GLU | LEU | SER | ||||
| 4 | GLN | GLN | GLU | LYS | ASP | VAL | LEU | PHE | GLY | SER | ||||
| 5 | SER | GLU | ASP | ASN | ASN | LYS | ASN | HIS | TYR | LYS | ||||
| 6 | PRO | ASN | TYR | LYS | ASN | ARG | LYS | PRO | ASN | LEU | ||||
| 7 | SER | ARG | ALA |
Entity 2, hit 122 residues - Formula weight is not available
| 1 | MET | SER | GLU | GLN | PRO | ARG | ALA | GLY | THR | GLU | ||||
| 2 | ALA | ASN | VAL | GLU | VAL | VAL | ASN | ASN | ASP | LYS | ||||
| 3 | ILE | ILE | ASN | SER | SER | LEU | ALA | MET | ASN | LYS | ||||
| 4 | THR | LEU | LYS | THR | LYS | ALA | PHE | ASP | ASP | ILE | ||||
| 5 | TYR | GLN | ASN | SER | ALA | GLU | LEU | GLN | GLU | LEU | ||||
| 6 | LEU | LYS | TYR | ASN | THR | VAL | LYS | PHE | HIS | LEU | ||||
| 7 | ALA | LYS | VAL | TYR | ARG | ILE | LEU | SER | SER | THR | ||||
| 8 | VAL | ASN | ASP | GLY | SER | SER | GLY | LYS | MET | ASN | ||||
| 9 | SER | ASP | LEU | GLN | LYS | GLU | LEU | ALA | VAL | ASN | ||||
| 10 | TYR | LEU | ASN | THR | LEU | ARG | TYR | GLY | GLY | ILE | ||||
| 11 | HIS | TYR | ASN | GLU | ALA | ILE | GLU | GLU | PHE | CYS | ||||
| 12 | GLN | ILE | LEU | LEU | ASP | LYS | LEU | ASN | ALA | VAL | ||||
| 13 | LYS | LYS |
Samples:
sample_1: rsa, [U-100% 13C; U-100% 15N], 1 mM; hit, [U-100% 13C; U-100% 15N], 1 mM; sodium chloride 150 mM; H2O 90%; D2O, [U-100% 2H], 10%
sample_conditions_1: ionic strength: 150 mM; pH: 6.4; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | 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 HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | 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 |
| 3D 1H-13C NOESY aromatic | 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 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.0, Bruker Biospin - collection, processing
CARA, Keller and Wuthrich - chemical shift assignment
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 950 MHz
Related Database Links:
| PDB | |
| DBJ | GAA26783 BAA01878 GAA24403 |
| EMBL | CAA97906 CAY86767 CAA89583 CBK33766 |
| GB | AHY77988 AJP41956 AJU23400 AJU24088 AJU24761 AAB39281 AAS56423 AHY79041 EDN63374 EDV12797 |
| REF | NP_015131 NP_012589 |
| SP | Q08932 P46973 |
| TPG | DAA11241 DAA08842 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts