BMRB Entry 28062
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28062
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Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for RPT1 of hSNF5 and SWIRM of BAF155 PubMed: 32244797
Deposition date: 2020-01-22 Original release date: 2021-07-16
Authors: Han, Jeongmin; Kim, Iktae; Suh, Jeong-Yong; Lee, Weontae
Citation: Han, Jeongmin; Kim, Iktae; Park, Jae-Hyun; Yun, Ji-Hye; Joo, Keehyoung; Kim, Taehee; Park, Gye-Young; Ryu, Kyoung-Seok; Ko, Yoon-Joo; Mizutani, Kenji; Park, Sam-Young; Seong, Rho Hyun; Lee, Jooyoung; Suh, Jeong-Yong; Lee, Weontae. "A Coil-to-Helix Transition Serves as a Binding Motif for hSNF5 and BAF155 Interaction" Int. J. Mol. Sci. 21, 2452-2452 (2020).
Assembly members:
RPT1, polymer, 88 residues, Formula weight is not available
SWIRM, polymer, 98 residues, Formula weight is not available
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 Vector: pET21b
Entity Sequences (FASTA):
RPT1: HDPAVIHENASQPEVLVPIR
LDMEIDGQKLRDAFTWNMNE
KLMTPEMFSEILCDDLDLNP
LTFVPAIASAIRQQIESYPT
DSILEDQS
SWIRM: IIIPSYASWFDYNCIHVIER
RALPEFFNGKNKSKTPEIYL
AYRNFMIDTYRLNPQEYLTS
TACRRNLTGDVCAVMRVHAF
LEQWGLVNYQVDPESRPM
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 157 |
| 15N chemical shifts | 75 |
| 1H chemical shifts | 75 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | subunit 1 | 1 |
| 2 | subunit 2 | 2 |
Entities:
Entity 1, subunit 1 88 residues - Formula weight is not available
| 1 | HIS | ASP | PRO | ALA | VAL | ILE | HIS | GLU | ASN | ALA | ||||
| 2 | SER | GLN | PRO | GLU | VAL | LEU | VAL | PRO | ILE | ARG | ||||
| 3 | LEU | ASP | MET | GLU | ILE | ASP | GLY | GLN | LYS | LEU | ||||
| 4 | ARG | ASP | ALA | PHE | THR | TRP | ASN | MET | ASN | GLU | ||||
| 5 | LYS | LEU | MET | THR | PRO | GLU | MET | PHE | SER | GLU | ||||
| 6 | ILE | LEU | CYS | ASP | ASP | LEU | ASP | LEU | ASN | PRO | ||||
| 7 | LEU | THR | PHE | VAL | PRO | ALA | ILE | ALA | SER | ALA | ||||
| 8 | ILE | ARG | GLN | GLN | ILE | GLU | SER | TYR | PRO | THR | ||||
| 9 | ASP | SER | ILE | LEU | GLU | ASP | GLN | SER |
Entity 2, subunit 2 98 residues - Formula weight is not available
| 1 | ILE | ILE | ILE | PRO | SER | TYR | ALA | SER | TRP | PHE | ||||
| 2 | ASP | TYR | ASN | CYS | ILE | HIS | VAL | ILE | GLU | ARG | ||||
| 3 | ARG | ALA | LEU | PRO | GLU | PHE | PHE | ASN | GLY | LYS | ||||
| 4 | ASN | LYS | SER | LYS | THR | PRO | GLU | ILE | TYR | LEU | ||||
| 5 | ALA | TYR | ARG | ASN | PHE | MET | ILE | ASP | THR | TYR | ||||
| 6 | ARG | LEU | ASN | PRO | GLN | GLU | TYR | LEU | THR | SER | ||||
| 7 | THR | ALA | CYS | ARG | ARG | ASN | LEU | THR | GLY | ASP | ||||
| 8 | VAL | CYS | ALA | VAL | MET | ARG | VAL | HIS | ALA | PHE | ||||
| 9 | LEU | GLU | GLN | TRP | GLY | LEU | VAL | ASN | TYR | GLN | ||||
| 10 | VAL | ASP | PRO | GLU | SER | ARG | PRO | MET |
Samples:
sample_1: RPT1, [U-99% 13C; U-99% 15N], 0.5 mM; SWIRM 0.5 mM; HEPES 10 mM; sodium chloride 100 mM; DTT 2 mM
sample_conditions_1: ionic strength: 100 M; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY vNMRFAM-SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Avance 500 MHz
- 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